data_9N5V
# 
_entry.id   9N5V 
# 
_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   9N5V         pdb_00009n5v 10.2210/pdb9n5v/pdb 
WWPDB D_1000292439 ?            ?                   
EMDB  EMD-49040    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-07 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9N5V 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-04 
_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 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Structure of the NAD(H)-bound Thermococcus sibiricus NfnABC complex' 
_pdbx_database_related.db_id          EMD-49040 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              Huilin.Li@vai.org 
_pdbx_contact_author.name_first         Huilin 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8085-8928 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xiao, X.' 1 ? 
'Li, H.'   2 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108410 
_citation.page_last                 108410 
_citation.title                     
;Cryo-EM structures define the electron bifurcating flavobicluster and ferredoxin binding site in an archaeal Nfn-Bfu transhydrogenase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108410 
_citation.pdbx_database_id_PubMed   40107619 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xiao, X.'       1 ? 
primary 'Schut, G.J.'    2 ? 
primary 'Feng, X.'       3 ? 
primary 'Nguyen, D.M.N.' 4 ? 
primary 'Huang, H.'      5 ? 
primary 'Wang, S.'       6 ? 
primary 'Li, H.'         7 ? 
primary 'Adams, M.W.W.'  8 ? 
# 
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 NfnA                              107912.820 1 ? ? ? ? 
2 polymer     man NfnB                              66237.703  1 ? ? ? ? 
3 polymer     man NfnC                              17382.266  1 ? ? ? ? 
4 non-polymer nat 'IRON/SULFUR CLUSTER'             351.640    8 ? ? ? ? 
5 non-polymer nat 'FLAVIN-ADENINE DINUCLEOTIDE'     785.550    1 ? ? ? ? 
6 non-polymer nat 'FE2/S2 (INORGANIC) CLUSTER'      175.820    1 ? ? ? ? 
7 non-polymer nat 'FLAVIN MONONUCLEOTIDE'           456.344    1 ? ? ? ? 
8 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE 663.425    1 ? ? ? ? 
9 non-polymer syn 'ZINC ION'                        65.409     2 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
2 'NADH:ubiquinone oxidoreductase, NADH-binding subunit F' 
3 'NADH:ubiquinone oxidoreductase, subunit E'              
# 
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 
;MPRRRVSEMVKITVNGKEFEAPKDKSLIEFLREITHVPGFCYTEAFDPYGSCRLCLVQTPRGITTSCTLKPMEGLSIETL
SDEIIEMRKTALELILSDHYGDCIGPCQNGCPAHSDVQGYLALIAMGRYHEAVKLMKEKYILPAVLGRVCPAFCEEECRR
NLVEEPLAIRQLKRFAADYDLENGPWMPEIPPSTGKRIAVVGGGPAGLACAYYLRTMGHDVTIFDAMPHLGGMMRYGIPP
YRLPKDVLDKDIATVINTGIEVKTNTALGKDIALEELREQYDAVFLGVGAWKSRKMGIEGEDLDGVIHGTEFLRKVNMGE
KVELGKRVIVVGGGNTAMDVARTALRLGADVTVVYRRSKSEMPANSREVEEAEEEGVKFMFLTNPVKIIGKEKVEEVELI
KMKLGEPDASGRRRPMPIEGSEFRVKVDNVILAIGQYCDEEFLRTIGIEAKRGRVLVDEVTLQTNKEGVFAGGDLVLGPS
TVIESIATGRRAAIMIDLYLKGKLEKAREVLLDPSKHIEEVIYDEDLYRVLFDLRPYNHWKKVTEKDYEHVERKPRVKVK
LLDPEIRKSNFKEVEPTMDEETVLTEAQRCMSCGCMEVFRCKLREYATLYDAKQDAFVGEQNKFEIDETHPNVVLDNNKC
VLCGQCVNFTHEIAREGIVDYLFRGFKTYIGPQLGERLEDQKGVFIGELTDICPVGAITEKLPFVKPGPWKTQPVKTVCN
GCSFACEMNIEVYNDILVRASSRKDSWNGYICDYCRFERPWAQDIAQPILKGNAVSWEDAEKFLEEKECALILTPSLTNE
EIMFLKELAERKGIPIGSTIDGEGSTATLEDIRNAKRVLLKVNIEKYPLLKLLLKGKEIVEEGYEVAIIEGPAEPMDVPT
LILHDGVNATGLIKAGVTGIPEAKAYVVIGNSPAISKLKGEYLILPSGLWAEKEGTVTNAFGMDLKVKKARKAHYDVKSL
FNF
;
;MPRRRVSEMVKITVNGKEFEAPKDKSLIEFLREITHVPGFCYTEAFDPYGSCRLCLVQTPRGITTSCTLKPMEGLSIETL
SDEIIEMRKTALELILSDHYGDCIGPCQNGCPAHSDVQGYLALIAMGRYHEAVKLMKEKYILPAVLGRVCPAFCEEECRR
NLVEEPLAIRQLKRFAADYDLENGPWMPEIPPSTGKRIAVVGGGPAGLACAYYLRTMGHDVTIFDAMPHLGGMMRYGIPP
YRLPKDVLDKDIATVINTGIEVKTNTALGKDIALEELREQYDAVFLGVGAWKSRKMGIEGEDLDGVIHGTEFLRKVNMGE
KVELGKRVIVVGGGNTAMDVARTALRLGADVTVVYRRSKSEMPANSREVEEAEEEGVKFMFLTNPVKIIGKEKVEEVELI
KMKLGEPDASGRRRPMPIEGSEFRVKVDNVILAIGQYCDEEFLRTIGIEAKRGRVLVDEVTLQTNKEGVFAGGDLVLGPS
TVIESIATGRRAAIMIDLYLKGKLEKAREVLLDPSKHIEEVIYDEDLYRVLFDLRPYNHWKKVTEKDYEHVERKPRVKVK
LLDPEIRKSNFKEVEPTMDEETVLTEAQRCMSCGCMEVFRCKLREYATLYDAKQDAFVGEQNKFEIDETHPNVVLDNNKC
VLCGQCVNFTHEIAREGIVDYLFRGFKTYIGPQLGERLEDQKGVFIGELTDICPVGAITEKLPFVKPGPWKTQPVKTVCN
GCSFACEMNIEVYNDILVRASSRKDSWNGYICDYCRFERPWAQDIAQPILKGNAVSWEDAEKFLEEKECALILTPSLTNE
EIMFLKELAERKGIPIGSTIDGEGSTATLEDIRNAKRVLLKVNIEKYPLLKLLLKGKEIVEEGYEVAIIEGPAEPMDVPT
LILHDGVNATGLIKAGVTGIPEAKAYVVIGNSPAISKLKGEYLILPSGLWAEKEGTVTNAFGMDLKVKKARKAHYDVKSL
FNF
;
A ? 
2 'polypeptide(L)' no no 
;MSEIKAIAVGMNSCGIAAGARETYEAVKEELEKRNLDIKLKIVGCVGMCYREPLLDIITDNEIITYGHVTPDRVPRIIEE
HVINGKPIEDWVVKKDWWENGQRKTWDFDGYFVKQKKIVLENSGYIDPENIEEYIAAGGYEALKKAFKMKPEEIIDFITK
SGLRGRGGAGFPTGLKWKFTRDAPGDEKYIVCNADEGDPGAFMDRNVLEGDPHRVIEGMIIGAYAIGATKGFIYVRAEYP
LAIKRLRIALKQAREKGFLGENILGSGFSFEIVIKEGAGAFVCGEETALIASIEGKRGMPRPRPPYPAQKGLWGRPTNIN
NVETWANVPWIIKHGWEAYAALGTEKSKGTKVFALSGKIKHGGNVEVPMGITLREILYEIGGGTKTGKKIKAVQLGGPSG
GCIPDYLFNTPVDYESVTATGAIMGSGGMVVMDEDTCMVDVAKFFLDFTVKESCGKCTFCRLGTKRMWELLDKITKGEGA
LEDIEKLEKLAPLVKTGSLCGLGQTAPNPVLTTLKYFKDEYLAHIEGRCPAKVCKPLIKYVIITEKCTGCTACAIMCPVK
AISGERGKPHLINQEACIKCGTCYEVCRFNAIEITDAKKEGE
;
;MSEIKAIAVGMNSCGIAAGARETYEAVKEELEKRNLDIKLKIVGCVGMCYREPLLDIITDNEIITYGHVTPDRVPRIIEE
HVINGKPIEDWVVKKDWWENGQRKTWDFDGYFVKQKKIVLENSGYIDPENIEEYIAAGGYEALKKAFKMKPEEIIDFITK
SGLRGRGGAGFPTGLKWKFTRDAPGDEKYIVCNADEGDPGAFMDRNVLEGDPHRVIEGMIIGAYAIGATKGFIYVRAEYP
LAIKRLRIALKQAREKGFLGENILGSGFSFEIVIKEGAGAFVCGEETALIASIEGKRGMPRPRPPYPAQKGLWGRPTNIN
NVETWANVPWIIKHGWEAYAALGTEKSKGTKVFALSGKIKHGGNVEVPMGITLREILYEIGGGTKTGKKIKAVQLGGPSG
GCIPDYLFNTPVDYESVTATGAIMGSGGMVVMDEDTCMVDVAKFFLDFTVKESCGKCTFCRLGTKRMWELLDKITKGEGA
LEDIEKLEKLAPLVKTGSLCGLGQTAPNPVLTTLKYFKDEYLAHIEGRCPAKVCKPLIKYVIITEKCTGCTACAIMCPVK
AISGERGKPHLINQEACIKCGTCYEVCRFNAIEITDAKKEGE
;
B ? 
3 'polypeptide(L)' no no 
;MNIQLEYIYHYEPNPSSLIPLLQKTQETFGYLPKEALEEISRYLKVPLSRVYGVATFYAQFRFEPLGKYVIKICHGTACH
VNGAVNISQAIREEVGIEEGQTTVDGLITLERVACLGCCSLAPVIMINEKVYGKLTPDKVRKIIRNLKEGKLNV
;
;MNIQLEYIYHYEPNPSSLIPLLQKTQETFGYLPKEALEEISRYLKVPLSRVYGVATFYAQFRFEPLGKYVIKICHGTACH
VNGAVNISQAIREEVGIEEGQTTVDGLITLERVACLGCCSLAPVIMINEKVYGKLTPDKVRKIIRNLKEGKLNV
;
C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'IRON/SULFUR CLUSTER'             SF4 
5 'FLAVIN-ADENINE DINUCLEOTIDE'     FAD 
6 'FE2/S2 (INORGANIC) CLUSTER'      FES 
7 'FLAVIN MONONUCLEOTIDE'           FMN 
8 NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD 
9 'ZINC ION'                        ZN  
# 
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   PRO n 
1 3   ARG n 
1 4   ARG n 
1 5   ARG n 
1 6   VAL n 
1 7   SER n 
1 8   GLU n 
1 9   MET n 
1 10  VAL n 
1 11  LYS n 
1 12  ILE n 
1 13  THR n 
1 14  VAL n 
1 15  ASN n 
1 16  GLY n 
1 17  LYS n 
1 18  GLU n 
1 19  PHE n 
1 20  GLU n 
1 21  ALA n 
1 22  PRO n 
1 23  LYS n 
1 24  ASP n 
1 25  LYS n 
1 26  SER n 
1 27  LEU n 
1 28  ILE n 
1 29  GLU n 
1 30  PHE n 
1 31  LEU n 
1 32  ARG n 
1 33  GLU n 
1 34  ILE n 
1 35  THR n 
1 36  HIS n 
1 37  VAL n 
1 38  PRO n 
1 39  GLY n 
1 40  PHE n 
1 41  CYS n 
1 42  TYR n 
1 43  THR n 
1 44  GLU n 
1 45  ALA n 
1 46  PHE n 
1 47  ASP n 
1 48  PRO n 
1 49  TYR n 
1 50  GLY n 
1 51  SER n 
1 52  CYS n 
1 53  ARG n 
1 54  LEU n 
1 55  CYS n 
1 56  LEU n 
1 57  VAL n 
1 58  GLN n 
1 59  THR n 
1 60  PRO n 
1 61  ARG n 
1 62  GLY n 
1 63  ILE n 
1 64  THR n 
1 65  THR n 
1 66  SER n 
1 67  CYS n 
1 68  THR n 
1 69  LEU n 
1 70  LYS n 
1 71  PRO n 
1 72  MET n 
1 73  GLU n 
1 74  GLY n 
1 75  LEU n 
1 76  SER n 
1 77  ILE n 
1 78  GLU n 
1 79  THR n 
1 80  LEU n 
1 81  SER n 
1 82  ASP n 
1 83  GLU n 
1 84  ILE n 
1 85  ILE n 
1 86  GLU n 
1 87  MET n 
1 88  ARG n 
1 89  LYS n 
1 90  THR n 
1 91  ALA n 
1 92  LEU n 
1 93  GLU n 
1 94  LEU n 
1 95  ILE n 
1 96  LEU n 
1 97  SER n 
1 98  ASP n 
1 99  HIS n 
1 100 TYR n 
1 101 GLY n 
1 102 ASP n 
1 103 CYS n 
1 104 ILE n 
1 105 GLY n 
1 106 PRO n 
1 107 CYS n 
1 108 GLN n 
1 109 ASN n 
1 110 GLY n 
1 111 CYS n 
1 112 PRO n 
1 113 ALA n 
1 114 HIS n 
1 115 SER n 
1 116 ASP n 
1 117 VAL n 
1 118 GLN n 
1 119 GLY n 
1 120 TYR n 
1 121 LEU n 
1 122 ALA n 
1 123 LEU n 
1 124 ILE n 
1 125 ALA n 
1 126 MET n 
1 127 GLY n 
1 128 ARG n 
1 129 TYR n 
1 130 HIS n 
1 131 GLU n 
1 132 ALA n 
1 133 VAL n 
1 134 LYS n 
1 135 LEU n 
1 136 MET n 
1 137 LYS n 
1 138 GLU n 
1 139 LYS n 
1 140 TYR n 
1 141 ILE n 
1 142 LEU n 
1 143 PRO n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 ARG n 
1 149 VAL n 
1 150 CYS n 
1 151 PRO n 
1 152 ALA n 
1 153 PHE n 
1 154 CYS n 
1 155 GLU n 
1 156 GLU n 
1 157 GLU n 
1 158 CYS n 
1 159 ARG n 
1 160 ARG n 
1 161 ASN n 
1 162 LEU n 
1 163 VAL n 
1 164 GLU n 
1 165 GLU n 
1 166 PRO n 
1 167 LEU n 
1 168 ALA n 
1 169 ILE n 
1 170 ARG n 
1 171 GLN n 
1 172 LEU n 
1 173 LYS n 
1 174 ARG n 
1 175 PHE n 
1 176 ALA n 
1 177 ALA n 
1 178 ASP n 
1 179 TYR n 
1 180 ASP n 
1 181 LEU n 
1 182 GLU n 
1 183 ASN n 
1 184 GLY n 
1 185 PRO n 
1 186 TRP n 
1 187 MET n 
1 188 PRO n 
1 189 GLU n 
1 190 ILE n 
1 191 PRO n 
1 192 PRO n 
1 193 SER n 
1 194 THR n 
1 195 GLY n 
1 196 LYS n 
1 197 ARG n 
1 198 ILE n 
1 199 ALA n 
1 200 VAL n 
1 201 VAL n 
1 202 GLY n 
1 203 GLY n 
1 204 GLY n 
1 205 PRO n 
1 206 ALA n 
1 207 GLY n 
1 208 LEU n 
1 209 ALA n 
1 210 CYS n 
1 211 ALA n 
1 212 TYR n 
1 213 TYR n 
1 214 LEU n 
1 215 ARG n 
1 216 THR n 
1 217 MET n 
1 218 GLY n 
1 219 HIS n 
1 220 ASP n 
1 221 VAL n 
1 222 THR n 
1 223 ILE n 
1 224 PHE n 
1 225 ASP n 
1 226 ALA n 
1 227 MET n 
1 228 PRO n 
1 229 HIS n 
1 230 LEU n 
1 231 GLY n 
1 232 GLY n 
1 233 MET n 
1 234 MET n 
1 235 ARG n 
1 236 TYR n 
1 237 GLY n 
1 238 ILE n 
1 239 PRO n 
1 240 PRO n 
1 241 TYR n 
1 242 ARG n 
1 243 LEU n 
1 244 PRO n 
1 245 LYS n 
1 246 ASP n 
1 247 VAL n 
1 248 LEU n 
1 249 ASP n 
1 250 LYS n 
1 251 ASP n 
1 252 ILE n 
1 253 ALA n 
1 254 THR n 
1 255 VAL n 
1 256 ILE n 
1 257 ASN n 
1 258 THR n 
1 259 GLY n 
1 260 ILE n 
1 261 GLU n 
1 262 VAL n 
1 263 LYS n 
1 264 THR n 
1 265 ASN n 
1 266 THR n 
1 267 ALA n 
1 268 LEU n 
1 269 GLY n 
1 270 LYS n 
1 271 ASP n 
1 272 ILE n 
1 273 ALA n 
1 274 LEU n 
1 275 GLU n 
1 276 GLU n 
1 277 LEU n 
1 278 ARG n 
1 279 GLU n 
1 280 GLN n 
1 281 TYR n 
1 282 ASP n 
1 283 ALA n 
1 284 VAL n 
1 285 PHE n 
1 286 LEU n 
1 287 GLY n 
1 288 VAL n 
1 289 GLY n 
1 290 ALA n 
1 291 TRP n 
1 292 LYS n 
1 293 SER n 
1 294 ARG n 
1 295 LYS n 
1 296 MET n 
1 297 GLY n 
1 298 ILE n 
1 299 GLU n 
1 300 GLY n 
1 301 GLU n 
1 302 ASP n 
1 303 LEU n 
1 304 ASP n 
1 305 GLY n 
1 306 VAL n 
1 307 ILE n 
1 308 HIS n 
1 309 GLY n 
1 310 THR n 
1 311 GLU n 
1 312 PHE n 
1 313 LEU n 
1 314 ARG n 
1 315 LYS n 
1 316 VAL n 
1 317 ASN n 
1 318 MET n 
1 319 GLY n 
1 320 GLU n 
1 321 LYS n 
1 322 VAL n 
1 323 GLU n 
1 324 LEU n 
1 325 GLY n 
1 326 LYS n 
1 327 ARG n 
1 328 VAL n 
1 329 ILE n 
1 330 VAL n 
1 331 VAL n 
1 332 GLY n 
1 333 GLY n 
1 334 GLY n 
1 335 ASN n 
1 336 THR n 
1 337 ALA n 
1 338 MET n 
1 339 ASP n 
1 340 VAL n 
1 341 ALA n 
1 342 ARG n 
1 343 THR n 
1 344 ALA n 
1 345 LEU n 
1 346 ARG n 
1 347 LEU n 
1 348 GLY n 
1 349 ALA n 
1 350 ASP n 
1 351 VAL n 
1 352 THR n 
1 353 VAL n 
1 354 VAL n 
1 355 TYR n 
1 356 ARG n 
1 357 ARG n 
1 358 SER n 
1 359 LYS n 
1 360 SER n 
1 361 GLU n 
1 362 MET n 
1 363 PRO n 
1 364 ALA n 
1 365 ASN n 
1 366 SER n 
1 367 ARG n 
1 368 GLU n 
1 369 VAL n 
1 370 GLU n 
1 371 GLU n 
1 372 ALA n 
1 373 GLU n 
1 374 GLU n 
1 375 GLU n 
1 376 GLY n 
1 377 VAL n 
1 378 LYS n 
1 379 PHE n 
1 380 MET n 
1 381 PHE n 
1 382 LEU n 
1 383 THR n 
1 384 ASN n 
1 385 PRO n 
1 386 VAL n 
1 387 LYS n 
1 388 ILE n 
1 389 ILE n 
1 390 GLY n 
1 391 LYS n 
1 392 GLU n 
1 393 LYS n 
1 394 VAL n 
1 395 GLU n 
1 396 GLU n 
1 397 VAL n 
1 398 GLU n 
1 399 LEU n 
1 400 ILE n 
1 401 LYS n 
1 402 MET n 
1 403 LYS n 
1 404 LEU n 
1 405 GLY n 
1 406 GLU n 
1 407 PRO n 
1 408 ASP n 
1 409 ALA n 
1 410 SER n 
1 411 GLY n 
1 412 ARG n 
1 413 ARG n 
1 414 ARG n 
1 415 PRO n 
1 416 MET n 
1 417 PRO n 
1 418 ILE n 
1 419 GLU n 
1 420 GLY n 
1 421 SER n 
1 422 GLU n 
1 423 PHE n 
1 424 ARG n 
1 425 VAL n 
1 426 LYS n 
1 427 VAL n 
1 428 ASP n 
1 429 ASN n 
1 430 VAL n 
1 431 ILE n 
1 432 LEU n 
1 433 ALA n 
1 434 ILE n 
1 435 GLY n 
1 436 GLN n 
1 437 TYR n 
1 438 CYS n 
1 439 ASP n 
1 440 GLU n 
1 441 GLU n 
1 442 PHE n 
1 443 LEU n 
1 444 ARG n 
1 445 THR n 
1 446 ILE n 
1 447 GLY n 
1 448 ILE n 
1 449 GLU n 
1 450 ALA n 
1 451 LYS n 
1 452 ARG n 
1 453 GLY n 
1 454 ARG n 
1 455 VAL n 
1 456 LEU n 
1 457 VAL n 
1 458 ASP n 
1 459 GLU n 
1 460 VAL n 
1 461 THR n 
1 462 LEU n 
1 463 GLN n 
1 464 THR n 
1 465 ASN n 
1 466 LYS n 
1 467 GLU n 
1 468 GLY n 
1 469 VAL n 
1 470 PHE n 
1 471 ALA n 
1 472 GLY n 
1 473 GLY n 
1 474 ASP n 
1 475 LEU n 
1 476 VAL n 
1 477 LEU n 
1 478 GLY n 
1 479 PRO n 
1 480 SER n 
1 481 THR n 
1 482 VAL n 
1 483 ILE n 
1 484 GLU n 
1 485 SER n 
1 486 ILE n 
1 487 ALA n 
1 488 THR n 
1 489 GLY n 
1 490 ARG n 
1 491 ARG n 
1 492 ALA n 
1 493 ALA n 
1 494 ILE n 
1 495 MET n 
1 496 ILE n 
1 497 ASP n 
1 498 LEU n 
1 499 TYR n 
1 500 LEU n 
1 501 LYS n 
1 502 GLY n 
1 503 LYS n 
1 504 LEU n 
1 505 GLU n 
1 506 LYS n 
1 507 ALA n 
1 508 ARG n 
1 509 GLU n 
1 510 VAL n 
1 511 LEU n 
1 512 LEU n 
1 513 ASP n 
1 514 PRO n 
1 515 SER n 
1 516 LYS n 
1 517 HIS n 
1 518 ILE n 
1 519 GLU n 
1 520 GLU n 
1 521 VAL n 
1 522 ILE n 
1 523 TYR n 
1 524 ASP n 
1 525 GLU n 
1 526 ASP n 
1 527 LEU n 
1 528 TYR n 
1 529 ARG n 
1 530 VAL n 
1 531 LEU n 
1 532 PHE n 
1 533 ASP n 
1 534 LEU n 
1 535 ARG n 
1 536 PRO n 
1 537 TYR n 
1 538 ASN n 
1 539 HIS n 
1 540 TRP n 
1 541 LYS n 
1 542 LYS n 
1 543 VAL n 
1 544 THR n 
1 545 GLU n 
1 546 LYS n 
1 547 ASP n 
1 548 TYR n 
1 549 GLU n 
1 550 HIS n 
1 551 VAL n 
1 552 GLU n 
1 553 ARG n 
1 554 LYS n 
1 555 PRO n 
1 556 ARG n 
1 557 VAL n 
1 558 LYS n 
1 559 VAL n 
1 560 LYS n 
1 561 LEU n 
1 562 LEU n 
1 563 ASP n 
1 564 PRO n 
1 565 GLU n 
1 566 ILE n 
1 567 ARG n 
1 568 LYS n 
1 569 SER n 
1 570 ASN n 
1 571 PHE n 
1 572 LYS n 
1 573 GLU n 
1 574 VAL n 
1 575 GLU n 
1 576 PRO n 
1 577 THR n 
1 578 MET n 
1 579 ASP n 
1 580 GLU n 
1 581 GLU n 
1 582 THR n 
1 583 VAL n 
1 584 LEU n 
1 585 THR n 
1 586 GLU n 
1 587 ALA n 
1 588 GLN n 
1 589 ARG n 
1 590 CYS n 
1 591 MET n 
1 592 SER n 
1 593 CYS n 
1 594 GLY n 
1 595 CYS n 
1 596 MET n 
1 597 GLU n 
1 598 VAL n 
1 599 PHE n 
1 600 ARG n 
1 601 CYS n 
1 602 LYS n 
1 603 LEU n 
1 604 ARG n 
1 605 GLU n 
1 606 TYR n 
1 607 ALA n 
1 608 THR n 
1 609 LEU n 
1 610 TYR n 
1 611 ASP n 
1 612 ALA n 
1 613 LYS n 
1 614 GLN n 
1 615 ASP n 
1 616 ALA n 
1 617 PHE n 
1 618 VAL n 
1 619 GLY n 
1 620 GLU n 
1 621 GLN n 
1 622 ASN n 
1 623 LYS n 
1 624 PHE n 
1 625 GLU n 
1 626 ILE n 
1 627 ASP n 
1 628 GLU n 
1 629 THR n 
1 630 HIS n 
1 631 PRO n 
1 632 ASN n 
1 633 VAL n 
1 634 VAL n 
1 635 LEU n 
1 636 ASP n 
1 637 ASN n 
1 638 ASN n 
1 639 LYS n 
1 640 CYS n 
1 641 VAL n 
1 642 LEU n 
1 643 CYS n 
1 644 GLY n 
1 645 GLN n 
1 646 CYS n 
1 647 VAL n 
1 648 ASN n 
1 649 PHE n 
1 650 THR n 
1 651 HIS n 
1 652 GLU n 
1 653 ILE n 
1 654 ALA n 
1 655 ARG n 
1 656 GLU n 
1 657 GLY n 
1 658 ILE n 
1 659 VAL n 
1 660 ASP n 
1 661 TYR n 
1 662 LEU n 
1 663 PHE n 
1 664 ARG n 
1 665 GLY n 
1 666 PHE n 
1 667 LYS n 
1 668 THR n 
1 669 TYR n 
1 670 ILE n 
1 671 GLY n 
1 672 PRO n 
1 673 GLN n 
1 674 LEU n 
1 675 GLY n 
1 676 GLU n 
1 677 ARG n 
1 678 LEU n 
1 679 GLU n 
1 680 ASP n 
1 681 GLN n 
1 682 LYS n 
1 683 GLY n 
1 684 VAL n 
1 685 PHE n 
1 686 ILE n 
1 687 GLY n 
1 688 GLU n 
1 689 LEU n 
1 690 THR n 
1 691 ASP n 
1 692 ILE n 
1 693 CYS n 
1 694 PRO n 
1 695 VAL n 
1 696 GLY n 
1 697 ALA n 
1 698 ILE n 
1 699 THR n 
1 700 GLU n 
1 701 LYS n 
1 702 LEU n 
1 703 PRO n 
1 704 PHE n 
1 705 VAL n 
1 706 LYS n 
1 707 PRO n 
1 708 GLY n 
1 709 PRO n 
1 710 TRP n 
1 711 LYS n 
1 712 THR n 
1 713 GLN n 
1 714 PRO n 
1 715 VAL n 
1 716 LYS n 
1 717 THR n 
1 718 VAL n 
1 719 CYS n 
1 720 ASN n 
1 721 GLY n 
1 722 CYS n 
1 723 SER n 
1 724 PHE n 
1 725 ALA n 
1 726 CYS n 
1 727 GLU n 
1 728 MET n 
1 729 ASN n 
1 730 ILE n 
1 731 GLU n 
1 732 VAL n 
1 733 TYR n 
1 734 ASN n 
1 735 ASP n 
1 736 ILE n 
1 737 LEU n 
1 738 VAL n 
1 739 ARG n 
1 740 ALA n 
1 741 SER n 
1 742 SER n 
1 743 ARG n 
1 744 LYS n 
1 745 ASP n 
1 746 SER n 
1 747 TRP n 
1 748 ASN n 
1 749 GLY n 
1 750 TYR n 
1 751 ILE n 
1 752 CYS n 
1 753 ASP n 
1 754 TYR n 
1 755 CYS n 
1 756 ARG n 
1 757 PHE n 
1 758 GLU n 
1 759 ARG n 
1 760 PRO n 
1 761 TRP n 
1 762 ALA n 
1 763 GLN n 
1 764 ASP n 
1 765 ILE n 
1 766 ALA n 
1 767 GLN n 
1 768 PRO n 
1 769 ILE n 
1 770 LEU n 
1 771 LYS n 
1 772 GLY n 
1 773 ASN n 
1 774 ALA n 
1 775 VAL n 
1 776 SER n 
1 777 TRP n 
1 778 GLU n 
1 779 ASP n 
1 780 ALA n 
1 781 GLU n 
1 782 LYS n 
1 783 PHE n 
1 784 LEU n 
1 785 GLU n 
1 786 GLU n 
1 787 LYS n 
1 788 GLU n 
1 789 CYS n 
1 790 ALA n 
1 791 LEU n 
1 792 ILE n 
1 793 LEU n 
1 794 THR n 
1 795 PRO n 
1 796 SER n 
1 797 LEU n 
1 798 THR n 
1 799 ASN n 
1 800 GLU n 
1 801 GLU n 
1 802 ILE n 
1 803 MET n 
1 804 PHE n 
1 805 LEU n 
1 806 LYS n 
1 807 GLU n 
1 808 LEU n 
1 809 ALA n 
1 810 GLU n 
1 811 ARG n 
1 812 LYS n 
1 813 GLY n 
1 814 ILE n 
1 815 PRO n 
1 816 ILE n 
1 817 GLY n 
1 818 SER n 
1 819 THR n 
1 820 ILE n 
1 821 ASP n 
1 822 GLY n 
1 823 GLU n 
1 824 GLY n 
1 825 SER n 
1 826 THR n 
1 827 ALA n 
1 828 THR n 
1 829 LEU n 
1 830 GLU n 
1 831 ASP n 
1 832 ILE n 
1 833 ARG n 
1 834 ASN n 
1 835 ALA n 
1 836 LYS n 
1 837 ARG n 
1 838 VAL n 
1 839 LEU n 
1 840 LEU n 
1 841 LYS n 
1 842 VAL n 
1 843 ASN n 
1 844 ILE n 
1 845 GLU n 
1 846 LYS n 
1 847 TYR n 
1 848 PRO n 
1 849 LEU n 
1 850 LEU n 
1 851 LYS n 
1 852 LEU n 
1 853 LEU n 
1 854 LEU n 
1 855 LYS n 
1 856 GLY n 
1 857 LYS n 
1 858 GLU n 
1 859 ILE n 
1 860 VAL n 
1 861 GLU n 
1 862 GLU n 
1 863 GLY n 
1 864 TYR n 
1 865 GLU n 
1 866 VAL n 
1 867 ALA n 
1 868 ILE n 
1 869 ILE n 
1 870 GLU n 
1 871 GLY n 
1 872 PRO n 
1 873 ALA n 
1 874 GLU n 
1 875 PRO n 
1 876 MET n 
1 877 ASP n 
1 878 VAL n 
1 879 PRO n 
1 880 THR n 
1 881 LEU n 
1 882 ILE n 
1 883 LEU n 
1 884 HIS n 
1 885 ASP n 
1 886 GLY n 
1 887 VAL n 
1 888 ASN n 
1 889 ALA n 
1 890 THR n 
1 891 GLY n 
1 892 LEU n 
1 893 ILE n 
1 894 LYS n 
1 895 ALA n 
1 896 GLY n 
1 897 VAL n 
1 898 THR n 
1 899 GLY n 
1 900 ILE n 
1 901 PRO n 
1 902 GLU n 
1 903 ALA n 
1 904 LYS n 
1 905 ALA n 
1 906 TYR n 
1 907 VAL n 
1 908 VAL n 
1 909 ILE n 
1 910 GLY n 
1 911 ASN n 
1 912 SER n 
1 913 PRO n 
1 914 ALA n 
1 915 ILE n 
1 916 SER n 
1 917 LYS n 
1 918 LEU n 
1 919 LYS n 
1 920 GLY n 
1 921 GLU n 
1 922 TYR n 
1 923 LEU n 
1 924 ILE n 
1 925 LEU n 
1 926 PRO n 
1 927 SER n 
1 928 GLY n 
1 929 LEU n 
1 930 TRP n 
1 931 ALA n 
1 932 GLU n 
1 933 LYS n 
1 934 GLU n 
1 935 GLY n 
1 936 THR n 
1 937 VAL n 
1 938 THR n 
1 939 ASN n 
1 940 ALA n 
1 941 PHE n 
1 942 GLY n 
1 943 MET n 
1 944 ASP n 
1 945 LEU n 
1 946 LYS n 
1 947 VAL n 
1 948 LYS n 
1 949 LYS n 
1 950 ALA n 
1 951 ARG n 
1 952 LYS n 
1 953 ALA n 
1 954 HIS n 
1 955 TYR n 
1 956 ASP n 
1 957 VAL n 
1 958 LYS n 
1 959 SER n 
1 960 LEU n 
1 961 PHE n 
1 962 ASN n 
1 963 PHE n 
2 1   MET n 
2 2   SER n 
2 3   GLU n 
2 4   ILE n 
2 5   LYS n 
2 6   ALA n 
2 7   ILE n 
2 8   ALA n 
2 9   VAL n 
2 10  GLY n 
2 11  MET n 
2 12  ASN n 
2 13  SER n 
2 14  CYS n 
2 15  GLY n 
2 16  ILE n 
2 17  ALA n 
2 18  ALA n 
2 19  GLY n 
2 20  ALA n 
2 21  ARG n 
2 22  GLU n 
2 23  THR n 
2 24  TYR n 
2 25  GLU n 
2 26  ALA n 
2 27  VAL n 
2 28  LYS n 
2 29  GLU n 
2 30  GLU n 
2 31  LEU n 
2 32  GLU n 
2 33  LYS n 
2 34  ARG n 
2 35  ASN n 
2 36  LEU n 
2 37  ASP n 
2 38  ILE n 
2 39  LYS n 
2 40  LEU n 
2 41  LYS n 
2 42  ILE n 
2 43  VAL n 
2 44  GLY n 
2 45  CYS n 
2 46  VAL n 
2 47  GLY n 
2 48  MET n 
2 49  CYS n 
2 50  TYR n 
2 51  ARG n 
2 52  GLU n 
2 53  PRO n 
2 54  LEU n 
2 55  LEU n 
2 56  ASP n 
2 57  ILE n 
2 58  ILE n 
2 59  THR n 
2 60  ASP n 
2 61  ASN n 
2 62  GLU n 
2 63  ILE n 
2 64  ILE n 
2 65  THR n 
2 66  TYR n 
2 67  GLY n 
2 68  HIS n 
2 69  VAL n 
2 70  THR n 
2 71  PRO n 
2 72  ASP n 
2 73  ARG n 
2 74  VAL n 
2 75  PRO n 
2 76  ARG n 
2 77  ILE n 
2 78  ILE n 
2 79  GLU n 
2 80  GLU n 
2 81  HIS n 
2 82  VAL n 
2 83  ILE n 
2 84  ASN n 
2 85  GLY n 
2 86  LYS n 
2 87  PRO n 
2 88  ILE n 
2 89  GLU n 
2 90  ASP n 
2 91  TRP n 
2 92  VAL n 
2 93  VAL n 
2 94  LYS n 
2 95  LYS n 
2 96  ASP n 
2 97  TRP n 
2 98  TRP n 
2 99  GLU n 
2 100 ASN n 
2 101 GLY n 
2 102 GLN n 
2 103 ARG n 
2 104 LYS n 
2 105 THR n 
2 106 TRP n 
2 107 ASP n 
2 108 PHE n 
2 109 ASP n 
2 110 GLY n 
2 111 TYR n 
2 112 PHE n 
2 113 VAL n 
2 114 LYS n 
2 115 GLN n 
2 116 LYS n 
2 117 LYS n 
2 118 ILE n 
2 119 VAL n 
2 120 LEU n 
2 121 GLU n 
2 122 ASN n 
2 123 SER n 
2 124 GLY n 
2 125 TYR n 
2 126 ILE n 
2 127 ASP n 
2 128 PRO n 
2 129 GLU n 
2 130 ASN n 
2 131 ILE n 
2 132 GLU n 
2 133 GLU n 
2 134 TYR n 
2 135 ILE n 
2 136 ALA n 
2 137 ALA n 
2 138 GLY n 
2 139 GLY n 
2 140 TYR n 
2 141 GLU n 
2 142 ALA n 
2 143 LEU n 
2 144 LYS n 
2 145 LYS n 
2 146 ALA n 
2 147 PHE n 
2 148 LYS n 
2 149 MET n 
2 150 LYS n 
2 151 PRO n 
2 152 GLU n 
2 153 GLU n 
2 154 ILE n 
2 155 ILE n 
2 156 ASP n 
2 157 PHE n 
2 158 ILE n 
2 159 THR n 
2 160 LYS n 
2 161 SER n 
2 162 GLY n 
2 163 LEU n 
2 164 ARG n 
2 165 GLY n 
2 166 ARG n 
2 167 GLY n 
2 168 GLY n 
2 169 ALA n 
2 170 GLY n 
2 171 PHE n 
2 172 PRO n 
2 173 THR n 
2 174 GLY n 
2 175 LEU n 
2 176 LYS n 
2 177 TRP n 
2 178 LYS n 
2 179 PHE n 
2 180 THR n 
2 181 ARG n 
2 182 ASP n 
2 183 ALA n 
2 184 PRO n 
2 185 GLY n 
2 186 ASP n 
2 187 GLU n 
2 188 LYS n 
2 189 TYR n 
2 190 ILE n 
2 191 VAL n 
2 192 CYS n 
2 193 ASN n 
2 194 ALA n 
2 195 ASP n 
2 196 GLU n 
2 197 GLY n 
2 198 ASP n 
2 199 PRO n 
2 200 GLY n 
2 201 ALA n 
2 202 PHE n 
2 203 MET n 
2 204 ASP n 
2 205 ARG n 
2 206 ASN n 
2 207 VAL n 
2 208 LEU n 
2 209 GLU n 
2 210 GLY n 
2 211 ASP n 
2 212 PRO n 
2 213 HIS n 
2 214 ARG n 
2 215 VAL n 
2 216 ILE n 
2 217 GLU n 
2 218 GLY n 
2 219 MET n 
2 220 ILE n 
2 221 ILE n 
2 222 GLY n 
2 223 ALA n 
2 224 TYR n 
2 225 ALA n 
2 226 ILE n 
2 227 GLY n 
2 228 ALA n 
2 229 THR n 
2 230 LYS n 
2 231 GLY n 
2 232 PHE n 
2 233 ILE n 
2 234 TYR n 
2 235 VAL n 
2 236 ARG n 
2 237 ALA n 
2 238 GLU n 
2 239 TYR n 
2 240 PRO n 
2 241 LEU n 
2 242 ALA n 
2 243 ILE n 
2 244 LYS n 
2 245 ARG n 
2 246 LEU n 
2 247 ARG n 
2 248 ILE n 
2 249 ALA n 
2 250 LEU n 
2 251 LYS n 
2 252 GLN n 
2 253 ALA n 
2 254 ARG n 
2 255 GLU n 
2 256 LYS n 
2 257 GLY n 
2 258 PHE n 
2 259 LEU n 
2 260 GLY n 
2 261 GLU n 
2 262 ASN n 
2 263 ILE n 
2 264 LEU n 
2 265 GLY n 
2 266 SER n 
2 267 GLY n 
2 268 PHE n 
2 269 SER n 
2 270 PHE n 
2 271 GLU n 
2 272 ILE n 
2 273 VAL n 
2 274 ILE n 
2 275 LYS n 
2 276 GLU n 
2 277 GLY n 
2 278 ALA n 
2 279 GLY n 
2 280 ALA n 
2 281 PHE n 
2 282 VAL n 
2 283 CYS n 
2 284 GLY n 
2 285 GLU n 
2 286 GLU n 
2 287 THR n 
2 288 ALA n 
2 289 LEU n 
2 290 ILE n 
2 291 ALA n 
2 292 SER n 
2 293 ILE n 
2 294 GLU n 
2 295 GLY n 
2 296 LYS n 
2 297 ARG n 
2 298 GLY n 
2 299 MET n 
2 300 PRO n 
2 301 ARG n 
2 302 PRO n 
2 303 ARG n 
2 304 PRO n 
2 305 PRO n 
2 306 TYR n 
2 307 PRO n 
2 308 ALA n 
2 309 GLN n 
2 310 LYS n 
2 311 GLY n 
2 312 LEU n 
2 313 TRP n 
2 314 GLY n 
2 315 ARG n 
2 316 PRO n 
2 317 THR n 
2 318 ASN n 
2 319 ILE n 
2 320 ASN n 
2 321 ASN n 
2 322 VAL n 
2 323 GLU n 
2 324 THR n 
2 325 TRP n 
2 326 ALA n 
2 327 ASN n 
2 328 VAL n 
2 329 PRO n 
2 330 TRP n 
2 331 ILE n 
2 332 ILE n 
2 333 LYS n 
2 334 HIS n 
2 335 GLY n 
2 336 TRP n 
2 337 GLU n 
2 338 ALA n 
2 339 TYR n 
2 340 ALA n 
2 341 ALA n 
2 342 LEU n 
2 343 GLY n 
2 344 THR n 
2 345 GLU n 
2 346 LYS n 
2 347 SER n 
2 348 LYS n 
2 349 GLY n 
2 350 THR n 
2 351 LYS n 
2 352 VAL n 
2 353 PHE n 
2 354 ALA n 
2 355 LEU n 
2 356 SER n 
2 357 GLY n 
2 358 LYS n 
2 359 ILE n 
2 360 LYS n 
2 361 HIS n 
2 362 GLY n 
2 363 GLY n 
2 364 ASN n 
2 365 VAL n 
2 366 GLU n 
2 367 VAL n 
2 368 PRO n 
2 369 MET n 
2 370 GLY n 
2 371 ILE n 
2 372 THR n 
2 373 LEU n 
2 374 ARG n 
2 375 GLU n 
2 376 ILE n 
2 377 LEU n 
2 378 TYR n 
2 379 GLU n 
2 380 ILE n 
2 381 GLY n 
2 382 GLY n 
2 383 GLY n 
2 384 THR n 
2 385 LYS n 
2 386 THR n 
2 387 GLY n 
2 388 LYS n 
2 389 LYS n 
2 390 ILE n 
2 391 LYS n 
2 392 ALA n 
2 393 VAL n 
2 394 GLN n 
2 395 LEU n 
2 396 GLY n 
2 397 GLY n 
2 398 PRO n 
2 399 SER n 
2 400 GLY n 
2 401 GLY n 
2 402 CYS n 
2 403 ILE n 
2 404 PRO n 
2 405 ASP n 
2 406 TYR n 
2 407 LEU n 
2 408 PHE n 
2 409 ASN n 
2 410 THR n 
2 411 PRO n 
2 412 VAL n 
2 413 ASP n 
2 414 TYR n 
2 415 GLU n 
2 416 SER n 
2 417 VAL n 
2 418 THR n 
2 419 ALA n 
2 420 THR n 
2 421 GLY n 
2 422 ALA n 
2 423 ILE n 
2 424 MET n 
2 425 GLY n 
2 426 SER n 
2 427 GLY n 
2 428 GLY n 
2 429 MET n 
2 430 VAL n 
2 431 VAL n 
2 432 MET n 
2 433 ASP n 
2 434 GLU n 
2 435 ASP n 
2 436 THR n 
2 437 CYS n 
2 438 MET n 
2 439 VAL n 
2 440 ASP n 
2 441 VAL n 
2 442 ALA n 
2 443 LYS n 
2 444 PHE n 
2 445 PHE n 
2 446 LEU n 
2 447 ASP n 
2 448 PHE n 
2 449 THR n 
2 450 VAL n 
2 451 LYS n 
2 452 GLU n 
2 453 SER n 
2 454 CYS n 
2 455 GLY n 
2 456 LYS n 
2 457 CYS n 
2 458 THR n 
2 459 PHE n 
2 460 CYS n 
2 461 ARG n 
2 462 LEU n 
2 463 GLY n 
2 464 THR n 
2 465 LYS n 
2 466 ARG n 
2 467 MET n 
2 468 TRP n 
2 469 GLU n 
2 470 LEU n 
2 471 LEU n 
2 472 ASP n 
2 473 LYS n 
2 474 ILE n 
2 475 THR n 
2 476 LYS n 
2 477 GLY n 
2 478 GLU n 
2 479 GLY n 
2 480 ALA n 
2 481 LEU n 
2 482 GLU n 
2 483 ASP n 
2 484 ILE n 
2 485 GLU n 
2 486 LYS n 
2 487 LEU n 
2 488 GLU n 
2 489 LYS n 
2 490 LEU n 
2 491 ALA n 
2 492 PRO n 
2 493 LEU n 
2 494 VAL n 
2 495 LYS n 
2 496 THR n 
2 497 GLY n 
2 498 SER n 
2 499 LEU n 
2 500 CYS n 
2 501 GLY n 
2 502 LEU n 
2 503 GLY n 
2 504 GLN n 
2 505 THR n 
2 506 ALA n 
2 507 PRO n 
2 508 ASN n 
2 509 PRO n 
2 510 VAL n 
2 511 LEU n 
2 512 THR n 
2 513 THR n 
2 514 LEU n 
2 515 LYS n 
2 516 TYR n 
2 517 PHE n 
2 518 LYS n 
2 519 ASP n 
2 520 GLU n 
2 521 TYR n 
2 522 LEU n 
2 523 ALA n 
2 524 HIS n 
2 525 ILE n 
2 526 GLU n 
2 527 GLY n 
2 528 ARG n 
2 529 CYS n 
2 530 PRO n 
2 531 ALA n 
2 532 LYS n 
2 533 VAL n 
2 534 CYS n 
2 535 LYS n 
2 536 PRO n 
2 537 LEU n 
2 538 ILE n 
2 539 LYS n 
2 540 TYR n 
2 541 VAL n 
2 542 ILE n 
2 543 ILE n 
2 544 THR n 
2 545 GLU n 
2 546 LYS n 
2 547 CYS n 
2 548 THR n 
2 549 GLY n 
2 550 CYS n 
2 551 THR n 
2 552 ALA n 
2 553 CYS n 
2 554 ALA n 
2 555 ILE n 
2 556 MET n 
2 557 CYS n 
2 558 PRO n 
2 559 VAL n 
2 560 LYS n 
2 561 ALA n 
2 562 ILE n 
2 563 SER n 
2 564 GLY n 
2 565 GLU n 
2 566 ARG n 
2 567 GLY n 
2 568 LYS n 
2 569 PRO n 
2 570 HIS n 
2 571 LEU n 
2 572 ILE n 
2 573 ASN n 
2 574 GLN n 
2 575 GLU n 
2 576 ALA n 
2 577 CYS n 
2 578 ILE n 
2 579 LYS n 
2 580 CYS n 
2 581 GLY n 
2 582 THR n 
2 583 CYS n 
2 584 TYR n 
2 585 GLU n 
2 586 VAL n 
2 587 CYS n 
2 588 ARG n 
2 589 PHE n 
2 590 ASN n 
2 591 ALA n 
2 592 ILE n 
2 593 GLU n 
2 594 ILE n 
2 595 THR n 
2 596 ASP n 
2 597 ALA n 
2 598 LYS n 
2 599 LYS n 
2 600 GLU n 
2 601 GLY n 
2 602 GLU n 
3 1   MET n 
3 2   ASN n 
3 3   ILE n 
3 4   GLN n 
3 5   LEU n 
3 6   GLU n 
3 7   TYR n 
3 8   ILE n 
3 9   TYR n 
3 10  HIS n 
3 11  TYR n 
3 12  GLU n 
3 13  PRO n 
3 14  ASN n 
3 15  PRO n 
3 16  SER n 
3 17  SER n 
3 18  LEU n 
3 19  ILE n 
3 20  PRO n 
3 21  LEU n 
3 22  LEU n 
3 23  GLN n 
3 24  LYS n 
3 25  THR n 
3 26  GLN n 
3 27  GLU n 
3 28  THR n 
3 29  PHE n 
3 30  GLY n 
3 31  TYR n 
3 32  LEU n 
3 33  PRO n 
3 34  LYS n 
3 35  GLU n 
3 36  ALA n 
3 37  LEU n 
3 38  GLU n 
3 39  GLU n 
3 40  ILE n 
3 41  SER n 
3 42  ARG n 
3 43  TYR n 
3 44  LEU n 
3 45  LYS n 
3 46  VAL n 
3 47  PRO n 
3 48  LEU n 
3 49  SER n 
3 50  ARG n 
3 51  VAL n 
3 52  TYR n 
3 53  GLY n 
3 54  VAL n 
3 55  ALA n 
3 56  THR n 
3 57  PHE n 
3 58  TYR n 
3 59  ALA n 
3 60  GLN n 
3 61  PHE n 
3 62  ARG n 
3 63  PHE n 
3 64  GLU n 
3 65  PRO n 
3 66  LEU n 
3 67  GLY n 
3 68  LYS n 
3 69  TYR n 
3 70  VAL n 
3 71  ILE n 
3 72  LYS n 
3 73  ILE n 
3 74  CYS n 
3 75  HIS n 
3 76  GLY n 
3 77  THR n 
3 78  ALA n 
3 79  CYS n 
3 80  HIS n 
3 81  VAL n 
3 82  ASN n 
3 83  GLY n 
3 84  ALA n 
3 85  VAL n 
3 86  ASN n 
3 87  ILE n 
3 88  SER n 
3 89  GLN n 
3 90  ALA n 
3 91  ILE n 
3 92  ARG n 
3 93  GLU n 
3 94  GLU n 
3 95  VAL n 
3 96  GLY n 
3 97  ILE n 
3 98  GLU n 
3 99  GLU n 
3 100 GLY n 
3 101 GLN n 
3 102 THR n 
3 103 THR n 
3 104 VAL n 
3 105 ASP n 
3 106 GLY n 
3 107 LEU n 
3 108 ILE n 
3 109 THR n 
3 110 LEU n 
3 111 GLU n 
3 112 ARG n 
3 113 VAL n 
3 114 ALA n 
3 115 CYS n 
3 116 LEU n 
3 117 GLY n 
3 118 CYS n 
3 119 CYS n 
3 120 SER n 
3 121 LEU n 
3 122 ALA n 
3 123 PRO n 
3 124 VAL n 
3 125 ILE n 
3 126 MET n 
3 127 ILE n 
3 128 ASN n 
3 129 GLU n 
3 130 LYS n 
3 131 VAL n 
3 132 TYR n 
3 133 GLY n 
3 134 LYS n 
3 135 LEU n 
3 136 THR n 
3 137 PRO n 
3 138 ASP n 
3 139 LYS n 
3 140 VAL n 
3 141 ARG n 
3 142 LYS n 
3 143 ILE n 
3 144 ILE n 
3 145 ARG n 
3 146 ASN n 
3 147 LEU n 
3 148 LYS n 
3 149 GLU n 
3 150 GLY n 
3 151 LYS n 
3 152 LEU n 
3 153 ASN n 
3 154 VAL 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' 1 963 ? ? TSIB_1517 ? ? ? ? ? ? 'Thermococcus sibiricus' 172049 ? ? ? ? ? ? ? ? 
'Pyrococcus furiosus' 2261 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 602 ? ? XD54_1074 ? ? ? ? ? ? 'Thermococcus sibiricus' 172049 ? ? ? ? ? ? ? ? 
'Pyrococcus furiosus' 2261 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 154 ? ? XD54_1073 ? ? ? ? ? ? 'Thermococcus sibiricus' 172049 ? ? ? ? ? ? ? ? 
'Pyrococcus furiosus' 2261 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ?                          'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                          ?                          'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?                          'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?                          'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                          ?                          'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'     ?                          'C27 H33 N9 O15 P2' 785.550 
FES non-polymer         . 'FE2/S2 (INORGANIC) CLUSTER'      ?                          'Fe2 S2'            175.820 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE'           'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P'   456.344 
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 
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ?                          'C21 H27 N7 O14 P2' 663.425 
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 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'             ?                          'Fe4 S4'            351.640 
THR 'L-peptide linking' y THREONINE                         ?                          'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?                          'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                          ?                          'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                            ?                          'C5 H11 N O2'       117.146 
ZN  non-polymer         . 'ZINC ION'                        ?                          'Zn 2'              65.409  
# 
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   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   ARG 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   MET 9   9   ?   ?   ?   A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  CYS 52  52  52  CYS CYS A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  CYS 55  55  55  CYS CYS A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  CYS 67  67  67  CYS CYS A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  MET 72  72  72  MET MET A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  MET 87  87  87  MET MET A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  HIS 99  99  99  HIS HIS A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 CYS 103 103 103 CYS CYS A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 CYS 107 107 107 CYS CYS A . n 
A 1 108 GLN 108 108 108 GLN GLN A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 TYR 120 120 120 TYR TYR A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 MET 126 126 126 MET MET A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 TYR 129 129 129 TYR TYR A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 CYS 150 150 150 CYS CYS A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 CYS 154 154 154 CYS CYS A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 CYS 158 158 158 CYS CYS A . n 
A 1 159 ARG 159 159 159 ARG ARG A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 GLN 171 171 171 GLN GLN A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 TYR 179 179 179 TYR TYR A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 TRP 186 186 186 TRP TRP A . n 
A 1 187 MET 187 187 187 MET MET A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 CYS 210 210 210 CYS CYS A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 TYR 212 212 212 TYR TYR A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 MET 217 217 217 MET MET A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 HIS 219 219 219 HIS HIS A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 PHE 224 224 224 PHE PHE A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 HIS 229 229 229 HIS HIS A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 MET 234 234 234 MET MET 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 GLY 237 237 237 GLY GLY A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 ASN 257 257 257 ASN ASN A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 GLU 261 261 261 GLU GLU A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 ASN 265 265 265 ASN ASN A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 GLN 280 280 280 GLN GLN A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 PHE 285 285 285 PHE PHE A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 TRP 291 291 291 TRP TRP A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 HIS 308 308 308 HIS HIS A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 THR 310 310 310 THR THR A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 ASN 317 317 317 ASN ASN A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 ARG 327 327 327 ARG ARG A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 ASN 335 335 335 ASN ASN A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 ALA 337 337 337 ALA ALA A . n 
A 1 338 MET 338 338 338 MET MET A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 ARG 342 342 342 ARG ARG A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 ALA 349 349 349 ALA ALA A . n 
A 1 350 ASP 350 350 350 ASP ASP A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 VAL 353 353 353 VAL VAL A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 TYR 355 355 355 TYR TYR A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 ARG 357 357 357 ARG ARG A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 MET 362 362 362 MET MET A . n 
A 1 363 PRO 363 363 363 PRO PRO A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 SER 366 366 366 SER SER A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 VAL 369 369 369 VAL VAL A . n 
A 1 370 GLU 370 370 370 GLU GLU A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 VAL 377 377 377 VAL VAL A . n 
A 1 378 LYS 378 378 378 LYS LYS A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 MET 380 380 380 MET MET A . n 
A 1 381 PHE 381 381 381 PHE PHE A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 PRO 385 385 385 PRO PRO A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 LYS 393 393 393 LYS LYS A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
A 1 395 GLU 395 395 395 GLU GLU A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 VAL 397 397 397 VAL VAL A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 LEU 399 399 399 LEU LEU A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 LYS 401 401 401 LYS LYS A . n 
A 1 402 MET 402 402 402 MET MET A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 GLY 405 405 405 GLY GLY A . n 
A 1 406 GLU 406 406 406 GLU GLU A . n 
A 1 407 PRO 407 407 407 PRO PRO A . n 
A 1 408 ASP 408 408 ?   ?   ?   A . n 
A 1 409 ALA 409 409 ?   ?   ?   A . n 
A 1 410 SER 410 410 ?   ?   ?   A . n 
A 1 411 GLY 411 411 ?   ?   ?   A . n 
A 1 412 ARG 412 412 412 ARG ARG A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 PRO 415 415 415 PRO PRO A . n 
A 1 416 MET 416 416 416 MET MET A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 ILE 418 418 418 ILE ILE A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 GLY 420 420 420 GLY GLY A . n 
A 1 421 SER 421 421 421 SER SER A . n 
A 1 422 GLU 422 422 422 GLU GLU A . n 
A 1 423 PHE 423 423 423 PHE PHE A . n 
A 1 424 ARG 424 424 424 ARG ARG A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 LYS 426 426 426 LYS LYS A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 ASN 429 429 429 ASN ASN A . n 
A 1 430 VAL 430 430 430 VAL VAL A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 LEU 432 432 432 LEU LEU A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 GLN 436 436 436 GLN GLN A . n 
A 1 437 TYR 437 437 437 TYR TYR A . n 
A 1 438 CYS 438 438 438 CYS CYS A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 GLU 440 440 440 GLU GLU A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 PHE 442 442 442 PHE PHE A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 ARG 444 444 444 ARG ARG A . n 
A 1 445 THR 445 445 445 THR THR A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 GLY 447 447 447 GLY GLY A . n 
A 1 448 ILE 448 448 448 ILE ILE A . n 
A 1 449 GLU 449 449 449 GLU GLU A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 ARG 454 454 454 ARG ARG A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 ASP 458 458 458 ASP ASP A . n 
A 1 459 GLU 459 459 459 GLU GLU A . n 
A 1 460 VAL 460 460 460 VAL VAL A . n 
A 1 461 THR 461 461 461 THR THR A . n 
A 1 462 LEU 462 462 462 LEU LEU A . n 
A 1 463 GLN 463 463 463 GLN GLN A . n 
A 1 464 THR 464 464 464 THR THR A . n 
A 1 465 ASN 465 465 465 ASN ASN A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 GLU 467 467 467 GLU GLU A . n 
A 1 468 GLY 468 468 468 GLY GLY A . n 
A 1 469 VAL 469 469 469 VAL VAL A . n 
A 1 470 PHE 470 470 470 PHE PHE A . n 
A 1 471 ALA 471 471 471 ALA ALA A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 GLY 473 473 473 GLY GLY A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 LEU 475 475 475 LEU LEU A . n 
A 1 476 VAL 476 476 476 VAL VAL A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 GLY 478 478 478 GLY GLY A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 SER 480 480 480 SER SER A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 VAL 482 482 482 VAL VAL A . n 
A 1 483 ILE 483 483 483 ILE ILE A . n 
A 1 484 GLU 484 484 484 GLU GLU A . n 
A 1 485 SER 485 485 485 SER SER A . n 
A 1 486 ILE 486 486 486 ILE ILE A . n 
A 1 487 ALA 487 487 487 ALA ALA A . n 
A 1 488 THR 488 488 488 THR THR A . n 
A 1 489 GLY 489 489 489 GLY GLY A . n 
A 1 490 ARG 490 490 490 ARG ARG A . n 
A 1 491 ARG 491 491 491 ARG ARG A . n 
A 1 492 ALA 492 492 492 ALA ALA A . n 
A 1 493 ALA 493 493 493 ALA ALA A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 MET 495 495 495 MET MET A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 ASP 497 497 497 ASP ASP A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 TYR 499 499 499 TYR TYR A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 LYS 501 501 501 LYS LYS A . n 
A 1 502 GLY 502 502 502 GLY GLY A . n 
A 1 503 LYS 503 503 503 LYS LYS A . n 
A 1 504 LEU 504 504 504 LEU LEU A . n 
A 1 505 GLU 505 505 505 GLU GLU A . n 
A 1 506 LYS 506 506 506 LYS LYS A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 ARG 508 508 508 ARG ARG A . n 
A 1 509 GLU 509 509 509 GLU GLU A . n 
A 1 510 VAL 510 510 510 VAL VAL A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 LEU 512 512 512 LEU LEU A . n 
A 1 513 ASP 513 513 513 ASP ASP A . n 
A 1 514 PRO 514 514 514 PRO PRO A . n 
A 1 515 SER 515 515 515 SER SER A . n 
A 1 516 LYS 516 516 516 LYS LYS A . n 
A 1 517 HIS 517 517 517 HIS HIS A . n 
A 1 518 ILE 518 518 518 ILE ILE A . n 
A 1 519 GLU 519 519 519 GLU GLU A . n 
A 1 520 GLU 520 520 520 GLU GLU A . n 
A 1 521 VAL 521 521 521 VAL VAL A . n 
A 1 522 ILE 522 522 522 ILE ILE A . n 
A 1 523 TYR 523 523 523 TYR TYR A . n 
A 1 524 ASP 524 524 524 ASP ASP A . n 
A 1 525 GLU 525 525 525 GLU GLU A . n 
A 1 526 ASP 526 526 526 ASP ASP A . n 
A 1 527 LEU 527 527 527 LEU LEU A . n 
A 1 528 TYR 528 528 528 TYR TYR A . n 
A 1 529 ARG 529 529 529 ARG ARG A . n 
A 1 530 VAL 530 530 530 VAL VAL A . n 
A 1 531 LEU 531 531 531 LEU LEU A . n 
A 1 532 PHE 532 532 532 PHE PHE A . n 
A 1 533 ASP 533 533 533 ASP ASP A . n 
A 1 534 LEU 534 534 534 LEU LEU A . n 
A 1 535 ARG 535 535 535 ARG ARG A . n 
A 1 536 PRO 536 536 536 PRO PRO A . n 
A 1 537 TYR 537 537 537 TYR TYR A . n 
A 1 538 ASN 538 538 538 ASN ASN A . n 
A 1 539 HIS 539 539 539 HIS HIS A . n 
A 1 540 TRP 540 540 540 TRP TRP A . n 
A 1 541 LYS 541 541 541 LYS LYS A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 VAL 543 543 543 VAL VAL A . n 
A 1 544 THR 544 544 544 THR THR A . n 
A 1 545 GLU 545 545 545 GLU GLU A . n 
A 1 546 LYS 546 546 546 LYS LYS A . n 
A 1 547 ASP 547 547 547 ASP ASP A . n 
A 1 548 TYR 548 548 548 TYR TYR A . n 
A 1 549 GLU 549 549 549 GLU GLU A . n 
A 1 550 HIS 550 550 550 HIS HIS A . n 
A 1 551 VAL 551 551 551 VAL VAL A . n 
A 1 552 GLU 552 552 552 GLU GLU A . n 
A 1 553 ARG 553 553 553 ARG ARG A . n 
A 1 554 LYS 554 554 554 LYS LYS A . n 
A 1 555 PRO 555 555 555 PRO PRO A . n 
A 1 556 ARG 556 556 556 ARG ARG A . n 
A 1 557 VAL 557 557 557 VAL VAL A . n 
A 1 558 LYS 558 558 558 LYS LYS A . n 
A 1 559 VAL 559 559 559 VAL VAL 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 LEU 562 562 562 LEU LEU A . n 
A 1 563 ASP 563 563 563 ASP ASP A . n 
A 1 564 PRO 564 564 564 PRO PRO A . n 
A 1 565 GLU 565 565 565 GLU GLU A . n 
A 1 566 ILE 566 566 566 ILE ILE A . n 
A 1 567 ARG 567 567 567 ARG ARG A . n 
A 1 568 LYS 568 568 568 LYS LYS A . n 
A 1 569 SER 569 569 569 SER SER A . n 
A 1 570 ASN 570 570 570 ASN ASN A . n 
A 1 571 PHE 571 571 571 PHE PHE A . n 
A 1 572 LYS 572 572 572 LYS LYS A . n 
A 1 573 GLU 573 573 573 GLU GLU A . n 
A 1 574 VAL 574 574 574 VAL VAL A . n 
A 1 575 GLU 575 575 575 GLU GLU A . n 
A 1 576 PRO 576 576 576 PRO PRO A . n 
A 1 577 THR 577 577 577 THR THR A . n 
A 1 578 MET 578 578 578 MET MET A . n 
A 1 579 ASP 579 579 579 ASP ASP A . n 
A 1 580 GLU 580 580 580 GLU GLU A . n 
A 1 581 GLU 581 581 581 GLU GLU A . n 
A 1 582 THR 582 582 582 THR THR A . n 
A 1 583 VAL 583 583 583 VAL VAL A . n 
A 1 584 LEU 584 584 584 LEU LEU A . n 
A 1 585 THR 585 585 585 THR THR A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 ALA 587 587 587 ALA ALA A . n 
A 1 588 GLN 588 588 588 GLN GLN A . n 
A 1 589 ARG 589 589 589 ARG ARG A . n 
A 1 590 CYS 590 590 590 CYS CYS A . n 
A 1 591 MET 591 591 591 MET MET A . n 
A 1 592 SER 592 592 592 SER SER A . n 
A 1 593 CYS 593 593 593 CYS CYS A . n 
A 1 594 GLY 594 594 594 GLY GLY A . n 
A 1 595 CYS 595 595 595 CYS CYS A . n 
A 1 596 MET 596 596 596 MET MET A . n 
A 1 597 GLU 597 597 597 GLU GLU A . n 
A 1 598 VAL 598 598 598 VAL VAL A . n 
A 1 599 PHE 599 599 599 PHE PHE A . n 
A 1 600 ARG 600 600 600 ARG ARG A . n 
A 1 601 CYS 601 601 601 CYS CYS A . n 
A 1 602 LYS 602 602 602 LYS LYS A . n 
A 1 603 LEU 603 603 603 LEU LEU A . n 
A 1 604 ARG 604 604 604 ARG ARG A . n 
A 1 605 GLU 605 605 605 GLU GLU A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 ALA 607 607 607 ALA ALA A . n 
A 1 608 THR 608 608 608 THR THR A . n 
A 1 609 LEU 609 609 609 LEU LEU A . n 
A 1 610 TYR 610 610 610 TYR TYR A . n 
A 1 611 ASP 611 611 611 ASP ASP A . n 
A 1 612 ALA 612 612 612 ALA ALA A . n 
A 1 613 LYS 613 613 613 LYS LYS A . n 
A 1 614 GLN 614 614 614 GLN GLN A . n 
A 1 615 ASP 615 615 615 ASP ASP A . n 
A 1 616 ALA 616 616 616 ALA ALA A . n 
A 1 617 PHE 617 617 617 PHE PHE A . n 
A 1 618 VAL 618 618 618 VAL VAL A . n 
A 1 619 GLY 619 619 619 GLY GLY A . n 
A 1 620 GLU 620 620 620 GLU GLU A . n 
A 1 621 GLN 621 621 621 GLN GLN A . n 
A 1 622 ASN 622 622 622 ASN ASN A . n 
A 1 623 LYS 623 623 623 LYS LYS A . n 
A 1 624 PHE 624 624 624 PHE PHE A . n 
A 1 625 GLU 625 625 625 GLU GLU A . n 
A 1 626 ILE 626 626 626 ILE ILE A . n 
A 1 627 ASP 627 627 627 ASP ASP A . n 
A 1 628 GLU 628 628 628 GLU GLU A . n 
A 1 629 THR 629 629 629 THR THR A . n 
A 1 630 HIS 630 630 630 HIS HIS A . n 
A 1 631 PRO 631 631 631 PRO PRO A . n 
A 1 632 ASN 632 632 632 ASN ASN A . n 
A 1 633 VAL 633 633 633 VAL VAL A . n 
A 1 634 VAL 634 634 634 VAL VAL A . n 
A 1 635 LEU 635 635 635 LEU LEU A . n 
A 1 636 ASP 636 636 636 ASP ASP A . n 
A 1 637 ASN 637 637 637 ASN ASN A . n 
A 1 638 ASN 638 638 638 ASN ASN A . n 
A 1 639 LYS 639 639 639 LYS LYS A . n 
A 1 640 CYS 640 640 640 CYS CYS A . n 
A 1 641 VAL 641 641 641 VAL VAL A . n 
A 1 642 LEU 642 642 642 LEU LEU A . n 
A 1 643 CYS 643 643 643 CYS CYS A . n 
A 1 644 GLY 644 644 644 GLY GLY A . n 
A 1 645 GLN 645 645 645 GLN GLN A . n 
A 1 646 CYS 646 646 646 CYS CYS A . n 
A 1 647 VAL 647 647 647 VAL VAL A . n 
A 1 648 ASN 648 648 648 ASN ASN A . n 
A 1 649 PHE 649 649 649 PHE PHE A . n 
A 1 650 THR 650 650 650 THR THR A . n 
A 1 651 HIS 651 651 651 HIS HIS A . n 
A 1 652 GLU 652 652 652 GLU GLU A . n 
A 1 653 ILE 653 653 653 ILE ILE A . n 
A 1 654 ALA 654 654 654 ALA ALA A . n 
A 1 655 ARG 655 655 655 ARG ARG A . n 
A 1 656 GLU 656 656 656 GLU GLU A . n 
A 1 657 GLY 657 657 657 GLY GLY A . n 
A 1 658 ILE 658 658 658 ILE ILE A . n 
A 1 659 VAL 659 659 659 VAL VAL A . n 
A 1 660 ASP 660 660 660 ASP ASP A . n 
A 1 661 TYR 661 661 661 TYR TYR A . n 
A 1 662 LEU 662 662 662 LEU LEU A . n 
A 1 663 PHE 663 663 663 PHE PHE A . n 
A 1 664 ARG 664 664 664 ARG ARG A . n 
A 1 665 GLY 665 665 665 GLY GLY A . n 
A 1 666 PHE 666 666 666 PHE PHE A . n 
A 1 667 LYS 667 667 667 LYS LYS A . n 
A 1 668 THR 668 668 668 THR THR A . n 
A 1 669 TYR 669 669 669 TYR TYR A . n 
A 1 670 ILE 670 670 670 ILE ILE A . n 
A 1 671 GLY 671 671 671 GLY GLY A . n 
A 1 672 PRO 672 672 672 PRO PRO A . n 
A 1 673 GLN 673 673 673 GLN GLN A . n 
A 1 674 LEU 674 674 674 LEU LEU A . n 
A 1 675 GLY 675 675 675 GLY GLY A . n 
A 1 676 GLU 676 676 676 GLU GLU A . n 
A 1 677 ARG 677 677 677 ARG ARG A . n 
A 1 678 LEU 678 678 678 LEU LEU A . n 
A 1 679 GLU 679 679 679 GLU GLU A . n 
A 1 680 ASP 680 680 680 ASP ASP A . n 
A 1 681 GLN 681 681 681 GLN GLN A . n 
A 1 682 LYS 682 682 682 LYS LYS A . n 
A 1 683 GLY 683 683 683 GLY GLY A . n 
A 1 684 VAL 684 684 684 VAL VAL A . n 
A 1 685 PHE 685 685 685 PHE PHE A . n 
A 1 686 ILE 686 686 686 ILE ILE A . n 
A 1 687 GLY 687 687 687 GLY GLY A . n 
A 1 688 GLU 688 688 688 GLU GLU A . n 
A 1 689 LEU 689 689 689 LEU LEU A . n 
A 1 690 THR 690 690 690 THR THR A . n 
A 1 691 ASP 691 691 691 ASP ASP A . n 
A 1 692 ILE 692 692 692 ILE ILE A . n 
A 1 693 CYS 693 693 693 CYS CYS A . n 
A 1 694 PRO 694 694 694 PRO PRO A . n 
A 1 695 VAL 695 695 695 VAL VAL A . n 
A 1 696 GLY 696 696 696 GLY GLY A . n 
A 1 697 ALA 697 697 697 ALA ALA A . n 
A 1 698 ILE 698 698 698 ILE ILE A . n 
A 1 699 THR 699 699 699 THR THR A . n 
A 1 700 GLU 700 700 700 GLU GLU A . n 
A 1 701 LYS 701 701 701 LYS LYS A . n 
A 1 702 LEU 702 702 702 LEU LEU A . n 
A 1 703 PRO 703 703 703 PRO PRO A . n 
A 1 704 PHE 704 704 704 PHE PHE A . n 
A 1 705 VAL 705 705 705 VAL VAL A . n 
A 1 706 LYS 706 706 706 LYS LYS A . n 
A 1 707 PRO 707 707 707 PRO PRO A . n 
A 1 708 GLY 708 708 708 GLY GLY A . n 
A 1 709 PRO 709 709 709 PRO PRO A . n 
A 1 710 TRP 710 710 710 TRP TRP A . n 
A 1 711 LYS 711 711 711 LYS LYS A . n 
A 1 712 THR 712 712 712 THR THR A . n 
A 1 713 GLN 713 713 713 GLN GLN A . n 
A 1 714 PRO 714 714 714 PRO PRO A . n 
A 1 715 VAL 715 715 715 VAL VAL A . n 
A 1 716 LYS 716 716 716 LYS LYS A . n 
A 1 717 THR 717 717 717 THR THR A . n 
A 1 718 VAL 718 718 718 VAL VAL A . n 
A 1 719 CYS 719 719 719 CYS CYS A . n 
A 1 720 ASN 720 720 720 ASN ASN A . n 
A 1 721 GLY 721 721 721 GLY GLY A . n 
A 1 722 CYS 722 722 722 CYS CYS A . n 
A 1 723 SER 723 723 723 SER SER A . n 
A 1 724 PHE 724 724 724 PHE PHE A . n 
A 1 725 ALA 725 725 725 ALA ALA A . n 
A 1 726 CYS 726 726 726 CYS CYS A . n 
A 1 727 GLU 727 727 727 GLU GLU A . n 
A 1 728 MET 728 728 728 MET MET A . n 
A 1 729 ASN 729 729 729 ASN ASN A . n 
A 1 730 ILE 730 730 730 ILE ILE A . n 
A 1 731 GLU 731 731 731 GLU GLU A . n 
A 1 732 VAL 732 732 732 VAL VAL A . n 
A 1 733 TYR 733 733 733 TYR TYR A . n 
A 1 734 ASN 734 734 734 ASN ASN A . n 
A 1 735 ASP 735 735 735 ASP ASP A . n 
A 1 736 ILE 736 736 736 ILE ILE A . n 
A 1 737 LEU 737 737 737 LEU LEU A . n 
A 1 738 VAL 738 738 738 VAL VAL A . n 
A 1 739 ARG 739 739 739 ARG ARG A . n 
A 1 740 ALA 740 740 740 ALA ALA A . n 
A 1 741 SER 741 741 741 SER SER A . n 
A 1 742 SER 742 742 742 SER SER A . n 
A 1 743 ARG 743 743 743 ARG ARG A . n 
A 1 744 LYS 744 744 744 LYS LYS A . n 
A 1 745 ASP 745 745 745 ASP ASP A . n 
A 1 746 SER 746 746 746 SER SER A . n 
A 1 747 TRP 747 747 747 TRP TRP A . n 
A 1 748 ASN 748 748 748 ASN ASN A . n 
A 1 749 GLY 749 749 749 GLY GLY A . n 
A 1 750 TYR 750 750 750 TYR TYR A . n 
A 1 751 ILE 751 751 751 ILE ILE A . n 
A 1 752 CYS 752 752 752 CYS CYS A . n 
A 1 753 ASP 753 753 753 ASP ASP A . n 
A 1 754 TYR 754 754 754 TYR TYR A . n 
A 1 755 CYS 755 755 755 CYS CYS A . n 
A 1 756 ARG 756 756 756 ARG ARG A . n 
A 1 757 PHE 757 757 757 PHE PHE A . n 
A 1 758 GLU 758 758 758 GLU GLU A . n 
A 1 759 ARG 759 759 759 ARG ARG A . n 
A 1 760 PRO 760 760 760 PRO PRO A . n 
A 1 761 TRP 761 761 761 TRP TRP A . n 
A 1 762 ALA 762 762 762 ALA ALA A . n 
A 1 763 GLN 763 763 763 GLN GLN A . n 
A 1 764 ASP 764 764 764 ASP ASP A . n 
A 1 765 ILE 765 765 765 ILE ILE A . n 
A 1 766 ALA 766 766 766 ALA ALA A . n 
A 1 767 GLN 767 767 767 GLN GLN A . n 
A 1 768 PRO 768 768 768 PRO PRO A . n 
A 1 769 ILE 769 769 769 ILE ILE A . n 
A 1 770 LEU 770 770 770 LEU LEU A . n 
A 1 771 LYS 771 771 771 LYS LYS A . n 
A 1 772 GLY 772 772 772 GLY GLY A . n 
A 1 773 ASN 773 773 773 ASN ASN A . n 
A 1 774 ALA 774 774 774 ALA ALA A . n 
A 1 775 VAL 775 775 775 VAL VAL A . n 
A 1 776 SER 776 776 776 SER SER A . n 
A 1 777 TRP 777 777 777 TRP TRP A . n 
A 1 778 GLU 778 778 778 GLU GLU A . n 
A 1 779 ASP 779 779 779 ASP ASP A . n 
A 1 780 ALA 780 780 780 ALA ALA A . n 
A 1 781 GLU 781 781 781 GLU GLU A . n 
A 1 782 LYS 782 782 782 LYS LYS A . n 
A 1 783 PHE 783 783 783 PHE PHE A . n 
A 1 784 LEU 784 784 784 LEU LEU A . n 
A 1 785 GLU 785 785 785 GLU GLU A . n 
A 1 786 GLU 786 786 786 GLU GLU A . n 
A 1 787 LYS 787 787 787 LYS LYS A . n 
A 1 788 GLU 788 788 788 GLU GLU A . n 
A 1 789 CYS 789 789 789 CYS CYS A . n 
A 1 790 ALA 790 790 790 ALA ALA A . n 
A 1 791 LEU 791 791 791 LEU LEU A . n 
A 1 792 ILE 792 792 792 ILE ILE A . n 
A 1 793 LEU 793 793 793 LEU LEU A . n 
A 1 794 THR 794 794 794 THR THR A . n 
A 1 795 PRO 795 795 795 PRO PRO A . n 
A 1 796 SER 796 796 796 SER SER A . n 
A 1 797 LEU 797 797 797 LEU LEU A . n 
A 1 798 THR 798 798 798 THR THR A . n 
A 1 799 ASN 799 799 799 ASN ASN A . n 
A 1 800 GLU 800 800 800 GLU GLU A . n 
A 1 801 GLU 801 801 801 GLU GLU A . n 
A 1 802 ILE 802 802 802 ILE ILE A . n 
A 1 803 MET 803 803 803 MET MET A . n 
A 1 804 PHE 804 804 804 PHE PHE A . n 
A 1 805 LEU 805 805 805 LEU LEU A . n 
A 1 806 LYS 806 806 806 LYS LYS A . n 
A 1 807 GLU 807 807 807 GLU GLU A . n 
A 1 808 LEU 808 808 808 LEU LEU A . n 
A 1 809 ALA 809 809 809 ALA ALA A . n 
A 1 810 GLU 810 810 810 GLU GLU A . n 
A 1 811 ARG 811 811 811 ARG ARG A . n 
A 1 812 LYS 812 812 812 LYS LYS A . n 
A 1 813 GLY 813 813 813 GLY GLY A . n 
A 1 814 ILE 814 814 814 ILE ILE A . n 
A 1 815 PRO 815 815 815 PRO PRO A . n 
A 1 816 ILE 816 816 816 ILE ILE A . n 
A 1 817 GLY 817 817 817 GLY GLY A . n 
A 1 818 SER 818 818 818 SER SER A . n 
A 1 819 THR 819 819 819 THR THR A . n 
A 1 820 ILE 820 820 820 ILE ILE A . n 
A 1 821 ASP 821 821 821 ASP ASP A . n 
A 1 822 GLY 822 822 822 GLY GLY A . n 
A 1 823 GLU 823 823 823 GLU GLU A . n 
A 1 824 GLY 824 824 824 GLY GLY A . n 
A 1 825 SER 825 825 825 SER SER A . n 
A 1 826 THR 826 826 826 THR THR A . n 
A 1 827 ALA 827 827 827 ALA ALA A . n 
A 1 828 THR 828 828 828 THR THR A . n 
A 1 829 LEU 829 829 829 LEU LEU A . n 
A 1 830 GLU 830 830 830 GLU GLU A . n 
A 1 831 ASP 831 831 831 ASP ASP A . n 
A 1 832 ILE 832 832 832 ILE ILE A . n 
A 1 833 ARG 833 833 833 ARG ARG A . n 
A 1 834 ASN 834 834 834 ASN ASN A . n 
A 1 835 ALA 835 835 835 ALA ALA A . n 
A 1 836 LYS 836 836 836 LYS LYS A . n 
A 1 837 ARG 837 837 837 ARG ARG A . n 
A 1 838 VAL 838 838 838 VAL VAL A . n 
A 1 839 LEU 839 839 839 LEU LEU A . n 
A 1 840 LEU 840 840 840 LEU LEU A . n 
A 1 841 LYS 841 841 841 LYS LYS A . n 
A 1 842 VAL 842 842 842 VAL VAL A . n 
A 1 843 ASN 843 843 843 ASN ASN A . n 
A 1 844 ILE 844 844 844 ILE ILE A . n 
A 1 845 GLU 845 845 845 GLU GLU A . n 
A 1 846 LYS 846 846 846 LYS LYS A . n 
A 1 847 TYR 847 847 847 TYR TYR A . n 
A 1 848 PRO 848 848 848 PRO PRO A . n 
A 1 849 LEU 849 849 849 LEU LEU A . n 
A 1 850 LEU 850 850 850 LEU LEU A . n 
A 1 851 LYS 851 851 851 LYS LYS A . n 
A 1 852 LEU 852 852 852 LEU LEU A . n 
A 1 853 LEU 853 853 853 LEU LEU A . n 
A 1 854 LEU 854 854 854 LEU LEU A . n 
A 1 855 LYS 855 855 855 LYS LYS A . n 
A 1 856 GLY 856 856 856 GLY GLY A . n 
A 1 857 LYS 857 857 857 LYS LYS A . n 
A 1 858 GLU 858 858 858 GLU GLU A . n 
A 1 859 ILE 859 859 859 ILE ILE A . n 
A 1 860 VAL 860 860 860 VAL VAL A . n 
A 1 861 GLU 861 861 861 GLU GLU A . n 
A 1 862 GLU 862 862 862 GLU GLU A . n 
A 1 863 GLY 863 863 863 GLY GLY A . n 
A 1 864 TYR 864 864 864 TYR TYR A . n 
A 1 865 GLU 865 865 865 GLU GLU A . n 
A 1 866 VAL 866 866 866 VAL VAL A . n 
A 1 867 ALA 867 867 867 ALA ALA A . n 
A 1 868 ILE 868 868 868 ILE ILE A . n 
A 1 869 ILE 869 869 869 ILE ILE A . n 
A 1 870 GLU 870 870 870 GLU GLU A . n 
A 1 871 GLY 871 871 871 GLY GLY A . n 
A 1 872 PRO 872 872 872 PRO PRO A . n 
A 1 873 ALA 873 873 873 ALA ALA A . n 
A 1 874 GLU 874 874 874 GLU GLU A . n 
A 1 875 PRO 875 875 875 PRO PRO A . n 
A 1 876 MET 876 876 876 MET MET A . n 
A 1 877 ASP 877 877 877 ASP ASP A . n 
A 1 878 VAL 878 878 878 VAL VAL A . n 
A 1 879 PRO 879 879 879 PRO PRO A . n 
A 1 880 THR 880 880 880 THR THR A . n 
A 1 881 LEU 881 881 881 LEU LEU A . n 
A 1 882 ILE 882 882 882 ILE ILE A . n 
A 1 883 LEU 883 883 883 LEU LEU A . n 
A 1 884 HIS 884 884 884 HIS HIS A . n 
A 1 885 ASP 885 885 885 ASP ASP A . n 
A 1 886 GLY 886 886 886 GLY GLY A . n 
A 1 887 VAL 887 887 887 VAL VAL A . n 
A 1 888 ASN 888 888 888 ASN ASN A . n 
A 1 889 ALA 889 889 889 ALA ALA A . n 
A 1 890 THR 890 890 890 THR THR A . n 
A 1 891 GLY 891 891 891 GLY GLY A . n 
A 1 892 LEU 892 892 892 LEU LEU A . n 
A 1 893 ILE 893 893 893 ILE ILE A . n 
A 1 894 LYS 894 894 894 LYS LYS A . n 
A 1 895 ALA 895 895 895 ALA ALA A . n 
A 1 896 GLY 896 896 896 GLY GLY A . n 
A 1 897 VAL 897 897 897 VAL VAL A . n 
A 1 898 THR 898 898 898 THR THR A . n 
A 1 899 GLY 899 899 899 GLY GLY A . n 
A 1 900 ILE 900 900 900 ILE ILE A . n 
A 1 901 PRO 901 901 901 PRO PRO A . n 
A 1 902 GLU 902 902 902 GLU GLU A . n 
A 1 903 ALA 903 903 903 ALA ALA A . n 
A 1 904 LYS 904 904 904 LYS LYS A . n 
A 1 905 ALA 905 905 905 ALA ALA A . n 
A 1 906 TYR 906 906 906 TYR TYR A . n 
A 1 907 VAL 907 907 907 VAL VAL A . n 
A 1 908 VAL 908 908 908 VAL VAL A . n 
A 1 909 ILE 909 909 909 ILE ILE A . n 
A 1 910 GLY 910 910 910 GLY GLY A . n 
A 1 911 ASN 911 911 911 ASN ASN A . n 
A 1 912 SER 912 912 912 SER SER A . n 
A 1 913 PRO 913 913 913 PRO PRO A . n 
A 1 914 ALA 914 914 914 ALA ALA A . n 
A 1 915 ILE 915 915 915 ILE ILE A . n 
A 1 916 SER 916 916 916 SER SER A . n 
A 1 917 LYS 917 917 917 LYS LYS A . n 
A 1 918 LEU 918 918 918 LEU LEU A . n 
A 1 919 LYS 919 919 919 LYS LYS A . n 
A 1 920 GLY 920 920 920 GLY GLY A . n 
A 1 921 GLU 921 921 921 GLU GLU A . n 
A 1 922 TYR 922 922 922 TYR TYR A . n 
A 1 923 LEU 923 923 923 LEU LEU A . n 
A 1 924 ILE 924 924 924 ILE ILE A . n 
A 1 925 LEU 925 925 925 LEU LEU A . n 
A 1 926 PRO 926 926 926 PRO PRO A . n 
A 1 927 SER 927 927 927 SER SER A . n 
A 1 928 GLY 928 928 928 GLY GLY A . n 
A 1 929 LEU 929 929 929 LEU LEU A . n 
A 1 930 TRP 930 930 930 TRP TRP A . n 
A 1 931 ALA 931 931 931 ALA ALA A . n 
A 1 932 GLU 932 932 932 GLU GLU A . n 
A 1 933 LYS 933 933 933 LYS LYS A . n 
A 1 934 GLU 934 934 934 GLU GLU A . n 
A 1 935 GLY 935 935 935 GLY GLY A . n 
A 1 936 THR 936 936 936 THR THR A . n 
A 1 937 VAL 937 937 937 VAL VAL A . n 
A 1 938 THR 938 938 938 THR THR A . n 
A 1 939 ASN 939 939 939 ASN ASN A . n 
A 1 940 ALA 940 940 940 ALA ALA A . n 
A 1 941 PHE 941 941 941 PHE PHE A . n 
A 1 942 GLY 942 942 942 GLY GLY A . n 
A 1 943 MET 943 943 943 MET MET A . n 
A 1 944 ASP 944 944 944 ASP ASP A . n 
A 1 945 LEU 945 945 945 LEU LEU A . n 
A 1 946 LYS 946 946 946 LYS LYS A . n 
A 1 947 VAL 947 947 947 VAL VAL A . n 
A 1 948 LYS 948 948 948 LYS LYS A . n 
A 1 949 LYS 949 949 949 LYS LYS A . n 
A 1 950 ALA 950 950 950 ALA ALA A . n 
A 1 951 ARG 951 951 951 ARG ARG A . n 
A 1 952 LYS 952 952 952 LYS LYS A . n 
A 1 953 ALA 953 953 953 ALA ALA A . n 
A 1 954 HIS 954 954 954 HIS HIS A . n 
A 1 955 TYR 955 955 955 TYR TYR A . n 
A 1 956 ASP 956 956 956 ASP ASP A . n 
A 1 957 VAL 957 957 957 VAL VAL A . n 
A 1 958 LYS 958 958 958 LYS LYS A . n 
A 1 959 SER 959 959 959 SER SER A . n 
A 1 960 LEU 960 960 960 LEU LEU A . n 
A 1 961 PHE 961 961 ?   ?   ?   A . n 
A 1 962 ASN 962 962 ?   ?   ?   A . n 
A 1 963 PHE 963 963 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   2   SER SER B . n 
B 2 3   GLU 3   3   3   GLU GLU B . n 
B 2 4   ILE 4   4   4   ILE ILE B . n 
B 2 5   LYS 5   5   5   LYS LYS B . n 
B 2 6   ALA 6   6   6   ALA ALA B . n 
B 2 7   ILE 7   7   7   ILE ILE B . n 
B 2 8   ALA 8   8   8   ALA ALA B . n 
B 2 9   VAL 9   9   9   VAL VAL B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  MET 11  11  11  MET MET B . n 
B 2 12  ASN 12  12  12  ASN ASN B . n 
B 2 13  SER 13  13  13  SER SER B . n 
B 2 14  CYS 14  14  14  CYS CYS B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  ALA 17  17  17  ALA ALA B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  GLY 19  19  19  GLY GLY B . n 
B 2 20  ALA 20  20  20  ALA ALA B . n 
B 2 21  ARG 21  21  21  ARG ARG B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  THR 23  23  23  THR THR B . n 
B 2 24  TYR 24  24  24  TYR TYR B . n 
B 2 25  GLU 25  25  25  GLU GLU B . n 
B 2 26  ALA 26  26  26  ALA ALA B . n 
B 2 27  VAL 27  27  27  VAL VAL B . n 
B 2 28  LYS 28  28  28  LYS LYS B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  GLU 30  30  30  GLU GLU B . n 
B 2 31  LEU 31  31  31  LEU LEU B . n 
B 2 32  GLU 32  32  32  GLU GLU B . n 
B 2 33  LYS 33  33  33  LYS LYS B . n 
B 2 34  ARG 34  34  34  ARG ARG B . n 
B 2 35  ASN 35  35  35  ASN ASN B . n 
B 2 36  LEU 36  36  36  LEU LEU B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  ILE 38  38  38  ILE ILE B . n 
B 2 39  LYS 39  39  39  LYS LYS B . n 
B 2 40  LEU 40  40  40  LEU LEU B . n 
B 2 41  LYS 41  41  41  LYS LYS B . n 
B 2 42  ILE 42  42  42  ILE ILE B . n 
B 2 43  VAL 43  43  43  VAL VAL B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  CYS 45  45  45  CYS CYS B . n 
B 2 46  VAL 46  46  46  VAL VAL B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  MET 48  48  48  MET MET B . n 
B 2 49  CYS 49  49  49  CYS CYS B . n 
B 2 50  TYR 50  50  50  TYR TYR B . n 
B 2 51  ARG 51  51  51  ARG ARG B . n 
B 2 52  GLU 52  52  52  GLU GLU B . n 
B 2 53  PRO 53  53  53  PRO PRO B . n 
B 2 54  LEU 54  54  54  LEU LEU B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  ASP 56  56  56  ASP ASP B . n 
B 2 57  ILE 57  57  57  ILE ILE B . n 
B 2 58  ILE 58  58  58  ILE ILE B . n 
B 2 59  THR 59  59  59  THR THR B . n 
B 2 60  ASP 60  60  60  ASP ASP B . n 
B 2 61  ASN 61  61  61  ASN ASN B . n 
B 2 62  GLU 62  62  62  GLU GLU B . n 
B 2 63  ILE 63  63  63  ILE ILE B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  THR 65  65  65  THR THR B . n 
B 2 66  TYR 66  66  66  TYR TYR B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  HIS 68  68  68  HIS HIS B . n 
B 2 69  VAL 69  69  69  VAL VAL B . n 
B 2 70  THR 70  70  70  THR THR B . n 
B 2 71  PRO 71  71  71  PRO PRO B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  ARG 73  73  73  ARG ARG B . n 
B 2 74  VAL 74  74  74  VAL VAL B . n 
B 2 75  PRO 75  75  75  PRO PRO B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  ILE 78  78  78  ILE ILE B . n 
B 2 79  GLU 79  79  79  GLU GLU B . n 
B 2 80  GLU 80  80  80  GLU GLU B . n 
B 2 81  HIS 81  81  81  HIS HIS B . n 
B 2 82  VAL 82  82  82  VAL VAL B . n 
B 2 83  ILE 83  83  83  ILE ILE B . n 
B 2 84  ASN 84  84  84  ASN ASN B . n 
B 2 85  GLY 85  85  85  GLY GLY B . n 
B 2 86  LYS 86  86  86  LYS LYS B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  ILE 88  88  88  ILE ILE B . n 
B 2 89  GLU 89  89  89  GLU GLU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  TRP 91  91  91  TRP TRP B . n 
B 2 92  VAL 92  92  92  VAL VAL B . n 
B 2 93  VAL 93  93  93  VAL VAL B . n 
B 2 94  LYS 94  94  94  LYS LYS B . n 
B 2 95  LYS 95  95  95  LYS LYS B . n 
B 2 96  ASP 96  96  96  ASP ASP B . n 
B 2 97  TRP 97  97  97  TRP TRP B . n 
B 2 98  TRP 98  98  98  TRP TRP B . n 
B 2 99  GLU 99  99  99  GLU GLU B . n 
B 2 100 ASN 100 100 100 ASN ASN B . n 
B 2 101 GLY 101 101 101 GLY GLY B . n 
B 2 102 GLN 102 102 102 GLN GLN B . n 
B 2 103 ARG 103 103 103 ARG ARG B . n 
B 2 104 LYS 104 104 104 LYS LYS B . n 
B 2 105 THR 105 105 105 THR THR B . n 
B 2 106 TRP 106 106 106 TRP TRP B . n 
B 2 107 ASP 107 107 107 ASP ASP B . n 
B 2 108 PHE 108 108 108 PHE PHE B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 GLY 110 110 110 GLY GLY B . n 
B 2 111 TYR 111 111 111 TYR TYR B . n 
B 2 112 PHE 112 112 112 PHE PHE B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 LYS 114 114 114 LYS LYS B . n 
B 2 115 GLN 115 115 115 GLN GLN B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 LYS 117 117 117 LYS LYS B . n 
B 2 118 ILE 118 118 118 ILE ILE B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 LEU 120 120 120 LEU LEU B . n 
B 2 121 GLU 121 121 121 GLU GLU B . n 
B 2 122 ASN 122 122 122 ASN ASN B . n 
B 2 123 SER 123 123 123 SER SER B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 TYR 125 125 125 TYR TYR B . n 
B 2 126 ILE 126 126 126 ILE ILE B . n 
B 2 127 ASP 127 127 127 ASP ASP B . n 
B 2 128 PRO 128 128 128 PRO PRO B . n 
B 2 129 GLU 129 129 129 GLU GLU B . n 
B 2 130 ASN 130 130 130 ASN ASN B . n 
B 2 131 ILE 131 131 131 ILE ILE B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 GLU 133 133 133 GLU GLU B . n 
B 2 134 TYR 134 134 134 TYR TYR B . n 
B 2 135 ILE 135 135 135 ILE ILE B . n 
B 2 136 ALA 136 136 136 ALA ALA B . n 
B 2 137 ALA 137 137 137 ALA ALA B . n 
B 2 138 GLY 138 138 138 GLY GLY B . n 
B 2 139 GLY 139 139 139 GLY GLY B . n 
B 2 140 TYR 140 140 140 TYR TYR B . n 
B 2 141 GLU 141 141 141 GLU GLU B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 LEU 143 143 143 LEU LEU B . n 
B 2 144 LYS 144 144 144 LYS LYS B . n 
B 2 145 LYS 145 145 145 LYS LYS B . n 
B 2 146 ALA 146 146 146 ALA ALA B . n 
B 2 147 PHE 147 147 147 PHE PHE B . n 
B 2 148 LYS 148 148 148 LYS LYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 LYS 150 150 150 LYS LYS B . n 
B 2 151 PRO 151 151 151 PRO PRO B . n 
B 2 152 GLU 152 152 152 GLU GLU B . n 
B 2 153 GLU 153 153 153 GLU GLU B . n 
B 2 154 ILE 154 154 154 ILE ILE B . n 
B 2 155 ILE 155 155 155 ILE ILE B . n 
B 2 156 ASP 156 156 156 ASP ASP B . n 
B 2 157 PHE 157 157 157 PHE PHE B . n 
B 2 158 ILE 158 158 158 ILE ILE B . n 
B 2 159 THR 159 159 159 THR THR B . n 
B 2 160 LYS 160 160 160 LYS LYS B . n 
B 2 161 SER 161 161 161 SER SER B . n 
B 2 162 GLY 162 162 162 GLY GLY B . n 
B 2 163 LEU 163 163 163 LEU LEU B . n 
B 2 164 ARG 164 164 164 ARG ARG B . n 
B 2 165 GLY 165 165 165 GLY GLY B . n 
B 2 166 ARG 166 166 166 ARG ARG B . n 
B 2 167 GLY 167 167 167 GLY GLY B . n 
B 2 168 GLY 168 168 168 GLY GLY B . n 
B 2 169 ALA 169 169 169 ALA ALA B . n 
B 2 170 GLY 170 170 170 GLY GLY B . n 
B 2 171 PHE 171 171 171 PHE PHE B . n 
B 2 172 PRO 172 172 172 PRO PRO B . n 
B 2 173 THR 173 173 173 THR THR B . n 
B 2 174 GLY 174 174 174 GLY GLY B . n 
B 2 175 LEU 175 175 175 LEU LEU B . n 
B 2 176 LYS 176 176 176 LYS LYS B . n 
B 2 177 TRP 177 177 177 TRP TRP B . n 
B 2 178 LYS 178 178 178 LYS LYS B . n 
B 2 179 PHE 179 179 179 PHE PHE B . n 
B 2 180 THR 180 180 180 THR THR B . n 
B 2 181 ARG 181 181 181 ARG ARG B . n 
B 2 182 ASP 182 182 182 ASP ASP B . n 
B 2 183 ALA 183 183 183 ALA ALA B . n 
B 2 184 PRO 184 184 184 PRO PRO B . n 
B 2 185 GLY 185 185 185 GLY GLY B . n 
B 2 186 ASP 186 186 186 ASP ASP B . n 
B 2 187 GLU 187 187 187 GLU GLU B . n 
B 2 188 LYS 188 188 188 LYS LYS B . n 
B 2 189 TYR 189 189 189 TYR TYR B . n 
B 2 190 ILE 190 190 190 ILE ILE B . n 
B 2 191 VAL 191 191 191 VAL VAL B . n 
B 2 192 CYS 192 192 192 CYS CYS B . n 
B 2 193 ASN 193 193 193 ASN ASN B . n 
B 2 194 ALA 194 194 194 ALA ALA B . n 
B 2 195 ASP 195 195 195 ASP ASP B . n 
B 2 196 GLU 196 196 196 GLU GLU B . n 
B 2 197 GLY 197 197 197 GLY GLY B . n 
B 2 198 ASP 198 198 198 ASP ASP B . n 
B 2 199 PRO 199 199 199 PRO PRO B . n 
B 2 200 GLY 200 200 200 GLY GLY B . n 
B 2 201 ALA 201 201 201 ALA ALA B . n 
B 2 202 PHE 202 202 202 PHE PHE B . n 
B 2 203 MET 203 203 203 MET MET B . n 
B 2 204 ASP 204 204 204 ASP ASP B . n 
B 2 205 ARG 205 205 205 ARG ARG B . n 
B 2 206 ASN 206 206 206 ASN ASN B . n 
B 2 207 VAL 207 207 207 VAL VAL B . n 
B 2 208 LEU 208 208 208 LEU LEU B . n 
B 2 209 GLU 209 209 209 GLU GLU B . n 
B 2 210 GLY 210 210 210 GLY GLY B . n 
B 2 211 ASP 211 211 211 ASP ASP B . n 
B 2 212 PRO 212 212 212 PRO PRO B . n 
B 2 213 HIS 213 213 213 HIS HIS B . n 
B 2 214 ARG 214 214 214 ARG ARG B . n 
B 2 215 VAL 215 215 215 VAL VAL B . n 
B 2 216 ILE 216 216 216 ILE ILE B . n 
B 2 217 GLU 217 217 217 GLU GLU B . n 
B 2 218 GLY 218 218 218 GLY GLY B . n 
B 2 219 MET 219 219 219 MET MET B . n 
B 2 220 ILE 220 220 220 ILE ILE B . n 
B 2 221 ILE 221 221 221 ILE ILE B . n 
B 2 222 GLY 222 222 222 GLY GLY B . n 
B 2 223 ALA 223 223 223 ALA ALA B . n 
B 2 224 TYR 224 224 224 TYR TYR B . n 
B 2 225 ALA 225 225 225 ALA ALA B . n 
B 2 226 ILE 226 226 226 ILE ILE B . n 
B 2 227 GLY 227 227 227 GLY GLY B . n 
B 2 228 ALA 228 228 228 ALA ALA B . n 
B 2 229 THR 229 229 229 THR THR B . n 
B 2 230 LYS 230 230 230 LYS LYS B . n 
B 2 231 GLY 231 231 231 GLY GLY B . n 
B 2 232 PHE 232 232 232 PHE PHE B . n 
B 2 233 ILE 233 233 233 ILE ILE B . n 
B 2 234 TYR 234 234 234 TYR TYR B . n 
B 2 235 VAL 235 235 235 VAL VAL B . n 
B 2 236 ARG 236 236 236 ARG ARG B . n 
B 2 237 ALA 237 237 237 ALA ALA B . n 
B 2 238 GLU 238 238 238 GLU GLU B . n 
B 2 239 TYR 239 239 239 TYR TYR B . n 
B 2 240 PRO 240 240 240 PRO PRO B . n 
B 2 241 LEU 241 241 241 LEU LEU B . n 
B 2 242 ALA 242 242 242 ALA ALA B . n 
B 2 243 ILE 243 243 243 ILE ILE B . n 
B 2 244 LYS 244 244 244 LYS LYS B . n 
B 2 245 ARG 245 245 245 ARG ARG B . n 
B 2 246 LEU 246 246 246 LEU LEU B . n 
B 2 247 ARG 247 247 247 ARG ARG B . n 
B 2 248 ILE 248 248 248 ILE ILE B . n 
B 2 249 ALA 249 249 249 ALA ALA B . n 
B 2 250 LEU 250 250 250 LEU LEU B . n 
B 2 251 LYS 251 251 251 LYS LYS B . n 
B 2 252 GLN 252 252 252 GLN GLN B . n 
B 2 253 ALA 253 253 253 ALA ALA B . n 
B 2 254 ARG 254 254 254 ARG ARG B . n 
B 2 255 GLU 255 255 255 GLU GLU B . n 
B 2 256 LYS 256 256 256 LYS LYS B . n 
B 2 257 GLY 257 257 257 GLY GLY B . n 
B 2 258 PHE 258 258 258 PHE PHE B . n 
B 2 259 LEU 259 259 259 LEU LEU B . n 
B 2 260 GLY 260 260 260 GLY GLY B . n 
B 2 261 GLU 261 261 261 GLU GLU B . n 
B 2 262 ASN 262 262 262 ASN ASN B . n 
B 2 263 ILE 263 263 263 ILE ILE B . n 
B 2 264 LEU 264 264 264 LEU LEU B . n 
B 2 265 GLY 265 265 265 GLY GLY B . n 
B 2 266 SER 266 266 266 SER SER B . n 
B 2 267 GLY 267 267 267 GLY GLY B . n 
B 2 268 PHE 268 268 268 PHE PHE B . n 
B 2 269 SER 269 269 269 SER SER B . n 
B 2 270 PHE 270 270 270 PHE PHE B . n 
B 2 271 GLU 271 271 271 GLU GLU B . n 
B 2 272 ILE 272 272 272 ILE ILE B . n 
B 2 273 VAL 273 273 273 VAL VAL B . n 
B 2 274 ILE 274 274 274 ILE ILE B . n 
B 2 275 LYS 275 275 275 LYS LYS B . n 
B 2 276 GLU 276 276 276 GLU GLU B . n 
B 2 277 GLY 277 277 277 GLY GLY B . n 
B 2 278 ALA 278 278 278 ALA ALA B . n 
B 2 279 GLY 279 279 279 GLY GLY B . n 
B 2 280 ALA 280 280 280 ALA ALA B . n 
B 2 281 PHE 281 281 281 PHE PHE B . n 
B 2 282 VAL 282 282 282 VAL VAL B . n 
B 2 283 CYS 283 283 283 CYS CYS B . n 
B 2 284 GLY 284 284 284 GLY GLY B . n 
B 2 285 GLU 285 285 285 GLU GLU B . n 
B 2 286 GLU 286 286 286 GLU GLU B . n 
B 2 287 THR 287 287 287 THR THR B . n 
B 2 288 ALA 288 288 288 ALA ALA B . n 
B 2 289 LEU 289 289 289 LEU LEU B . n 
B 2 290 ILE 290 290 290 ILE ILE B . n 
B 2 291 ALA 291 291 291 ALA ALA B . n 
B 2 292 SER 292 292 292 SER SER B . n 
B 2 293 ILE 293 293 293 ILE ILE B . n 
B 2 294 GLU 294 294 294 GLU GLU B . n 
B 2 295 GLY 295 295 295 GLY GLY B . n 
B 2 296 LYS 296 296 296 LYS LYS B . n 
B 2 297 ARG 297 297 297 ARG ARG B . n 
B 2 298 GLY 298 298 298 GLY GLY B . n 
B 2 299 MET 299 299 299 MET MET B . n 
B 2 300 PRO 300 300 300 PRO PRO B . n 
B 2 301 ARG 301 301 301 ARG ARG B . n 
B 2 302 PRO 302 302 302 PRO PRO B . n 
B 2 303 ARG 303 303 303 ARG ARG B . n 
B 2 304 PRO 304 304 304 PRO PRO B . n 
B 2 305 PRO 305 305 305 PRO PRO B . n 
B 2 306 TYR 306 306 306 TYR TYR B . n 
B 2 307 PRO 307 307 307 PRO PRO B . n 
B 2 308 ALA 308 308 308 ALA ALA B . n 
B 2 309 GLN 309 309 309 GLN GLN B . n 
B 2 310 LYS 310 310 310 LYS LYS B . n 
B 2 311 GLY 311 311 311 GLY GLY B . n 
B 2 312 LEU 312 312 312 LEU LEU B . n 
B 2 313 TRP 313 313 313 TRP TRP B . n 
B 2 314 GLY 314 314 314 GLY GLY B . n 
B 2 315 ARG 315 315 315 ARG ARG B . n 
B 2 316 PRO 316 316 316 PRO PRO B . n 
B 2 317 THR 317 317 317 THR THR B . n 
B 2 318 ASN 318 318 318 ASN ASN B . n 
B 2 319 ILE 319 319 319 ILE ILE B . n 
B 2 320 ASN 320 320 320 ASN ASN B . n 
B 2 321 ASN 321 321 321 ASN ASN B . n 
B 2 322 VAL 322 322 322 VAL VAL B . n 
B 2 323 GLU 323 323 323 GLU GLU B . n 
B 2 324 THR 324 324 324 THR THR B . n 
B 2 325 TRP 325 325 325 TRP TRP B . n 
B 2 326 ALA 326 326 326 ALA ALA B . n 
B 2 327 ASN 327 327 327 ASN ASN B . n 
B 2 328 VAL 328 328 328 VAL VAL B . n 
B 2 329 PRO 329 329 329 PRO PRO B . n 
B 2 330 TRP 330 330 330 TRP TRP B . n 
B 2 331 ILE 331 331 331 ILE ILE B . n 
B 2 332 ILE 332 332 332 ILE ILE B . n 
B 2 333 LYS 333 333 333 LYS LYS B . n 
B 2 334 HIS 334 334 334 HIS HIS B . n 
B 2 335 GLY 335 335 335 GLY GLY B . n 
B 2 336 TRP 336 336 336 TRP TRP B . n 
B 2 337 GLU 337 337 337 GLU GLU B . n 
B 2 338 ALA 338 338 338 ALA ALA B . n 
B 2 339 TYR 339 339 339 TYR TYR B . n 
B 2 340 ALA 340 340 340 ALA ALA B . n 
B 2 341 ALA 341 341 341 ALA ALA B . n 
B 2 342 LEU 342 342 342 LEU LEU B . n 
B 2 343 GLY 343 343 343 GLY GLY B . n 
B 2 344 THR 344 344 344 THR THR B . n 
B 2 345 GLU 345 345 345 GLU GLU B . n 
B 2 346 LYS 346 346 346 LYS LYS B . n 
B 2 347 SER 347 347 347 SER SER B . n 
B 2 348 LYS 348 348 348 LYS LYS B . n 
B 2 349 GLY 349 349 349 GLY GLY B . n 
B 2 350 THR 350 350 350 THR THR B . n 
B 2 351 LYS 351 351 351 LYS LYS B . n 
B 2 352 VAL 352 352 352 VAL VAL B . n 
B 2 353 PHE 353 353 353 PHE PHE B . n 
B 2 354 ALA 354 354 354 ALA ALA B . n 
B 2 355 LEU 355 355 355 LEU LEU B . n 
B 2 356 SER 356 356 356 SER SER B . n 
B 2 357 GLY 357 357 357 GLY GLY B . n 
B 2 358 LYS 358 358 358 LYS LYS B . n 
B 2 359 ILE 359 359 359 ILE ILE B . n 
B 2 360 LYS 360 360 360 LYS LYS B . n 
B 2 361 HIS 361 361 361 HIS HIS B . n 
B 2 362 GLY 362 362 362 GLY GLY B . n 
B 2 363 GLY 363 363 363 GLY GLY B . n 
B 2 364 ASN 364 364 364 ASN ASN B . n 
B 2 365 VAL 365 365 365 VAL VAL B . n 
B 2 366 GLU 366 366 366 GLU GLU B . n 
B 2 367 VAL 367 367 367 VAL VAL B . n 
B 2 368 PRO 368 368 368 PRO PRO B . n 
B 2 369 MET 369 369 369 MET MET B . n 
B 2 370 GLY 370 370 370 GLY GLY B . n 
B 2 371 ILE 371 371 371 ILE ILE B . n 
B 2 372 THR 372 372 372 THR THR B . n 
B 2 373 LEU 373 373 373 LEU LEU B . n 
B 2 374 ARG 374 374 374 ARG ARG B . n 
B 2 375 GLU 375 375 375 GLU GLU B . n 
B 2 376 ILE 376 376 376 ILE ILE B . n 
B 2 377 LEU 377 377 377 LEU LEU B . n 
B 2 378 TYR 378 378 378 TYR TYR B . n 
B 2 379 GLU 379 379 379 GLU GLU B . n 
B 2 380 ILE 380 380 380 ILE ILE B . n 
B 2 381 GLY 381 381 381 GLY GLY B . n 
B 2 382 GLY 382 382 382 GLY GLY B . n 
B 2 383 GLY 383 383 383 GLY GLY B . n 
B 2 384 THR 384 384 384 THR THR B . n 
B 2 385 LYS 385 385 385 LYS LYS B . n 
B 2 386 THR 386 386 386 THR THR B . n 
B 2 387 GLY 387 387 387 GLY GLY B . n 
B 2 388 LYS 388 388 388 LYS LYS B . n 
B 2 389 LYS 389 389 389 LYS LYS B . n 
B 2 390 ILE 390 390 390 ILE ILE B . n 
B 2 391 LYS 391 391 391 LYS LYS B . n 
B 2 392 ALA 392 392 392 ALA ALA B . n 
B 2 393 VAL 393 393 393 VAL VAL B . n 
B 2 394 GLN 394 394 394 GLN GLN B . n 
B 2 395 LEU 395 395 395 LEU LEU B . n 
B 2 396 GLY 396 396 396 GLY GLY B . n 
B 2 397 GLY 397 397 397 GLY GLY B . n 
B 2 398 PRO 398 398 398 PRO PRO B . n 
B 2 399 SER 399 399 399 SER SER B . n 
B 2 400 GLY 400 400 400 GLY GLY B . n 
B 2 401 GLY 401 401 401 GLY GLY B . n 
B 2 402 CYS 402 402 402 CYS CYS B . n 
B 2 403 ILE 403 403 403 ILE ILE B . n 
B 2 404 PRO 404 404 404 PRO PRO B . n 
B 2 405 ASP 405 405 405 ASP ASP B . n 
B 2 406 TYR 406 406 406 TYR TYR B . n 
B 2 407 LEU 407 407 407 LEU LEU B . n 
B 2 408 PHE 408 408 408 PHE PHE B . n 
B 2 409 ASN 409 409 409 ASN ASN B . n 
B 2 410 THR 410 410 410 THR THR B . n 
B 2 411 PRO 411 411 411 PRO PRO B . n 
B 2 412 VAL 412 412 412 VAL VAL B . n 
B 2 413 ASP 413 413 413 ASP ASP B . n 
B 2 414 TYR 414 414 414 TYR TYR B . n 
B 2 415 GLU 415 415 415 GLU GLU B . n 
B 2 416 SER 416 416 416 SER SER B . n 
B 2 417 VAL 417 417 417 VAL VAL B . n 
B 2 418 THR 418 418 418 THR THR B . n 
B 2 419 ALA 419 419 419 ALA ALA B . n 
B 2 420 THR 420 420 420 THR THR B . n 
B 2 421 GLY 421 421 421 GLY GLY B . n 
B 2 422 ALA 422 422 422 ALA ALA B . n 
B 2 423 ILE 423 423 423 ILE ILE B . n 
B 2 424 MET 424 424 424 MET MET B . n 
B 2 425 GLY 425 425 425 GLY GLY B . n 
B 2 426 SER 426 426 426 SER SER B . n 
B 2 427 GLY 427 427 427 GLY GLY B . n 
B 2 428 GLY 428 428 428 GLY GLY B . n 
B 2 429 MET 429 429 429 MET MET B . n 
B 2 430 VAL 430 430 430 VAL VAL B . n 
B 2 431 VAL 431 431 431 VAL VAL B . n 
B 2 432 MET 432 432 432 MET MET B . n 
B 2 433 ASP 433 433 433 ASP ASP B . n 
B 2 434 GLU 434 434 434 GLU GLU B . n 
B 2 435 ASP 435 435 435 ASP ASP B . n 
B 2 436 THR 436 436 436 THR THR B . n 
B 2 437 CYS 437 437 437 CYS CYS B . n 
B 2 438 MET 438 438 438 MET MET B . n 
B 2 439 VAL 439 439 439 VAL VAL B . n 
B 2 440 ASP 440 440 440 ASP ASP B . n 
B 2 441 VAL 441 441 441 VAL VAL B . n 
B 2 442 ALA 442 442 442 ALA ALA B . n 
B 2 443 LYS 443 443 443 LYS LYS B . n 
B 2 444 PHE 444 444 444 PHE PHE B . n 
B 2 445 PHE 445 445 445 PHE PHE B . n 
B 2 446 LEU 446 446 446 LEU LEU B . n 
B 2 447 ASP 447 447 447 ASP ASP B . n 
B 2 448 PHE 448 448 448 PHE PHE B . n 
B 2 449 THR 449 449 449 THR THR B . n 
B 2 450 VAL 450 450 450 VAL VAL B . n 
B 2 451 LYS 451 451 451 LYS LYS B . n 
B 2 452 GLU 452 452 452 GLU GLU B . n 
B 2 453 SER 453 453 453 SER SER B . n 
B 2 454 CYS 454 454 454 CYS CYS B . n 
B 2 455 GLY 455 455 455 GLY GLY B . n 
B 2 456 LYS 456 456 456 LYS LYS B . n 
B 2 457 CYS 457 457 457 CYS CYS B . n 
B 2 458 THR 458 458 458 THR THR B . n 
B 2 459 PHE 459 459 459 PHE PHE B . n 
B 2 460 CYS 460 460 460 CYS CYS B . n 
B 2 461 ARG 461 461 461 ARG ARG B . n 
B 2 462 LEU 462 462 462 LEU LEU B . n 
B 2 463 GLY 463 463 463 GLY GLY B . n 
B 2 464 THR 464 464 464 THR THR B . n 
B 2 465 LYS 465 465 465 LYS LYS B . n 
B 2 466 ARG 466 466 466 ARG ARG B . n 
B 2 467 MET 467 467 467 MET MET B . n 
B 2 468 TRP 468 468 468 TRP TRP B . n 
B 2 469 GLU 469 469 469 GLU GLU B . n 
B 2 470 LEU 470 470 470 LEU LEU B . n 
B 2 471 LEU 471 471 471 LEU LEU B . n 
B 2 472 ASP 472 472 472 ASP ASP B . n 
B 2 473 LYS 473 473 473 LYS LYS B . n 
B 2 474 ILE 474 474 474 ILE ILE B . n 
B 2 475 THR 475 475 475 THR THR B . n 
B 2 476 LYS 476 476 476 LYS LYS B . n 
B 2 477 GLY 477 477 477 GLY GLY B . n 
B 2 478 GLU 478 478 478 GLU GLU B . n 
B 2 479 GLY 479 479 479 GLY GLY B . n 
B 2 480 ALA 480 480 480 ALA ALA B . n 
B 2 481 LEU 481 481 481 LEU LEU B . n 
B 2 482 GLU 482 482 482 GLU GLU B . n 
B 2 483 ASP 483 483 483 ASP ASP B . n 
B 2 484 ILE 484 484 484 ILE ILE B . n 
B 2 485 GLU 485 485 485 GLU GLU B . n 
B 2 486 LYS 486 486 486 LYS LYS B . n 
B 2 487 LEU 487 487 487 LEU LEU B . n 
B 2 488 GLU 488 488 488 GLU GLU B . n 
B 2 489 LYS 489 489 489 LYS LYS B . n 
B 2 490 LEU 490 490 490 LEU LEU B . n 
B 2 491 ALA 491 491 491 ALA ALA B . n 
B 2 492 PRO 492 492 492 PRO PRO B . n 
B 2 493 LEU 493 493 493 LEU LEU B . n 
B 2 494 VAL 494 494 494 VAL VAL B . n 
B 2 495 LYS 495 495 495 LYS LYS B . n 
B 2 496 THR 496 496 496 THR THR B . n 
B 2 497 GLY 497 497 497 GLY GLY B . n 
B 2 498 SER 498 498 498 SER SER B . n 
B 2 499 LEU 499 499 499 LEU LEU B . n 
B 2 500 CYS 500 500 500 CYS CYS B . n 
B 2 501 GLY 501 501 501 GLY GLY B . n 
B 2 502 LEU 502 502 502 LEU LEU B . n 
B 2 503 GLY 503 503 503 GLY GLY B . n 
B 2 504 GLN 504 504 504 GLN GLN B . n 
B 2 505 THR 505 505 505 THR THR B . n 
B 2 506 ALA 506 506 506 ALA ALA B . n 
B 2 507 PRO 507 507 507 PRO PRO B . n 
B 2 508 ASN 508 508 508 ASN ASN B . n 
B 2 509 PRO 509 509 509 PRO PRO B . n 
B 2 510 VAL 510 510 510 VAL VAL B . n 
B 2 511 LEU 511 511 511 LEU LEU B . n 
B 2 512 THR 512 512 512 THR THR B . n 
B 2 513 THR 513 513 513 THR THR B . n 
B 2 514 LEU 514 514 514 LEU LEU B . n 
B 2 515 LYS 515 515 515 LYS LYS B . n 
B 2 516 TYR 516 516 516 TYR TYR B . n 
B 2 517 PHE 517 517 517 PHE PHE B . n 
B 2 518 LYS 518 518 518 LYS LYS B . n 
B 2 519 ASP 519 519 519 ASP ASP B . n 
B 2 520 GLU 520 520 520 GLU GLU B . n 
B 2 521 TYR 521 521 521 TYR TYR B . n 
B 2 522 LEU 522 522 522 LEU LEU B . n 
B 2 523 ALA 523 523 523 ALA ALA B . n 
B 2 524 HIS 524 524 524 HIS HIS B . n 
B 2 525 ILE 525 525 525 ILE ILE B . n 
B 2 526 GLU 526 526 526 GLU GLU B . n 
B 2 527 GLY 527 527 527 GLY GLY B . n 
B 2 528 ARG 528 528 528 ARG ARG B . n 
B 2 529 CYS 529 529 529 CYS CYS B . n 
B 2 530 PRO 530 530 530 PRO PRO B . n 
B 2 531 ALA 531 531 531 ALA ALA B . n 
B 2 532 LYS 532 532 532 LYS LYS B . n 
B 2 533 VAL 533 533 533 VAL VAL B . n 
B 2 534 CYS 534 534 534 CYS CYS B . n 
B 2 535 LYS 535 535 535 LYS LYS B . n 
B 2 536 PRO 536 536 536 PRO PRO B . n 
B 2 537 LEU 537 537 537 LEU LEU B . n 
B 2 538 ILE 538 538 538 ILE ILE B . n 
B 2 539 LYS 539 539 539 LYS LYS B . n 
B 2 540 TYR 540 540 540 TYR TYR B . n 
B 2 541 VAL 541 541 541 VAL VAL B . n 
B 2 542 ILE 542 542 542 ILE ILE B . n 
B 2 543 ILE 543 543 543 ILE ILE B . n 
B 2 544 THR 544 544 544 THR THR B . n 
B 2 545 GLU 545 545 545 GLU GLU B . n 
B 2 546 LYS 546 546 546 LYS LYS B . n 
B 2 547 CYS 547 547 547 CYS CYS B . n 
B 2 548 THR 548 548 548 THR THR B . n 
B 2 549 GLY 549 549 549 GLY GLY B . n 
B 2 550 CYS 550 550 550 CYS CYS B . n 
B 2 551 THR 551 551 551 THR THR B . n 
B 2 552 ALA 552 552 552 ALA ALA B . n 
B 2 553 CYS 553 553 553 CYS CYS B . n 
B 2 554 ALA 554 554 554 ALA ALA B . n 
B 2 555 ILE 555 555 555 ILE ILE B . n 
B 2 556 MET 556 556 556 MET MET B . n 
B 2 557 CYS 557 557 557 CYS CYS B . n 
B 2 558 PRO 558 558 558 PRO PRO B . n 
B 2 559 VAL 559 559 559 VAL VAL B . n 
B 2 560 LYS 560 560 ?   ?   ?   B . n 
B 2 561 ALA 561 561 ?   ?   ?   B . n 
B 2 562 ILE 562 562 ?   ?   ?   B . n 
B 2 563 SER 563 563 ?   ?   ?   B . n 
B 2 564 GLY 564 564 ?   ?   ?   B . n 
B 2 565 GLU 565 565 ?   ?   ?   B . n 
B 2 566 ARG 566 566 566 ARG ARG B . n 
B 2 567 GLY 567 567 567 GLY GLY B . n 
B 2 568 LYS 568 568 568 LYS LYS B . n 
B 2 569 PRO 569 569 569 PRO PRO B . n 
B 2 570 HIS 570 570 570 HIS HIS B . n 
B 2 571 LEU 571 571 571 LEU LEU B . n 
B 2 572 ILE 572 572 572 ILE ILE B . n 
B 2 573 ASN 573 573 573 ASN ASN B . n 
B 2 574 GLN 574 574 574 GLN GLN B . n 
B 2 575 GLU 575 575 575 GLU GLU B . n 
B 2 576 ALA 576 576 576 ALA ALA B . n 
B 2 577 CYS 577 577 577 CYS CYS B . n 
B 2 578 ILE 578 578 578 ILE ILE B . n 
B 2 579 LYS 579 579 579 LYS LYS B . n 
B 2 580 CYS 580 580 580 CYS CYS B . n 
B 2 581 GLY 581 581 581 GLY GLY B . n 
B 2 582 THR 582 582 582 THR THR B . n 
B 2 583 CYS 583 583 583 CYS CYS B . n 
B 2 584 TYR 584 584 584 TYR TYR B . n 
B 2 585 GLU 585 585 585 GLU GLU B . n 
B 2 586 VAL 586 586 586 VAL VAL B . n 
B 2 587 CYS 587 587 587 CYS CYS B . n 
B 2 588 ARG 588 588 588 ARG ARG B . n 
B 2 589 PHE 589 589 589 PHE PHE B . n 
B 2 590 ASN 590 590 590 ASN ASN B . n 
B 2 591 ALA 591 591 591 ALA ALA B . n 
B 2 592 ILE 592 592 592 ILE ILE B . n 
B 2 593 GLU 593 593 593 GLU GLU B . n 
B 2 594 ILE 594 594 594 ILE ILE B . n 
B 2 595 THR 595 595 595 THR THR B . n 
B 2 596 ASP 596 596 596 ASP ASP B . n 
B 2 597 ALA 597 597 597 ALA ALA B . n 
B 2 598 LYS 598 598 ?   ?   ?   B . n 
B 2 599 LYS 599 599 ?   ?   ?   B . n 
B 2 600 GLU 600 600 ?   ?   ?   B . n 
B 2 601 GLY 601 601 ?   ?   ?   B . n 
B 2 602 GLU 602 602 ?   ?   ?   B . n 
C 3 1   MET 1   1   ?   ?   ?   C . n 
C 3 2   ASN 2   2   ?   ?   ?   C . n 
C 3 3   ILE 3   3   3   ILE ILE C . n 
C 3 4   GLN 4   4   4   GLN GLN C . n 
C 3 5   LEU 5   5   5   LEU LEU C . n 
C 3 6   GLU 6   6   6   GLU GLU C . n 
C 3 7   TYR 7   7   7   TYR TYR C . n 
C 3 8   ILE 8   8   8   ILE ILE C . n 
C 3 9   TYR 9   9   9   TYR TYR C . n 
C 3 10  HIS 10  10  10  HIS HIS C . n 
C 3 11  TYR 11  11  11  TYR TYR C . n 
C 3 12  GLU 12  12  12  GLU GLU C . n 
C 3 13  PRO 13  13  13  PRO PRO C . n 
C 3 14  ASN 14  14  14  ASN ASN C . n 
C 3 15  PRO 15  15  15  PRO PRO C . n 
C 3 16  SER 16  16  16  SER SER C . n 
C 3 17  SER 17  17  17  SER SER C . n 
C 3 18  LEU 18  18  18  LEU LEU C . n 
C 3 19  ILE 19  19  19  ILE ILE C . n 
C 3 20  PRO 20  20  20  PRO PRO C . n 
C 3 21  LEU 21  21  21  LEU LEU C . n 
C 3 22  LEU 22  22  22  LEU LEU C . n 
C 3 23  GLN 23  23  23  GLN GLN C . n 
C 3 24  LYS 24  24  24  LYS LYS C . n 
C 3 25  THR 25  25  25  THR THR C . n 
C 3 26  GLN 26  26  26  GLN GLN C . n 
C 3 27  GLU 27  27  27  GLU GLU C . n 
C 3 28  THR 28  28  28  THR THR C . n 
C 3 29  PHE 29  29  29  PHE PHE C . n 
C 3 30  GLY 30  30  30  GLY GLY C . n 
C 3 31  TYR 31  31  31  TYR TYR C . n 
C 3 32  LEU 32  32  32  LEU LEU C . n 
C 3 33  PRO 33  33  33  PRO PRO C . n 
C 3 34  LYS 34  34  34  LYS LYS C . n 
C 3 35  GLU 35  35  35  GLU GLU C . n 
C 3 36  ALA 36  36  36  ALA ALA C . n 
C 3 37  LEU 37  37  37  LEU LEU C . n 
C 3 38  GLU 38  38  38  GLU GLU C . n 
C 3 39  GLU 39  39  39  GLU GLU C . n 
C 3 40  ILE 40  40  40  ILE ILE C . n 
C 3 41  SER 41  41  41  SER SER C . n 
C 3 42  ARG 42  42  42  ARG ARG C . n 
C 3 43  TYR 43  43  43  TYR TYR C . n 
C 3 44  LEU 44  44  44  LEU LEU C . n 
C 3 45  LYS 45  45  45  LYS LYS C . n 
C 3 46  VAL 46  46  46  VAL VAL C . n 
C 3 47  PRO 47  47  47  PRO PRO C . n 
C 3 48  LEU 48  48  48  LEU LEU C . n 
C 3 49  SER 49  49  49  SER SER C . n 
C 3 50  ARG 50  50  50  ARG ARG C . n 
C 3 51  VAL 51  51  51  VAL VAL C . n 
C 3 52  TYR 52  52  52  TYR TYR C . n 
C 3 53  GLY 53  53  53  GLY GLY C . n 
C 3 54  VAL 54  54  54  VAL VAL C . n 
C 3 55  ALA 55  55  55  ALA ALA C . n 
C 3 56  THR 56  56  56  THR THR C . n 
C 3 57  PHE 57  57  57  PHE PHE C . n 
C 3 58  TYR 58  58  58  TYR TYR C . n 
C 3 59  ALA 59  59  59  ALA ALA C . n 
C 3 60  GLN 60  60  60  GLN GLN C . n 
C 3 61  PHE 61  61  61  PHE PHE C . n 
C 3 62  ARG 62  62  62  ARG ARG C . n 
C 3 63  PHE 63  63  63  PHE PHE C . n 
C 3 64  GLU 64  64  64  GLU GLU C . n 
C 3 65  PRO 65  65  65  PRO PRO C . n 
C 3 66  LEU 66  66  66  LEU LEU C . n 
C 3 67  GLY 67  67  ?   ?   ?   C . n 
C 3 68  LYS 68  68  ?   ?   ?   C . n 
C 3 69  TYR 69  69  ?   ?   ?   C . n 
C 3 70  VAL 70  70  ?   ?   ?   C . n 
C 3 71  ILE 71  71  ?   ?   ?   C . n 
C 3 72  LYS 72  72  ?   ?   ?   C . n 
C 3 73  ILE 73  73  ?   ?   ?   C . n 
C 3 74  CYS 74  74  ?   ?   ?   C . n 
C 3 75  HIS 75  75  ?   ?   ?   C . n 
C 3 76  GLY 76  76  ?   ?   ?   C . n 
C 3 77  THR 77  77  ?   ?   ?   C . n 
C 3 78  ALA 78  78  ?   ?   ?   C . n 
C 3 79  CYS 79  79  ?   ?   ?   C . n 
C 3 80  HIS 80  80  ?   ?   ?   C . n 
C 3 81  VAL 81  81  ?   ?   ?   C . n 
C 3 82  ASN 82  82  ?   ?   ?   C . n 
C 3 83  GLY 83  83  ?   ?   ?   C . n 
C 3 84  ALA 84  84  ?   ?   ?   C . n 
C 3 85  VAL 85  85  ?   ?   ?   C . n 
C 3 86  ASN 86  86  ?   ?   ?   C . n 
C 3 87  ILE 87  87  ?   ?   ?   C . n 
C 3 88  SER 88  88  ?   ?   ?   C . n 
C 3 89  GLN 89  89  ?   ?   ?   C . n 
C 3 90  ALA 90  90  ?   ?   ?   C . n 
C 3 91  ILE 91  91  ?   ?   ?   C . n 
C 3 92  ARG 92  92  ?   ?   ?   C . n 
C 3 93  GLU 93  93  ?   ?   ?   C . n 
C 3 94  GLU 94  94  ?   ?   ?   C . n 
C 3 95  VAL 95  95  ?   ?   ?   C . n 
C 3 96  GLY 96  96  ?   ?   ?   C . n 
C 3 97  ILE 97  97  ?   ?   ?   C . n 
C 3 98  GLU 98  98  ?   ?   ?   C . n 
C 3 99  GLU 99  99  ?   ?   ?   C . n 
C 3 100 GLY 100 100 ?   ?   ?   C . n 
C 3 101 GLN 101 101 ?   ?   ?   C . n 
C 3 102 THR 102 102 ?   ?   ?   C . n 
C 3 103 THR 103 103 ?   ?   ?   C . n 
C 3 104 VAL 104 104 ?   ?   ?   C . n 
C 3 105 ASP 105 105 ?   ?   ?   C . n 
C 3 106 GLY 106 106 ?   ?   ?   C . n 
C 3 107 LEU 107 107 ?   ?   ?   C . n 
C 3 108 ILE 108 108 ?   ?   ?   C . n 
C 3 109 THR 109 109 ?   ?   ?   C . n 
C 3 110 LEU 110 110 ?   ?   ?   C . n 
C 3 111 GLU 111 111 ?   ?   ?   C . n 
C 3 112 ARG 112 112 ?   ?   ?   C . n 
C 3 113 VAL 113 113 ?   ?   ?   C . n 
C 3 114 ALA 114 114 ?   ?   ?   C . n 
C 3 115 CYS 115 115 ?   ?   ?   C . n 
C 3 116 LEU 116 116 ?   ?   ?   C . n 
C 3 117 GLY 117 117 ?   ?   ?   C . n 
C 3 118 CYS 118 118 ?   ?   ?   C . n 
C 3 119 CYS 119 119 ?   ?   ?   C . n 
C 3 120 SER 120 120 ?   ?   ?   C . n 
C 3 121 LEU 121 121 ?   ?   ?   C . n 
C 3 122 ALA 122 122 ?   ?   ?   C . n 
C 3 123 PRO 123 123 ?   ?   ?   C . n 
C 3 124 VAL 124 124 ?   ?   ?   C . n 
C 3 125 ILE 125 125 ?   ?   ?   C . n 
C 3 126 MET 126 126 ?   ?   ?   C . n 
C 3 127 ILE 127 127 ?   ?   ?   C . n 
C 3 128 ASN 128 128 ?   ?   ?   C . n 
C 3 129 GLU 129 129 ?   ?   ?   C . n 
C 3 130 LYS 130 130 ?   ?   ?   C . n 
C 3 131 VAL 131 131 ?   ?   ?   C . n 
C 3 132 TYR 132 132 ?   ?   ?   C . n 
C 3 133 GLY 133 133 ?   ?   ?   C . n 
C 3 134 LYS 134 134 ?   ?   ?   C . n 
C 3 135 LEU 135 135 ?   ?   ?   C . n 
C 3 136 THR 136 136 ?   ?   ?   C . n 
C 3 137 PRO 137 137 ?   ?   ?   C . n 
C 3 138 ASP 138 138 ?   ?   ?   C . n 
C 3 139 LYS 139 139 ?   ?   ?   C . n 
C 3 140 VAL 140 140 ?   ?   ?   C . n 
C 3 141 ARG 141 141 ?   ?   ?   C . n 
C 3 142 LYS 142 142 ?   ?   ?   C . n 
C 3 143 ILE 143 143 ?   ?   ?   C . n 
C 3 144 ILE 144 144 ?   ?   ?   C . n 
C 3 145 ARG 145 145 ?   ?   ?   C . n 
C 3 146 ASN 146 146 ?   ?   ?   C . n 
C 3 147 LEU 147 147 ?   ?   ?   C . n 
C 3 148 LYS 148 148 ?   ?   ?   C . n 
C 3 149 GLU 149 149 ?   ?   ?   C . n 
C 3 150 GLY 150 150 ?   ?   ?   C . n 
C 3 151 LYS 151 151 ?   ?   ?   C . n 
C 3 152 LEU 152 152 ?   ?   ?   C . n 
C 3 153 ASN 153 153 ?   ?   ?   C . n 
C 3 154 VAL 154 154 ?   ?   ?   C . 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 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FES ? ? FES ? ? 'SUBJECT OF INVESTIGATION' ? 
3 FMN ? ? FMN ? ? 'SUBJECT OF INVESTIGATION' ? 
4 NAD ? ? NAD ? ? 'SUBJECT OF INVESTIGATION' ? 
5 SF4 ? ? SF4 ? ? 'SUBJECT OF INVESTIGATION' ? 
6 ZN  ? ? ZN  ? ? '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 
D 4 SF4 1 1001 1002 SF4 SF4 A . 
E 4 SF4 1 1002 1003 SF4 SF4 A . 
F 4 SF4 1 1003 1004 SF4 SF4 A . 
G 4 SF4 1 1004 1005 SF4 SF4 A . 
H 5 FAD 1 1005 1006 FAD FAD A . 
I 4 SF4 1 1006 1007 SF4 SF4 A . 
J 6 FES 1 1007 1008 FES FES A . 
K 4 SF4 1 701  601  SF4 SF4 B . 
L 7 FMN 1 702  604  FMN FMN B . 
M 4 SF4 1 703  605  SF4 SF4 B . 
N 4 SF4 1 704  606  SF4 SF4 B . 
O 8 NAD 1 705  607  NAD NAD B . 
P 9 ZN  1 706  609  ZN  ZN  B . 
Q 9 ZN  1 707  610  ZN  ZN  B . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9N5V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9N5V 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9N5V 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9N5V 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.76 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003  ? 12999 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.522  ? 17640 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 12.012 ? 4903  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.044  ? 1965  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005  ? 2224  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9N5V 
_struct.title                        'Structure of the NAD(H)-bound Thermococcus sibiricus NfnABC 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        9N5V 
_struct_keywords.text            
'Flavin-based electron bifurcation, Bfu family, NfnABC, cryo-EM structures, flavo-FeS cluster, ELECTRON TRANSPORT' 
_struct_keywords.pdbx_keywords   'ELECTRON TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 4 ? 
J N N 6 ? 
K N N 4 ? 
L N N 7 ? 
M N N 4 ? 
N N N 4 ? 
O N N 8 ? 
P N N 9 ? 
Q N N 9 ? 
# 
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 C6A4M3_THESM     C6A4M3     ? 1 
;MPRRRVSEMVKITVNGKEFEAPKDKSLIEFLREITHVPGFCYTEAFDPYGSCRLCLVQTPRGITTSCTLKPMEGLSIETL
SDEIIEMRKTALELILSDHYGDCIGPCQNGCPAHSDVQGYLALIAMGRYHEAVKLMKEKYILPAVLGRVCPAFCEEECRR
NLVEEPLAIRQLKRFAADYDLENGPWMPEIPPSTGKRIAVVGGGPAGLACAYYLRTMGHDVTIFDAMPHLGGMMRYGIPP
YRLPKDVLDKDIATVINTGIEVKTNTALGKDIALEELREQYDAVFLGVGAWKSRKMGIEGEDLDGVIHGTEFLRKVNMGE
KVELGKRVIVVGGGNTAMDVARTALRLGADVTVVYRRSKSEMPANSREVEEAEEEGVKFMFLTNPVKIIGKEKVEEVELI
KMKLGEPDASGRRRPMPIEGSEFRVKVDNVILAIGQYCDEEFLRTIGIEAKRGRVLVDEVTLQTNKEGVFAGGDLVLGPS
TVIESIATGRRAAIMIDLYLKGKLEKAREVLLDPSKHIEEVIYDEDLYRVLFDLRPYNHWKKVTEKDYEHVERKPRVKVK
LLDPEIRKSNFKEVEPTMDEETVLTEAQRCMSCGCMEVFRCKLREYATLYDAKQDAFVGEQNKFEIDETHPNVVLDNNKC
VLCGQCVNFTHEIAREGIVDYLFRGFKTYIGPQLGERLEDQKGVFIGELTDICPVGAITEKLPFVKPGPWKTQPVKTVCN
GCSFACEMNIEVYNDILVRASSRKDSWNGYICDYCRFERPWAQDIAQPILKGNAVSWEDAEKFLEEKECALILTPSLTNE
EIMFLKELAERKGIPIGSTIDGEGSTATLEDIRNAKRVLLKVNIEKYPLLKLLLKGKEIVEEGYEVAIIEGPAEPMDVPT
LILHDGVNATGLIKAGVTGIPEAKAYVVIGNSPAISKLKGEYLILPSGLWAEKEGTVTNAFGMDLKVKKARKAHYDVKSL
FNF
;
1 
2 UNP A0A117L1A0_9EURY A0A117L1A0 ? 2 
;MSEIKAIAVGMNSCGIAAGARETYEAVKEELEKRNLDIKLKIVGCVGMCYREPLLDIITDNEIITYGHVTPDRVPRIIEE
HVINGKPIEDWVVKKDWWENGQRKTWDFDGYFVKQKKIVLENSGYIDPENIEEYIAAGGYEALKKAFKMKPEEIIDFITK
SGLRGRGGAGFPTGLKWKFTRDAPGDEKYIVCNADEGDPGAFMDRNVLEGDPHRVIEGMIIGAYAIGATKGFIYVRAEYP
LAIKRLRIALKQAREKGFLGENILGSGFSFEIVIKEGAGAFVCGEETALIASIEGKRGMPRPRPPYPAQKGLWGRPTNIN
NVETWANVPWIIKHGWEAYAALGTEKSKGTKVFALSGKIKHGGNVEVPMGITLREILYEIGGGTKTGKKIKAVQLGGPSG
GCIPDYLFNTPVDYESVTATGAIMGSGGMVVMDEDTCMVDVAKFFLDFTVKESCGKCTFCRLGTKRMWELLDKITKGEGA
LEDIEKLEKLAPLVKTGSLCGLGQTAPNPVLTTLKYFKDEYLAHIEGRCPAKVCKPLIKYVIITEKCTGCTACAIMCPVK
AISGERGKPHLINQEACIKCGTCYEVCRFNAIEITDAKKEGE
;
1 
3 UNP A0A117L1U2_9EURY A0A117L1U2 ? 3 
;MNIQLEYIYHYEPNPSSLIPLLQKTQETFGYLPKEALEEISRYLKVPLSRVYGVATFYAQFRFEPLGKYVIKICHGTACH
VNGAVNISQAIREEVGIEEGQTTVDGLITLERVACLGCCSLAPVIMINEKVYGKLTPDKVRKIIRNLKEGKLNV
;
3 
# 
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 9N5V A 1 ? 963 ? C6A4M3     1 ? 963 ? 1 963 
2 2 9N5V B 1 ? 602 ? A0A117L1A0 1 ? 602 ? 1 602 
3 3 9N5V C 1 ? 154 ? A0A117L1U2 3 ? 156 ? 1 154 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 26  ? THR A 35  ? SER A 26  THR A 35  1 ? 10 
HELX_P HELX_P2  AA2 SER A 81  ? HIS A 99  ? SER A 81  HIS A 99  1 ? 19 
HELX_P HELX_P3  AA3 GLY A 105 ? CYS A 111 ? GLY A 105 CYS A 111 1 ? 7  
HELX_P HELX_P4  AA4 ASP A 116 ? GLY A 127 ? ASP A 116 GLY A 127 1 ? 12 
HELX_P HELX_P5  AA5 ARG A 128 ? GLU A 138 ? ARG A 128 GLU A 138 1 ? 11 
HELX_P HELX_P6  AA6 LEU A 142 ? CYS A 150 ? LEU A 142 CYS A 150 1 ? 9  
HELX_P HELX_P7  AA7 ALA A 168 ? ASN A 183 ? ALA A 168 ASN A 183 1 ? 16 
HELX_P HELX_P8  AA8 GLY A 204 ? THR A 216 ? GLY A 204 THR A 216 1 ? 13 
HELX_P HELX_P9  AA9 GLY A 231 ? ARG A 235 ? GLY A 231 ARG A 235 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 244 ? ASN A 257 ? PRO A 244 ASN A 257 1 ? 14 
HELX_P HELX_P11 AB2 ALA A 273 ? GLN A 280 ? ALA A 273 GLN A 280 1 ? 8  
HELX_P HELX_P12 AB3 GLY A 309 ? GLY A 319 ? GLY A 309 GLY A 319 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 334 ? LEU A 347 ? GLY A 334 LEU A 347 1 ? 14 
HELX_P HELX_P14 AB5 ASN A 365 ? GLY A 376 ? ASN A 365 GLY A 376 1 ? 12 
HELX_P HELX_P15 AB6 ASP A 439 ? ILE A 446 ? ASP A 439 ILE A 446 1 ? 8  
HELX_P HELX_P16 AB7 GLY A 473 ? GLY A 478 ? GLY A 473 GLY A 478 1 ? 6  
HELX_P HELX_P17 AB8 THR A 481 ? LYS A 501 ? THR A 481 LYS A 501 1 ? 21 
HELX_P HELX_P18 AB9 LYS A 503 ? ASP A 513 ? LYS A 503 ASP A 513 1 ? 11 
HELX_P HELX_P19 AC1 PRO A 514 ? LYS A 516 ? PRO A 514 LYS A 516 5 ? 3  
HELX_P HELX_P20 AC2 HIS A 517 ? ASP A 524 ? HIS A 517 ASP A 524 1 ? 8  
HELX_P HELX_P21 AC3 ASP A 524 ? ARG A 535 ? ASP A 524 ARG A 535 1 ? 12 
HELX_P HELX_P22 AC4 THR A 544 ? GLU A 549 ? THR A 544 GLU A 549 5 ? 6  
HELX_P HELX_P23 AC5 ASP A 563 ? LYS A 568 ? ASP A 563 LYS A 568 1 ? 6  
HELX_P HELX_P24 AC6 ASP A 579 ? GLN A 588 ? ASP A 579 GLN A 588 1 ? 10 
HELX_P HELX_P25 AC7 CYS A 601 ? TYR A 610 ? CYS A 601 TYR A 610 1 ? 10 
HELX_P HELX_P26 AC8 ASN A 637 ? CYS A 640 ? ASN A 637 CYS A 640 5 ? 4  
HELX_P HELX_P27 AC9 GLY A 644 ? ILE A 653 ? GLY A 644 ILE A 653 1 ? 10 
HELX_P HELX_P28 AD1 ARG A 664 ? THR A 668 ? ARG A 664 THR A 668 5 ? 5  
HELX_P HELX_P29 AD2 ARG A 677 ? GLN A 681 ? ARG A 677 GLN A 681 5 ? 5  
HELX_P HELX_P30 AD3 GLU A 688 ? CYS A 693 ? GLU A 688 CYS A 693 1 ? 6  
HELX_P HELX_P31 AD4 CYS A 752 ? GLU A 758 ? CYS A 752 GLU A 758 1 ? 7  
HELX_P HELX_P32 AD5 ARG A 759 ? GLN A 763 ? ARG A 759 GLN A 763 5 ? 5  
HELX_P HELX_P33 AD6 SER A 776 ? LYS A 787 ? SER A 776 LYS A 787 1 ? 12 
HELX_P HELX_P34 AD7 THR A 798 ? GLY A 813 ? THR A 798 GLY A 813 1 ? 16 
HELX_P HELX_P35 AD8 THR A 828 ? ALA A 835 ? THR A 828 ALA A 835 1 ? 8  
HELX_P HELX_P36 AD9 PRO A 848 ? LEU A 854 ? PRO A 848 LEU A 854 1 ? 7  
HELX_P HELX_P37 AE1 ASN A 888 ? ILE A 893 ? ASN A 888 ILE A 893 5 ? 6  
HELX_P HELX_P38 AE2 SER A 912 ? LEU A 918 ? SER A 912 LEU A 918 5 ? 7  
HELX_P HELX_P39 AE3 LEU A 929 ? LYS A 933 ? LEU A 929 LYS A 933 5 ? 5  
HELX_P HELX_P40 AE4 ASN B 12  ? GLY B 19  ? ASN B 12  GLY B 19  1 ? 8  
HELX_P HELX_P41 AE5 GLY B 19  ? ARG B 34  ? GLY B 19  ARG B 34  1 ? 16 
HELX_P HELX_P42 AE6 MET B 48  ? GLU B 52  ? MET B 48  GLU B 52  5 ? 5  
HELX_P HELX_P43 AE7 ARG B 73  ? VAL B 82  ? ARG B 73  VAL B 82  1 ? 10 
HELX_P HELX_P44 AE8 ASN B 130 ? ALA B 137 ? ASN B 130 ALA B 137 1 ? 8  
HELX_P HELX_P45 AE9 TYR B 140 ? LYS B 148 ? TYR B 140 LYS B 148 1 ? 9  
HELX_P HELX_P46 AF1 LYS B 150 ? SER B 161 ? LYS B 150 SER B 161 1 ? 12 
HELX_P HELX_P47 AF2 PRO B 172 ? ALA B 183 ? PRO B 172 ALA B 183 1 ? 12 
HELX_P HELX_P48 AF3 PHE B 202 ? ASP B 211 ? PHE B 202 ASP B 211 1 ? 10 
HELX_P HELX_P49 AF4 ASP B 211 ? GLY B 227 ? ASP B 211 GLY B 227 1 ? 17 
HELX_P HELX_P50 AF5 TYR B 239 ? LYS B 256 ? TYR B 239 LYS B 256 1 ? 18 
HELX_P HELX_P51 AF6 ASN B 262 ? SER B 266 ? ASN B 262 SER B 266 5 ? 5  
HELX_P HELX_P52 AF7 GLU B 285 ? GLU B 294 ? GLU B 285 GLU B 294 1 ? 10 
HELX_P HELX_P53 AF8 GLY B 311 ? ARG B 315 ? GLY B 311 ARG B 315 5 ? 5  
HELX_P HELX_P54 AF9 VAL B 322 ? ALA B 341 ? VAL B 322 ALA B 341 1 ? 20 
HELX_P HELX_P55 AG1 LEU B 373 ? GLU B 379 ? LEU B 373 GLU B 379 1 ? 7  
HELX_P HELX_P56 AG2 GLY B 397 ? GLY B 400 ? GLY B 397 GLY B 400 5 ? 4  
HELX_P HELX_P57 AG3 TYR B 406 ? PHE B 408 ? TYR B 406 PHE B 408 5 ? 3  
HELX_P HELX_P58 AG4 ASP B 413 ? GLY B 421 ? ASP B 413 GLY B 421 1 ? 9  
HELX_P HELX_P59 AG5 CYS B 437 ? SER B 453 ? CYS B 437 SER B 453 1 ? 17 
HELX_P HELX_P60 AG6 CYS B 457 ? LYS B 476 ? CYS B 457 LYS B 476 1 ? 20 
HELX_P HELX_P61 AG7 ALA B 480 ? SER B 498 ? ALA B 480 SER B 498 1 ? 19 
HELX_P HELX_P62 AG8 CYS B 500 ? THR B 505 ? CYS B 500 THR B 505 1 ? 6  
HELX_P HELX_P63 AG9 PRO B 507 ? PHE B 517 ? PRO B 507 PHE B 517 1 ? 11 
HELX_P HELX_P64 AH1 PHE B 517 ? GLU B 526 ? PHE B 517 GLU B 526 1 ? 10 
HELX_P HELX_P65 AH2 ALA B 552 ? CYS B 557 ? ALA B 552 CYS B 557 1 ? 6  
HELX_P HELX_P66 AH3 ILE C 3   ? TYR C 11  ? ILE C 3   TYR C 11  5 ? 9  
HELX_P HELX_P67 AH4 ASN C 14  ? SER C 16  ? ASN C 14  SER C 16  5 ? 3  
HELX_P HELX_P68 AH5 SER C 17  ? GLY C 30  ? SER C 17  GLY C 30  1 ? 14 
HELX_P HELX_P69 AH6 PRO C 33  ? LYS C 45  ? PRO C 33  LYS C 45  1 ? 13 
HELX_P HELX_P70 AH7 PRO C 47  ? TYR C 58  ? PRO C 47  TYR C 58  1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 41  SG  ? ? ? 1_555 J FES . FE1 ? ? A CYS 41  A FES 1007 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc2  metalc ? ? A CYS 52  SG  ? ? ? 1_555 J FES . FE1 ? ? A CYS 52  A FES 1007 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc3  metalc ? ? A CYS 55  SG  ? ? ? 1_555 J FES . FE2 ? ? A CYS 55  A FES 1007 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc4  metalc ? ? A CYS 67  SG  ? ? ? 1_555 J FES . FE2 ? ? A CYS 67  A FES 1007 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc5  metalc ? ? A HIS 99  ND1 ? ? ? 1_555 G SF4 . FE4 ? ? A HIS 99  A SF4 1004 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc6  metalc ? ? A HIS 99  NE2 ? ? ? 1_555 G SF4 . FE4 ? ? A HIS 99  A SF4 1004 1_555 ? ? ? ? ? ? ? 2.504 ? ? 
metalc7  metalc ? ? A CYS 103 SG  ? ? ? 1_555 G SF4 . FE2 ? ? A CYS 103 A SF4 1004 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc8  metalc ? ? A CYS 107 SG  ? ? ? 1_555 F SF4 . FE3 ? ? A CYS 107 A SF4 1003 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc9  metalc ? ? A CYS 111 SG  ? ? ? 1_555 E SF4 . FE1 ? ? A CYS 111 A SF4 1002 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc10 metalc ? ? A CYS 150 SG  ? ? ? 1_555 E SF4 . FE2 ? ? A CYS 150 A SF4 1002 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc11 metalc ? ? A CYS 154 SG  ? ? ? 1_555 E SF4 . FE4 ? ? A CYS 154 A SF4 1002 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc12 metalc ? ? A CYS 158 SG  ? ? ? 1_555 F SF4 . FE4 ? ? A CYS 158 A SF4 1003 1_555 ? ? ? ? ? ? ? 2.260 ? ? 
metalc13 metalc ? ? A LYS 173 NZ  ? ? ? 1_555 E SF4 . FE3 ? ? A LYS 173 A SF4 1002 1_555 ? ? ? ? ? ? ? 2.775 ? ? 
metalc14 metalc ? ? A CYS 590 SG  ? ? ? 1_555 F SF4 . FE1 ? ? A CYS 590 A SF4 1003 1_555 ? ? ? ? ? ? ? 2.276 ? ? 
metalc15 metalc ? ? A CYS 593 SG  ? ? ? 1_555 F SF4 . FE2 ? ? A CYS 593 A SF4 1003 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc16 metalc ? ? A CYS 595 SG  ? ? ? 1_555 G SF4 . FE3 ? ? A CYS 595 A SF4 1004 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc17 metalc ? ? A CYS 601 SG  ? ? ? 1_555 G SF4 . FE1 ? ? A CYS 601 A SF4 1004 1_555 ? ? ? ? ? ? ? 2.261 ? ? 
metalc18 metalc ? ? A CYS 640 SG  ? ? ? 1_555 D SF4 . FE1 ? ? A CYS 640 A SF4 1001 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc19 metalc ? ? A CYS 643 SG  ? ? ? 1_555 D SF4 . FE2 ? ? A CYS 643 A SF4 1001 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc20 metalc ? ? A CYS 646 SG  ? ? ? 1_555 D SF4 . FE3 ? ? A CYS 646 A SF4 1001 1_555 ? ? ? ? ? ? ? 2.260 ? ? 
metalc21 metalc ? ? A CYS 693 SG  ? ? ? 1_555 D SF4 . FE4 ? ? A CYS 693 A SF4 1001 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc22 metalc ? ? A CYS 719 SG  ? ? ? 1_555 I SF4 . FE4 ? ? A CYS 719 A SF4 1006 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc23 metalc ? ? A CYS 722 SG  ? ? ? 1_555 I SF4 . FE3 ? ? A CYS 722 A SF4 1006 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc24 metalc ? ? A CYS 726 SG  ? ? ? 1_555 I SF4 . FE2 ? ? A CYS 726 A SF4 1006 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc25 metalc ? ? A CYS 752 SG  ? ? ? 1_555 I SF4 . FE1 ? ? A CYS 752 A SF4 1006 1_555 ? ? ? ? ? ? ? 2.260 ? ? 
metalc26 metalc ? ? B CYS 14  SG  ? ? ? 1_555 Q ZN  . ZN  ? ? B CYS 14  B ZN  707  1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc27 metalc ? ? B CYS 45  SG  ? ? ? 1_555 Q ZN  . ZN  ? ? B CYS 45  B ZN  707  1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc28 metalc ? ? B CYS 49  SG  ? ? ? 1_555 Q ZN  . ZN  ? ? B CYS 49  B ZN  707  1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc29 metalc ? ? B CYS 437 SG  ? ? ? 1_555 P ZN  . ZN  ? ? B CYS 437 B ZN  706  1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc30 metalc ? ? B CYS 454 SG  ? ? ? 1_555 K SF4 . FE4 ? ? B CYS 454 B SF4 701  1_555 ? ? ? ? ? ? ? 2.260 ? ? 
metalc31 metalc ? ? B CYS 457 SG  ? ? ? 1_555 K SF4 . FE3 ? ? B CYS 457 B SF4 701  1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc32 metalc ? ? B CYS 460 SG  ? ? ? 1_555 K SF4 . FE2 ? ? B CYS 460 B SF4 701  1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc33 metalc ? ? B CYS 500 SG  ? ? ? 1_555 K SF4 . FE1 ? ? B CYS 500 B SF4 701  1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc34 metalc ? ? B HIS 524 NE2 ? ? ? 1_555 P ZN  . ZN  ? ? B HIS 524 B ZN  706  1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc35 metalc ? ? B CYS 529 SG  ? ? ? 1_555 P ZN  . ZN  ? ? B CYS 529 B ZN  706  1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc36 metalc ? ? B CYS 534 SG  ? ? ? 1_555 P ZN  . ZN  ? ? B CYS 534 B ZN  706  1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc37 metalc ? ? B CYS 547 SG  ? ? ? 1_555 M SF4 . FE3 ? ? B CYS 547 B SF4 703  1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc38 metalc ? ? B CYS 550 SG  ? ? ? 1_555 M SF4 . FE4 ? ? B CYS 550 B SF4 703  1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc39 metalc ? ? B CYS 553 SG  ? ? ? 1_555 M SF4 . FE1 ? ? B CYS 553 B SF4 703  1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc40 metalc ? ? B CYS 557 SG  ? ? ? 1_555 N SF4 . FE4 ? ? B CYS 557 B SF4 704  1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc41 metalc ? ? B CYS 577 SG  ? ? ? 1_555 N SF4 . FE3 ? ? B CYS 577 B SF4 704  1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc42 metalc ? ? B CYS 580 SG  ? ? ? 1_555 N SF4 . FE1 ? ? B CYS 580 B SF4 704  1_555 ? ? ? ? ? ? ? 2.272 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   SG  ? A CYS 41  ? A CYS 41   ? 1_555 FE1 ? J FES . ? A FES 1007 ? 1_555 S1  ? J FES .   ? A FES 1007 ? 1_555 118.2 ? 
2   SG  ? A CYS 41  ? A CYS 41   ? 1_555 FE1 ? J FES . ? A FES 1007 ? 1_555 S2  ? J FES .   ? A FES 1007 ? 1_555 114.0 ? 
3   S1  ? J FES .   ? A FES 1007 ? 1_555 FE1 ? J FES . ? A FES 1007 ? 1_555 S2  ? J FES .   ? A FES 1007 ? 1_555 104.2 ? 
4   SG  ? A CYS 41  ? A CYS 41   ? 1_555 FE1 ? J FES . ? A FES 1007 ? 1_555 SG  ? A CYS 52  ? A CYS 52   ? 1_555 106.0 ? 
5   S1  ? J FES .   ? A FES 1007 ? 1_555 FE1 ? J FES . ? A FES 1007 ? 1_555 SG  ? A CYS 52  ? A CYS 52   ? 1_555 106.7 ? 
6   S2  ? J FES .   ? A FES 1007 ? 1_555 FE1 ? J FES . ? A FES 1007 ? 1_555 SG  ? A CYS 52  ? A CYS 52   ? 1_555 107.1 ? 
7   SG  ? A CYS 55  ? A CYS 55   ? 1_555 FE2 ? J FES . ? A FES 1007 ? 1_555 S1  ? J FES .   ? A FES 1007 ? 1_555 110.4 ? 
8   SG  ? A CYS 55  ? A CYS 55   ? 1_555 FE2 ? J FES . ? A FES 1007 ? 1_555 S2  ? J FES .   ? A FES 1007 ? 1_555 113.8 ? 
9   S1  ? J FES .   ? A FES 1007 ? 1_555 FE2 ? J FES . ? A FES 1007 ? 1_555 S2  ? J FES .   ? A FES 1007 ? 1_555 104.2 ? 
10  SG  ? A CYS 55  ? A CYS 55   ? 1_555 FE2 ? J FES . ? A FES 1007 ? 1_555 SG  ? A CYS 67  ? A CYS 67   ? 1_555 98.3  ? 
11  S1  ? J FES .   ? A FES 1007 ? 1_555 FE2 ? J FES . ? A FES 1007 ? 1_555 SG  ? A CYS 67  ? A CYS 67   ? 1_555 118.1 ? 
12  S2  ? J FES .   ? A FES 1007 ? 1_555 FE2 ? J FES . ? A FES 1007 ? 1_555 SG  ? A CYS 67  ? A CYS 67   ? 1_555 112.5 ? 
13  ND1 ? A HIS 99  ? A HIS 99   ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 S1  ? G SF4 .   ? A SF4 1004 ? 1_555 120.7 ? 
14  ND1 ? A HIS 99  ? A HIS 99   ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 S2  ? G SF4 .   ? A SF4 1004 ? 1_555 124.6 ? 
15  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 S2  ? G SF4 .   ? A SF4 1004 ? 1_555 103.7 ? 
16  ND1 ? A HIS 99  ? A HIS 99   ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 96.0  ? 
17  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
18  S2  ? G SF4 .   ? A SF4 1004 ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 104.0 ? 
19  ND1 ? A HIS 99  ? A HIS 99   ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 NE2 ? A HIS 99  ? A HIS 99   ? 1_555 54.5  ? 
20  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 NE2 ? A HIS 99  ? A HIS 99   ? 1_555 148.3 ? 
21  S2  ? G SF4 .   ? A SF4 1004 ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 NE2 ? A HIS 99  ? A HIS 99   ? 1_555 70.1  ? 
22  S3  ? G SF4 .   ? A SF4 1004 ? 1_555 FE4 ? G SF4 . ? A SF4 1004 ? 1_555 NE2 ? A HIS 99  ? A HIS 99   ? 1_555 107.5 ? 
23  SG  ? A CYS 103 ? A CYS 103  ? 1_555 FE2 ? G SF4 . ? A SF4 1004 ? 1_555 S1  ? G SF4 .   ? A SF4 1004 ? 1_555 119.9 ? 
24  SG  ? A CYS 103 ? A CYS 103  ? 1_555 FE2 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 112.8 ? 
25  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE2 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
26  SG  ? A CYS 103 ? A CYS 103  ? 1_555 FE2 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 110.1 ? 
27  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE2 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
28  S3  ? G SF4 .   ? A SF4 1004 ? 1_555 FE2 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
29  SG  ? A CYS 107 ? A CYS 107  ? 1_555 FE3 ? F SF4 . ? A SF4 1003 ? 1_555 S1  ? F SF4 .   ? A SF4 1003 ? 1_555 112.4 ? 
30  SG  ? A CYS 107 ? A CYS 107  ? 1_555 FE3 ? F SF4 . ? A SF4 1003 ? 1_555 S2  ? F SF4 .   ? A SF4 1003 ? 1_555 109.3 ? 
31  S1  ? F SF4 .   ? A SF4 1003 ? 1_555 FE3 ? F SF4 . ? A SF4 1003 ? 1_555 S2  ? F SF4 .   ? A SF4 1003 ? 1_555 104.1 ? 
32  SG  ? A CYS 107 ? A CYS 107  ? 1_555 FE3 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 121.2 ? 
33  S1  ? F SF4 .   ? A SF4 1003 ? 1_555 FE3 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.1 ? 
34  S2  ? F SF4 .   ? A SF4 1003 ? 1_555 FE3 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.1 ? 
35  SG  ? A CYS 111 ? A CYS 111  ? 1_555 FE1 ? E SF4 . ? A SF4 1002 ? 1_555 S2  ? E SF4 .   ? A SF4 1002 ? 1_555 106.0 ? 
36  SG  ? A CYS 111 ? A CYS 111  ? 1_555 FE1 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 113.8 ? 
37  S2  ? E SF4 .   ? A SF4 1002 ? 1_555 FE1 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
38  SG  ? A CYS 111 ? A CYS 111  ? 1_555 FE1 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 122.9 ? 
39  S2  ? E SF4 .   ? A SF4 1002 ? 1_555 FE1 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
40  S3  ? E SF4 .   ? A SF4 1002 ? 1_555 FE1 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
41  SG  ? A CYS 150 ? A CYS 150  ? 1_555 FE2 ? E SF4 . ? A SF4 1002 ? 1_555 S1  ? E SF4 .   ? A SF4 1002 ? 1_555 113.1 ? 
42  SG  ? A CYS 150 ? A CYS 150  ? 1_555 FE2 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 115.4 ? 
43  S1  ? E SF4 .   ? A SF4 1002 ? 1_555 FE2 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
44  SG  ? A CYS 150 ? A CYS 150  ? 1_555 FE2 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 114.7 ? 
45  S1  ? E SF4 .   ? A SF4 1002 ? 1_555 FE2 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 104.2 ? 
46  S3  ? E SF4 .   ? A SF4 1002 ? 1_555 FE2 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
47  SG  ? A CYS 154 ? A CYS 154  ? 1_555 FE4 ? E SF4 . ? A SF4 1002 ? 1_555 S1  ? E SF4 .   ? A SF4 1002 ? 1_555 113.0 ? 
48  SG  ? A CYS 154 ? A CYS 154  ? 1_555 FE4 ? E SF4 . ? A SF4 1002 ? 1_555 S2  ? E SF4 .   ? A SF4 1002 ? 1_555 111.4 ? 
49  S1  ? E SF4 .   ? A SF4 1002 ? 1_555 FE4 ? E SF4 . ? A SF4 1002 ? 1_555 S2  ? E SF4 .   ? A SF4 1002 ? 1_555 104.2 ? 
50  SG  ? A CYS 154 ? A CYS 154  ? 1_555 FE4 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 118.5 ? 
51  S1  ? E SF4 .   ? A SF4 1002 ? 1_555 FE4 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 104.2 ? 
52  S2  ? E SF4 .   ? A SF4 1002 ? 1_555 FE4 ? E SF4 . ? A SF4 1002 ? 1_555 S3  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
53  SG  ? A CYS 158 ? A CYS 158  ? 1_555 FE4 ? F SF4 . ? A SF4 1003 ? 1_555 S1  ? F SF4 .   ? A SF4 1003 ? 1_555 104.3 ? 
54  SG  ? A CYS 158 ? A CYS 158  ? 1_555 FE4 ? F SF4 . ? A SF4 1003 ? 1_555 S2  ? F SF4 .   ? A SF4 1003 ? 1_555 116.5 ? 
55  S1  ? F SF4 .   ? A SF4 1003 ? 1_555 FE4 ? F SF4 . ? A SF4 1003 ? 1_555 S2  ? F SF4 .   ? A SF4 1003 ? 1_555 104.2 ? 
56  SG  ? A CYS 158 ? A CYS 158  ? 1_555 FE4 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 121.6 ? 
57  S1  ? F SF4 .   ? A SF4 1003 ? 1_555 FE4 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 104.2 ? 
58  S2  ? F SF4 .   ? A SF4 1003 ? 1_555 FE4 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 104.1 ? 
59  NZ  ? A LYS 173 ? A LYS 173  ? 1_555 FE3 ? E SF4 . ? A SF4 1002 ? 1_555 S1  ? E SF4 .   ? A SF4 1002 ? 1_555 70.3  ? 
60  NZ  ? A LYS 173 ? A LYS 173  ? 1_555 FE3 ? E SF4 . ? A SF4 1002 ? 1_555 S2  ? E SF4 .   ? A SF4 1002 ? 1_555 161.0 ? 
61  S1  ? E SF4 .   ? A SF4 1002 ? 1_555 FE3 ? E SF4 . ? A SF4 1002 ? 1_555 S2  ? E SF4 .   ? A SF4 1002 ? 1_555 104.2 ? 
62  NZ  ? A LYS 173 ? A LYS 173  ? 1_555 FE3 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 94.7  ? 
63  S1  ? E SF4 .   ? A SF4 1002 ? 1_555 FE3 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 104.1 ? 
64  S2  ? E SF4 .   ? A SF4 1002 ? 1_555 FE3 ? E SF4 . ? A SF4 1002 ? 1_555 S4  ? E SF4 .   ? A SF4 1002 ? 1_555 104.2 ? 
65  SG  ? A CYS 590 ? A CYS 590  ? 1_555 FE1 ? F SF4 . ? A SF4 1003 ? 1_555 S2  ? F SF4 .   ? A SF4 1003 ? 1_555 122.3 ? 
66  SG  ? A CYS 590 ? A CYS 590  ? 1_555 FE1 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 115.8 ? 
67  S2  ? F SF4 .   ? A SF4 1003 ? 1_555 FE1 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 104.0 ? 
68  SG  ? A CYS 590 ? A CYS 590  ? 1_555 FE1 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.5 ? 
69  S2  ? F SF4 .   ? A SF4 1003 ? 1_555 FE1 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.1 ? 
70  S3  ? F SF4 .   ? A SF4 1003 ? 1_555 FE1 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.3 ? 
71  SG  ? A CYS 593 ? A CYS 593  ? 1_555 FE2 ? F SF4 . ? A SF4 1003 ? 1_555 S1  ? F SF4 .   ? A SF4 1003 ? 1_555 118.4 ? 
72  SG  ? A CYS 593 ? A CYS 593  ? 1_555 FE2 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 111.1 ? 
73  S1  ? F SF4 .   ? A SF4 1003 ? 1_555 FE2 ? F SF4 . ? A SF4 1003 ? 1_555 S3  ? F SF4 .   ? A SF4 1003 ? 1_555 104.1 ? 
74  SG  ? A CYS 593 ? A CYS 593  ? 1_555 FE2 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 113.5 ? 
75  S1  ? F SF4 .   ? A SF4 1003 ? 1_555 FE2 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.0 ? 
76  S3  ? F SF4 .   ? A SF4 1003 ? 1_555 FE2 ? F SF4 . ? A SF4 1003 ? 1_555 S4  ? F SF4 .   ? A SF4 1003 ? 1_555 104.2 ? 
77  SG  ? A CYS 595 ? A CYS 595  ? 1_555 FE3 ? G SF4 . ? A SF4 1004 ? 1_555 S1  ? G SF4 .   ? A SF4 1004 ? 1_555 124.4 ? 
78  SG  ? A CYS 595 ? A CYS 595  ? 1_555 FE3 ? G SF4 . ? A SF4 1004 ? 1_555 S2  ? G SF4 .   ? A SF4 1004 ? 1_555 112.2 ? 
79  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE3 ? G SF4 . ? A SF4 1004 ? 1_555 S2  ? G SF4 .   ? A SF4 1004 ? 1_555 103.8 ? 
80  SG  ? A CYS 595 ? A CYS 595  ? 1_555 FE3 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 106.1 ? 
81  S1  ? G SF4 .   ? A SF4 1004 ? 1_555 FE3 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
82  S2  ? G SF4 .   ? A SF4 1004 ? 1_555 FE3 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
83  SG  ? A CYS 601 ? A CYS 601  ? 1_555 FE1 ? G SF4 . ? A SF4 1004 ? 1_555 S2  ? G SF4 .   ? A SF4 1004 ? 1_555 110.4 ? 
84  SG  ? A CYS 601 ? A CYS 601  ? 1_555 FE1 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 117.3 ? 
85  S2  ? G SF4 .   ? A SF4 1004 ? 1_555 FE1 ? G SF4 . ? A SF4 1004 ? 1_555 S3  ? G SF4 .   ? A SF4 1004 ? 1_555 104.1 ? 
86  SG  ? A CYS 601 ? A CYS 601  ? 1_555 FE1 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 115.4 ? 
87  S2  ? G SF4 .   ? A SF4 1004 ? 1_555 FE1 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
88  S3  ? G SF4 .   ? A SF4 1004 ? 1_555 FE1 ? G SF4 . ? A SF4 1004 ? 1_555 S4  ? G SF4 .   ? A SF4 1004 ? 1_555 104.2 ? 
89  SG  ? A CYS 640 ? A CYS 640  ? 1_555 FE1 ? D SF4 . ? A SF4 1001 ? 1_555 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 114.5 ? 
90  SG  ? A CYS 640 ? A CYS 640  ? 1_555 FE1 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 116.8 ? 
91  S2  ? D SF4 .   ? A SF4 1001 ? 1_555 FE1 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
92  SG  ? A CYS 640 ? A CYS 640  ? 1_555 FE1 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 111.7 ? 
93  S2  ? D SF4 .   ? A SF4 1001 ? 1_555 FE1 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 104.2 ? 
94  S3  ? D SF4 .   ? A SF4 1001 ? 1_555 FE1 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
95  SG  ? A CYS 643 ? A CYS 643  ? 1_555 FE2 ? D SF4 . ? A SF4 1001 ? 1_555 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 102.1 ? 
96  SG  ? A CYS 643 ? A CYS 643  ? 1_555 FE2 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 114.0 ? 
97  S1  ? D SF4 .   ? A SF4 1001 ? 1_555 FE2 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 104.3 ? 
98  SG  ? A CYS 643 ? A CYS 643  ? 1_555 FE2 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 125.9 ? 
99  S1  ? D SF4 .   ? A SF4 1001 ? 1_555 FE2 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
100 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 FE2 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 104.0 ? 
101 SG  ? A CYS 646 ? A CYS 646  ? 1_555 FE3 ? D SF4 . ? A SF4 1001 ? 1_555 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 111.1 ? 
102 SG  ? A CYS 646 ? A CYS 646  ? 1_555 FE3 ? D SF4 . ? A SF4 1001 ? 1_555 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 117.3 ? 
103 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 FE3 ? D SF4 . ? A SF4 1001 ? 1_555 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
104 SG  ? A CYS 646 ? A CYS 646  ? 1_555 FE3 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 114.6 ? 
105 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 FE3 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
106 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 FE3 ? D SF4 . ? A SF4 1001 ? 1_555 S4  ? D SF4 .   ? A SF4 1001 ? 1_555 104.2 ? 
107 SG  ? A CYS 693 ? A CYS 693  ? 1_555 FE4 ? D SF4 . ? A SF4 1001 ? 1_555 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 111.8 ? 
108 SG  ? A CYS 693 ? A CYS 693  ? 1_555 FE4 ? D SF4 . ? A SF4 1001 ? 1_555 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 120.9 ? 
109 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 FE4 ? D SF4 . ? A SF4 1001 ? 1_555 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
110 SG  ? A CYS 693 ? A CYS 693  ? 1_555 FE4 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 110.3 ? 
111 S1  ? D SF4 .   ? A SF4 1001 ? 1_555 FE4 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 104.2 ? 
112 S2  ? D SF4 .   ? A SF4 1001 ? 1_555 FE4 ? D SF4 . ? A SF4 1001 ? 1_555 S3  ? D SF4 .   ? A SF4 1001 ? 1_555 104.1 ? 
113 SG  ? A CYS 719 ? A CYS 719  ? 1_555 FE4 ? I SF4 . ? A SF4 1006 ? 1_555 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 114.5 ? 
114 SG  ? A CYS 719 ? A CYS 719  ? 1_555 FE4 ? I SF4 . ? A SF4 1006 ? 1_555 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 113.2 ? 
115 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 FE4 ? I SF4 . ? A SF4 1006 ? 1_555 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
116 SG  ? A CYS 719 ? A CYS 719  ? 1_555 FE4 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 115.6 ? 
117 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 FE4 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
118 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 FE4 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 104.2 ? 
119 SG  ? A CYS 722 ? A CYS 722  ? 1_555 FE3 ? I SF4 . ? A SF4 1006 ? 1_555 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 107.0 ? 
120 SG  ? A CYS 722 ? A CYS 722  ? 1_555 FE3 ? I SF4 . ? A SF4 1006 ? 1_555 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 118.1 ? 
121 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 FE3 ? I SF4 . ? A SF4 1006 ? 1_555 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
122 SG  ? A CYS 722 ? A CYS 722  ? 1_555 FE3 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 117.7 ? 
123 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 FE3 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 104.2 ? 
124 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 FE3 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
125 SG  ? A CYS 726 ? A CYS 726  ? 1_555 FE2 ? I SF4 . ? A SF4 1006 ? 1_555 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 109.5 ? 
126 SG  ? A CYS 726 ? A CYS 726  ? 1_555 FE2 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 118.1 ? 
127 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 FE2 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
128 SG  ? A CYS 726 ? A CYS 726  ? 1_555 FE2 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 115.3 ? 
129 S1  ? I SF4 .   ? A SF4 1006 ? 1_555 FE2 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 104.2 ? 
130 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 FE2 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 104.2 ? 
131 SG  ? A CYS 752 ? A CYS 752  ? 1_555 FE1 ? I SF4 . ? A SF4 1006 ? 1_555 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 97.7  ? 
132 SG  ? A CYS 752 ? A CYS 752  ? 1_555 FE1 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 115.8 ? 
133 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 FE1 ? I SF4 . ? A SF4 1006 ? 1_555 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 104.2 ? 
134 SG  ? A CYS 752 ? A CYS 752  ? 1_555 FE1 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 127.6 ? 
135 S2  ? I SF4 .   ? A SF4 1006 ? 1_555 FE1 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
136 S3  ? I SF4 .   ? A SF4 1006 ? 1_555 FE1 ? I SF4 . ? A SF4 1006 ? 1_555 S4  ? I SF4 .   ? A SF4 1006 ? 1_555 104.1 ? 
137 SG  ? B CYS 14  ? B CYS 14   ? 1_555 ZN  ? Q ZN  . ? B ZN  707  ? 1_555 SG  ? B CYS 45  ? B CYS 45   ? 1_555 90.9  ? 
138 SG  ? B CYS 14  ? B CYS 14   ? 1_555 ZN  ? Q ZN  . ? B ZN  707  ? 1_555 SG  ? B CYS 49  ? B CYS 49   ? 1_555 146.3 ? 
139 SG  ? B CYS 45  ? B CYS 45   ? 1_555 ZN  ? Q ZN  . ? B ZN  707  ? 1_555 SG  ? B CYS 49  ? B CYS 49   ? 1_555 105.1 ? 
140 SG  ? B CYS 437 ? B CYS 437  ? 1_555 ZN  ? P ZN  . ? B ZN  706  ? 1_555 NE2 ? B HIS 524 ? B HIS 524  ? 1_555 92.0  ? 
141 SG  ? B CYS 437 ? B CYS 437  ? 1_555 ZN  ? P ZN  . ? B ZN  706  ? 1_555 SG  ? B CYS 529 ? B CYS 529  ? 1_555 112.3 ? 
142 NE2 ? B HIS 524 ? B HIS 524  ? 1_555 ZN  ? P ZN  . ? B ZN  706  ? 1_555 SG  ? B CYS 529 ? B CYS 529  ? 1_555 115.2 ? 
143 SG  ? B CYS 437 ? B CYS 437  ? 1_555 ZN  ? P ZN  . ? B ZN  706  ? 1_555 SG  ? B CYS 534 ? B CYS 534  ? 1_555 112.9 ? 
144 NE2 ? B HIS 524 ? B HIS 524  ? 1_555 ZN  ? P ZN  . ? B ZN  706  ? 1_555 SG  ? B CYS 534 ? B CYS 534  ? 1_555 114.0 ? 
145 SG  ? B CYS 529 ? B CYS 529  ? 1_555 ZN  ? P ZN  . ? B ZN  706  ? 1_555 SG  ? B CYS 534 ? B CYS 534  ? 1_555 109.6 ? 
146 SG  ? B CYS 454 ? B CYS 454  ? 1_555 FE4 ? K SF4 . ? B SF4 701  ? 1_555 S1  ? K SF4 .   ? B SF4 701  ? 1_555 123.1 ? 
147 SG  ? B CYS 454 ? B CYS 454  ? 1_555 FE4 ? K SF4 . ? B SF4 701  ? 1_555 S2  ? K SF4 .   ? B SF4 701  ? 1_555 114.3 ? 
148 S1  ? K SF4 .   ? B SF4 701  ? 1_555 FE4 ? K SF4 . ? B SF4 701  ? 1_555 S2  ? K SF4 .   ? B SF4 701  ? 1_555 104.1 ? 
149 SG  ? B CYS 454 ? B CYS 454  ? 1_555 FE4 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 105.0 ? 
150 S1  ? K SF4 .   ? B SF4 701  ? 1_555 FE4 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 104.0 ? 
151 S2  ? K SF4 .   ? B SF4 701  ? 1_555 FE4 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 104.4 ? 
152 SG  ? B CYS 457 ? B CYS 457  ? 1_555 FE3 ? K SF4 . ? B SF4 701  ? 1_555 S1  ? K SF4 .   ? B SF4 701  ? 1_555 103.9 ? 
153 SG  ? B CYS 457 ? B CYS 457  ? 1_555 FE3 ? K SF4 . ? B SF4 701  ? 1_555 S2  ? K SF4 .   ? B SF4 701  ? 1_555 136.3 ? 
154 S1  ? K SF4 .   ? B SF4 701  ? 1_555 FE3 ? K SF4 . ? B SF4 701  ? 1_555 S2  ? K SF4 .   ? B SF4 701  ? 1_555 104.1 ? 
155 SG  ? B CYS 457 ? B CYS 457  ? 1_555 FE3 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 100.7 ? 
156 S1  ? K SF4 .   ? B SF4 701  ? 1_555 FE3 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 104.4 ? 
157 S2  ? K SF4 .   ? B SF4 701  ? 1_555 FE3 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 104.1 ? 
158 SG  ? B CYS 460 ? B CYS 460  ? 1_555 FE2 ? K SF4 . ? B SF4 701  ? 1_555 S1  ? K SF4 .   ? B SF4 701  ? 1_555 108.8 ? 
159 SG  ? B CYS 460 ? B CYS 460  ? 1_555 FE2 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 134.8 ? 
160 S1  ? K SF4 .   ? B SF4 701  ? 1_555 FE2 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 104.0 ? 
161 SG  ? B CYS 460 ? B CYS 460  ? 1_555 FE2 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 97.1  ? 
162 S1  ? K SF4 .   ? B SF4 701  ? 1_555 FE2 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 104.3 ? 
163 S3  ? K SF4 .   ? B SF4 701  ? 1_555 FE2 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 104.1 ? 
164 SG  ? B CYS 500 ? B CYS 500  ? 1_555 FE1 ? K SF4 . ? B SF4 701  ? 1_555 S2  ? K SF4 .   ? B SF4 701  ? 1_555 122.7 ? 
165 SG  ? B CYS 500 ? B CYS 500  ? 1_555 FE1 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 97.0  ? 
166 S2  ? K SF4 .   ? B SF4 701  ? 1_555 FE1 ? K SF4 . ? B SF4 701  ? 1_555 S3  ? K SF4 .   ? B SF4 701  ? 1_555 104.4 ? 
167 SG  ? B CYS 500 ? B CYS 500  ? 1_555 FE1 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 121.2 ? 
168 S2  ? K SF4 .   ? B SF4 701  ? 1_555 FE1 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 104.0 ? 
169 S3  ? K SF4 .   ? B SF4 701  ? 1_555 FE1 ? K SF4 . ? B SF4 701  ? 1_555 S4  ? K SF4 .   ? B SF4 701  ? 1_555 104.1 ? 
170 SG  ? B CYS 547 ? B CYS 547  ? 1_555 FE3 ? M SF4 . ? B SF4 703  ? 1_555 S1  ? M SF4 .   ? B SF4 703  ? 1_555 118.7 ? 
171 SG  ? B CYS 547 ? B CYS 547  ? 1_555 FE3 ? M SF4 . ? B SF4 703  ? 1_555 S2  ? M SF4 .   ? B SF4 703  ? 1_555 127.4 ? 
172 S1  ? M SF4 .   ? B SF4 703  ? 1_555 FE3 ? M SF4 . ? B SF4 703  ? 1_555 S2  ? M SF4 .   ? B SF4 703  ? 1_555 104.1 ? 
173 SG  ? B CYS 547 ? B CYS 547  ? 1_555 FE3 ? M SF4 . ? B SF4 703  ? 1_555 S4  ? M SF4 .   ? B SF4 703  ? 1_555 93.9  ? 
174 S1  ? M SF4 .   ? B SF4 703  ? 1_555 FE3 ? M SF4 . ? B SF4 703  ? 1_555 S4  ? M SF4 .   ? B SF4 703  ? 1_555 104.2 ? 
175 S2  ? M SF4 .   ? B SF4 703  ? 1_555 FE3 ? M SF4 . ? B SF4 703  ? 1_555 S4  ? M SF4 .   ? B SF4 703  ? 1_555 104.1 ? 
176 SG  ? B CYS 550 ? B CYS 550  ? 1_555 FE4 ? M SF4 . ? B SF4 703  ? 1_555 S1  ? M SF4 .   ? B SF4 703  ? 1_555 109.1 ? 
177 SG  ? B CYS 550 ? B CYS 550  ? 1_555 FE4 ? M SF4 . ? B SF4 703  ? 1_555 S2  ? M SF4 .   ? B SF4 703  ? 1_555 124.0 ? 
178 S1  ? M SF4 .   ? B SF4 703  ? 1_555 FE4 ? M SF4 . ? B SF4 703  ? 1_555 S2  ? M SF4 .   ? B SF4 703  ? 1_555 104.2 ? 
179 SG  ? B CYS 550 ? B CYS 550  ? 1_555 FE4 ? M SF4 . ? B SF4 703  ? 1_555 S3  ? M SF4 .   ? B SF4 703  ? 1_555 109.5 ? 
180 S1  ? M SF4 .   ? B SF4 703  ? 1_555 FE4 ? M SF4 . ? B SF4 703  ? 1_555 S3  ? M SF4 .   ? B SF4 703  ? 1_555 104.1 ? 
181 S2  ? M SF4 .   ? B SF4 703  ? 1_555 FE4 ? M SF4 . ? B SF4 703  ? 1_555 S3  ? M SF4 .   ? B SF4 703  ? 1_555 104.2 ? 
182 SG  ? B CYS 553 ? B CYS 553  ? 1_555 FE1 ? M SF4 . ? B SF4 703  ? 1_555 S2  ? M SF4 .   ? B SF4 703  ? 1_555 125.3 ? 
183 SG  ? B CYS 553 ? B CYS 553  ? 1_555 FE1 ? M SF4 . ? B SF4 703  ? 1_555 S3  ? M SF4 .   ? B SF4 703  ? 1_555 109.1 ? 
184 S2  ? M SF4 .   ? B SF4 703  ? 1_555 FE1 ? M SF4 . ? B SF4 703  ? 1_555 S3  ? M SF4 .   ? B SF4 703  ? 1_555 104.2 ? 
185 SG  ? B CYS 553 ? B CYS 553  ? 1_555 FE1 ? M SF4 . ? B SF4 703  ? 1_555 S4  ? M SF4 .   ? B SF4 703  ? 1_555 108.1 ? 
186 S2  ? M SF4 .   ? B SF4 703  ? 1_555 FE1 ? M SF4 . ? B SF4 703  ? 1_555 S4  ? M SF4 .   ? B SF4 703  ? 1_555 104.0 ? 
187 S3  ? M SF4 .   ? B SF4 703  ? 1_555 FE1 ? M SF4 . ? B SF4 703  ? 1_555 S4  ? M SF4 .   ? B SF4 703  ? 1_555 104.2 ? 
188 SG  ? B CYS 557 ? B CYS 557  ? 1_555 FE4 ? N SF4 . ? B SF4 704  ? 1_555 S1  ? N SF4 .   ? B SF4 704  ? 1_555 131.3 ? 
189 SG  ? B CYS 557 ? B CYS 557  ? 1_555 FE4 ? N SF4 . ? B SF4 704  ? 1_555 S2  ? N SF4 .   ? B SF4 704  ? 1_555 97.3  ? 
190 S1  ? N SF4 .   ? B SF4 704  ? 1_555 FE4 ? N SF4 . ? B SF4 704  ? 1_555 S2  ? N SF4 .   ? B SF4 704  ? 1_555 104.1 ? 
191 SG  ? B CYS 557 ? B CYS 557  ? 1_555 FE4 ? N SF4 . ? B SF4 704  ? 1_555 S3  ? N SF4 .   ? B SF4 704  ? 1_555 112.2 ? 
192 S1  ? N SF4 .   ? B SF4 704  ? 1_555 FE4 ? N SF4 . ? B SF4 704  ? 1_555 S3  ? N SF4 .   ? B SF4 704  ? 1_555 104.2 ? 
193 S2  ? N SF4 .   ? B SF4 704  ? 1_555 FE4 ? N SF4 . ? B SF4 704  ? 1_555 S3  ? N SF4 .   ? B SF4 704  ? 1_555 104.3 ? 
194 SG  ? B CYS 577 ? B CYS 577  ? 1_555 FE3 ? N SF4 . ? B SF4 704  ? 1_555 S1  ? N SF4 .   ? B SF4 704  ? 1_555 114.1 ? 
195 SG  ? B CYS 577 ? B CYS 577  ? 1_555 FE3 ? N SF4 . ? B SF4 704  ? 1_555 S2  ? N SF4 .   ? B SF4 704  ? 1_555 109.0 ? 
196 S1  ? N SF4 .   ? B SF4 704  ? 1_555 FE3 ? N SF4 . ? B SF4 704  ? 1_555 S2  ? N SF4 .   ? B SF4 704  ? 1_555 104.1 ? 
197 SG  ? B CYS 577 ? B CYS 577  ? 1_555 FE3 ? N SF4 . ? B SF4 704  ? 1_555 S4  ? N SF4 .   ? B SF4 704  ? 1_555 119.8 ? 
198 S1  ? N SF4 .   ? B SF4 704  ? 1_555 FE3 ? N SF4 . ? B SF4 704  ? 1_555 S4  ? N SF4 .   ? B SF4 704  ? 1_555 104.1 ? 
199 S2  ? N SF4 .   ? B SF4 704  ? 1_555 FE3 ? N SF4 . ? B SF4 704  ? 1_555 S4  ? N SF4 .   ? B SF4 704  ? 1_555 104.1 ? 
200 SG  ? B CYS 580 ? B CYS 580  ? 1_555 FE1 ? N SF4 . ? B SF4 704  ? 1_555 S2  ? N SF4 .   ? B SF4 704  ? 1_555 97.2  ? 
201 SG  ? B CYS 580 ? B CYS 580  ? 1_555 FE1 ? N SF4 . ? B SF4 704  ? 1_555 S3  ? N SF4 .   ? B SF4 704  ? 1_555 96.1  ? 
202 S2  ? N SF4 .   ? B SF4 704  ? 1_555 FE1 ? N SF4 . ? B SF4 704  ? 1_555 S3  ? N SF4 .   ? B SF4 704  ? 1_555 104.4 ? 
203 SG  ? B CYS 580 ? B CYS 580  ? 1_555 FE1 ? N SF4 . ? B SF4 704  ? 1_555 S4  ? N SF4 .   ? B SF4 704  ? 1_555 145.9 ? 
204 S2  ? N SF4 .   ? B SF4 704  ? 1_555 FE1 ? N SF4 . ? B SF4 704  ? 1_555 S4  ? N SF4 .   ? B SF4 704  ? 1_555 104.0 ? 
205 S3  ? N SF4 .   ? B SF4 704  ? 1_555 FE1 ? N SF4 . ? B SF4 704  ? 1_555 S4  ? N SF4 .   ? B SF4 704  ? 1_555 103.9 ? 
# 
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 GLY 871 A . ? GLY 871 A PRO 872 A ? PRO 872 A 1 -1.72 
2 GLU 52  B . ? GLU 52  B PRO 53  B ? PRO 53  B 1 0.67  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
AA5 ? 3 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 6 ? 
AB6 ? 4 ? 
AB7 ? 5 ? 
AB8 ? 2 ? 
AB9 ? 2 ? 
# 
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 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB2 5 6 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? parallel      
AB7 3 4 ? anti-parallel 
AB7 4 5 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? 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 LYS A 17  ? GLU A 20  ? LYS A 17  GLU A 20  
AA1 2 LYS A 11  ? VAL A 14  ? LYS A 11  VAL A 14  
AA1 3 SER A 76  ? ILE A 77  ? SER A 76  ILE A 77  
AA2 1 LEU A 56  ? THR A 59  ? LEU A 56  THR A 59  
AA2 2 GLY A 62  ? THR A 65  ? GLY A 62  THR A 65  
AA3 1 GLU A 261 ? THR A 264 ? GLU A 261 THR A 264 
AA3 2 ASP A 220 ? ASP A 225 ? ASP A 220 ASP A 225 
AA3 3 ARG A 197 ? VAL A 201 ? ARG A 197 VAL A 201 
AA3 4 ALA A 283 ? LEU A 286 ? ALA A 283 LEU A 286 
AA3 5 VAL A 469 ? ALA A 471 ? VAL A 469 ALA A 471 
AA4 1 VAL A 306 ? HIS A 308 ? VAL A 306 HIS A 308 
AA4 2 ASN A 429 ? LEU A 432 ? ASN A 429 LEU A 432 
AA4 3 ARG A 327 ? VAL A 331 ? ARG A 327 VAL A 331 
AA4 4 ASP A 350 ? TYR A 355 ? ASP A 350 TYR A 355 
AA4 5 LYS A 378 ? PHE A 381 ? LYS A 378 PHE A 381 
AA5 1 THR A 383 ? ILE A 389 ? THR A 383 ILE A 389 
AA5 2 GLU A 396 ? LYS A 403 ? GLU A 396 LYS A 403 
AA5 3 MET A 416 ? PRO A 417 ? MET A 416 PRO A 417 
AA6 1 THR A 383 ? ILE A 389 ? THR A 383 ILE A 389 
AA6 2 GLU A 396 ? LYS A 403 ? GLU A 396 LYS A 403 
AA6 3 PHE A 423 ? LYS A 426 ? PHE A 423 LYS A 426 
AA7 1 ALA A 450 ? LYS A 451 ? ALA A 450 LYS A 451 
AA7 2 ARG A 454 ? VAL A 455 ? ARG A 454 VAL A 455 
AA8 1 VAL A 633 ? LEU A 635 ? VAL A 633 LEU A 635 
AA8 2 ILE A 698 ? GLU A 700 ? ILE A 698 GLU A 700 
AA9 1 ASP A 660 ? LEU A 662 ? ASP A 660 LEU A 662 
AA9 2 TYR A 669 ? GLY A 671 ? TYR A 669 GLY A 671 
AB1 1 GLN A 713 ? VAL A 718 ? GLN A 713 VAL A 718 
AB1 2 GLU A 727 ? TYR A 733 ? GLU A 727 TYR A 733 
AB1 3 ILE A 736 ? SER A 741 ? ILE A 736 SER A 741 
AB2 1 ASN A 773 ? ALA A 774 ? ASN A 773 ALA A 774 
AB2 2 ILE A 769 ? LEU A 770 ? ILE A 769 LEU A 770 
AB2 3 TYR A 922 ? LEU A 925 ? TYR A 922 LEU A 925 
AB2 4 TYR A 906 ? ILE A 909 ? TYR A 906 ILE A 909 
AB2 5 ALA A 790 ? LEU A 793 ? ALA A 790 LEU A 793 
AB2 6 ILE A 816 ? SER A 818 ? ILE A 816 SER A 818 
AB3 1 GLU A 858 ? ILE A 859 ? GLU A 858 ILE A 859 
AB3 2 ARG A 837 ? LEU A 840 ? ARG A 837 LEU A 840 
AB3 3 VAL A 866 ? GLU A 870 ? VAL A 866 GLU A 870 
AB3 4 THR A 880 ? LEU A 883 ? THR A 880 LEU A 883 
AB4 1 GLY A 935 ? THR A 938 ? GLY A 935 THR A 938 
AB4 2 ASP A 944 ? VAL A 947 ? ASP A 944 VAL A 947 
AB5 1 LYS B 39  ? VAL B 43  ? LYS B 39  VAL B 43  
AB5 2 ALA B 6   ? GLY B 10  ? ALA B 6   GLY B 10  
AB5 3 LEU B 54  ? ILE B 58  ? LEU B 54  ILE B 58  
AB5 4 GLU B 62  ? GLY B 67  ? GLU B 62  GLY B 67  
AB5 5 VAL B 92  ? GLU B 99  ? VAL B 92  GLU B 99  
AB5 6 GLN B 102 ? ASP B 107 ? GLN B 102 ASP B 107 
AB6 1 GLU B 271 ? GLY B 277 ? GLU B 271 GLY B 277 
AB6 2 LYS B 230 ? ARG B 236 ? LYS B 230 ARG B 236 
AB6 3 TYR B 189 ? ALA B 194 ? TYR B 189 ALA B 194 
AB6 4 THR B 317 ? ASN B 321 ? THR B 317 ASN B 321 
AB7 1 GLY B 363 ? PRO B 368 ? GLY B 363 PRO B 368 
AB7 2 THR B 350 ? GLY B 357 ? THR B 350 GLY B 357 
AB7 3 GLY B 428 ? ASP B 433 ? GLY B 428 ASP B 433 
AB7 4 ILE B 390 ? LEU B 395 ? ILE B 390 LEU B 395 
AB7 5 GLY B 401 ? PRO B 404 ? GLY B 401 PRO B 404 
AB8 1 ILE B 371 ? THR B 372 ? ILE B 371 THR B 372 
AB8 2 PRO B 411 ? VAL B 412 ? PRO B 411 VAL B 412 
AB9 1 VAL B 541 ? ILE B 542 ? VAL B 541 ILE B 542 
AB9 2 ILE B 592 ? GLU B 593 ? ILE B 592 GLU B 593 
# 
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 O PHE A 19  ? O PHE A 19  N ILE A 12  ? N ILE A 12  
AA1 2 3 N THR A 13  ? N THR A 13  O ILE A 77  ? O ILE A 77  
AA2 1 2 N THR A 59  ? N THR A 59  O GLY A 62  ? O GLY A 62  
AA3 1 2 O LYS A 263 ? O LYS A 263 N ILE A 223 ? N ILE A 223 
AA3 2 3 O PHE A 224 ? O PHE A 224 N VAL A 200 ? N VAL A 200 
AA3 3 4 N VAL A 201 ? N VAL A 201 O PHE A 285 ? O PHE A 285 
AA3 4 5 N LEU A 286 ? N LEU A 286 O PHE A 470 ? O PHE A 470 
AA4 1 2 N ILE A 307 ? N ILE A 307 O VAL A 430 ? O VAL A 430 
AA4 2 3 O ILE A 431 ? O ILE A 431 N VAL A 331 ? N VAL A 331 
AA4 3 4 N VAL A 330 ? N VAL A 330 O VAL A 354 ? O VAL A 354 
AA4 4 5 N VAL A 353 ? N VAL A 353 O MET A 380 ? O MET A 380 
AA5 1 2 N VAL A 386 ? N VAL A 386 O GLU A 398 ? O GLU A 398 
AA5 2 3 N LYS A 403 ? N LYS A 403 O MET A 416 ? O MET A 416 
AA6 1 2 N VAL A 386 ? N VAL A 386 O GLU A 398 ? O GLU A 398 
AA6 2 3 N LEU A 399 ? N LEU A 399 O PHE A 423 ? O PHE A 423 
AA7 1 2 N LYS A 451 ? N LYS A 451 O ARG A 454 ? O ARG A 454 
AA8 1 2 N VAL A 634 ? N VAL A 634 O THR A 699 ? O THR A 699 
AA9 1 2 N LEU A 662 ? N LEU A 662 O TYR A 669 ? O TYR A 669 
AB1 1 2 N THR A 717 ? N THR A 717 O MET A 728 ? O MET A 728 
AB1 2 3 N ASN A 729 ? N ASN A 729 O SER A 741 ? O SER A 741 
AB2 1 2 O ASN A 773 ? O ASN A 773 N LEU A 770 ? N LEU A 770 
AB2 2 3 N ILE A 769 ? N ILE A 769 O ILE A 924 ? O ILE A 924 
AB2 3 4 O LEU A 923 ? O LEU A 923 N TYR A 906 ? N TYR A 906 
AB2 4 5 O VAL A 907 ? O VAL A 907 N ILE A 792 ? N ILE A 792 
AB2 5 6 N LEU A 791 ? N LEU A 791 O GLY A 817 ? O GLY A 817 
AB3 1 2 O GLU A 858 ? O GLU A 858 N VAL A 838 ? N VAL A 838 
AB3 2 3 N LEU A 839 ? N LEU A 839 O ILE A 868 ? O ILE A 868 
AB3 3 4 N ILE A 869 ? N ILE A 869 O LEU A 881 ? O LEU A 881 
AB4 1 2 N GLY A 935 ? N GLY A 935 O VAL A 947 ? O VAL A 947 
AB5 1 2 O LYS B 39  ? O LYS B 39  N ILE B 7   ? N ILE B 7   
AB5 2 3 N ALA B 8   ? N ALA B 8   O ASP B 56  ? O ASP B 56  
AB5 3 4 N LEU B 55  ? N LEU B 55  O TYR B 66  ? O TYR B 66  
AB5 4 5 N ILE B 63  ? N ILE B 63  O ASP B 96  ? O ASP B 96  
AB5 5 6 N TRP B 97  ? N TRP B 97  O LYS B 104 ? O LYS B 104 
AB6 1 2 O VAL B 273 ? O VAL B 273 N GLY B 231 ? N GLY B 231 
AB6 2 3 O PHE B 232 ? O PHE B 232 N CYS B 192 ? N CYS B 192 
AB6 3 4 N VAL B 191 ? N VAL B 191 O ASN B 318 ? O ASN B 318 
AB7 1 2 O GLY B 363 ? O GLY B 363 N LEU B 355 ? N LEU B 355 
AB7 2 3 N ALA B 354 ? N ALA B 354 O MET B 429 ? O MET B 429 
AB7 3 4 O MET B 432 ? O MET B 432 N ALA B 392 ? N ALA B 392 
AB7 4 5 N VAL B 393 ? N VAL B 393 O ILE B 403 ? O ILE B 403 
AB8 1 2 N ILE B 371 ? N ILE B 371 O VAL B 412 ? O VAL B 412 
AB9 1 2 N VAL B 541 ? N VAL B 541 O GLU B 593 ? O GLU B 593 
# 
_pdbx_entry_details.entry_id                   9N5V 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 CE1 A HIS 99  ? ? FE4 A SF4 1004 ? ? 1.31 
2 1 CB  B CYS 553 ? ? FE1 B SF4 703  ? ? 2.06 
# 
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 CYS A 55  ? ? -91.59  30.89   
2  1 ALA A 152 ? ? 60.34   64.13   
3  1 VAL A 163 ? ? -111.61 -72.75  
4  1 GLU A 164 ? ? -127.40 -56.57  
5  1 ASN A 183 ? ? -99.32  35.49   
6  1 SER A 569 ? ? -140.23 16.99   
7  1 PHE A 571 ? ? -93.35  52.83   
8  1 PHE A 663 ? ? 62.43   175.91  
9  1 LYS A 682 ? ? -98.81  34.04   
10 1 ASP A 764 ? ? -161.93 -168.27 
11 1 SER A 796 ? ? -97.07  33.78   
12 1 THR A 898 ? ? 58.39   -169.71 
13 1 ALA A 905 ? ? 66.83   149.59  
14 1 GLU B 196 ? ? -69.98  94.35   
15 1 LYS B 358 ? ? -95.24  31.87   
16 1 ASP B 433 ? ? -117.46 -169.69 
17 1 LYS B 456 ? ? -93.25  -61.61  
18 1 THR B 551 ? ? 67.01   -2.60   
19 1 THR B 582 ? ? -89.34  45.89   
20 1 CYS B 583 ? ? -132.17 -37.70  
21 1 PHE B 589 ? ? 59.41   -139.78 
22 1 ILE B 594 ? ? -94.85  -64.85  
23 1 THR B 595 ? ? 59.31   170.67  
24 1 TYR C 31  ? ? -163.59 -167.25 
25 1 PRO C 65  ? ? -57.32  -8.71   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9N5V 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      'AB INITIO MODEL' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_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                   AlphaFold 
_em_3d_fitting_list.type                          'in silico model' 
_em_3d_fitting_list.accession_code                ? 
_em_3d_fitting_list.initial_refinement_model_id   ? 
# 
_em_3d_reconstruction.entry_id                    9N5V 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.76 
_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               458032 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Ternary complex of the NAD(H)-bound Tsi NfnABC complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
# 
_em_image_scans.entry_id                9N5V 
_em_image_scans.id                      1 
_em_image_scans.number_digital_images   ? 
_em_image_scans.details                 ? 
_em_image_scans.scanner_model           ? 
_em_image_scans.sampling_size           ? 
_em_image_scans.od_range                ? 
_em_image_scans.quant_bit_size          ? 
_em_image_scans.citation_id             ? 
_em_image_scans.dimension_height        ? 
_em_image_scans.dimension_width         ? 
_em_image_scans.frames_per_image        30 
_em_image_scans.image_recording_id      1 
_em_image_scans.used_frames_per_image   ? 
# 
_em_imaging.entry_id                        9N5V 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_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            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1300 
_em_imaging.nominal_defocus_max             1800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_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            100 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_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              9N5V 
_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   283.15 
_em_vitrification.instrument            'FEI VITROBOT MARK II' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9N5V 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A PRO 2   ? A PRO 2   
3   1 Y 1 A ARG 3   ? A ARG 3   
4   1 Y 1 A ARG 4   ? A ARG 4   
5   1 Y 1 A ARG 5   ? A ARG 5   
6   1 Y 1 A VAL 6   ? A VAL 6   
7   1 Y 1 A SER 7   ? A SER 7   
8   1 Y 1 A GLU 8   ? A GLU 8   
9   1 Y 1 A MET 9   ? A MET 9   
10  1 Y 1 A ASP 408 ? A ASP 408 
11  1 Y 1 A ALA 409 ? A ALA 409 
12  1 Y 1 A SER 410 ? A SER 410 
13  1 Y 1 A GLY 411 ? A GLY 411 
14  1 Y 1 A PHE 961 ? A PHE 961 
15  1 Y 1 A ASN 962 ? A ASN 962 
16  1 Y 1 A PHE 963 ? A PHE 963 
17  1 Y 1 B MET 1   ? B MET 1   
18  1 Y 1 B LYS 560 ? B LYS 560 
19  1 Y 1 B ALA 561 ? B ALA 561 
20  1 Y 1 B ILE 562 ? B ILE 562 
21  1 Y 1 B SER 563 ? B SER 563 
22  1 Y 1 B GLY 564 ? B GLY 564 
23  1 Y 1 B GLU 565 ? B GLU 565 
24  1 Y 1 B LYS 598 ? B LYS 598 
25  1 Y 1 B LYS 599 ? B LYS 599 
26  1 Y 1 B GLU 600 ? B GLU 600 
27  1 Y 1 B GLY 601 ? B GLY 601 
28  1 Y 1 B GLU 602 ? B GLU 602 
29  1 Y 1 C MET 1   ? C MET 1   
30  1 Y 1 C ASN 2   ? C ASN 2   
31  1 Y 1 C GLY 67  ? C GLY 67  
32  1 Y 1 C LYS 68  ? C LYS 68  
33  1 Y 1 C TYR 69  ? C TYR 69  
34  1 Y 1 C VAL 70  ? C VAL 70  
35  1 Y 1 C ILE 71  ? C ILE 71  
36  1 Y 1 C LYS 72  ? C LYS 72  
37  1 Y 1 C ILE 73  ? C ILE 73  
38  1 Y 1 C CYS 74  ? C CYS 74  
39  1 Y 1 C HIS 75  ? C HIS 75  
40  1 Y 1 C GLY 76  ? C GLY 76  
41  1 Y 1 C THR 77  ? C THR 77  
42  1 Y 1 C ALA 78  ? C ALA 78  
43  1 Y 1 C CYS 79  ? C CYS 79  
44  1 Y 1 C HIS 80  ? C HIS 80  
45  1 Y 1 C VAL 81  ? C VAL 81  
46  1 Y 1 C ASN 82  ? C ASN 82  
47  1 Y 1 C GLY 83  ? C GLY 83  
48  1 Y 1 C ALA 84  ? C ALA 84  
49  1 Y 1 C VAL 85  ? C VAL 85  
50  1 Y 1 C ASN 86  ? C ASN 86  
51  1 Y 1 C ILE 87  ? C ILE 87  
52  1 Y 1 C SER 88  ? C SER 88  
53  1 Y 1 C GLN 89  ? C GLN 89  
54  1 Y 1 C ALA 90  ? C ALA 90  
55  1 Y 1 C ILE 91  ? C ILE 91  
56  1 Y 1 C ARG 92  ? C ARG 92  
57  1 Y 1 C GLU 93  ? C GLU 93  
58  1 Y 1 C GLU 94  ? C GLU 94  
59  1 Y 1 C VAL 95  ? C VAL 95  
60  1 Y 1 C GLY 96  ? C GLY 96  
61  1 Y 1 C ILE 97  ? C ILE 97  
62  1 Y 1 C GLU 98  ? C GLU 98  
63  1 Y 1 C GLU 99  ? C GLU 99  
64  1 Y 1 C GLY 100 ? C GLY 100 
65  1 Y 1 C GLN 101 ? C GLN 101 
66  1 Y 1 C THR 102 ? C THR 102 
67  1 Y 1 C THR 103 ? C THR 103 
68  1 Y 1 C VAL 104 ? C VAL 104 
69  1 Y 1 C ASP 105 ? C ASP 105 
70  1 Y 1 C GLY 106 ? C GLY 106 
71  1 Y 1 C LEU 107 ? C LEU 107 
72  1 Y 1 C ILE 108 ? C ILE 108 
73  1 Y 1 C THR 109 ? C THR 109 
74  1 Y 1 C LEU 110 ? C LEU 110 
75  1 Y 1 C GLU 111 ? C GLU 111 
76  1 Y 1 C ARG 112 ? C ARG 112 
77  1 Y 1 C VAL 113 ? C VAL 113 
78  1 Y 1 C ALA 114 ? C ALA 114 
79  1 Y 1 C CYS 115 ? C CYS 115 
80  1 Y 1 C LEU 116 ? C LEU 116 
81  1 Y 1 C GLY 117 ? C GLY 117 
82  1 Y 1 C CYS 118 ? C CYS 118 
83  1 Y 1 C CYS 119 ? C CYS 119 
84  1 Y 1 C SER 120 ? C SER 120 
85  1 Y 1 C LEU 121 ? C LEU 121 
86  1 Y 1 C ALA 122 ? C ALA 122 
87  1 Y 1 C PRO 123 ? C PRO 123 
88  1 Y 1 C VAL 124 ? C VAL 124 
89  1 Y 1 C ILE 125 ? C ILE 125 
90  1 Y 1 C MET 126 ? C MET 126 
91  1 Y 1 C ILE 127 ? C ILE 127 
92  1 Y 1 C ASN 128 ? C ASN 128 
93  1 Y 1 C GLU 129 ? C GLU 129 
94  1 Y 1 C LYS 130 ? C LYS 130 
95  1 Y 1 C VAL 131 ? C VAL 131 
96  1 Y 1 C TYR 132 ? C TYR 132 
97  1 Y 1 C GLY 133 ? C GLY 133 
98  1 Y 1 C LYS 134 ? C LYS 134 
99  1 Y 1 C LEU 135 ? C LEU 135 
100 1 Y 1 C THR 136 ? C THR 136 
101 1 Y 1 C PRO 137 ? C PRO 137 
102 1 Y 1 C ASP 138 ? C ASP 138 
103 1 Y 1 C LYS 139 ? C LYS 139 
104 1 Y 1 C VAL 140 ? C VAL 140 
105 1 Y 1 C ARG 141 ? C ARG 141 
106 1 Y 1 C LYS 142 ? C LYS 142 
107 1 Y 1 C ILE 143 ? C ILE 143 
108 1 Y 1 C ILE 144 ? C ILE 144 
109 1 Y 1 C ARG 145 ? C ARG 145 
110 1 Y 1 C ASN 146 ? C ASN 146 
111 1 Y 1 C LEU 147 ? C LEU 147 
112 1 Y 1 C LYS 148 ? C LYS 148 
113 1 Y 1 C GLU 149 ? C GLU 149 
114 1 Y 1 C GLY 150 ? C GLY 150 
115 1 Y 1 C LYS 151 ? C LYS 151 
116 1 Y 1 C LEU 152 ? C LEU 152 
117 1 Y 1 C ASN 153 ? C ASN 153 
118 1 Y 1 C VAL 154 ? C VAL 154 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
FAD PA     P  N R 88  
FAD O1A    O  N N 89  
FAD O2A    O  N N 90  
FAD O5B    O  N N 91  
FAD C5B    C  N N 92  
FAD C4B    C  N R 93  
FAD O4B    O  N N 94  
FAD C3B    C  N S 95  
FAD O3B    O  N N 96  
FAD C2B    C  N R 97  
FAD O2B    O  N N 98  
FAD C1B    C  N R 99  
FAD N9A    N  Y N 100 
FAD C8A    C  Y N 101 
FAD N7A    N  Y N 102 
FAD C5A    C  Y N 103 
FAD C6A    C  Y N 104 
FAD N6A    N  N N 105 
FAD N1A    N  Y N 106 
FAD C2A    C  Y N 107 
FAD N3A    N  Y N 108 
FAD C4A    C  Y N 109 
FAD N1     N  N N 110 
FAD C2     C  N N 111 
FAD O2     O  N N 112 
FAD N3     N  N N 113 
FAD C4     C  N N 114 
FAD O4     O  N N 115 
FAD C4X    C  N N 116 
FAD N5     N  N N 117 
FAD C5X    C  Y N 118 
FAD C6     C  Y N 119 
FAD C7     C  Y N 120 
FAD C7M    C  N N 121 
FAD C8     C  Y N 122 
FAD C8M    C  N N 123 
FAD C9     C  Y N 124 
FAD C9A    C  Y N 125 
FAD N10    N  N N 126 
FAD C10    C  N N 127 
FAD "C1'"  C  N N 128 
FAD "C2'"  C  N S 129 
FAD "O2'"  O  N N 130 
FAD "C3'"  C  N S 131 
FAD "O3'"  O  N N 132 
FAD "C4'"  C  N R 133 
FAD "O4'"  O  N N 134 
FAD "C5'"  C  N N 135 
FAD "O5'"  O  N N 136 
FAD P      P  N R 137 
FAD O1P    O  N N 138 
FAD O2P    O  N N 139 
FAD O3P    O  N N 140 
FAD HOA2   H  N N 141 
FAD H51A   H  N N 142 
FAD H52A   H  N N 143 
FAD H4B    H  N N 144 
FAD H3B    H  N N 145 
FAD HO3A   H  N N 146 
FAD H2B    H  N N 147 
FAD HO2A   H  N N 148 
FAD H1B    H  N N 149 
FAD H8A    H  N N 150 
FAD H61A   H  N N 151 
FAD H62A   H  N N 152 
FAD H2A    H  N N 153 
FAD HN3    H  N N 154 
FAD H6     H  N N 155 
FAD HM71   H  N N 156 
FAD HM72   H  N N 157 
FAD HM73   H  N N 158 
FAD HM81   H  N N 159 
FAD HM82   H  N N 160 
FAD HM83   H  N N 161 
FAD H9     H  N N 162 
FAD "H1'1" H  N N 163 
FAD "H1'2" H  N N 164 
FAD "H2'"  H  N N 165 
FAD "HO2'" H  N N 166 
FAD "H3'"  H  N N 167 
FAD "HO3'" H  N N 168 
FAD "H4'"  H  N N 169 
FAD "HO4'" H  N N 170 
FAD "H5'1" H  N N 171 
FAD "H5'2" H  N N 172 
FAD HOP2   H  N N 173 
FES FE1    FE N N 174 
FES FE2    FE N N 175 
FES S1     S  N N 176 
FES S2     S  N N 177 
FMN N1     N  N N 178 
FMN C2     C  N N 179 
FMN O2     O  N N 180 
FMN N3     N  N N 181 
FMN C4     C  N N 182 
FMN O4     O  N N 183 
FMN C4A    C  N N 184 
FMN N5     N  N N 185 
FMN C5A    C  Y N 186 
FMN C6     C  Y N 187 
FMN C7     C  Y N 188 
FMN C7M    C  N N 189 
FMN C8     C  Y N 190 
FMN C8M    C  N N 191 
FMN C9     C  Y N 192 
FMN C9A    C  Y N 193 
FMN N10    N  N N 194 
FMN C10    C  N N 195 
FMN "C1'"  C  N N 196 
FMN "C2'"  C  N S 197 
FMN "O2'"  O  N N 198 
FMN "C3'"  C  N S 199 
FMN "O3'"  O  N N 200 
FMN "C4'"  C  N R 201 
FMN "O4'"  O  N N 202 
FMN "C5'"  C  N N 203 
FMN "O5'"  O  N N 204 
FMN P      P  N N 205 
FMN O1P    O  N N 206 
FMN O2P    O  N N 207 
FMN O3P    O  N N 208 
FMN HN3    H  N N 209 
FMN H6     H  N N 210 
FMN HM71   H  N N 211 
FMN HM72   H  N N 212 
FMN HM73   H  N N 213 
FMN HM81   H  N N 214 
FMN HM82   H  N N 215 
FMN HM83   H  N N 216 
FMN H9     H  N N 217 
FMN "H1'1" H  N N 218 
FMN "H1'2" H  N N 219 
FMN "H2'"  H  N N 220 
FMN "HO2'" H  N N 221 
FMN "H3'"  H  N N 222 
FMN "HO3'" H  N N 223 
FMN "H4'"  H  N N 224 
FMN "HO4'" H  N N 225 
FMN "H5'1" H  N N 226 
FMN "H5'2" H  N N 227 
FMN HOP2   H  N N 228 
FMN HOP3   H  N N 229 
GLN N      N  N N 230 
GLN CA     C  N S 231 
GLN C      C  N N 232 
GLN O      O  N N 233 
GLN CB     C  N N 234 
GLN CG     C  N N 235 
GLN CD     C  N N 236 
GLN OE1    O  N N 237 
GLN NE2    N  N N 238 
GLN OXT    O  N N 239 
GLN H      H  N N 240 
GLN H2     H  N N 241 
GLN HA     H  N N 242 
GLN HB2    H  N N 243 
GLN HB3    H  N N 244 
GLN HG2    H  N N 245 
GLN HG3    H  N N 246 
GLN HE21   H  N N 247 
GLN HE22   H  N N 248 
GLN HXT    H  N N 249 
GLU N      N  N N 250 
GLU CA     C  N S 251 
GLU C      C  N N 252 
GLU O      O  N N 253 
GLU CB     C  N N 254 
GLU CG     C  N N 255 
GLU CD     C  N N 256 
GLU OE1    O  N N 257 
GLU OE2    O  N N 258 
GLU OXT    O  N N 259 
GLU H      H  N N 260 
GLU H2     H  N N 261 
GLU HA     H  N N 262 
GLU HB2    H  N N 263 
GLU HB3    H  N N 264 
GLU HG2    H  N N 265 
GLU HG3    H  N N 266 
GLU HE2    H  N N 267 
GLU HXT    H  N N 268 
GLY N      N  N N 269 
GLY CA     C  N N 270 
GLY C      C  N N 271 
GLY O      O  N N 272 
GLY OXT    O  N N 273 
GLY H      H  N N 274 
GLY H2     H  N N 275 
GLY HA2    H  N N 276 
GLY HA3    H  N N 277 
GLY HXT    H  N N 278 
HIS N      N  N N 279 
HIS CA     C  N S 280 
HIS C      C  N N 281 
HIS O      O  N N 282 
HIS CB     C  N N 283 
HIS CG     C  Y N 284 
HIS ND1    N  Y N 285 
HIS CD2    C  Y N 286 
HIS CE1    C  Y N 287 
HIS NE2    N  Y N 288 
HIS OXT    O  N N 289 
HIS H      H  N N 290 
HIS H2     H  N N 291 
HIS HA     H  N N 292 
HIS HB2    H  N N 293 
HIS HB3    H  N N 294 
HIS HD1    H  N N 295 
HIS HD2    H  N N 296 
HIS HE1    H  N N 297 
HIS HE2    H  N N 298 
HIS HXT    H  N N 299 
ILE N      N  N N 300 
ILE CA     C  N S 301 
ILE C      C  N N 302 
ILE O      O  N N 303 
ILE CB     C  N S 304 
ILE CG1    C  N N 305 
ILE CG2    C  N N 306 
ILE CD1    C  N N 307 
ILE OXT    O  N N 308 
ILE H      H  N N 309 
ILE H2     H  N N 310 
ILE HA     H  N N 311 
ILE HB     H  N N 312 
ILE HG12   H  N N 313 
ILE HG13   H  N N 314 
ILE HG21   H  N N 315 
ILE HG22   H  N N 316 
ILE HG23   H  N N 317 
ILE HD11   H  N N 318 
ILE HD12   H  N N 319 
ILE HD13   H  N N 320 
ILE HXT    H  N N 321 
LEU N      N  N N 322 
LEU CA     C  N S 323 
LEU C      C  N N 324 
LEU O      O  N N 325 
LEU CB     C  N N 326 
LEU CG     C  N N 327 
LEU CD1    C  N N 328 
LEU CD2    C  N N 329 
LEU OXT    O  N N 330 
LEU H      H  N N 331 
LEU H2     H  N N 332 
LEU HA     H  N N 333 
LEU HB2    H  N N 334 
LEU HB3    H  N N 335 
LEU HG     H  N N 336 
LEU HD11   H  N N 337 
LEU HD12   H  N N 338 
LEU HD13   H  N N 339 
LEU HD21   H  N N 340 
LEU HD22   H  N N 341 
LEU HD23   H  N N 342 
LEU HXT    H  N N 343 
LYS N      N  N N 344 
LYS CA     C  N S 345 
LYS C      C  N N 346 
LYS O      O  N N 347 
LYS CB     C  N N 348 
LYS CG     C  N N 349 
LYS CD     C  N N 350 
LYS CE     C  N N 351 
LYS NZ     N  N N 352 
LYS OXT    O  N N 353 
LYS H      H  N N 354 
LYS H2     H  N N 355 
LYS HA     H  N N 356 
LYS HB2    H  N N 357 
LYS HB3    H  N N 358 
LYS HG2    H  N N 359 
LYS HG3    H  N N 360 
LYS HD2    H  N N 361 
LYS HD3    H  N N 362 
LYS HE2    H  N N 363 
LYS HE3    H  N N 364 
LYS HZ1    H  N N 365 
LYS HZ2    H  N N 366 
LYS HZ3    H  N N 367 
LYS HXT    H  N N 368 
MET N      N  N N 369 
MET CA     C  N S 370 
MET C      C  N N 371 
MET O      O  N N 372 
MET CB     C  N N 373 
MET CG     C  N N 374 
MET SD     S  N N 375 
MET CE     C  N N 376 
MET OXT    O  N N 377 
MET H      H  N N 378 
MET H2     H  N N 379 
MET HA     H  N N 380 
MET HB2    H  N N 381 
MET HB3    H  N N 382 
MET HG2    H  N N 383 
MET HG3    H  N N 384 
MET HE1    H  N N 385 
MET HE2    H  N N 386 
MET HE3    H  N N 387 
MET HXT    H  N N 388 
NAD PA     P  N S 389 
NAD O1A    O  N N 390 
NAD O2A    O  N N 391 
NAD O5B    O  N N 392 
NAD C5B    C  N N 393 
NAD C4B    C  N R 394 
NAD O4B    O  N N 395 
NAD C3B    C  N S 396 
NAD O3B    O  N N 397 
NAD C2B    C  N R 398 
NAD O2B    O  N N 399 
NAD C1B    C  N R 400 
NAD N9A    N  Y N 401 
NAD C8A    C  Y N 402 
NAD N7A    N  Y N 403 
NAD C5A    C  Y N 404 
NAD C6A    C  Y N 405 
NAD N6A    N  N N 406 
NAD N1A    N  Y N 407 
NAD C2A    C  Y N 408 
NAD N3A    N  Y N 409 
NAD C4A    C  Y N 410 
NAD O3     O  N N 411 
NAD PN     P  N N 412 
NAD O1N    O  N N 413 
NAD O2N    O  N N 414 
NAD O5D    O  N N 415 
NAD C5D    C  N N 416 
NAD C4D    C  N R 417 
NAD O4D    O  N N 418 
NAD C3D    C  N S 419 
NAD O3D    O  N N 420 
NAD C2D    C  N R 421 
NAD O2D    O  N N 422 
NAD C1D    C  N R 423 
NAD N1N    N  Y N 424 
NAD C2N    C  Y N 425 
NAD C3N    C  Y N 426 
NAD C7N    C  N N 427 
NAD O7N    O  N N 428 
NAD N7N    N  N N 429 
NAD C4N    C  Y N 430 
NAD C5N    C  Y N 431 
NAD C6N    C  Y N 432 
NAD HOA2   H  N N 433 
NAD H51A   H  N N 434 
NAD H52A   H  N N 435 
NAD H4B    H  N N 436 
NAD H3B    H  N N 437 
NAD HO3A   H  N N 438 
NAD H2B    H  N N 439 
NAD HO2A   H  N N 440 
NAD H1B    H  N N 441 
NAD H8A    H  N N 442 
NAD H61A   H  N N 443 
NAD H62A   H  N N 444 
NAD H2A    H  N N 445 
NAD H51N   H  N N 446 
NAD H52N   H  N N 447 
NAD H4D    H  N N 448 
NAD H3D    H  N N 449 
NAD HO3N   H  N N 450 
NAD H2D    H  N N 451 
NAD HO2N   H  N N 452 
NAD H1D    H  N N 453 
NAD H2N    H  N N 454 
NAD H71N   H  N N 455 
NAD H72N   H  N N 456 
NAD H4N    H  N N 457 
NAD H5N    H  N N 458 
NAD H6N    H  N N 459 
PHE N      N  N N 460 
PHE CA     C  N S 461 
PHE C      C  N N 462 
PHE O      O  N N 463 
PHE CB     C  N N 464 
PHE CG     C  Y N 465 
PHE CD1    C  Y N 466 
PHE CD2    C  Y N 467 
PHE CE1    C  Y N 468 
PHE CE2    C  Y N 469 
PHE CZ     C  Y N 470 
PHE OXT    O  N N 471 
PHE H      H  N N 472 
PHE H2     H  N N 473 
PHE HA     H  N N 474 
PHE HB2    H  N N 475 
PHE HB3    H  N N 476 
PHE HD1    H  N N 477 
PHE HD2    H  N N 478 
PHE HE1    H  N N 479 
PHE HE2    H  N N 480 
PHE HZ     H  N N 481 
PHE HXT    H  N N 482 
PRO N      N  N N 483 
PRO CA     C  N S 484 
PRO C      C  N N 485 
PRO O      O  N N 486 
PRO CB     C  N N 487 
PRO CG     C  N N 488 
PRO CD     C  N N 489 
PRO OXT    O  N N 490 
PRO H      H  N N 491 
PRO HA     H  N N 492 
PRO HB2    H  N N 493 
PRO HB3    H  N N 494 
PRO HG2    H  N N 495 
PRO HG3    H  N N 496 
PRO HD2    H  N N 497 
PRO HD3    H  N N 498 
PRO HXT    H  N N 499 
SER N      N  N N 500 
SER CA     C  N S 501 
SER C      C  N N 502 
SER O      O  N N 503 
SER CB     C  N N 504 
SER OG     O  N N 505 
SER OXT    O  N N 506 
SER H      H  N N 507 
SER H2     H  N N 508 
SER HA     H  N N 509 
SER HB2    H  N N 510 
SER HB3    H  N N 511 
SER HG     H  N N 512 
SER HXT    H  N N 513 
SF4 FE1    FE N N 514 
SF4 FE2    FE N N 515 
SF4 FE3    FE N N 516 
SF4 FE4    FE N N 517 
SF4 S1     S  N N 518 
SF4 S2     S  N N 519 
SF4 S3     S  N N 520 
SF4 S4     S  N N 521 
THR N      N  N N 522 
THR CA     C  N S 523 
THR C      C  N N 524 
THR O      O  N N 525 
THR CB     C  N R 526 
THR OG1    O  N N 527 
THR CG2    C  N N 528 
THR OXT    O  N N 529 
THR H      H  N N 530 
THR H2     H  N N 531 
THR HA     H  N N 532 
THR HB     H  N N 533 
THR HG1    H  N N 534 
THR HG21   H  N N 535 
THR HG22   H  N N 536 
THR HG23   H  N N 537 
THR HXT    H  N N 538 
TRP N      N  N N 539 
TRP CA     C  N S 540 
TRP C      C  N N 541 
TRP O      O  N N 542 
TRP CB     C  N N 543 
TRP CG     C  Y N 544 
TRP CD1    C  Y N 545 
TRP CD2    C  Y N 546 
TRP NE1    N  Y N 547 
TRP CE2    C  Y N 548 
TRP CE3    C  Y N 549 
TRP CZ2    C  Y N 550 
TRP CZ3    C  Y N 551 
TRP CH2    C  Y N 552 
TRP OXT    O  N N 553 
TRP H      H  N N 554 
TRP H2     H  N N 555 
TRP HA     H  N N 556 
TRP HB2    H  N N 557 
TRP HB3    H  N N 558 
TRP HD1    H  N N 559 
TRP HE1    H  N N 560 
TRP HE3    H  N N 561 
TRP HZ2    H  N N 562 
TRP HZ3    H  N N 563 
TRP HH2    H  N N 564 
TRP HXT    H  N N 565 
TYR N      N  N N 566 
TYR CA     C  N S 567 
TYR C      C  N N 568 
TYR O      O  N N 569 
TYR CB     C  N N 570 
TYR CG     C  Y N 571 
TYR CD1    C  Y N 572 
TYR CD2    C  Y N 573 
TYR CE1    C  Y N 574 
TYR CE2    C  Y N 575 
TYR CZ     C  Y N 576 
TYR OH     O  N N 577 
TYR OXT    O  N N 578 
TYR H      H  N N 579 
TYR H2     H  N N 580 
TYR HA     H  N N 581 
TYR HB2    H  N N 582 
TYR HB3    H  N N 583 
TYR HD1    H  N N 584 
TYR HD2    H  N N 585 
TYR HE1    H  N N 586 
TYR HE2    H  N N 587 
TYR HH     H  N N 588 
TYR HXT    H  N N 589 
VAL N      N  N N 590 
VAL CA     C  N S 591 
VAL C      C  N N 592 
VAL O      O  N N 593 
VAL CB     C  N N 594 
VAL CG1    C  N N 595 
VAL CG2    C  N N 596 
VAL OXT    O  N N 597 
VAL H      H  N N 598 
VAL H2     H  N N 599 
VAL HA     H  N N 600 
VAL HB     H  N N 601 
VAL HG11   H  N N 602 
VAL HG12   H  N N 603 
VAL HG13   H  N N 604 
VAL HG21   H  N N 605 
VAL HG22   H  N N 606 
VAL HG23   H  N N 607 
VAL HXT    H  N N 608 
ZN  ZN     ZN N N 609 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
FES FE1   S1     sing N N 174 
FES FE1   S2     sing N N 175 
FES FE2   S1     sing N N 176 
FES FE2   S2     sing N N 177 
FMN N1    C2     sing N N 178 
FMN N1    C10    doub N N 179 
FMN C2    O2     doub N N 180 
FMN C2    N3     sing N N 181 
FMN N3    C4     sing N N 182 
FMN N3    HN3    sing N N 183 
FMN C4    O4     doub N N 184 
FMN C4    C4A    sing N N 185 
FMN C4A   N5     doub N N 186 
FMN C4A   C10    sing N N 187 
FMN N5    C5A    sing N N 188 
FMN C5A   C6     doub Y N 189 
FMN C5A   C9A    sing Y N 190 
FMN C6    C7     sing Y N 191 
FMN C6    H6     sing N N 192 
FMN C7    C7M    sing N N 193 
FMN C7    C8     doub Y N 194 
FMN C7M   HM71   sing N N 195 
FMN C7M   HM72   sing N N 196 
FMN C7M   HM73   sing N N 197 
FMN C8    C8M    sing N N 198 
FMN C8    C9     sing Y N 199 
FMN C8M   HM81   sing N N 200 
FMN C8M   HM82   sing N N 201 
FMN C8M   HM83   sing N N 202 
FMN C9    C9A    doub Y N 203 
FMN C9    H9     sing N N 204 
FMN C9A   N10    sing N N 205 
FMN N10   C10    sing N N 206 
FMN N10   "C1'"  sing N N 207 
FMN "C1'" "C2'"  sing N N 208 
FMN "C1'" "H1'1" sing N N 209 
FMN "C1'" "H1'2" sing N N 210 
FMN "C2'" "O2'"  sing N N 211 
FMN "C2'" "C3'"  sing N N 212 
FMN "C2'" "H2'"  sing N N 213 
FMN "O2'" "HO2'" sing N N 214 
FMN "C3'" "O3'"  sing N N 215 
FMN "C3'" "C4'"  sing N N 216 
FMN "C3'" "H3'"  sing N N 217 
FMN "O3'" "HO3'" sing N N 218 
FMN "C4'" "O4'"  sing N N 219 
FMN "C4'" "C5'"  sing N N 220 
FMN "C4'" "H4'"  sing N N 221 
FMN "O4'" "HO4'" sing N N 222 
FMN "C5'" "O5'"  sing N N 223 
FMN "C5'" "H5'1" sing N N 224 
FMN "C5'" "H5'2" sing N N 225 
FMN "O5'" P      sing N N 226 
FMN P     O1P    doub N N 227 
FMN P     O2P    sing N N 228 
FMN P     O3P    sing N N 229 
FMN O2P   HOP2   sing N N 230 
FMN O3P   HOP3   sing N N 231 
GLN N     CA     sing N N 232 
GLN N     H      sing N N 233 
GLN N     H2     sing N N 234 
GLN CA    C      sing N N 235 
GLN CA    CB     sing N N 236 
GLN CA    HA     sing N N 237 
GLN C     O      doub N N 238 
GLN C     OXT    sing N N 239 
GLN CB    CG     sing N N 240 
GLN CB    HB2    sing N N 241 
GLN CB    HB3    sing N N 242 
GLN CG    CD     sing N N 243 
GLN CG    HG2    sing N N 244 
GLN CG    HG3    sing N N 245 
GLN CD    OE1    doub N N 246 
GLN CD    NE2    sing N N 247 
GLN NE2   HE21   sing N N 248 
GLN NE2   HE22   sing N N 249 
GLN OXT   HXT    sing N N 250 
GLU N     CA     sing N N 251 
GLU N     H      sing N N 252 
GLU N     H2     sing N N 253 
GLU CA    C      sing N N 254 
GLU CA    CB     sing N N 255 
GLU CA    HA     sing N N 256 
GLU C     O      doub N N 257 
GLU C     OXT    sing N N 258 
GLU CB    CG     sing N N 259 
GLU CB    HB2    sing N N 260 
GLU CB    HB3    sing N N 261 
GLU CG    CD     sing N N 262 
GLU CG    HG2    sing N N 263 
GLU CG    HG3    sing N N 264 
GLU CD    OE1    doub N N 265 
GLU CD    OE2    sing N N 266 
GLU OE2   HE2    sing N N 267 
GLU OXT   HXT    sing N N 268 
GLY N     CA     sing N N 269 
GLY N     H      sing N N 270 
GLY N     H2     sing N N 271 
GLY CA    C      sing N N 272 
GLY CA    HA2    sing N N 273 
GLY CA    HA3    sing N N 274 
GLY C     O      doub N N 275 
GLY C     OXT    sing N N 276 
GLY OXT   HXT    sing N N 277 
HIS N     CA     sing N N 278 
HIS N     H      sing N N 279 
HIS N     H2     sing N N 280 
HIS CA    C      sing N N 281 
HIS CA    CB     sing N N 282 
HIS CA    HA     sing N N 283 
HIS C     O      doub N N 284 
HIS C     OXT    sing N N 285 
HIS CB    CG     sing N N 286 
HIS CB    HB2    sing N N 287 
HIS CB    HB3    sing N N 288 
HIS CG    ND1    sing Y N 289 
HIS CG    CD2    doub Y N 290 
HIS ND1   CE1    doub Y N 291 
HIS ND1   HD1    sing N N 292 
HIS CD2   NE2    sing Y N 293 
HIS CD2   HD2    sing N N 294 
HIS CE1   NE2    sing Y N 295 
HIS CE1   HE1    sing N N 296 
HIS NE2   HE2    sing N N 297 
HIS OXT   HXT    sing N N 298 
ILE N     CA     sing N N 299 
ILE N     H      sing N N 300 
ILE N     H2     sing N N 301 
ILE CA    C      sing N N 302 
ILE CA    CB     sing N N 303 
ILE CA    HA     sing N N 304 
ILE C     O      doub N N 305 
ILE C     OXT    sing N N 306 
ILE CB    CG1    sing N N 307 
ILE CB    CG2    sing N N 308 
ILE CB    HB     sing N N 309 
ILE CG1   CD1    sing N N 310 
ILE CG1   HG12   sing N N 311 
ILE CG1   HG13   sing N N 312 
ILE CG2   HG21   sing N N 313 
ILE CG2   HG22   sing N N 314 
ILE CG2   HG23   sing N N 315 
ILE CD1   HD11   sing N N 316 
ILE CD1   HD12   sing N N 317 
ILE CD1   HD13   sing N N 318 
ILE OXT   HXT    sing N N 319 
LEU N     CA     sing N N 320 
LEU N     H      sing N N 321 
LEU N     H2     sing N N 322 
LEU CA    C      sing N N 323 
LEU CA    CB     sing N N 324 
LEU CA    HA     sing N N 325 
LEU C     O      doub N N 326 
LEU C     OXT    sing N N 327 
LEU CB    CG     sing N N 328 
LEU CB    HB2    sing N N 329 
LEU CB    HB3    sing N N 330 
LEU CG    CD1    sing N N 331 
LEU CG    CD2    sing N N 332 
LEU CG    HG     sing N N 333 
LEU CD1   HD11   sing N N 334 
LEU CD1   HD12   sing N N 335 
LEU CD1   HD13   sing N N 336 
LEU CD2   HD21   sing N N 337 
LEU CD2   HD22   sing N N 338 
LEU CD2   HD23   sing N N 339 
LEU OXT   HXT    sing N N 340 
LYS N     CA     sing N N 341 
LYS N     H      sing N N 342 
LYS N     H2     sing N N 343 
LYS CA    C      sing N N 344 
LYS CA    CB     sing N N 345 
LYS CA    HA     sing N N 346 
LYS C     O      doub N N 347 
LYS C     OXT    sing N N 348 
LYS CB    CG     sing N N 349 
LYS CB    HB2    sing N N 350 
LYS CB    HB3    sing N N 351 
LYS CG    CD     sing N N 352 
LYS CG    HG2    sing N N 353 
LYS CG    HG3    sing N N 354 
LYS CD    CE     sing N N 355 
LYS CD    HD2    sing N N 356 
LYS CD    HD3    sing N N 357 
LYS CE    NZ     sing N N 358 
LYS CE    HE2    sing N N 359 
LYS CE    HE3    sing N N 360 
LYS NZ    HZ1    sing N N 361 
LYS NZ    HZ2    sing N N 362 
LYS NZ    HZ3    sing N N 363 
LYS OXT   HXT    sing N N 364 
MET N     CA     sing N N 365 
MET N     H      sing N N 366 
MET N     H2     sing N N 367 
MET CA    C      sing N N 368 
MET CA    CB     sing N N 369 
MET CA    HA     sing N N 370 
MET C     O      doub N N 371 
MET C     OXT    sing N N 372 
MET CB    CG     sing N N 373 
MET CB    HB2    sing N N 374 
MET CB    HB3    sing N N 375 
MET CG    SD     sing N N 376 
MET CG    HG2    sing N N 377 
MET CG    HG3    sing N N 378 
MET SD    CE     sing N N 379 
MET CE    HE1    sing N N 380 
MET CE    HE2    sing N N 381 
MET CE    HE3    sing N N 382 
MET OXT   HXT    sing N N 383 
NAD PA    O1A    doub N N 384 
NAD PA    O2A    sing N N 385 
NAD PA    O5B    sing N N 386 
NAD PA    O3     sing N N 387 
NAD O2A   HOA2   sing N N 388 
NAD O5B   C5B    sing N N 389 
NAD C5B   C4B    sing N N 390 
NAD C5B   H51A   sing N N 391 
NAD C5B   H52A   sing N N 392 
NAD C4B   O4B    sing N N 393 
NAD C4B   C3B    sing N N 394 
NAD C4B   H4B    sing N N 395 
NAD O4B   C1B    sing N N 396 
NAD C3B   O3B    sing N N 397 
NAD C3B   C2B    sing N N 398 
NAD C3B   H3B    sing N N 399 
NAD O3B   HO3A   sing N N 400 
NAD C2B   O2B    sing N N 401 
NAD C2B   C1B    sing N N 402 
NAD C2B   H2B    sing N N 403 
NAD O2B   HO2A   sing N N 404 
NAD C1B   N9A    sing N N 405 
NAD C1B   H1B    sing N N 406 
NAD N9A   C8A    sing Y N 407 
NAD N9A   C4A    sing Y N 408 
NAD C8A   N7A    doub Y N 409 
NAD C8A   H8A    sing N N 410 
NAD N7A   C5A    sing Y N 411 
NAD C5A   C6A    sing Y N 412 
NAD C5A   C4A    doub Y N 413 
NAD C6A   N6A    sing N N 414 
NAD C6A   N1A    doub Y N 415 
NAD N6A   H61A   sing N N 416 
NAD N6A   H62A   sing N N 417 
NAD N1A   C2A    sing Y N 418 
NAD C2A   N3A    doub Y N 419 
NAD C2A   H2A    sing N N 420 
NAD N3A   C4A    sing Y N 421 
NAD O3    PN     sing N N 422 
NAD PN    O1N    doub N N 423 
NAD PN    O2N    sing N N 424 
NAD PN    O5D    sing N N 425 
NAD O5D   C5D    sing N N 426 
NAD C5D   C4D    sing N N 427 
NAD C5D   H51N   sing N N 428 
NAD C5D   H52N   sing N N 429 
NAD C4D   O4D    sing N N 430 
NAD C4D   C3D    sing N N 431 
NAD C4D   H4D    sing N N 432 
NAD O4D   C1D    sing N N 433 
NAD C3D   O3D    sing N N 434 
NAD C3D   C2D    sing N N 435 
NAD C3D   H3D    sing N N 436 
NAD O3D   HO3N   sing N N 437 
NAD C2D   O2D    sing N N 438 
NAD C2D   C1D    sing N N 439 
NAD C2D   H2D    sing N N 440 
NAD O2D   HO2N   sing N N 441 
NAD C1D   N1N    sing N N 442 
NAD C1D   H1D    sing N N 443 
NAD N1N   C2N    sing Y N 444 
NAD N1N   C6N    doub Y N 445 
NAD C2N   C3N    doub Y N 446 
NAD C2N   H2N    sing N N 447 
NAD C3N   C7N    sing N N 448 
NAD C3N   C4N    sing Y N 449 
NAD C7N   O7N    doub N N 450 
NAD C7N   N7N    sing N N 451 
NAD N7N   H71N   sing N N 452 
NAD N7N   H72N   sing N N 453 
NAD C4N   C5N    doub Y N 454 
NAD C4N   H4N    sing N N 455 
NAD C5N   C6N    sing Y N 456 
NAD C5N   H5N    sing N N 457 
NAD C6N   H6N    sing N N 458 
PHE N     CA     sing N N 459 
PHE N     H      sing N N 460 
PHE N     H2     sing N N 461 
PHE CA    C      sing N N 462 
PHE CA    CB     sing N N 463 
PHE CA    HA     sing N N 464 
PHE C     O      doub N N 465 
PHE C     OXT    sing N N 466 
PHE CB    CG     sing N N 467 
PHE CB    HB2    sing N N 468 
PHE CB    HB3    sing N N 469 
PHE CG    CD1    doub Y N 470 
PHE CG    CD2    sing Y N 471 
PHE CD1   CE1    sing Y N 472 
PHE CD1   HD1    sing N N 473 
PHE CD2   CE2    doub Y N 474 
PHE CD2   HD2    sing N N 475 
PHE CE1   CZ     doub Y N 476 
PHE CE1   HE1    sing N N 477 
PHE CE2   CZ     sing Y N 478 
PHE CE2   HE2    sing N N 479 
PHE CZ    HZ     sing N N 480 
PHE OXT   HXT    sing N N 481 
PRO N     CA     sing N N 482 
PRO N     CD     sing N N 483 
PRO N     H      sing N N 484 
PRO CA    C      sing N N 485 
PRO CA    CB     sing N N 486 
PRO CA    HA     sing N N 487 
PRO C     O      doub N N 488 
PRO C     OXT    sing N N 489 
PRO CB    CG     sing N N 490 
PRO CB    HB2    sing N N 491 
PRO CB    HB3    sing N N 492 
PRO CG    CD     sing N N 493 
PRO CG    HG2    sing N N 494 
PRO CG    HG3    sing N N 495 
PRO CD    HD2    sing N N 496 
PRO CD    HD3    sing N N 497 
PRO OXT   HXT    sing N N 498 
SER N     CA     sing N N 499 
SER N     H      sing N N 500 
SER N     H2     sing N N 501 
SER CA    C      sing N N 502 
SER CA    CB     sing N N 503 
SER CA    HA     sing N N 504 
SER C     O      doub N N 505 
SER C     OXT    sing N N 506 
SER CB    OG     sing N N 507 
SER CB    HB2    sing N N 508 
SER CB    HB3    sing N N 509 
SER OG    HG     sing N N 510 
SER OXT   HXT    sing N N 511 
SF4 FE1   S2     sing N N 512 
SF4 FE1   S3     sing N N 513 
SF4 FE1   S4     sing N N 514 
SF4 FE2   S1     sing N N 515 
SF4 FE2   S3     sing N N 516 
SF4 FE2   S4     sing N N 517 
SF4 FE3   S1     sing N N 518 
SF4 FE3   S2     sing N N 519 
SF4 FE3   S4     sing N N 520 
SF4 FE4   S1     sing N N 521 
SF4 FE4   S2     sing N N 522 
SF4 FE4   S3     sing N N 523 
THR N     CA     sing N N 524 
THR N     H      sing N N 525 
THR N     H2     sing N N 526 
THR CA    C      sing N N 527 
THR CA    CB     sing N N 528 
THR CA    HA     sing N N 529 
THR C     O      doub N N 530 
THR C     OXT    sing N N 531 
THR CB    OG1    sing N N 532 
THR CB    CG2    sing N N 533 
THR CB    HB     sing N N 534 
THR OG1   HG1    sing N N 535 
THR CG2   HG21   sing N N 536 
THR CG2   HG22   sing N N 537 
THR CG2   HG23   sing N N 538 
THR OXT   HXT    sing N N 539 
TRP N     CA     sing N N 540 
TRP N     H      sing N N 541 
TRP N     H2     sing N N 542 
TRP CA    C      sing N N 543 
TRP CA    CB     sing N N 544 
TRP CA    HA     sing N N 545 
TRP C     O      doub N N 546 
TRP C     OXT    sing N N 547 
TRP CB    CG     sing N N 548 
TRP CB    HB2    sing N N 549 
TRP CB    HB3    sing N N 550 
TRP CG    CD1    doub Y N 551 
TRP CG    CD2    sing Y N 552 
TRP CD1   NE1    sing Y N 553 
TRP CD1   HD1    sing N N 554 
TRP CD2   CE2    doub Y N 555 
TRP CD2   CE3    sing Y N 556 
TRP NE1   CE2    sing Y N 557 
TRP NE1   HE1    sing N N 558 
TRP CE2   CZ2    sing Y N 559 
TRP CE3   CZ3    doub Y N 560 
TRP CE3   HE3    sing N N 561 
TRP CZ2   CH2    doub Y N 562 
TRP CZ2   HZ2    sing N N 563 
TRP CZ3   CH2    sing Y N 564 
TRP CZ3   HZ3    sing N N 565 
TRP CH2   HH2    sing N N 566 
TRP OXT   HXT    sing N N 567 
TYR N     CA     sing N N 568 
TYR N     H      sing N N 569 
TYR N     H2     sing N N 570 
TYR CA    C      sing N N 571 
TYR CA    CB     sing N N 572 
TYR CA    HA     sing N N 573 
TYR C     O      doub N N 574 
TYR C     OXT    sing N N 575 
TYR CB    CG     sing N N 576 
TYR CB    HB2    sing N N 577 
TYR CB    HB3    sing N N 578 
TYR CG    CD1    doub Y N 579 
TYR CG    CD2    sing Y N 580 
TYR CD1   CE1    sing Y N 581 
TYR CD1   HD1    sing N N 582 
TYR CD2   CE2    doub Y N 583 
TYR CD2   HD2    sing N N 584 
TYR CE1   CZ     doub Y N 585 
TYR CE1   HE1    sing N N 586 
TYR CE2   CZ     sing Y N 587 
TYR CE2   HE2    sing N N 588 
TYR CZ    OH     sing N N 589 
TYR OH    HH     sing N N 590 
TYR OXT   HXT    sing N N 591 
VAL N     CA     sing N N 592 
VAL N     H      sing N N 593 
VAL N     H2     sing N N 594 
VAL CA    C      sing N N 595 
VAL CA    CB     sing N N 596 
VAL CA    HA     sing N N 597 
VAL C     O      doub N N 598 
VAL C     OXT    sing N N 599 
VAL CB    CG1    sing N N 600 
VAL CB    CG2    sing N N 601 
VAL CB    HB     sing N N 602 
VAL CG1   HG11   sing N N 603 
VAL CG1   HG12   sing N N 604 
VAL CG1   HG13   sing N N 605 
VAL CG2   HG21   sing N N 606 
VAL CG2   HG22   sing N N 607 
VAL CG2   HG23   sing N N 608 
VAL OXT   HXT    sing N N 609 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2025-02-04 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9N5V 
_em_admin.last_update        2025-05-07 
_em_admin.map_release_date   2025-05-07 
_em_admin.title              'Cryo-EM map of the NAD(H)-bound Thermococcus sibiricus NfnABC 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          172049 
_em_entity_assembly_naturalsource.organism             'Thermococcus sibiricus' 
_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          2261 
_em_entity_assembly_recombinant.organism             'Pyrococcus furiosus' 
_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               1.5 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       SUPER-RESOLUTION 
_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                     20798 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_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                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   12889202 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? cryoSPARC       ?   
'IMAGE ACQUISITION'             ? 2  ? ? 1 SerialEM        4.0 
MASKING                         ? 3  ? ? ? ?               ?   
'CTF CORRECTION'                ? 4  1 ? ? cryoSPARC       ?   
'LAYERLINE INDEXING'            ? 5  ? ? ? ?               ?   
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?               ?   
'MODEL FITTING'                 ? 7  ? 1 ? 'UCSF ChimeraX' ?   
OTHER                           ? 8  ? ? ? ?               ?   
'MODEL REFINEMENT'              ? 9  ? 1 ? PHENIX          ?   
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? cryoSPARC       ?   
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC       ?   
CLASSIFICATION                  ? 12 1 ? ? cryoSPARC       ?   
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC       ?   
'VOLUME SELECTION'              ? 14 1 1 1 ?               ?   
'SERIES ALIGNMENT'              ? 15 1 1 1 ?               ?   
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?               ?   
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?               ?   
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?               ?   
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?               ?   
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Department of Energy (DOE, United States)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9N5V 
_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  
FE 
H  
N  
O  
P  
S  
ZN 
# 
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 10  ? 104.508 116.803 146.164 1.00 103.67 ? 10   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 10  ? 104.058 118.171 146.383 1.00 103.83 ? 10   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 10  ? 103.799 118.853 145.048 1.00 104.24 ? 10   VAL A C     1 
ATOM   4     O  O     . VAL A 1 10  ? 104.312 118.425 144.016 1.00 103.98 ? 10   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 10  ? 105.079 118.965 147.215 1.00 102.63 ? 10   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 10  ? 105.330 118.272 148.545 1.00 103.22 ? 10   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 10  ? 106.378 119.133 146.444 1.00 102.68 ? 10   VAL A CG2   1 
ATOM   8     N  N     . LYS A 1 11  ? 103.002 119.916 145.069 1.00 102.95 ? 11   LYS A N     1 
ATOM   9     C  CA    . LYS A 1 11  ? 102.672 120.667 143.867 1.00 102.86 ? 11   LYS A CA    1 
ATOM   10    C  C     . LYS A 1 11  ? 103.069 122.125 144.042 1.00 103.31 ? 11   LYS A C     1 
ATOM   11    O  O     . LYS A 1 11  ? 102.886 122.706 145.116 1.00 103.40 ? 11   LYS A O     1 
ATOM   12    C  CB    . LYS A 1 11  ? 101.179 120.561 143.534 1.00 102.83 ? 11   LYS A CB    1 
ATOM   13    C  CG    . LYS A 1 11  ? 100.251 121.009 144.646 1.00 102.38 ? 11   LYS A CG    1 
ATOM   14    C  CD    . LYS A 1 11  ? 98.799  120.890 144.227 1.00 102.83 ? 11   LYS A CD    1 
ATOM   15    C  CE    . LYS A 1 11  ? 97.870  121.387 145.320 1.00 103.03 ? 11   LYS A CE    1 
ATOM   16    N  NZ    . LYS A 1 11  ? 98.118  122.818 145.647 1.00 103.12 ? 11   LYS A NZ    1 
ATOM   17    N  N     . ILE A 1 12  ? 103.632 122.705 142.983 1.00 92.34  ? 12   ILE A N     1 
ATOM   18    C  CA    . ILE A 1 12  ? 104.037 124.103 142.973 1.00 90.99  ? 12   ILE A CA    1 
ATOM   19    C  C     . ILE A 1 12  ? 103.453 124.763 141.733 1.00 90.96  ? 12   ILE A C     1 
ATOM   20    O  O     . ILE A 1 12  ? 103.034 124.100 140.782 1.00 90.22  ? 12   ILE A O     1 
ATOM   21    C  CB    . ILE A 1 12  ? 105.571 124.281 142.997 1.00 91.42  ? 12   ILE A CB    1 
ATOM   22    C  CG1   . ILE A 1 12  ? 106.180 123.864 141.661 1.00 91.13  ? 12   ILE A CG1   1 
ATOM   23    C  CG2   . ILE A 1 12  ? 106.194 123.480 144.121 1.00 91.12  ? 12   ILE A CG2   1 
ATOM   24    C  CD1   . ILE A 1 12  ? 107.637 124.201 141.541 1.00 87.62  ? 12   ILE A CD1   1 
ATOM   25    N  N     . THR A 1 13  ? 103.425 126.090 141.756 1.00 90.60  ? 13   THR A N     1 
ATOM   26    C  CA    . THR A 1 13  ? 102.936 126.885 140.639 1.00 90.07  ? 13   THR A CA    1 
ATOM   27    C  C     . THR A 1 13  ? 104.101 127.665 140.048 1.00 90.26  ? 13   THR A C     1 
ATOM   28    O  O     . THR A 1 13  ? 104.770 128.421 140.759 1.00 88.75  ? 13   THR A O     1 
ATOM   29    C  CB    . THR A 1 13  ? 101.823 127.833 141.084 1.00 90.19  ? 13   THR A CB    1 
ATOM   30    O  OG1   . THR A 1 13  ? 102.305 128.680 142.132 1.00 90.31  ? 13   THR A OG1   1 
ATOM   31    C  CG2   . THR A 1 13  ? 100.630 127.045 141.591 1.00 91.23  ? 13   THR A CG2   1 
ATOM   32    N  N     . VAL A 1 14  ? 104.343 127.479 138.755 1.00 83.56  ? 14   VAL A N     1 
ATOM   33    C  CA    . VAL A 1 14  ? 105.401 128.183 138.041 1.00 80.56  ? 14   VAL A CA    1 
ATOM   34    C  C     . VAL A 1 14  ? 104.748 129.032 136.962 1.00 81.18  ? 14   VAL A C     1 
ATOM   35    O  O     . VAL A 1 14  ? 104.079 128.499 136.067 1.00 80.42  ? 14   VAL A O     1 
ATOM   36    C  CB    . VAL A 1 14  ? 106.428 127.217 137.433 1.00 80.21  ? 14   VAL A CB    1 
ATOM   37    C  CG1   . VAL A 1 14  ? 107.544 127.992 136.762 1.00 78.78  ? 14   VAL A CG1   1 
ATOM   38    C  CG2   . VAL A 1 14  ? 106.986 126.298 138.503 1.00 80.74  ? 14   VAL A CG2   1 
ATOM   39    N  N     . ASN A 1 15  ? 104.946 130.349 137.048 1.00 77.63  ? 15   ASN A N     1 
ATOM   40    C  CA    . ASN A 1 15  ? 104.383 131.315 136.104 1.00 76.34  ? 15   ASN A CA    1 
ATOM   41    C  C     . ASN A 1 15  ? 102.864 131.197 136.005 1.00 77.09  ? 15   ASN A C     1 
ATOM   42    O  O     . ASN A 1 15  ? 102.282 131.413 134.940 1.00 77.50  ? 15   ASN A O     1 
ATOM   43    C  CB    . ASN A 1 15  ? 105.022 131.182 134.719 1.00 75.04  ? 15   ASN A CB    1 
ATOM   44    C  CG    . ASN A 1 15  ? 106.478 131.601 134.705 1.00 72.13  ? 15   ASN A CG    1 
ATOM   45    O  OD1   . ASN A 1 15  ? 106.892 132.474 135.466 1.00 67.59  ? 15   ASN A OD1   1 
ATOM   46    N  ND2   . ASN A 1 15  ? 107.262 130.982 133.835 1.00 72.38  ? 15   ASN A ND2   1 
ATOM   47    N  N     . GLY A 1 16  ? 102.212 130.853 137.113 1.00 84.59  ? 16   GLY A N     1 
ATOM   48    C  CA    . GLY A 1 16  ? 100.769 130.793 137.167 1.00 84.77  ? 16   GLY A CA    1 
ATOM   49    C  C     . GLY A 1 16  ? 100.148 129.486 136.726 1.00 86.29  ? 16   GLY A C     1 
ATOM   50    O  O     . GLY A 1 16  ? 98.920  129.352 136.796 1.00 88.24  ? 16   GLY A O     1 
ATOM   51    N  N     . LYS A 1 17  ? 100.943 128.522 136.276 1.00 86.85  ? 17   LYS A N     1 
ATOM   52    C  CA    . LYS A 1 17  ? 100.439 127.226 135.845 1.00 89.22  ? 17   LYS A CA    1 
ATOM   53    C  C     . LYS A 1 17  ? 100.765 126.186 136.907 1.00 91.09  ? 17   LYS A C     1 
ATOM   54    O  O     . LYS A 1 17  ? 101.893 126.136 137.406 1.00 92.65  ? 17   LYS A O     1 
ATOM   55    C  CB    . LYS A 1 17  ? 101.042 126.825 134.500 1.00 88.22  ? 17   LYS A CB    1 
ATOM   56    C  CG    . LYS A 1 17  ? 100.388 125.615 133.866 1.00 89.20  ? 17   LYS A CG    1 
ATOM   57    C  CD    . LYS A 1 17  ? 101.027 125.295 132.527 1.00 89.94  ? 17   LYS A CD    1 
ATOM   58    C  CE    . LYS A 1 17  ? 101.014 126.503 131.607 1.00 90.35  ? 17   LYS A CE    1 
ATOM   59    N  NZ    . LYS A 1 17  ? 99.634  126.999 131.357 1.00 89.41  ? 17   LYS A NZ    1 
ATOM   60    N  N     . GLU A 1 18  ? 99.776  125.369 137.257 1.00 93.69  ? 18   GLU A N     1 
ATOM   61    C  CA    . GLU A 1 18  ? 99.945  124.389 138.320 1.00 93.58  ? 18   GLU A CA    1 
ATOM   62    C  C     . GLU A 1 18  ? 100.800 123.226 137.835 1.00 94.25  ? 18   GLU A C     1 
ATOM   63    O  O     . GLU A 1 18  ? 100.587 122.702 136.737 1.00 92.73  ? 18   GLU A O     1 
ATOM   64    C  CB    . GLU A 1 18  ? 98.585  123.887 138.801 1.00 94.11  ? 18   GLU A CB    1 
ATOM   65    C  CG    . GLU A 1 18  ? 98.653  122.970 140.006 1.00 93.98  ? 18   GLU A CG    1 
ATOM   66    C  CD    . GLU A 1 18  ? 97.280  122.602 140.532 1.00 95.57  ? 18   GLU A CD    1 
ATOM   67    O  OE1   . GLU A 1 18  ? 96.280  123.131 140.004 1.00 95.37  ? 18   GLU A OE1   1 
ATOM   68    O  OE2   . GLU A 1 18  ? 97.201  121.783 141.471 1.00 95.80  ? 18   GLU A OE2   1 
ATOM   69    N  N     . PHE A 1 19  ? 101.763 122.822 138.658 1.00 91.65  ? 19   PHE A N     1 
ATOM   70    C  CA    . PHE A 1 19  ? 102.703 121.768 138.312 1.00 90.34  ? 19   PHE A CA    1 
ATOM   71    C  C     . PHE A 1 19  ? 102.864 120.805 139.478 1.00 91.15  ? 19   PHE A C     1 
ATOM   72    O  O     . PHE A 1 19  ? 102.624 121.150 140.637 1.00 89.70  ? 19   PHE A O     1 
ATOM   73    C  CB    . PHE A 1 19  ? 104.074 122.339 137.933 1.00 88.27  ? 19   PHE A CB    1 
ATOM   74    C  CG    . PHE A 1 19  ? 104.112 122.982 136.580 1.00 88.84  ? 19   PHE A CG    1 
ATOM   75    C  CD1   . PHE A 1 19  ? 103.952 122.224 135.435 1.00 89.98  ? 19   PHE A CD1   1 
ATOM   76    C  CD2   . PHE A 1 19  ? 104.327 124.341 136.453 1.00 88.69  ? 19   PHE A CD2   1 
ATOM   77    C  CE1   . PHE A 1 19  ? 103.992 122.812 134.189 1.00 89.86  ? 19   PHE A CE1   1 
ATOM   78    C  CE2   . PHE A 1 19  ? 104.368 124.934 135.210 1.00 88.02  ? 19   PHE A CE2   1 
ATOM   79    C  CZ    . PHE A 1 19  ? 104.202 124.169 134.077 1.00 87.94  ? 19   PHE A CZ    1 
ATOM   80    N  N     . GLU A 1 20  ? 103.278 119.584 139.153 1.00 96.45  ? 20   GLU A N     1 
ATOM   81    C  CA    . GLU A 1 20  ? 103.623 118.568 140.139 1.00 96.53  ? 20   GLU A CA    1 
ATOM   82    C  C     . GLU A 1 20  ? 105.104 118.243 140.014 1.00 96.31  ? 20   GLU A C     1 
ATOM   83    O  O     . GLU A 1 20  ? 105.580 117.920 138.921 1.00 96.05  ? 20   GLU A O     1 
ATOM   84    C  CB    . GLU A 1 20  ? 102.781 117.306 139.945 1.00 96.56  ? 20   GLU A CB    1 
ATOM   85    C  CG    . GLU A 1 20  ? 101.675 117.143 140.967 1.00 96.81  ? 20   GLU A CG    1 
ATOM   86    C  CD    . GLU A 1 20  ? 102.208 116.818 142.347 1.00 97.45  ? 20   GLU A CD    1 
ATOM   87    O  OE1   . GLU A 1 20  ? 103.308 116.233 142.436 1.00 96.22  ? 20   GLU A OE1   1 
ATOM   88    O  OE2   . GLU A 1 20  ? 101.530 117.148 143.342 1.00 96.83  ? 20   GLU A OE2   1 
ATOM   89    N  N     . ALA A 1 21  ? 105.827 118.323 141.126 1.00 97.74  ? 21   ALA A N     1 
ATOM   90    C  CA    . ALA A 1 21  ? 107.267 118.128 141.106 1.00 96.81  ? 21   ALA A CA    1 
ATOM   91    C  C     . ALA A 1 21  ? 107.704 117.192 142.222 1.00 96.67  ? 21   ALA A C     1 
ATOM   92    O  O     . ALA A 1 21  ? 107.070 117.141 143.281 1.00 95.56  ? 21   ALA A O     1 
ATOM   93    C  CB    . ALA A 1 21  ? 108.002 119.468 141.249 1.00 95.62  ? 21   ALA A CB    1 
ATOM   94    N  N     . PRO A 1 22  ? 108.778 116.432 142.008 1.00 94.23  ? 22   PRO A N     1 
ATOM   95    C  CA    . PRO A 1 22  ? 109.327 115.607 143.090 1.00 94.00  ? 22   PRO A CA    1 
ATOM   96    C  C     . PRO A 1 22  ? 109.889 116.463 144.213 1.00 93.31  ? 22   PRO A C     1 
ATOM   97    O  O     . PRO A 1 22  ? 110.418 117.554 143.990 1.00 92.44  ? 22   PRO A O     1 
ATOM   98    C  CB    . PRO A 1 22  ? 110.435 114.804 142.400 1.00 91.47  ? 22   PRO A CB    1 
ATOM   99    C  CG    . PRO A 1 22  ? 110.082 114.832 140.952 1.00 91.97  ? 22   PRO A CG    1 
ATOM   100   C  CD    . PRO A 1 22  ? 109.442 116.165 140.723 1.00 93.32  ? 22   PRO A CD    1 
ATOM   101   N  N     . LYS A 1 23  ? 109.782 115.944 145.434 1.00 89.14  ? 23   LYS A N     1 
ATOM   102   C  CA    . LYS A 1 23  ? 110.086 116.729 146.623 1.00 87.41  ? 23   LYS A CA    1 
ATOM   103   C  C     . LYS A 1 23  ? 111.563 116.748 146.988 1.00 87.61  ? 23   LYS A C     1 
ATOM   104   O  O     . LYS A 1 23  ? 112.001 117.677 147.674 1.00 86.61  ? 23   LYS A O     1 
ATOM   105   C  CB    . LYS A 1 23  ? 109.281 116.207 147.816 1.00 87.42  ? 23   LYS A CB    1 
ATOM   106   C  CG    . LYS A 1 23  ? 109.436 114.719 148.063 1.00 88.34  ? 23   LYS A CG    1 
ATOM   107   C  CD    . LYS A 1 23  ? 108.594 114.269 149.242 1.00 89.13  ? 23   LYS A CD    1 
ATOM   108   C  CE    . LYS A 1 23  ? 108.990 115.000 150.512 1.00 89.09  ? 23   LYS A CE    1 
ATOM   109   N  NZ    . LYS A 1 23  ? 108.185 114.554 151.682 1.00 89.97  ? 23   LYS A NZ    1 
ATOM   110   N  N     . ASP A 1 24  ? 112.339 115.758 146.556 1.00 87.46  ? 24   ASP A N     1 
ATOM   111   C  CA    . ASP A 1 24  ? 113.745 115.670 146.929 1.00 87.02  ? 24   ASP A CA    1 
ATOM   112   C  C     . ASP A 1 24  ? 114.681 116.276 145.895 1.00 84.31  ? 24   ASP A C     1 
ATOM   113   O  O     . ASP A 1 24  ? 115.668 116.917 146.266 1.00 83.85  ? 24   ASP A O     1 
ATOM   114   C  CB    . ASP A 1 24  ? 114.140 114.210 147.173 1.00 86.42  ? 24   ASP A CB    1 
ATOM   115   C  CG    . ASP A 1 24  ? 113.596 113.669 148.480 1.00 86.75  ? 24   ASP A CG    1 
ATOM   116   O  OD1   . ASP A 1 24  ? 112.382 113.391 148.553 1.00 85.63  ? 24   ASP A OD1   1 
ATOM   117   O  OD2   . ASP A 1 24  ? 114.385 113.524 149.438 1.00 86.61  ? 24   ASP A OD2   1 
ATOM   118   N  N     . LYS A 1 25  ? 114.399 116.087 144.610 1.00 73.13  ? 25   LYS A N     1 
ATOM   119   C  CA    . LYS A 1 25  ? 115.260 116.627 143.570 1.00 73.33  ? 25   LYS A CA    1 
ATOM   120   C  C     . LYS A 1 25  ? 115.210 118.149 143.566 1.00 71.57  ? 25   LYS A C     1 
ATOM   121   O  O     . LYS A 1 25  ? 114.240 118.764 144.014 1.00 72.45  ? 25   LYS A O     1 
ATOM   122   C  CB    . LYS A 1 25  ? 114.850 116.092 142.200 1.00 73.16  ? 25   LYS A CB    1 
ATOM   123   C  CG    . LYS A 1 25  ? 115.092 114.610 142.012 1.00 71.36  ? 25   LYS A CG    1 
ATOM   124   C  CD    . LYS A 1 25  ? 114.709 114.171 140.610 1.00 73.93  ? 25   LYS A CD    1 
ATOM   125   C  CE    . LYS A 1 25  ? 115.015 112.700 140.391 1.00 73.45  ? 25   LYS A CE    1 
ATOM   126   N  NZ    . LYS A 1 25  ? 114.288 111.831 141.357 1.00 70.47  ? 25   LYS A NZ    1 
ATOM   127   N  N     . SER A 1 26  ? 116.280 118.754 143.063 1.00 54.20  ? 26   SER A N     1 
ATOM   128   C  CA    . SER A 1 26  ? 116.341 120.202 142.966 1.00 50.57  ? 26   SER A CA    1 
ATOM   129   C  C     . SER A 1 26  ? 115.320 120.712 141.956 1.00 51.46  ? 26   SER A C     1 
ATOM   130   O  O     . SER A 1 26  ? 114.898 119.995 141.046 1.00 51.36  ? 26   SER A O     1 
ATOM   131   C  CB    . SER A 1 26  ? 117.744 120.653 142.568 1.00 48.13  ? 26   SER A CB    1 
ATOM   132   O  OG    . SER A 1 26  ? 118.080 120.183 141.277 1.00 45.65  ? 26   SER A OG    1 
ATOM   133   N  N     . LEU A 1 27  ? 114.910 121.966 142.136 1.00 30.00  ? 27   LEU A N     1 
ATOM   134   C  CA    . LEU A 1 27  ? 113.914 122.549 141.248 1.00 30.00  ? 27   LEU A CA    1 
ATOM   135   C  C     . LEU A 1 27  ? 114.468 122.838 139.862 1.00 30.00  ? 27   LEU A C     1 
ATOM   136   O  O     . LEU A 1 27  ? 113.687 122.934 138.910 1.00 30.00  ? 27   LEU A O     1 
ATOM   137   C  CB    . LEU A 1 27  ? 113.354 123.835 141.852 1.00 30.00  ? 27   LEU A CB    1 
ATOM   138   C  CG    . LEU A 1 27  ? 111.840 123.916 142.039 1.00 30.00  ? 27   LEU A CG    1 
ATOM   139   C  CD1   . LEU A 1 27  ? 111.445 125.315 142.462 1.00 30.00  ? 27   LEU A CD1   1 
ATOM   140   C  CD2   . LEU A 1 27  ? 111.113 123.512 140.776 1.00 30.00  ? 27   LEU A CD2   1 
ATOM   141   N  N     . ILE A 1 28  ? 115.789 122.987 139.727 1.00 34.39  ? 28   ILE A N     1 
ATOM   142   C  CA    . ILE A 1 28  ? 116.352 123.377 138.439 1.00 30.22  ? 28   ILE A CA    1 
ATOM   143   C  C     . ILE A 1 28  ? 116.124 122.291 137.395 1.00 36.83  ? 28   ILE A C     1 
ATOM   144   O  O     . ILE A 1 28  ? 115.922 122.595 136.217 1.00 47.10  ? 28   ILE A O     1 
ATOM   145   C  CB    . ILE A 1 28  ? 117.843 123.740 138.584 1.00 30.99  ? 28   ILE A CB    1 
ATOM   146   C  CG1   . ILE A 1 28  ? 118.366 124.387 137.302 1.00 28.48  ? 28   ILE A CG1   1 
ATOM   147   C  CG2   . ILE A 1 28  ? 118.677 122.526 138.954 1.00 32.30  ? 28   ILE A CG2   1 
ATOM   148   C  CD1   . ILE A 1 28  ? 119.787 124.877 137.403 1.00 26.41  ? 28   ILE A CD1   1 
ATOM   149   N  N     . GLU A 1 29  ? 116.106 121.021 137.804 1.00 39.72  ? 29   GLU A N     1 
ATOM   150   C  CA    . GLU A 1 29  ? 115.853 119.937 136.860 1.00 40.03  ? 29   GLU A CA    1 
ATOM   151   C  C     . GLU A 1 29  ? 114.446 120.028 136.278 1.00 48.53  ? 29   GLU A C     1 
ATOM   152   O  O     . GLU A 1 29  ? 114.263 120.035 135.054 1.00 50.42  ? 29   GLU A O     1 
ATOM   153   C  CB    . GLU A 1 29  ? 116.069 118.595 137.558 1.00 40.55  ? 29   GLU A CB    1 
ATOM   154   C  CG    . GLU A 1 29  ? 115.837 117.386 136.681 1.00 45.76  ? 29   GLU A CG    1 
ATOM   155   C  CD    . GLU A 1 29  ? 116.130 116.091 137.405 1.00 52.17  ? 29   GLU A CD    1 
ATOM   156   O  OE1   . GLU A 1 29  ? 116.564 116.153 138.574 1.00 48.25  ? 29   GLU A OE1   1 
ATOM   157   O  OE2   . GLU A 1 29  ? 115.927 115.014 136.809 1.00 50.17  ? 29   GLU A OE2   1 
ATOM   158   N  N     . PHE A 1 30  ? 113.438 120.125 137.148 1.00 53.04  ? 30   PHE A N     1 
ATOM   159   C  CA    . PHE A 1 30  ? 112.056 120.220 136.689 1.00 48.99  ? 30   PHE A CA    1 
ATOM   160   C  C     . PHE A 1 30  ? 111.823 121.493 135.881 1.00 46.41  ? 30   PHE A C     1 
ATOM   161   O  O     . PHE A 1 30  ? 111.135 121.472 134.851 1.00 51.26  ? 30   PHE A O     1 
ATOM   162   C  CB    . PHE A 1 30  ? 111.116 120.158 137.894 1.00 49.13  ? 30   PHE A CB    1 
ATOM   163   C  CG    . PHE A 1 30  ? 109.682 120.416 137.559 1.00 50.86  ? 30   PHE A CG    1 
ATOM   164   C  CD1   . PHE A 1 30  ? 108.928 119.457 136.913 1.00 53.23  ? 30   PHE A CD1   1 
ATOM   165   C  CD2   . PHE A 1 30  ? 109.085 121.615 137.899 1.00 53.24  ? 30   PHE A CD2   1 
ATOM   166   C  CE1   . PHE A 1 30  ? 107.610 119.690 136.604 1.00 54.17  ? 30   PHE A CE1   1 
ATOM   167   C  CE2   . PHE A 1 30  ? 107.766 121.853 137.592 1.00 53.78  ? 30   PHE A CE2   1 
ATOM   168   C  CZ    . PHE A 1 30  ? 107.030 120.889 136.943 1.00 54.49  ? 30   PHE A CZ    1 
ATOM   169   N  N     . LEU A 1 31  ? 112.398 122.610 136.331 1.00 38.33  ? 31   LEU A N     1 
ATOM   170   C  CA    . LEU A 1 31  ? 112.229 123.872 135.619 1.00 37.92  ? 31   LEU A CA    1 
ATOM   171   C  C     . LEU A 1 31  ? 112.880 123.834 134.241 1.00 36.99  ? 31   LEU A C     1 
ATOM   172   O  O     . LEU A 1 31  ? 112.295 124.314 133.265 1.00 39.85  ? 31   LEU A O     1 
ATOM   173   C  CB    . LEU A 1 31  ? 112.789 125.019 136.455 1.00 37.72  ? 31   LEU A CB    1 
ATOM   174   C  CG    . LEU A 1 31  ? 111.942 125.442 137.652 1.00 34.68  ? 31   LEU A CG    1 
ATOM   175   C  CD1   . LEU A 1 31  ? 112.593 126.605 138.368 1.00 38.30  ? 31   LEU A CD1   1 
ATOM   176   C  CD2   . LEU A 1 31  ? 110.545 125.807 137.202 1.00 38.83  ? 31   LEU A CD2   1 
ATOM   177   N  N     . ARG A 1 32  ? 114.086 123.269 134.135 1.00 33.97  ? 32   ARG A N     1 
ATOM   178   C  CA    . ARG A 1 32  ? 114.717 123.111 132.830 1.00 37.26  ? 32   ARG A CA    1 
ATOM   179   C  C     . ARG A 1 32  ? 113.930 122.160 131.945 1.00 43.98  ? 32   ARG A C     1 
ATOM   180   O  O     . ARG A 1 32  ? 113.972 122.280 130.716 1.00 44.84  ? 32   ARG A O     1 
ATOM   181   C  CB    . ARG A 1 32  ? 116.148 122.605 132.988 1.00 32.21  ? 32   ARG A CB    1 
ATOM   182   C  CG    . ARG A 1 32  ? 117.168 123.670 133.308 1.00 26.41  ? 32   ARG A CG    1 
ATOM   183   C  CD    . ARG A 1 32  ? 118.549 123.056 133.356 1.00 29.83  ? 32   ARG A CD    1 
ATOM   184   N  NE    . ARG A 1 32  ? 119.585 124.023 133.686 1.00 33.50  ? 32   ARG A NE    1 
ATOM   185   C  CZ    . ARG A 1 32  ? 120.825 123.696 134.018 1.00 36.63  ? 32   ARG A CZ    1 
ATOM   186   N  NH1   . ARG A 1 32  ? 121.212 122.434 134.088 1.00 37.27  ? 32   ARG A NH1   1 
ATOM   187   N  NH2   . ARG A 1 32  ? 121.698 124.658 134.291 1.00 37.77  ? 32   ARG A NH2   1 
ATOM   188   N  N     . GLU A 1 33  ? 113.230 121.197 132.545 1.00 49.43  ? 33   GLU A N     1 
ATOM   189   C  CA    . GLU A 1 33  ? 112.315 120.376 131.762 1.00 49.46  ? 33   GLU A CA    1 
ATOM   190   C  C     . GLU A 1 33  ? 111.173 121.211 131.194 1.00 49.30  ? 33   GLU A C     1 
ATOM   191   O  O     . GLU A 1 33  ? 110.797 121.045 130.028 1.00 50.20  ? 33   GLU A O     1 
ATOM   192   C  CB    . GLU A 1 33  ? 111.770 119.229 132.611 1.00 45.02  ? 33   GLU A CB    1 
ATOM   193   C  CG    . GLU A 1 33  ? 112.777 118.138 132.899 1.00 47.81  ? 33   GLU A CG    1 
ATOM   194   C  CD    . GLU A 1 33  ? 112.211 117.052 133.786 1.00 53.82  ? 33   GLU A CD    1 
ATOM   195   O  OE1   . GLU A 1 33  ? 111.027 117.153 134.165 1.00 52.26  ? 33   GLU A OE1   1 
ATOM   196   O  OE2   . GLU A 1 33  ? 112.949 116.098 134.107 1.00 54.58  ? 33   GLU A OE2   1 
ATOM   197   N  N     . ILE A 1 34  ? 110.611 122.117 131.993 1.00 44.73  ? 34   ILE A N     1 
ATOM   198   C  CA    . ILE A 1 34  ? 109.434 122.844 131.521 1.00 44.76  ? 34   ILE A CA    1 
ATOM   199   C  C     . ILE A 1 34  ? 109.778 124.172 130.842 1.00 46.52  ? 34   ILE A C     1 
ATOM   200   O  O     . ILE A 1 34  ? 109.108 124.557 129.879 1.00 51.70  ? 34   ILE A O     1 
ATOM   201   C  CB    . ILE A 1 34  ? 108.423 123.057 132.662 1.00 47.07  ? 34   ILE A CB    1 
ATOM   202   C  CG1   . ILE A 1 34  ? 109.033 123.870 133.802 1.00 44.63  ? 34   ILE A CG1   1 
ATOM   203   C  CG2   . ILE A 1 34  ? 107.908 121.720 133.168 1.00 45.77  ? 34   ILE A CG2   1 
ATOM   204   C  CD1   . ILE A 1 34  ? 108.038 124.247 134.870 1.00 48.61  ? 34   ILE A CD1   1 
ATOM   205   N  N     . THR A 1 35  ? 110.798 124.889 131.306 1.00 42.73  ? 35   THR A N     1 
ATOM   206   C  CA    . THR A 1 35  ? 111.133 126.185 130.724 1.00 44.82  ? 35   THR A CA    1 
ATOM   207   C  C     . THR A 1 35  ? 112.645 126.269 130.552 1.00 45.42  ? 35   THR A C     1 
ATOM   208   O  O     . THR A 1 35  ? 113.367 125.279 130.706 1.00 45.37  ? 35   THR A O     1 
ATOM   209   C  CB    . THR A 1 35  ? 110.588 127.337 131.580 1.00 45.43  ? 35   THR A CB    1 
ATOM   210   O  OG1   . THR A 1 35  ? 110.975 128.588 130.998 1.00 45.03  ? 35   THR A OG1   1 
ATOM   211   C  CG2   . THR A 1 35  ? 111.129 127.265 132.994 1.00 42.62  ? 35   THR A CG2   1 
ATOM   212   N  N     . HIS A 1 36  ? 113.125 127.461 130.215 1.00 38.88  ? 36   HIS A N     1 
ATOM   213   C  CA    . HIS A 1 36  ? 114.548 127.716 130.029 1.00 36.38  ? 36   HIS A CA    1 
ATOM   214   C  C     . HIS A 1 36  ? 115.092 128.346 131.303 1.00 39.56  ? 36   HIS A C     1 
ATOM   215   O  O     . HIS A 1 36  ? 114.729 129.473 131.652 1.00 36.47  ? 36   HIS A O     1 
ATOM   216   C  CB    . HIS A 1 36  ? 114.791 128.624 128.828 1.00 40.85  ? 36   HIS A CB    1 
ATOM   217   C  CG    . HIS A 1 36  ? 116.158 129.232 128.797 1.00 41.75  ? 36   HIS A CG    1 
ATOM   218   N  ND1   . HIS A 1 36  ? 117.266 128.552 128.340 1.00 41.01  ? 36   HIS A ND1   1 
ATOM   219   C  CD2   . HIS A 1 36  ? 116.597 130.458 129.168 1.00 36.75  ? 36   HIS A CD2   1 
ATOM   220   C  CE1   . HIS A 1 36  ? 118.327 129.333 128.427 1.00 37.87  ? 36   HIS A CE1   1 
ATOM   221   N  NE2   . HIS A 1 36  ? 117.949 130.496 128.927 1.00 34.48  ? 36   HIS A NE2   1 
ATOM   222   N  N     . VAL A 1 37  ? 115.950 127.612 132.000 1.00 42.17  ? 37   VAL A N     1 
ATOM   223   C  CA    . VAL A 1 37  ? 116.625 128.131 133.184 1.00 30.55  ? 37   VAL A CA    1 
ATOM   224   C  C     . VAL A 1 37  ? 118.125 128.002 132.954 1.00 25.74  ? 37   VAL A C     1 
ATOM   225   O  O     . VAL A 1 37  ? 118.661 126.886 132.988 1.00 34.82  ? 37   VAL A O     1 
ATOM   226   C  CB    . VAL A 1 37  ? 116.177 127.393 134.454 1.00 30.59  ? 37   VAL A CB    1 
ATOM   227   C  CG1   . VAL A 1 37  ? 116.771 128.043 135.675 1.00 32.64  ? 37   VAL A CG1   1 
ATOM   228   C  CG2   . VAL A 1 37  ? 114.669 127.386 134.552 1.00 38.59  ? 37   VAL A CG2   1 
ATOM   229   N  N     . PRO A 1 38  ? 118.832 129.096 132.689 1.00 15.10  ? 38   PRO A N     1 
ATOM   230   C  CA    . PRO A 1 38  ? 120.279 129.002 132.478 1.00 26.23  ? 38   PRO A CA    1 
ATOM   231   C  C     . PRO A 1 38  ? 121.014 128.618 133.751 1.00 25.20  ? 38   PRO A C     1 
ATOM   232   O  O     . PRO A 1 38  ? 120.564 128.885 134.867 1.00 33.42  ? 38   PRO A O     1 
ATOM   233   C  CB    . PRO A 1 38  ? 120.663 130.412 132.016 1.00 25.20  ? 38   PRO A CB    1 
ATOM   234   C  CG    . PRO A 1 38  ? 119.586 131.286 132.534 1.00 21.36  ? 38   PRO A CG    1 
ATOM   235   C  CD    . PRO A 1 38  ? 118.334 130.467 132.501 1.00 24.28  ? 38   PRO A CD    1 
ATOM   236   N  N     . GLY A 1 39  ? 122.163 127.976 133.568 1.00 19.09  ? 39   GLY A N     1 
ATOM   237   C  CA    . GLY A 1 39  ? 123.001 127.591 134.683 1.00 8.66   ? 39   GLY A CA    1 
ATOM   238   C  C     . GLY A 1 39  ? 124.170 126.727 134.263 1.00 19.99  ? 39   GLY A C     1 
ATOM   239   O  O     . GLY A 1 39  ? 124.013 125.802 133.462 1.00 30.86  ? 39   GLY A O     1 
ATOM   240   N  N     . PHE A 1 40  ? 125.348 127.016 134.808 1.00 26.66  ? 40   PHE A N     1 
ATOM   241   C  CA    . PHE A 1 40  ? 126.575 126.310 134.466 1.00 11.81  ? 40   PHE A CA    1 
ATOM   242   C  C     . PHE A 1 40  ? 126.943 125.222 135.464 1.00 10.83  ? 40   PHE A C     1 
ATOM   243   O  O     . PHE A 1 40  ? 127.398 124.149 135.062 1.00 24.25  ? 40   PHE A O     1 
ATOM   244   C  CB    . PHE A 1 40  ? 127.746 127.294 134.375 1.00 7.08   ? 40   PHE A CB    1 
ATOM   245   C  CG    . PHE A 1 40  ? 127.593 128.339 133.309 1.00 14.41  ? 40   PHE A CG    1 
ATOM   246   C  CD1   . PHE A 1 40  ? 126.929 128.060 132.131 1.00 19.94  ? 40   PHE A CD1   1 
ATOM   247   C  CD2   . PHE A 1 40  ? 128.132 129.602 133.487 1.00 18.36  ? 40   PHE A CD2   1 
ATOM   248   C  CE1   . PHE A 1 40  ? 126.802 129.024 131.154 1.00 16.44  ? 40   PHE A CE1   1 
ATOM   249   C  CE2   . PHE A 1 40  ? 128.004 130.568 132.515 1.00 19.21  ? 40   PHE A CE2   1 
ATOM   250   C  CZ    . PHE A 1 40  ? 127.339 130.278 131.348 1.00 17.43  ? 40   PHE A CZ    1 
ATOM   251   N  N     . CYS A 1 41  ? 126.749 125.472 136.758 1.00 13.80  ? 41   CYS A N     1 
ATOM   252   C  CA    . CYS A 1 41  ? 127.415 124.718 137.812 1.00 26.98  ? 41   CYS A CA    1 
ATOM   253   C  C     . CYS A 1 41  ? 126.513 123.686 138.477 1.00 23.80  ? 41   CYS A C     1 
ATOM   254   O  O     . CYS A 1 41  ? 126.685 123.396 139.664 1.00 32.38  ? 41   CYS A O     1 
ATOM   255   C  CB    . CYS A 1 41  ? 127.969 125.675 138.865 1.00 25.14  ? 41   CYS A CB    1 
ATOM   256   S  SG    . CYS A 1 41  ? 126.729 126.729 139.637 1.00 24.50  ? 41   CYS A SG    1 
ATOM   257   N  N     . TYR A 1 42  ? 125.562 123.115 137.751 1.00 26.85  ? 42   TYR A N     1 
ATOM   258   C  CA    . TYR A 1 42  ? 124.711 122.088 138.327 1.00 26.76  ? 42   TYR A CA    1 
ATOM   259   C  C     . TYR A 1 42  ? 124.845 120.780 137.564 1.00 37.91  ? 42   TYR A C     1 
ATOM   260   O  O     . TYR A 1 42  ? 124.878 120.763 136.330 1.00 41.38  ? 42   TYR A O     1 
ATOM   261   C  CB    . TYR A 1 42  ? 123.240 122.501 138.358 1.00 20.24  ? 42   TYR A CB    1 
ATOM   262   C  CG    . TYR A 1 42  ? 122.389 121.444 139.020 1.00 24.25  ? 42   TYR A CG    1 
ATOM   263   C  CD1   . TYR A 1 42  ? 122.400 121.283 140.397 1.00 28.84  ? 42   TYR A CD1   1 
ATOM   264   C  CD2   . TYR A 1 42  ? 121.608 120.580 138.267 1.00 32.38  ? 42   TYR A CD2   1 
ATOM   265   C  CE1   . TYR A 1 42  ? 121.643 120.309 141.007 1.00 30.54  ? 42   TYR A CE1   1 
ATOM   266   C  CE2   . TYR A 1 42  ? 120.847 119.602 138.869 1.00 34.07  ? 42   TYR A CE2   1 
ATOM   267   C  CZ    . TYR A 1 42  ? 120.869 119.471 140.238 1.00 31.31  ? 42   TYR A CZ    1 
ATOM   268   O  OH    . TYR A 1 42  ? 120.109 118.499 140.842 1.00 35.47  ? 42   TYR A OH    1 
ATOM   269   N  N     . THR A 1 43  ? 124.928 119.690 138.321 1.00 28.69  ? 43   THR A N     1 
ATOM   270   C  CA    . THR A 1 43  ? 124.807 118.337 137.802 1.00 23.25  ? 43   THR A CA    1 
ATOM   271   C  C     . THR A 1 43  ? 124.360 117.438 138.944 1.00 27.65  ? 43   THR A C     1 
ATOM   272   O  O     . THR A 1 43  ? 124.621 117.727 140.114 1.00 32.37  ? 43   THR A O     1 
ATOM   273   C  CB    . THR A 1 43  ? 126.121 117.837 137.197 1.00 27.67  ? 43   THR A CB    1 
ATOM   274   O  OG1   . THR A 1 43  ? 126.163 116.407 137.249 1.00 37.60  ? 43   THR A OG1   1 
ATOM   275   C  CG2   . THR A 1 43  ? 127.292 118.405 137.953 1.00 30.21  ? 43   THR A CG2   1 
ATOM   276   N  N     . GLU A 1 44  ? 123.677 116.349 138.592 1.00 25.99  ? 44   GLU A N     1 
ATOM   277   C  CA    . GLU A 1 44  ? 123.118 115.466 139.611 1.00 26.12  ? 44   GLU A CA    1 
ATOM   278   C  C     . GLU A 1 44  ? 124.200 114.714 140.373 1.00 29.36  ? 44   GLU A C     1 
ATOM   279   O  O     . GLU A 1 44  ? 123.961 114.264 141.498 1.00 31.89  ? 44   GLU A O     1 
ATOM   280   C  CB    . GLU A 1 44  ? 122.150 114.476 138.967 1.00 31.02  ? 44   GLU A CB    1 
ATOM   281   C  CG    . GLU A 1 44  ? 121.030 115.128 138.183 1.00 33.72  ? 44   GLU A CG    1 
ATOM   282   C  CD    . GLU A 1 44  ? 120.036 115.850 139.071 1.00 38.45  ? 44   GLU A CD    1 
ATOM   283   O  OE1   . GLU A 1 44  ? 119.919 115.485 140.260 1.00 38.86  ? 44   GLU A OE1   1 
ATOM   284   O  OE2   . GLU A 1 44  ? 119.370 116.786 138.580 1.00 36.51  ? 44   GLU A OE2   1 
ATOM   285   N  N     . ALA A 1 45  ? 125.388 114.573 139.782 1.00 28.79  ? 45   ALA A N     1 
ATOM   286   C  CA    . ALA A 1 45  ? 126.431 113.742 140.373 1.00 32.05  ? 45   ALA A CA    1 
ATOM   287   C  C     . ALA A 1 45  ? 126.942 114.308 141.690 1.00 28.19  ? 45   ALA A C     1 
ATOM   288   O  O     . ALA A 1 45  ? 127.307 113.542 142.589 1.00 28.78  ? 45   ALA A O     1 
ATOM   289   C  CB    . ALA A 1 45  ? 127.585 113.576 139.388 1.00 26.78  ? 45   ALA A CB    1 
ATOM   290   N  N     . PHE A 1 46  ? 126.984 115.628 141.826 1.00 24.33  ? 46   PHE A N     1 
ATOM   291   C  CA    . PHE A 1 46  ? 127.460 116.269 143.040 1.00 26.98  ? 46   PHE A CA    1 
ATOM   292   C  C     . PHE A 1 46  ? 126.332 117.071 143.675 1.00 29.97  ? 46   PHE A C     1 
ATOM   293   O  O     . PHE A 1 46  ? 125.242 117.211 143.116 1.00 27.15  ? 46   PHE A O     1 
ATOM   294   C  CB    . PHE A 1 46  ? 128.665 117.175 142.753 1.00 27.34  ? 46   PHE A CB    1 
ATOM   295   C  CG    . PHE A 1 46  ? 129.464 116.762 141.549 1.00 29.16  ? 46   PHE A CG    1 
ATOM   296   C  CD1   . PHE A 1 46  ? 130.162 115.567 141.535 1.00 29.24  ? 46   PHE A CD1   1 
ATOM   297   C  CD2   . PHE A 1 46  ? 129.525 117.577 140.434 1.00 27.80  ? 46   PHE A CD2   1 
ATOM   298   C  CE1   . PHE A 1 46  ? 130.894 115.193 140.423 1.00 28.89  ? 46   PHE A CE1   1 
ATOM   299   C  CE2   . PHE A 1 46  ? 130.255 117.207 139.323 1.00 22.09  ? 46   PHE A CE2   1 
ATOM   300   C  CZ    . PHE A 1 46  ? 130.935 116.016 139.315 1.00 23.85  ? 46   PHE A CZ    1 
ATOM   301   N  N     . ASP A 1 47  ? 126.609 117.597 144.865 1.00 26.41  ? 47   ASP A N     1 
ATOM   302   C  CA    . ASP A 1 47  ? 125.649 118.428 145.566 1.00 26.00  ? 47   ASP A CA    1 
ATOM   303   C  C     . ASP A 1 47  ? 125.438 119.736 144.808 1.00 29.59  ? 47   ASP A C     1 
ATOM   304   O  O     . ASP A 1 47  ? 126.262 120.116 143.973 1.00 24.50  ? 47   ASP A O     1 
ATOM   305   C  CB    . ASP A 1 47  ? 126.133 118.710 146.987 1.00 18.98  ? 47   ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 47  ? 125.936 117.530 147.914 1.00 33.46  ? 47   ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 47  ? 125.511 116.459 147.432 1.00 33.12  ? 47   ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 47  ? 126.201 117.674 149.125 1.00 34.80  ? 47   ASP A OD2   1 
ATOM   309   N  N     . PRO A 1 48  ? 124.322 120.425 145.054 1.00 31.99  ? 48   PRO A N     1 
ATOM   310   C  CA    . PRO A 1 48  ? 124.094 121.709 144.381 1.00 23.01  ? 48   PRO A CA    1 
ATOM   311   C  C     . PRO A 1 48  ? 125.209 122.705 144.663 1.00 22.53  ? 48   PRO A C     1 
ATOM   312   O  O     . PRO A 1 48  ? 125.751 122.777 145.767 1.00 20.12  ? 48   PRO A O     1 
ATOM   313   C  CB    . PRO A 1 48  ? 122.751 122.181 144.954 1.00 16.28  ? 48   PRO A CB    1 
ATOM   314   C  CG    . PRO A 1 48  ? 122.472 121.290 146.121 1.00 28.08  ? 48   PRO A CG    1 
ATOM   315   C  CD    . PRO A 1 48  ? 123.131 119.996 145.803 1.00 29.53  ? 48   PRO A CD    1 
ATOM   316   N  N     . TYR A 1 49  ? 125.553 123.464 143.631 1.00 22.41  ? 49   TYR A N     1 
ATOM   317   C  CA    . TYR A 1 49  ? 126.627 124.443 143.658 1.00 14.14  ? 49   TYR A CA    1 
ATOM   318   C  C     . TYR A 1 49  ? 126.033 125.788 143.272 1.00 31.87  ? 49   TYR A C     1 
ATOM   319   O  O     . TYR A 1 49  ? 125.243 125.869 142.327 1.00 32.19  ? 49   TYR A O     1 
ATOM   320   C  CB    . TYR A 1 49  ? 127.735 124.033 142.684 1.00 19.84  ? 49   TYR A CB    1 
ATOM   321   C  CG    . TYR A 1 49  ? 129.155 124.284 143.136 1.00 17.41  ? 49   TYR A CG    1 
ATOM   322   C  CD1   . TYR A 1 49  ? 129.712 123.567 144.183 1.00 21.23  ? 49   TYR A CD1   1 
ATOM   323   C  CD2   . TYR A 1 49  ? 129.955 125.203 142.477 1.00 20.67  ? 49   TYR A CD2   1 
ATOM   324   C  CE1   . TYR A 1 49  ? 131.018 123.785 144.581 1.00 20.28  ? 49   TYR A CE1   1 
ATOM   325   C  CE2   . TYR A 1 49  ? 131.256 125.429 142.868 1.00 19.60  ? 49   TYR A CE2   1 
ATOM   326   C  CZ    . TYR A 1 49  ? 131.784 124.718 143.917 1.00 20.82  ? 49   TYR A CZ    1 
ATOM   327   O  OH    . TYR A 1 49  ? 133.083 124.946 144.300 1.00 24.73  ? 49   TYR A OH    1 
ATOM   328   N  N     . GLY A 1 50  ? 126.394 126.835 144.006 1.00 30.52  ? 50   GLY A N     1 
ATOM   329   C  CA    . GLY A 1 50  ? 125.855 128.152 143.729 1.00 21.21  ? 50   GLY A CA    1 
ATOM   330   C  C     . GLY A 1 50  ? 126.876 129.127 143.181 1.00 24.61  ? 50   GLY A C     1 
ATOM   331   O  O     . GLY A 1 50  ? 126.911 130.289 143.594 1.00 33.29  ? 50   GLY A O     1 
ATOM   332   N  N     . SER A 1 51  ? 127.719 128.672 142.255 1.00 1.64   ? 51   SER A N     1 
ATOM   333   C  CA    . SER A 1 51  ? 128.846 129.468 141.793 1.00 3.54   ? 51   SER A CA    1 
ATOM   334   C  C     . SER A 1 51  ? 128.569 130.269 140.526 1.00 25.91  ? 51   SER A C     1 
ATOM   335   O  O     . SER A 1 51  ? 129.423 131.067 140.128 1.00 33.56  ? 51   SER A O     1 
ATOM   336   C  CB    . SER A 1 51  ? 130.065 128.571 141.560 1.00 15.01  ? 51   SER A CB    1 
ATOM   337   O  OG    . SER A 1 51  ? 129.858 127.700 140.466 1.00 32.90  ? 51   SER A OG    1 
ATOM   338   N  N     . CYS A 1 52  ? 127.421 130.087 139.877 1.00 28.95  ? 52   CYS A N     1 
ATOM   339   C  CA    . CYS A 1 52  ? 127.117 130.850 138.672 1.00 13.14  ? 52   CYS A CA    1 
ATOM   340   C  C     . CYS A 1 52  ? 125.954 131.814 138.836 1.00 20.53  ? 52   CYS A C     1 
ATOM   341   O  O     . CYS A 1 52  ? 125.927 132.842 138.157 1.00 27.37  ? 52   CYS A O     1 
ATOM   342   C  CB    . CYS A 1 52  ? 126.828 129.910 137.493 1.00 12.27  ? 52   CYS A CB    1 
ATOM   343   S  SG    . CYS A 1 52  ? 125.172 129.210 137.436 1.00 26.53  ? 52   CYS A SG    1 
ATOM   344   N  N     . ARG A 1 53  ? 125.004 131.507 139.723 1.00 23.55  ? 53   ARG A N     1 
ATOM   345   C  CA    . ARG A 1 53  ? 123.903 132.406 140.081 1.00 16.70  ? 53   ARG A CA    1 
ATOM   346   C  C     . ARG A 1 53  ? 123.049 132.788 138.875 1.00 17.67  ? 53   ARG A C     1 
ATOM   347   O  O     . ARG A 1 53  ? 122.544 133.909 138.795 1.00 22.00  ? 53   ARG A O     1 
ATOM   348   C  CB    . ARG A 1 53  ? 124.426 133.663 140.780 1.00 15.41  ? 53   ARG A CB    1 
ATOM   349   C  CG    . ARG A 1 53  ? 125.470 133.396 141.848 1.00 21.88  ? 53   ARG A CG    1 
ATOM   350   C  CD    . ARG A 1 53  ? 124.856 133.246 143.225 1.00 21.67  ? 53   ARG A CD    1 
ATOM   351   N  NE    . ARG A 1 53  ? 124.247 131.944 143.450 1.00 25.85  ? 53   ARG A NE    1 
ATOM   352   C  CZ    . ARG A 1 53  ? 123.393 131.685 144.429 1.00 26.43  ? 53   ARG A CZ    1 
ATOM   353   N  NH1   . ARG A 1 53  ? 122.979 132.635 145.250 1.00 32.98  ? 53   ARG A NH1   1 
ATOM   354   N  NH2   . ARG A 1 53  ? 122.945 130.445 144.590 1.00 22.73  ? 53   ARG A NH2   1 
ATOM   355   N  N     . LEU A 1 54  ? 122.869 131.861 137.936 1.00 18.04  ? 54   LEU A N     1 
ATOM   356   C  CA    . LEU A 1 54  ? 122.114 132.124 136.718 1.00 17.00  ? 54   LEU A CA    1 
ATOM   357   C  C     . LEU A 1 54  ? 120.727 131.497 136.713 1.00 21.57  ? 54   LEU A C     1 
ATOM   358   O  O     . LEU A 1 54  ? 119.909 131.855 135.861 1.00 30.88  ? 54   LEU A O     1 
ATOM   359   C  CB    . LEU A 1 54  ? 122.890 131.625 135.494 1.00 21.21  ? 54   LEU A CB    1 
ATOM   360   C  CG    . LEU A 1 54  ? 123.992 132.531 134.956 1.00 19.91  ? 54   LEU A CG    1 
ATOM   361   C  CD1   . LEU A 1 54  ? 124.660 131.883 133.765 1.00 22.52  ? 54   LEU A CD1   1 
ATOM   362   C  CD2   . LEU A 1 54  ? 123.410 133.869 134.571 1.00 21.89  ? 54   LEU A CD2   1 
ATOM   363   N  N     . CYS A 1 55  ? 120.438 130.586 137.640 1.00 16.85  ? 55   CYS A N     1 
ATOM   364   C  CA    . CYS A 1 55  ? 119.164 129.879 137.677 1.00 17.64  ? 55   CYS A CA    1 
ATOM   365   C  C     . CYS A 1 55  ? 118.132 130.582 138.545 1.00 30.20  ? 55   CYS A C     1 
ATOM   366   O  O     . CYS A 1 55  ? 117.277 129.921 139.147 1.00 34.64  ? 55   CYS A O     1 
ATOM   367   C  CB    . CYS A 1 55  ? 119.376 128.447 138.159 1.00 21.04  ? 55   CYS A CB    1 
ATOM   368   S  SG    . CYS A 1 55  ? 120.234 128.331 139.724 1.00 28.30  ? 55   CYS A SG    1 
ATOM   369   N  N     . LEU A 1 56  ? 118.201 131.907 138.625 1.00 32.72  ? 56   LEU A N     1 
ATOM   370   C  CA    . LEU A 1 56  ? 117.364 132.669 139.537 1.00 25.97  ? 56   LEU A CA    1 
ATOM   371   C  C     . LEU A 1 56  ? 115.888 132.543 139.179 1.00 28.30  ? 56   LEU A C     1 
ATOM   372   O  O     . LEU A 1 56  ? 115.513 132.494 138.005 1.00 28.23  ? 56   LEU A O     1 
ATOM   373   C  CB    . LEU A 1 56  ? 117.779 134.137 139.515 1.00 19.41  ? 56   LEU A CB    1 
ATOM   374   C  CG    . LEU A 1 56  ? 119.281 134.404 139.601 1.00 21.34  ? 56   LEU A CG    1 
ATOM   375   C  CD1   . LEU A 1 56  ? 119.590 135.802 139.115 1.00 30.22  ? 56   LEU A CD1   1 
ATOM   376   C  CD2   . LEU A 1 56  ? 119.781 134.216 141.018 1.00 23.69  ? 56   LEU A CD2   1 
ATOM   377   N  N     . VAL A 1 57  ? 115.051 132.479 140.212 1.00 35.39  ? 57   VAL A N     1 
ATOM   378   C  CA    . VAL A 1 57  ? 113.605 132.516 140.072 1.00 41.20  ? 57   VAL A CA    1 
ATOM   379   C  C     . VAL A 1 57  ? 113.069 133.504 141.097 1.00 42.75  ? 57   VAL A C     1 
ATOM   380   O  O     . VAL A 1 57  ? 113.745 133.861 142.063 1.00 40.13  ? 57   VAL A O     1 
ATOM   381   C  CB    . VAL A 1 57  ? 112.950 131.129 140.257 1.00 36.12  ? 57   VAL A CB    1 
ATOM   382   C  CG1   . VAL A 1 57  ? 113.329 130.201 139.120 1.00 37.70  ? 57   VAL A CG1   1 
ATOM   383   C  CG2   . VAL A 1 57  ? 113.349 130.523 141.588 1.00 34.63  ? 57   VAL A CG2   1 
ATOM   384   N  N     . GLN A 1 58  ? 111.842 133.957 140.872 1.00 50.34  ? 58   GLN A N     1 
ATOM   385   C  CA    . GLN A 1 58  ? 111.179 134.868 141.794 1.00 49.94  ? 58   GLN A CA    1 
ATOM   386   C  C     . GLN A 1 58  ? 110.265 134.068 142.710 1.00 54.07  ? 58   GLN A C     1 
ATOM   387   O  O     . GLN A 1 58  ? 109.329 133.409 142.244 1.00 59.12  ? 58   GLN A O     1 
ATOM   388   C  CB    . GLN A 1 58  ? 110.393 135.942 141.047 1.00 52.68  ? 58   GLN A CB    1 
ATOM   389   C  CG    . GLN A 1 58  ? 109.720 136.940 141.964 1.00 52.29  ? 58   GLN A CG    1 
ATOM   390   C  CD    . GLN A 1 58  ? 109.586 138.304 141.332 1.00 51.25  ? 58   GLN A CD    1 
ATOM   391   O  OE1   . GLN A 1 58  ? 110.159 138.569 140.277 1.00 49.83  ? 58   GLN A OE1   1 
ATOM   392   N  NE2   . GLN A 1 58  ? 108.828 139.182 141.975 1.00 48.32  ? 58   GLN A NE2   1 
ATOM   393   N  N     . THR A 1 59  ? 110.545 134.124 143.999 1.00 59.52  ? 59   THR A N     1 
ATOM   394   C  CA    . THR A 1 59  ? 109.802 133.453 145.046 1.00 60.38  ? 59   THR A CA    1 
ATOM   395   C  C     . THR A 1 59  ? 109.112 134.484 145.927 1.00 64.12  ? 59   THR A C     1 
ATOM   396   O  O     . THR A 1 59  ? 109.396 135.682 145.839 1.00 65.04  ? 59   THR A O     1 
ATOM   397   C  CB    . THR A 1 59  ? 110.749 132.585 145.885 1.00 63.15  ? 59   THR A CB    1 
ATOM   398   O  OG1   . THR A 1 59  ? 111.802 133.396 146.418 1.00 60.54  ? 59   THR A OG1   1 
ATOM   399   C  CG2   . THR A 1 59  ? 111.353 131.491 145.036 1.00 62.59  ? 59   THR A CG2   1 
ATOM   400   N  N     . PRO A 1 60  ? 108.165 134.058 146.769 1.00 70.15  ? 60   PRO A N     1 
ATOM   401   C  CA    . PRO A 1 60  ? 107.590 135.001 147.742 1.00 69.63  ? 60   PRO A CA    1 
ATOM   402   C  C     . PRO A 1 60  ? 108.616 135.634 148.666 1.00 67.98  ? 60   PRO A C     1 
ATOM   403   O  O     . PRO A 1 60  ? 108.454 136.800 149.044 1.00 67.06  ? 60   PRO A O     1 
ATOM   404   C  CB    . PRO A 1 60  ? 106.593 134.129 148.512 1.00 69.39  ? 60   PRO A CB    1 
ATOM   405   C  CG    . PRO A 1 60  ? 106.149 133.133 147.507 1.00 68.24  ? 60   PRO A CG    1 
ATOM   406   C  CD    . PRO A 1 60  ? 107.362 132.825 146.672 1.00 68.38  ? 60   PRO A CD    1 
ATOM   407   N  N     . ARG A 1 61  ? 109.673 134.911 149.037 1.00 71.63  ? 61   ARG A N     1 
ATOM   408   C  CA    . ARG A 1 61  ? 110.700 135.467 149.909 1.00 73.44  ? 61   ARG A CA    1 
ATOM   409   C  C     . ARG A 1 61  ? 111.713 136.329 149.170 1.00 73.57  ? 61   ARG A C     1 
ATOM   410   O  O     . ARG A 1 61  ? 112.559 136.952 149.819 1.00 72.82  ? 61   ARG A O     1 
ATOM   411   C  CB    . ARG A 1 61  ? 111.441 134.348 150.648 1.00 71.01  ? 61   ARG A CB    1 
ATOM   412   C  CG    . ARG A 1 61  ? 110.728 133.822 151.884 1.00 71.70  ? 61   ARG A CG    1 
ATOM   413   C  CD    . ARG A 1 61  ? 109.653 132.812 151.529 1.00 73.62  ? 61   ARG A CD    1 
ATOM   414   N  NE    . ARG A 1 61  ? 110.209 131.652 150.845 1.00 74.68  ? 61   ARG A NE    1 
ATOM   415   C  CZ    . ARG A 1 61  ? 109.505 130.594 150.471 1.00 74.56  ? 61   ARG A CZ    1 
ATOM   416   N  NH1   . ARG A 1 61  ? 108.204 130.516 150.696 1.00 73.81  ? 61   ARG A NH1   1 
ATOM   417   N  NH2   . ARG A 1 61  ? 110.121 129.589 149.858 1.00 75.24  ? 61   ARG A NH2   1 
ATOM   418   N  N     . GLY A 1 62  ? 111.658 136.379 147.844 1.00 59.90  ? 62   GLY A N     1 
ATOM   419   C  CA    . GLY A 1 62  ? 112.588 137.155 147.059 1.00 57.19  ? 62   GLY A CA    1 
ATOM   420   C  C     . GLY A 1 62  ? 113.119 136.334 145.909 1.00 56.64  ? 62   GLY A C     1 
ATOM   421   O  O     . GLY A 1 62  ? 112.526 135.325 145.515 1.00 56.49  ? 62   GLY A O     1 
ATOM   422   N  N     . ILE A 1 63  ? 114.247 136.769 145.369 1.00 44.34  ? 63   ILE A N     1 
ATOM   423   C  CA    . ILE A 1 63  ? 114.877 136.099 144.239 1.00 42.08  ? 63   ILE A CA    1 
ATOM   424   C  C     . ILE A 1 63  ? 115.929 135.138 144.772 1.00 38.08  ? 63   ILE A C     1 
ATOM   425   O  O     . ILE A 1 63  ? 116.800 135.530 145.556 1.00 43.23  ? 63   ILE A O     1 
ATOM   426   C  CB    . ILE A 1 63  ? 115.495 137.118 143.266 1.00 39.35  ? 63   ILE A CB    1 
ATOM   427   C  CG1   . ILE A 1 63  ? 114.413 137.777 142.407 1.00 30.49  ? 63   ILE A CG1   1 
ATOM   428   C  CG2   . ILE A 1 63  ? 116.537 136.458 142.382 1.00 42.69  ? 63   ILE A CG2   1 
ATOM   429   C  CD1   . ILE A 1 63  ? 113.755 138.979 143.041 1.00 41.02  ? 63   ILE A CD1   1 
ATOM   430   N  N     . THR A 1 64  ? 115.847 133.877 144.353 1.00 35.39  ? 64   THR A N     1 
ATOM   431   C  CA    . THR A 1 64  ? 116.782 132.866 144.818 1.00 39.14  ? 64   THR A CA    1 
ATOM   432   C  C     . THR A 1 64  ? 116.965 131.809 143.738 1.00 35.91  ? 64   THR A C     1 
ATOM   433   O  O     . THR A 1 64  ? 116.138 131.662 142.836 1.00 36.90  ? 64   THR A O     1 
ATOM   434   C  CB    . THR A 1 64  ? 116.311 132.227 146.126 1.00 42.02  ? 64   THR A CB    1 
ATOM   435   O  OG1   . THR A 1 64  ? 117.198 131.163 146.490 1.00 43.16  ? 64   THR A OG1   1 
ATOM   436   C  CG2   . THR A 1 64  ? 114.907 131.685 145.968 1.00 38.94  ? 64   THR A CG2   1 
ATOM   437   N  N     . THR A 1 65  ? 118.066 131.072 143.847 1.00 31.47  ? 65   THR A N     1 
ATOM   438   C  CA    . THR A 1 65  ? 118.464 130.132 142.811 1.00 29.46  ? 65   THR A CA    1 
ATOM   439   C  C     . THR A 1 65  ? 117.656 128.845 142.890 1.00 31.61  ? 65   THR A C     1 
ATOM   440   O  O     . THR A 1 65  ? 117.418 128.307 143.974 1.00 39.52  ? 65   THR A O     1 
ATOM   441   C  CB    . THR A 1 65  ? 119.956 129.822 142.922 1.00 23.14  ? 65   THR A CB    1 
ATOM   442   O  OG1   . THR A 1 65  ? 120.330 129.725 144.300 1.00 22.79  ? 65   THR A OG1   1 
ATOM   443   C  CG2   . THR A 1 65  ? 120.766 130.912 142.252 1.00 35.26  ? 65   THR A CG2   1 
ATOM   444   N  N     . SER A 1 66  ? 117.243 128.349 141.724 1.00 28.72  ? 66   SER A N     1 
ATOM   445   C  CA    . SER A 1 66  ? 116.379 127.179 141.659 1.00 26.31  ? 66   SER A CA    1 
ATOM   446   C  C     . SER A 1 66  ? 117.119 125.871 141.899 1.00 23.60  ? 66   SER A C     1 
ATOM   447   O  O     . SER A 1 66  ? 116.480 124.876 142.254 1.00 27.90  ? 66   SER A O     1 
ATOM   448   C  CB    . SER A 1 66  ? 115.670 127.125 140.306 1.00 28.51  ? 66   SER A CB    1 
ATOM   449   O  OG    . SER A 1 66  ? 116.601 127.035 139.245 1.00 33.89  ? 66   SER A OG    1 
ATOM   450   N  N     . CYS A 1 67  ? 118.440 125.840 141.713 1.00 28.50  ? 67   CYS A N     1 
ATOM   451   C  CA    . CYS A 1 67  ? 119.175 124.605 141.965 1.00 28.64  ? 67   CYS A CA    1 
ATOM   452   C  C     . CYS A 1 67  ? 119.242 124.289 143.453 1.00 30.75  ? 67   CYS A C     1 
ATOM   453   O  O     . CYS A 1 67  ? 119.283 123.115 143.837 1.00 33.34  ? 67   CYS A O     1 
ATOM   454   C  CB    . CYS A 1 67  ? 120.579 124.683 141.360 1.00 16.35  ? 67   CYS A CB    1 
ATOM   455   S  SG    . CYS A 1 67  ? 121.624 126.038 141.935 1.00 28.68  ? 67   CYS A SG    1 
ATOM   456   N  N     . THR A 1 68  ? 119.250 125.311 144.298 1.00 30.46  ? 68   THR A N     1 
ATOM   457   C  CA    . THR A 1 68  ? 119.237 125.125 145.740 1.00 27.98  ? 68   THR A CA    1 
ATOM   458   C  C     . THR A 1 68  ? 117.827 125.048 146.305 1.00 35.61  ? 68   THR A C     1 
ATOM   459   O  O     . THR A 1 68  ? 117.665 124.803 147.504 1.00 40.51  ? 68   THR A O     1 
ATOM   460   C  CB    . THR A 1 68  ? 120.005 126.260 146.420 1.00 28.64  ? 68   THR A CB    1 
ATOM   461   O  OG1   . THR A 1 68  ? 119.206 127.448 146.412 1.00 25.36  ? 68   THR A OG1   1 
ATOM   462   C  CG2   . THR A 1 68  ? 121.296 126.533 145.674 1.00 22.41  ? 68   THR A CG2   1 
ATOM   463   N  N     . LEU A 1 69  ? 116.811 125.247 145.475 1.00 38.46  ? 69   LEU A N     1 
ATOM   464   C  CA    . LEU A 1 69  ? 115.426 125.224 145.920 1.00 35.07  ? 69   LEU A CA    1 
ATOM   465   C  C     . LEU A 1 69  ? 114.869 123.815 145.792 1.00 44.39  ? 69   LEU A C     1 
ATOM   466   O  O     . LEU A 1 69  ? 114.795 123.267 144.688 1.00 48.31  ? 69   LEU A O     1 
ATOM   467   C  CB    . LEU A 1 69  ? 114.582 126.203 145.109 1.00 34.85  ? 69   LEU A CB    1 
ATOM   468   C  CG    . LEU A 1 69  ? 114.133 127.461 145.842 1.00 41.29  ? 69   LEU A CG    1 
ATOM   469   C  CD1   . LEU A 1 69  ? 115.323 128.139 146.486 1.00 42.34  ? 69   LEU A CD1   1 
ATOM   470   C  CD2   . LEU A 1 69  ? 113.433 128.400 144.884 1.00 41.70  ? 69   LEU A CD2   1 
ATOM   471   N  N     . LYS A 1 70  ? 114.517 123.252 146.868 1.00 62.27  ? 70   LYS A N     1 
ATOM   472   C  CA    . LYS A 1 70  ? 113.707 122.066 146.669 1.00 62.58  ? 70   LYS A CA    1 
ATOM   473   C  C     . LYS A 1 70  ? 112.233 122.446 146.717 1.00 64.02  ? 70   LYS A C     1 
ATOM   474   O  O     . LYS A 1 70  ? 111.851 123.374 147.437 1.00 63.97  ? 70   LYS A O     1 
ATOM   475   C  CB    . LYS A 1 70  ? 114.016 121.022 147.735 1.00 66.88  ? 70   LYS A CB    1 
ATOM   476   C  CG    . LYS A 1 70  ? 115.439 120.504 147.676 1.00 65.53  ? 70   LYS A CG    1 
ATOM   477   C  CD    . LYS A 1 70  ? 115.662 119.387 148.672 1.00 66.76  ? 70   LYS A CD    1 
ATOM   478   C  CE    . LYS A 1 70  ? 117.078 118.858 148.581 1.00 66.88  ? 70   LYS A CE    1 
ATOM   479   N  NZ    . LYS A 1 70  ? 118.079 119.925 148.849 1.00 67.06  ? 70   LYS A NZ    1 
ATOM   480   N  N     . PRO A 1 71  ? 111.395 121.766 145.937 1.00 73.73  ? 71   PRO A N     1 
ATOM   481   C  CA    . PRO A 1 71  ? 109.985 122.160 145.857 1.00 74.86  ? 71   PRO A CA    1 
ATOM   482   C  C     . PRO A 1 71  ? 109.296 122.109 147.212 1.00 76.38  ? 71   PRO A C     1 
ATOM   483   O  O     . PRO A 1 71  ? 109.474 121.171 147.992 1.00 79.48  ? 71   PRO A O     1 
ATOM   484   C  CB    . PRO A 1 71  ? 109.392 121.138 144.884 1.00 74.93  ? 71   PRO A CB    1 
ATOM   485   C  CG    . PRO A 1 71  ? 110.547 120.744 144.031 1.00 72.11  ? 71   PRO A CG    1 
ATOM   486   C  CD    . PRO A 1 71  ? 111.726 120.721 144.954 1.00 73.36  ? 71   PRO A CD    1 
ATOM   487   N  N     . MET A 1 72  ? 108.503 123.139 147.482 1.00 92.44  ? 72   MET A N     1 
ATOM   488   C  CA    . MET A 1 72  ? 107.714 123.241 148.696 1.00 94.13  ? 72   MET A CA    1 
ATOM   489   C  C     . MET A 1 72  ? 106.273 123.528 148.304 1.00 96.85  ? 72   MET A C     1 
ATOM   490   O  O     . MET A 1 72  ? 106.013 124.152 147.272 1.00 98.68  ? 72   MET A O     1 
ATOM   491   C  CB    . MET A 1 72  ? 108.257 124.338 149.620 1.00 93.93  ? 72   MET A CB    1 
ATOM   492   C  CG    . MET A 1 72  ? 107.687 124.326 151.021 1.00 96.29  ? 72   MET A CG    1 
ATOM   493   S  SD    . MET A 1 72  ? 108.468 125.560 152.073 1.00 101.30 ? 72   MET A SD    1 
ATOM   494   C  CE    . MET A 1 72  ? 110.179 125.043 151.969 1.00 96.33  ? 72   MET A CE    1 
ATOM   495   N  N     . GLU A 1 73  ? 105.340 123.056 149.128 1.00 101.99 ? 73   GLU A N     1 
ATOM   496   C  CA    . GLU A 1 73  ? 103.923 123.163 148.805 1.00 101.25 ? 73   GLU A CA    1 
ATOM   497   C  C     . GLU A 1 73  ? 103.501 124.616 148.635 1.00 99.58  ? 73   GLU A C     1 
ATOM   498   O  O     . GLU A 1 73  ? 103.807 125.470 149.472 1.00 99.59  ? 73   GLU A O     1 
ATOM   499   C  CB    . GLU A 1 73  ? 103.084 122.502 149.899 1.00 101.60 ? 73   GLU A CB    1 
ATOM   500   C  CG    . GLU A 1 73  ? 103.154 120.983 149.919 1.00 102.48 ? 73   GLU A CG    1 
ATOM   501   C  CD    . GLU A 1 73  ? 102.219 120.336 148.912 1.00 102.58 ? 73   GLU A CD    1 
ATOM   502   O  OE1   . GLU A 1 73  ? 101.580 121.068 148.126 1.00 102.34 ? 73   GLU A OE1   1 
ATOM   503   O  OE2   . GLU A 1 73  ? 102.118 119.092 148.911 1.00 102.76 ? 73   GLU A OE2   1 
ATOM   504   N  N     . GLY A 1 74  ? 102.795 124.891 147.541 1.00 104.17 ? 74   GLY A N     1 
ATOM   505   C  CA    . GLY A 1 74  ? 102.239 126.205 147.299 1.00 106.00 ? 74   GLY A CA    1 
ATOM   506   C  C     . GLY A 1 74  ? 103.225 127.264 146.865 1.00 107.23 ? 74   GLY A C     1 
ATOM   507   O  O     . GLY A 1 74  ? 102.877 128.449 146.878 1.00 106.94 ? 74   GLY A O     1 
ATOM   508   N  N     . LEU A 1 75  ? 104.439 126.884 146.481 1.00 93.44  ? 75   LEU A N     1 
ATOM   509   C  CA    . LEU A 1 75  ? 105.450 127.862 146.108 1.00 91.09  ? 75   LEU A CA    1 
ATOM   510   C  C     . LEU A 1 75  ? 105.153 128.430 144.726 1.00 88.95  ? 75   LEU A C     1 
ATOM   511   O  O     . LEU A 1 75  ? 104.840 127.685 143.793 1.00 88.08  ? 75   LEU A O     1 
ATOM   512   C  CB    . LEU A 1 75  ? 106.840 127.231 146.137 1.00 91.54  ? 75   LEU A CB    1 
ATOM   513   C  CG    . LEU A 1 75  ? 107.996 128.227 146.150 1.00 89.75  ? 75   LEU A CG    1 
ATOM   514   C  CD1   . LEU A 1 75  ? 107.896 129.114 147.374 1.00 87.79  ? 75   LEU A CD1   1 
ATOM   515   C  CD2   . LEU A 1 75  ? 109.330 127.506 146.109 1.00 88.05  ? 75   LEU A CD2   1 
ATOM   516   N  N     . SER A 1 76  ? 105.252 129.749 144.599 1.00 84.83  ? 76   SER A N     1 
ATOM   517   C  CA    . SER A 1 76  ? 105.029 130.437 143.336 1.00 87.04  ? 76   SER A CA    1 
ATOM   518   C  C     . SER A 1 76  ? 106.369 130.829 142.732 1.00 84.03  ? 76   SER A C     1 
ATOM   519   O  O     . SER A 1 76  ? 107.178 131.496 143.384 1.00 83.55  ? 76   SER A O     1 
ATOM   520   C  CB    . SER A 1 76  ? 104.153 131.674 143.533 1.00 86.70  ? 76   SER A CB    1 
ATOM   521   O  OG    . SER A 1 76  ? 103.900 132.321 142.300 1.00 84.40  ? 76   SER A OG    1 
ATOM   522   N  N     . ILE A 1 77  ? 106.595 130.419 141.488 1.00 67.93  ? 77   ILE A N     1 
ATOM   523   C  CA    . ILE A 1 77  ? 107.862 130.626 140.798 1.00 65.84  ? 77   ILE A CA    1 
ATOM   524   C  C     . ILE A 1 77  ? 107.608 131.475 139.563 1.00 68.98  ? 77   ILE A C     1 
ATOM   525   O  O     . ILE A 1 77  ? 106.792 131.108 138.709 1.00 69.64  ? 77   ILE A O     1 
ATOM   526   C  CB    . ILE A 1 77  ? 108.519 129.292 140.414 1.00 64.55  ? 77   ILE A CB    1 
ATOM   527   C  CG1   . ILE A 1 77  ? 108.955 128.537 141.666 1.00 64.80  ? 77   ILE A CG1   1 
ATOM   528   C  CG2   . ILE A 1 77  ? 109.696 129.523 139.485 1.00 65.70  ? 77   ILE A CG2   1 
ATOM   529   C  CD1   . ILE A 1 77  ? 109.917 129.311 142.522 1.00 64.55  ? 77   ILE A CD1   1 
ATOM   530   N  N     . GLU A 1 78  ? 108.304 132.605 139.465 1.00 61.46  ? 78   GLU A N     1 
ATOM   531   C  CA    . GLU A 1 78  ? 108.289 133.441 138.269 1.00 59.88  ? 78   GLU A CA    1 
ATOM   532   C  C     . GLU A 1 78  ? 109.660 133.342 137.615 1.00 60.96  ? 78   GLU A C     1 
ATOM   533   O  O     . GLU A 1 78  ? 110.653 133.840 138.156 1.00 52.33  ? 78   GLU A O     1 
ATOM   534   C  CB    . GLU A 1 78  ? 107.928 134.886 138.599 1.00 53.17  ? 78   GLU A CB    1 
ATOM   535   C  CG    . GLU A 1 78  ? 106.471 135.070 138.978 1.00 55.98  ? 78   GLU A CG    1 
ATOM   536   C  CD    . GLU A 1 78  ? 106.056 136.524 139.015 1.00 59.81  ? 78   GLU A CD    1 
ATOM   537   O  OE1   . GLU A 1 78  ? 106.935 137.399 138.871 1.00 60.52  ? 78   GLU A OE1   1 
ATOM   538   O  OE2   . GLU A 1 78  ? 104.849 136.794 139.186 1.00 59.36  ? 78   GLU A OE2   1 
ATOM   539   N  N     . THR A 1 79  ? 109.708 132.694 136.454 1.00 52.73  ? 79   THR A N     1 
ATOM   540   C  CA    . THR A 1 79  ? 110.965 132.416 135.775 1.00 43.72  ? 79   THR A CA    1 
ATOM   541   C  C     . THR A 1 79  ? 111.409 133.536 134.848 1.00 45.06  ? 79   THR A C     1 
ATOM   542   O  O     . THR A 1 79  ? 112.608 133.657 134.577 1.00 44.83  ? 79   THR A O     1 
ATOM   543   C  CB    . THR A 1 79  ? 110.852 131.118 134.971 1.00 44.11  ? 79   THR A CB    1 
ATOM   544   O  OG1   . THR A 1 79  ? 109.648 131.143 134.195 1.00 53.05  ? 79   THR A OG1   1 
ATOM   545   C  CG2   . THR A 1 79  ? 110.825 129.917 135.896 1.00 43.39  ? 79   THR A CG2   1 
ATOM   546   N  N     . LEU A 1 80  ? 110.485 134.346 134.339 1.00 45.82  ? 80   LEU A N     1 
ATOM   547   C  CA    . LEU A 1 80  ? 110.827 135.368 133.353 1.00 44.19  ? 80   LEU A CA    1 
ATOM   548   C  C     . LEU A 1 80  ? 110.161 136.699 133.686 1.00 41.57  ? 80   LEU A C     1 
ATOM   549   O  O     . LEU A 1 80  ? 109.534 137.337 132.840 1.00 48.76  ? 80   LEU A O     1 
ATOM   550   C  CB    . LEU A 1 80  ? 110.468 134.912 131.942 1.00 42.24  ? 80   LEU A CB    1 
ATOM   551   C  CG    . LEU A 1 80  ? 111.538 134.060 131.259 1.00 46.21  ? 80   LEU A CG    1 
ATOM   552   C  CD1   . LEU A 1 80  ? 111.115 133.686 129.850 1.00 45.68  ? 80   LEU A CD1   1 
ATOM   553   C  CD2   . LEU A 1 80  ? 112.870 134.792 131.246 1.00 41.25  ? 80   LEU A CD2   1 
ATOM   554   N  N     . SER A 1 81  ? 110.283 137.133 134.935 1.00 33.06  ? 81   SER A N     1 
ATOM   555   C  CA    . SER A 1 81  ? 109.896 138.494 135.258 1.00 30.48  ? 81   SER A CA    1 
ATOM   556   C  C     . SER A 1 81  ? 110.948 139.472 134.739 1.00 31.12  ? 81   SER A C     1 
ATOM   557   O  O     . SER A 1 81  ? 112.037 139.085 134.307 1.00 33.79  ? 81   SER A O     1 
ATOM   558   C  CB    . SER A 1 81  ? 109.701 138.662 136.764 1.00 31.51  ? 81   SER A CB    1 
ATOM   559   O  OG    . SER A 1 81  ? 110.939 138.638 137.448 1.00 33.93  ? 81   SER A OG    1 
ATOM   560   N  N     . ASP A 1 82  ? 110.603 140.760 134.767 1.00 32.30  ? 82   ASP A N     1 
ATOM   561   C  CA    . ASP A 1 82  ? 111.533 141.783 134.300 1.00 33.15  ? 82   ASP A CA    1 
ATOM   562   C  C     . ASP A 1 82  ? 112.791 141.813 135.157 1.00 36.85  ? 82   ASP A C     1 
ATOM   563   O  O     . ASP A 1 82  ? 113.904 141.955 134.636 1.00 35.00  ? 82   ASP A O     1 
ATOM   564   C  CB    . ASP A 1 82  ? 110.852 143.151 134.304 1.00 37.17  ? 82   ASP A CB    1 
ATOM   565   C  CG    . ASP A 1 82  ? 109.536 143.147 133.557 1.00 40.61  ? 82   ASP A CG    1 
ATOM   566   O  OD1   . ASP A 1 82  ? 109.422 142.410 132.557 1.00 37.59  ? 82   ASP A OD1   1 
ATOM   567   O  OD2   . ASP A 1 82  ? 108.614 143.878 133.973 1.00 34.67  ? 82   ASP A OD2   1 
ATOM   568   N  N     . GLU A 1 83  ? 112.632 141.677 136.474 1.00 32.10  ? 83   GLU A N     1 
ATOM   569   C  CA    . GLU A 1 83  ? 113.788 141.669 137.363 1.00 28.72  ? 83   GLU A CA    1 
ATOM   570   C  C     . GLU A 1 83  ? 114.653 140.436 137.139 1.00 34.85  ? 83   GLU A C     1 
ATOM   571   O  O     . GLU A 1 83  ? 115.881 140.520 137.206 1.00 36.45  ? 83   GLU A O     1 
ATOM   572   C  CB    . GLU A 1 83  ? 113.338 141.749 138.821 1.00 31.94  ? 83   GLU A CB    1 
ATOM   573   C  CG    . GLU A 1 83  ? 112.770 143.098 139.232 1.00 37.01  ? 83   GLU A CG    1 
ATOM   574   C  CD    . GLU A 1 83  ? 111.347 143.311 138.755 1.00 40.66  ? 83   GLU A CD    1 
ATOM   575   O  OE1   . GLU A 1 83  ? 110.724 142.339 138.282 1.00 36.40  ? 83   GLU A OE1   1 
ATOM   576   O  OE2   . GLU A 1 83  ? 110.851 144.453 138.854 1.00 44.28  ? 83   GLU A OE2   1 
ATOM   577   N  N     . ILE A 1 84  ? 114.034 139.282 136.880 1.00 36.38  ? 84   ILE A N     1 
ATOM   578   C  CA    . ILE A 1 84  ? 114.805 138.065 136.636 1.00 24.89  ? 84   ILE A CA    1 
ATOM   579   C  C     . ILE A 1 84  ? 115.612 138.188 135.349 1.00 27.68  ? 84   ILE A C     1 
ATOM   580   O  O     . ILE A 1 84  ? 116.791 137.813 135.302 1.00 34.61  ? 84   ILE A O     1 
ATOM   581   C  CB    . ILE A 1 84  ? 113.877 136.839 136.613 1.00 24.61  ? 84   ILE A CB    1 
ATOM   582   C  CG1   . ILE A 1 84  ? 113.347 136.552 138.016 1.00 29.79  ? 84   ILE A CG1   1 
ATOM   583   C  CG2   . ILE A 1 84  ? 114.607 135.625 136.081 1.00 27.79  ? 84   ILE A CG2   1 
ATOM   584   C  CD1   . ILE A 1 84  ? 114.426 136.222 139.013 1.00 35.43  ? 84   ILE A CD1   1 
ATOM   585   N  N     . ILE A 1 85  ? 114.995 138.714 134.288 1.00 29.11  ? 85   ILE A N     1 
ATOM   586   C  CA    . ILE A 1 85  ? 115.717 138.945 133.040 1.00 26.97  ? 85   ILE A CA    1 
ATOM   587   C  C     . ILE A 1 85  ? 116.854 139.931 133.261 1.00 32.28  ? 85   ILE A C     1 
ATOM   588   O  O     . ILE A 1 85  ? 117.965 139.740 132.755 1.00 24.75  ? 85   ILE A O     1 
ATOM   589   C  CB    . ILE A 1 85  ? 114.755 139.436 131.943 1.00 33.59  ? 85   ILE A CB    1 
ATOM   590   C  CG1   . ILE A 1 85  ? 113.818 138.314 131.504 1.00 34.78  ? 85   ILE A CG1   1 
ATOM   591   C  CG2   . ILE A 1 85  ? 115.526 139.973 130.749 1.00 29.61  ? 85   ILE A CG2   1 
ATOM   592   C  CD1   . ILE A 1 85  ? 112.880 138.718 130.393 1.00 31.65  ? 85   ILE A CD1   1 
ATOM   593   N  N     . GLU A 1 86  ? 116.595 141.000 134.016 1.00 35.66  ? 86   GLU A N     1 
ATOM   594   C  CA    . GLU A 1 86  ? 117.637 141.988 134.273 1.00 31.16  ? 86   GLU A CA    1 
ATOM   595   C  C     . GLU A 1 86  ? 118.802 141.375 135.039 1.00 29.74  ? 86   GLU A C     1 
ATOM   596   O  O     . GLU A 1 86  ? 119.968 141.605 134.699 1.00 36.31  ? 86   GLU A O     1 
ATOM   597   C  CB    . GLU A 1 86  ? 117.049 143.175 135.034 1.00 22.69  ? 86   GLU A CB    1 
ATOM   598   C  CG    . GLU A 1 86  ? 118.044 144.281 135.319 1.00 27.91  ? 86   GLU A CG    1 
ATOM   599   C  CD    . GLU A 1 86  ? 117.423 145.443 136.066 1.00 36.36  ? 86   GLU A CD    1 
ATOM   600   O  OE1   . GLU A 1 86  ? 116.207 145.389 136.346 1.00 35.14  ? 86   GLU A OE1   1 
ATOM   601   O  OE2   . GLU A 1 86  ? 118.149 146.411 136.373 1.00 35.54  ? 86   GLU A OE2   1 
ATOM   602   N  N     . MET A 1 87  ? 118.505 140.567 136.059 1.00 25.89  ? 87   MET A N     1 
ATOM   603   C  CA    . MET A 1 87  ? 119.561 139.933 136.842 1.00 27.70  ? 87   MET A CA    1 
ATOM   604   C  C     . MET A 1 87  ? 120.363 138.945 136.007 1.00 30.12  ? 87   MET A C     1 
ATOM   605   O  O     . MET A 1 87  ? 121.595 138.916 136.093 1.00 26.22  ? 87   MET A O     1 
ATOM   606   C  CB    . MET A 1 87  ? 118.969 139.230 138.062 1.00 26.20  ? 87   MET A CB    1 
ATOM   607   C  CG    . MET A 1 87  ? 118.372 140.158 139.095 1.00 28.94  ? 87   MET A CG    1 
ATOM   608   S  SD    . MET A 1 87  ? 118.551 139.503 140.757 1.00 50.45  ? 87   MET A SD    1 
ATOM   609   C  CE    . MET A 1 87  ? 120.329 139.561 140.899 1.00 30.00  ? 87   MET A CE    1 
ATOM   610   N  N     . ARG A 1 88  ? 119.687 138.124 135.199 1.00 29.76  ? 88   ARG A N     1 
ATOM   611   C  CA    . ARG A 1 88  ? 120.396 137.152 134.371 1.00 19.55  ? 88   ARG A CA    1 
ATOM   612   C  C     . ARG A 1 88  ? 121.233 137.838 133.299 1.00 20.56  ? 88   ARG A C     1 
ATOM   613   O  O     . ARG A 1 88  ? 122.359 137.412 133.020 1.00 18.76  ? 88   ARG A O     1 
ATOM   614   C  CB    . ARG A 1 88  ? 119.409 136.175 133.739 1.00 17.37  ? 88   ARG A CB    1 
ATOM   615   C  CG    . ARG A 1 88  ? 118.958 135.064 134.664 1.00 18.73  ? 88   ARG A CG    1 
ATOM   616   C  CD    . ARG A 1 88  ? 117.798 134.294 134.067 1.00 16.84  ? 88   ARG A CD    1 
ATOM   617   N  NE    . ARG A 1 88  ? 117.322 133.249 134.963 1.00 13.69  ? 88   ARG A NE    1 
ATOM   618   C  CZ    . ARG A 1 88  ? 116.153 132.638 134.841 1.00 24.47  ? 88   ARG A CZ    1 
ATOM   619   N  NH1   . ARG A 1 88  ? 115.307 132.950 133.875 1.00 29.30  ? 88   ARG A NH1   1 
ATOM   620   N  NH2   . ARG A 1 88  ? 115.820 131.694 135.717 1.00 28.21  ? 88   ARG A NH2   1 
ATOM   621   N  N     . LYS A 1 89  ? 120.703 138.901 132.689 1.00 26.76  ? 89   LYS A N     1 
ATOM   622   C  CA    . LYS A 1 89  ? 121.469 139.657 131.706 1.00 22.81  ? 89   LYS A CA    1 
ATOM   623   C  C     . LYS A 1 89  ? 122.694 140.295 132.341 1.00 26.07  ? 89   LYS A C     1 
ATOM   624   O  O     . LYS A 1 89  ? 123.784 140.277 131.759 1.00 21.60  ? 89   LYS A O     1 
ATOM   625   C  CB    . LYS A 1 89  ? 120.584 140.724 131.061 1.00 20.28  ? 89   LYS A CB    1 
ATOM   626   C  CG    . LYS A 1 89  ? 121.293 141.568 130.021 1.00 19.24  ? 89   LYS A CG    1 
ATOM   627   C  CD    . LYS A 1 89  ? 120.430 142.724 129.552 1.00 25.21  ? 89   LYS A CD    1 
ATOM   628   C  CE    . LYS A 1 89  ? 119.147 142.239 128.917 1.00 31.57  ? 89   LYS A CE    1 
ATOM   629   N  NZ    . LYS A 1 89  ? 118.349 143.365 128.368 1.00 31.52  ? 89   LYS A NZ    1 
ATOM   630   N  N     . THR A 1 90  ? 122.537 140.856 133.540 1.00 31.97  ? 90   THR A N     1 
ATOM   631   C  CA    . THR A 1 90  ? 123.673 141.460 134.223 1.00 22.09  ? 90   THR A CA    1 
ATOM   632   C  C     . THR A 1 90  ? 124.707 140.412 134.607 1.00 27.93  ? 90   THR A C     1 
ATOM   633   O  O     . THR A 1 90  ? 125.912 140.656 134.495 1.00 28.14  ? 90   THR A O     1 
ATOM   634   C  CB    . THR A 1 90  ? 123.194 142.227 135.453 1.00 14.48  ? 90   THR A CB    1 
ATOM   635   O  OG1   . THR A 1 90  ? 122.150 143.128 135.067 1.00 28.58  ? 90   THR A OG1   1 
ATOM   636   C  CG2   . THR A 1 90  ? 124.338 143.018 136.061 1.00 21.84  ? 90   THR A CG2   1 
ATOM   637   N  N     . ALA A 1 91  ? 124.258 139.235 135.049 1.00 28.64  ? 91   ALA A N     1 
ATOM   638   C  CA    . ALA A 1 91  ? 125.190 138.164 135.387 1.00 21.57  ? 91   ALA A CA    1 
ATOM   639   C  C     . ALA A 1 91  ? 125.951 137.682 134.159 1.00 25.72  ? 91   ALA A C     1 
ATOM   640   O  O     . ALA A 1 91  ? 127.164 137.447 134.221 1.00 27.64  ? 91   ALA A O     1 
ATOM   641   C  CB    . ALA A 1 91  ? 124.439 137.008 136.044 1.00 17.90  ? 91   ALA A CB    1 
ATOM   642   N  N     . LEU A 1 92  ? 125.255 137.533 133.030 1.00 25.97  ? 92   LEU A N     1 
ATOM   643   C  CA    . LEU A 1 92  ? 125.927 137.137 131.799 1.00 16.86  ? 92   LEU A CA    1 
ATOM   644   C  C     . LEU A 1 92  ? 126.914 138.200 131.339 1.00 16.15  ? 92   LEU A C     1 
ATOM   645   O  O     . LEU A 1 92  ? 127.997 137.873 130.850 1.00 28.29  ? 92   LEU A O     1 
ATOM   646   C  CB    . LEU A 1 92  ? 124.901 136.847 130.706 1.00 17.79  ? 92   LEU A CB    1 
ATOM   647   C  CG    . LEU A 1 92  ? 124.104 135.557 130.882 1.00 25.05  ? 92   LEU A CG    1 
ATOM   648   C  CD1   . LEU A 1 92  ? 123.030 135.464 129.824 1.00 22.00  ? 92   LEU A CD1   1 
ATOM   649   C  CD2   . LEU A 1 92  ? 125.025 134.354 130.824 1.00 19.64  ? 92   LEU A CD2   1 
ATOM   650   N  N     . GLU A 1 93  ? 126.556 139.479 131.476 1.00 22.31  ? 93   GLU A N     1 
ATOM   651   C  CA    . GLU A 1 93  ? 127.485 140.545 131.112 1.00 20.71  ? 93   GLU A CA    1 
ATOM   652   C  C     . GLU A 1 93  ? 128.703 140.551 132.028 1.00 27.92  ? 93   GLU A C     1 
ATOM   653   O  O     . GLU A 1 93  ? 129.826 140.796 131.574 1.00 25.51  ? 93   GLU A O     1 
ATOM   654   C  CB    . GLU A 1 93  ? 126.773 141.895 131.143 1.00 18.48  ? 93   GLU A CB    1 
ATOM   655   C  CG    . GLU A 1 93  ? 125.804 142.097 129.997 1.00 26.77  ? 93   GLU A CG    1 
ATOM   656   C  CD    . GLU A 1 93  ? 124.869 143.261 130.226 1.00 38.64  ? 93   GLU A CD    1 
ATOM   657   O  OE1   . GLU A 1 93  ? 124.964 143.897 131.295 1.00 36.59  ? 93   GLU A OE1   1 
ATOM   658   O  OE2   . GLU A 1 93  ? 124.039 143.544 129.338 1.00 33.04  ? 93   GLU A OE2   1 
ATOM   659   N  N     . LEU A 1 94  ? 128.501 140.267 133.316 1.00 22.06  ? 94   LEU A N     1 
ATOM   660   C  CA    . LEU A 1 94  ? 129.625 140.142 134.239 1.00 16.19  ? 94   LEU A CA    1 
ATOM   661   C  C     . LEU A 1 94  ? 130.544 138.996 133.837 1.00 25.25  ? 94   LEU A C     1 
ATOM   662   O  O     . LEU A 1 94  ? 131.772 139.129 133.887 1.00 32.11  ? 94   LEU A O     1 
ATOM   663   C  CB    . LEU A 1 94  ? 129.117 139.932 135.664 1.00 16.30  ? 94   LEU A CB    1 
ATOM   664   C  CG    . LEU A 1 94  ? 128.454 141.105 136.382 1.00 18.89  ? 94   LEU A CG    1 
ATOM   665   C  CD1   . LEU A 1 94  ? 127.910 140.651 137.724 1.00 27.92  ? 94   LEU A CD1   1 
ATOM   666   C  CD2   . LEU A 1 94  ? 129.432 142.241 136.564 1.00 17.49  ? 94   LEU A CD2   1 
ATOM   667   N  N     . ILE A 1 95  ? 129.965 137.858 133.451 1.00 24.53  ? 95   ILE A N     1 
ATOM   668   C  CA    . ILE A 1 95  ? 130.770 136.721 133.013 1.00 11.67  ? 95   ILE A CA    1 
ATOM   669   C  C     . ILE A 1 95  ? 131.519 137.053 131.727 1.00 14.38  ? 95   ILE A C     1 
ATOM   670   O  O     . ILE A 1 95  ? 132.703 136.728 131.580 1.00 26.44  ? 95   ILE A O     1 
ATOM   671   C  CB    . ILE A 1 95  ? 129.885 135.472 132.853 1.00 11.80  ? 95   ILE A CB    1 
ATOM   672   C  CG1   . ILE A 1 95  ? 129.337 135.031 134.208 1.00 23.37  ? 95   ILE A CG1   1 
ATOM   673   C  CG2   . ILE A 1 95  ? 130.662 134.340 132.214 1.00 11.64  ? 95   ILE A CG2   1 
ATOM   674   C  CD1   . ILE A 1 95  ? 128.432 133.828 134.135 1.00 16.72  ? 95   ILE A CD1   1 
ATOM   675   N  N     . LEU A 1 96  ? 130.844 137.707 130.779 1.00 22.91  ? 96   LEU A N     1 
ATOM   676   C  CA    . LEU A 1 96  ? 131.466 138.055 129.505 1.00 17.06  ? 96   LEU A CA    1 
ATOM   677   C  C     . LEU A 1 96  ? 132.557 139.101 129.671 1.00 21.65  ? 96   LEU A C     1 
ATOM   678   O  O     . LEU A 1 96  ? 133.479 139.165 128.851 1.00 25.35  ? 96   LEU A O     1 
ATOM   679   C  CB    . LEU A 1 96  ? 130.408 138.556 128.526 1.00 10.43  ? 96   LEU A CB    1 
ATOM   680   C  CG    . LEU A 1 96  ? 129.432 137.502 128.018 1.00 11.48  ? 96   LEU A CG    1 
ATOM   681   C  CD1   . LEU A 1 96  ? 128.308 138.167 127.263 1.00 16.79  ? 96   LEU A CD1   1 
ATOM   682   C  CD2   . LEU A 1 96  ? 130.154 136.501 127.145 1.00 17.22  ? 96   LEU A CD2   1 
ATOM   683   N  N     . SER A 1 97  ? 132.461 139.931 130.710 1.00 21.30  ? 97   SER A N     1 
ATOM   684   C  CA    . SER A 1 97  ? 133.521 140.884 131.009 1.00 18.26  ? 97   SER A CA    1 
ATOM   685   C  C     . SER A 1 97  ? 134.832 140.195 131.350 1.00 25.38  ? 97   SER A C     1 
ATOM   686   O  O     . SER A 1 97  ? 135.896 140.806 131.215 1.00 28.81  ? 97   SER A O     1 
ATOM   687   C  CB    . SER A 1 97  ? 133.091 141.783 132.161 1.00 22.99  ? 97   SER A CB    1 
ATOM   688   O  OG    . SER A 1 97  ? 131.899 142.469 131.831 1.00 30.13  ? 97   SER A OG    1 
ATOM   689   N  N     . ASP A 1 98  ? 134.777 138.940 131.793 1.00 25.77  ? 98   ASP A N     1 
ATOM   690   C  CA    . ASP A 1 98  ? 135.972 138.170 132.089 1.00 25.10  ? 98   ASP A CA    1 
ATOM   691   C  C     . ASP A 1 98  ? 136.312 137.155 131.005 1.00 28.88  ? 98   ASP A C     1 
ATOM   692   O  O     . ASP A 1 98  ? 137.449 136.674 130.968 1.00 31.96  ? 98   ASP A O     1 
ATOM   693   C  CB    . ASP A 1 98  ? 135.810 137.445 133.429 1.00 21.84  ? 98   ASP A CB    1 
ATOM   694   C  CG    . ASP A 1 98  ? 137.132 137.217 134.130 1.00 27.08  ? 98   ASP A CG    1 
ATOM   695   O  OD1   . ASP A 1 98  ? 138.162 137.726 133.639 1.00 20.44  ? 98   ASP A OD1   1 
ATOM   696   O  OD2   . ASP A 1 98  ? 137.144 136.530 135.173 1.00 40.85  ? 98   ASP A OD2   1 
ATOM   697   N  N     . HIS A 1 99  ? 135.366 136.825 130.129 1.00 26.05  ? 99   HIS A N     1 
ATOM   698   C  CA    . HIS A 1 99  ? 135.624 135.860 129.070 1.00 18.81  ? 99   HIS A CA    1 
ATOM   699   C  C     . HIS A 1 99  ? 136.642 136.416 128.084 1.00 20.56  ? 99   HIS A C     1 
ATOM   700   O  O     . HIS A 1 99  ? 136.643 137.608 127.769 1.00 31.33  ? 99   HIS A O     1 
ATOM   701   C  CB    . HIS A 1 99  ? 134.326 135.506 128.341 1.00 20.65  ? 99   HIS A CB    1 
ATOM   702   C  CG    . HIS A 1 99  ? 134.292 134.112 127.793 1.00 11.34  ? 99   HIS A CG    1 
ATOM   703   N  ND1   . HIS A 1 99  ? 134.144 133.838 126.448 1.00 16.07  ? 99   HIS A ND1   1 
ATOM   704   C  CD2   . HIS A 1 99  ? 134.368 132.911 128.412 1.00 13.47  ? 99   HIS A CD2   1 
ATOM   705   C  CE1   . HIS A 1 99  ? 134.137 132.532 126.265 1.00 16.36  ? 99   HIS A CE1   1 
ATOM   706   N  NE2   . HIS A 1 99  ? 134.272 131.946 127.441 1.00 18.30  ? 99   HIS A NE2   1 
ATOM   707   N  N     . TYR A 1 100 ? 137.518 135.542 127.603 1.00 20.63  ? 100  TYR A N     1 
ATOM   708   C  CA    . TYR A 1 100 ? 138.530 135.905 126.622 1.00 19.51  ? 100  TYR A CA    1 
ATOM   709   C  C     . TYR A 1 100 ? 138.501 134.872 125.509 1.00 21.74  ? 100  TYR A C     1 
ATOM   710   O  O     . TYR A 1 100 ? 138.634 133.673 125.772 1.00 24.33  ? 100  TYR A O     1 
ATOM   711   C  CB    . TYR A 1 100 ? 139.914 135.974 127.268 1.00 24.04  ? 100  TYR A CB    1 
ATOM   712   C  CG    . TYR A 1 100 ? 140.968 136.637 126.420 1.00 24.81  ? 100  TYR A CG    1 
ATOM   713   C  CD1   . TYR A 1 100 ? 140.932 138.002 126.178 1.00 24.58  ? 100  TYR A CD1   1 
ATOM   714   C  CD2   . TYR A 1 100 ? 142.012 135.905 125.881 1.00 28.23  ? 100  TYR A CD2   1 
ATOM   715   C  CE1   . TYR A 1 100 ? 141.898 138.616 125.413 1.00 26.23  ? 100  TYR A CE1   1 
ATOM   716   C  CE2   . TYR A 1 100 ? 142.985 136.511 125.116 1.00 29.52  ? 100  TYR A CE2   1 
ATOM   717   C  CZ    . TYR A 1 100 ? 142.924 137.867 124.887 1.00 28.68  ? 100  TYR A CZ    1 
ATOM   718   O  OH    . TYR A 1 100 ? 143.889 138.474 124.122 1.00 28.87  ? 100  TYR A OH    1 
ATOM   719   N  N     . GLY A 1 101 ? 138.316 135.326 124.284 1.00 21.01  ? 101  GLY A N     1 
ATOM   720   C  CA    . GLY A 1 101 ? 138.338 134.429 123.147 1.00 18.23  ? 101  GLY A CA    1 
ATOM   721   C  C     . GLY A 1 101 ? 137.448 134.931 122.033 1.00 19.39  ? 101  GLY A C     1 
ATOM   722   O  O     . GLY A 1 101 ? 136.721 135.911 122.169 1.00 23.78  ? 101  GLY A O     1 
ATOM   723   N  N     . ASP A 1 102 ? 137.527 134.228 120.909 1.00 21.18  ? 102  ASP A N     1 
ATOM   724   C  CA    . ASP A 1 102 ? 136.677 134.463 119.753 1.00 15.50  ? 102  ASP A CA    1 
ATOM   725   C  C     . ASP A 1 102 ? 135.739 133.279 119.583 1.00 12.81  ? 102  ASP A C     1 
ATOM   726   O  O     . ASP A 1 102 ? 136.190 132.130 119.561 1.00 19.34  ? 102  ASP A O     1 
ATOM   727   C  CB    . ASP A 1 102 ? 137.509 134.649 118.482 1.00 15.92  ? 102  ASP A CB    1 
ATOM   728   C  CG    . ASP A 1 102 ? 138.322 135.919 118.495 1.00 24.23  ? 102  ASP A CG    1 
ATOM   729   O  OD1   . ASP A 1 102 ? 137.803 136.955 118.952 1.00 33.39  ? 102  ASP A OD1   1 
ATOM   730   O  OD2   . ASP A 1 102 ? 139.483 135.880 118.041 1.00 26.81  ? 102  ASP A OD2   1 
ATOM   731   N  N     . CYS A 1 103 ? 134.440 133.556 119.474 1.00 3.87   ? 103  CYS A N     1 
ATOM   732   C  CA    . CYS A 1 103 ? 133.498 132.500 119.122 1.00 4.21   ? 103  CYS A CA    1 
ATOM   733   C  C     . CYS A 1 103 ? 133.745 132.016 117.701 1.00 16.96  ? 103  CYS A C     1 
ATOM   734   O  O     . CYS A 1 103 ? 133.881 130.814 117.454 1.00 17.91  ? 103  CYS A O     1 
ATOM   735   C  CB    . CYS A 1 103 ? 132.062 132.999 119.274 1.00 9.13   ? 103  CYS A CB    1 
ATOM   736   S  SG    . CYS A 1 103 ? 131.578 133.433 120.949 1.00 13.06  ? 103  CYS A SG    1 
ATOM   737   N  N     . ILE A 1 104 ? 133.820 132.949 116.758 1.00 25.17  ? 104  ILE A N     1 
ATOM   738   C  CA    . ILE A 1 104 ? 134.130 132.663 115.368 1.00 5.34   ? 104  ILE A CA    1 
ATOM   739   C  C     . ILE A 1 104 ? 135.377 133.451 115.000 1.00 7.98   ? 104  ILE A C     1 
ATOM   740   O  O     . ILE A 1 104 ? 135.793 134.369 115.709 1.00 26.29  ? 104  ILE A O     1 
ATOM   741   C  CB    . ILE A 1 104 ? 132.963 133.017 114.424 1.00 3.93   ? 104  ILE A CB    1 
ATOM   742   C  CG1   . ILE A 1 104 ? 132.758 134.531 114.379 1.00 2.82   ? 104  ILE A CG1   1 
ATOM   743   C  CG2   . ILE A 1 104 ? 131.689 132.329 114.871 1.00 5.79   ? 104  ILE A CG2   1 
ATOM   744   C  CD1   . ILE A 1 104 ? 131.658 134.970 113.456 1.00 10.86  ? 104  ILE A CD1   1 
ATOM   745   N  N     . GLY A 1 105 ? 135.984 133.075 113.882 1.00 0.00   ? 105  GLY A N     1 
ATOM   746   C  CA    . GLY A 1 105 ? 137.100 133.819 113.357 1.00 0.00   ? 105  GLY A CA    1 
ATOM   747   C  C     . GLY A 1 105 ? 136.629 135.085 112.674 1.00 7.04   ? 105  GLY A C     1 
ATOM   748   O  O     . GLY A 1 105 ? 135.491 135.172 112.205 1.00 28.49  ? 105  GLY A O     1 
ATOM   749   N  N     . PRO A 1 106 ? 137.498 136.096 112.608 1.00 1.23   ? 106  PRO A N     1 
ATOM   750   C  CA    . PRO A 1 106 ? 137.124 137.343 111.918 1.00 10.17  ? 106  PRO A CA    1 
ATOM   751   C  C     . PRO A 1 106 ? 136.840 137.151 110.442 1.00 19.84  ? 106  PRO A C     1 
ATOM   752   O  O     . PRO A 1 106 ? 136.196 138.011 109.832 1.00 10.72  ? 106  PRO A O     1 
ATOM   753   C  CB    . PRO A 1 106 ? 138.345 138.246 112.137 1.00 15.09  ? 106  PRO A CB    1 
ATOM   754   C  CG    . PRO A 1 106 ? 139.042 137.668 113.309 1.00 9.62   ? 106  PRO A CG    1 
ATOM   755   C  CD    . PRO A 1 106 ? 138.818 136.195 113.249 1.00 8.02   ? 106  PRO A CD    1 
ATOM   756   N  N     . CYS A 1 107 ? 137.315 136.052 109.854 1.00 24.00  ? 107  CYS A N     1 
ATOM   757   C  CA    . CYS A 1 107 ? 136.998 135.736 108.467 1.00 5.60   ? 107  CYS A CA    1 
ATOM   758   C  C     . CYS A 1 107 ? 135.500 135.544 108.268 1.00 17.35  ? 107  CYS A C     1 
ATOM   759   O  O     . CYS A 1 107 ? 134.952 135.915 107.224 1.00 27.37  ? 107  CYS A O     1 
ATOM   760   C  CB    . CYS A 1 107 ? 137.761 134.481 108.046 1.00 7.57   ? 107  CYS A CB    1 
ATOM   761   S  SG    . CYS A 1 107 ? 137.645 133.116 109.234 1.00 13.67  ? 107  CYS A SG    1 
ATOM   762   N  N     . GLN A 1 108 ? 134.824 134.949 109.249 1.00 7.57   ? 108  GLN A N     1 
ATOM   763   C  CA    . GLN A 1 108 ? 133.383 134.756 109.149 1.00 4.27   ? 108  GLN A CA    1 
ATOM   764   C  C     . GLN A 1 108 ? 132.618 136.054 109.372 1.00 15.06  ? 108  GLN A C     1 
ATOM   765   O  O     . GLN A 1 108 ? 131.573 136.269 108.751 1.00 23.53  ? 108  GLN A O     1 
ATOM   766   C  CB    . GLN A 1 108 ? 132.931 133.688 110.147 1.00 7.48   ? 108  GLN A CB    1 
ATOM   767   C  CG    . GLN A 1 108 ? 131.448 133.392 110.118 1.00 8.40   ? 108  GLN A CG    1 
ATOM   768   C  CD    . GLN A 1 108 ? 131.086 132.189 110.952 1.00 12.97  ? 108  GLN A CD    1 
ATOM   769   O  OE1   . GLN A 1 108 ? 131.951 131.408 111.342 1.00 17.43  ? 108  GLN A OE1   1 
ATOM   770   N  NE2   . GLN A 1 108 ? 129.801 132.030 111.233 1.00 14.68  ? 108  GLN A NE2   1 
ATOM   771   N  N     . ASN A 1 109 ? 133.121 136.928 110.244 1.00 14.13  ? 109  ASN A N     1 
ATOM   772   C  CA    . ASN A 1 109 ? 132.463 138.211 110.465 1.00 8.40   ? 109  ASN A CA    1 
ATOM   773   C  C     . ASN A 1 109 ? 132.620 139.129 109.261 1.00 18.34  ? 109  ASN A C     1 
ATOM   774   O  O     . ASN A 1 109 ? 131.702 139.883 108.922 1.00 25.56  ? 109  ASN A O     1 
ATOM   775   C  CB    . ASN A 1 109 ? 133.027 138.878 111.714 1.00 9.85   ? 109  ASN A CB    1 
ATOM   776   C  CG    . ASN A 1 109 ? 132.219 140.076 112.147 1.00 23.21  ? 109  ASN A CG    1 
ATOM   777   O  OD1   . ASN A 1 109 ? 130.993 140.071 112.066 1.00 29.47  ? 109  ASN A OD1   1 
ATOM   778   N  ND2   . ASN A 1 109 ? 132.902 141.114 112.608 1.00 21.83  ? 109  ASN A ND2   1 
ATOM   779   N  N     . GLY A 1 110 ? 133.783 139.091 108.611 1.00 20.64  ? 110  GLY A N     1 
ATOM   780   C  CA    . GLY A 1 110 ? 134.006 139.956 107.469 1.00 18.29  ? 110  GLY A CA    1 
ATOM   781   C  C     . GLY A 1 110 ? 133.223 139.548 106.242 1.00 18.44  ? 110  GLY A C     1 
ATOM   782   O  O     . GLY A 1 110 ? 132.882 140.395 105.413 1.00 30.70  ? 110  GLY A O     1 
ATOM   783   N  N     . CYS A 1 111 ? 132.931 138.265 106.105 1.00 5.69   ? 111  CYS A N     1 
ATOM   784   C  CA    . CYS A 1 111 ? 132.129 137.798 104.985 1.00 17.50  ? 111  CYS A CA    1 
ATOM   785   C  C     . CYS A 1 111 ? 130.711 138.332 105.122 1.00 24.75  ? 111  CYS A C     1 
ATOM   786   O  O     . CYS A 1 111 ? 130.080 138.121 106.165 1.00 24.88  ? 111  CYS A O     1 
ATOM   787   C  CB    . CYS A 1 111 ? 132.122 136.273 104.934 1.00 18.00  ? 111  CYS A CB    1 
ATOM   788   S  SG    . CYS A 1 111 ? 131.230 135.568 103.526 1.00 24.61  ? 111  CYS A SG    1 
ATOM   789   N  N     . PRO A 1 112 ? 130.182 139.043 104.123 1.00 13.56  ? 112  PRO A N     1 
ATOM   790   C  CA    . PRO A 1 112 ? 128.789 139.507 104.211 1.00 11.34  ? 112  PRO A CA    1 
ATOM   791   C  C     . PRO A 1 112 ? 127.781 138.385 104.376 1.00 18.06  ? 112  PRO A C     1 
ATOM   792   O  O     . PRO A 1 112 ? 126.754 138.585 105.035 1.00 21.49  ? 112  PRO A O     1 
ATOM   793   C  CB    . PRO A 1 112 ? 128.592 140.254 102.887 1.00 17.69  ? 112  PRO A CB    1 
ATOM   794   C  CG    . PRO A 1 112 ? 129.948 140.727 102.537 1.00 26.40  ? 112  PRO A CG    1 
ATOM   795   C  CD    . PRO A 1 112 ? 130.884 139.637 102.975 1.00 9.31   ? 112  PRO A CD    1 
ATOM   796   N  N     . ALA A 1 113 ? 128.036 137.211 103.800 1.00 22.43  ? 113  ALA A N     1 
ATOM   797   C  CA    . ALA A 1 113 ? 127.166 136.069 104.040 1.00 18.51  ? 113  ALA A CA    1 
ATOM   798   C  C     . ALA A 1 113 ? 127.439 135.386 105.372 1.00 21.37  ? 113  ALA A C     1 
ATOM   799   O  O     . ALA A 1 113 ? 126.602 134.596 105.817 1.00 26.08  ? 113  ALA A O     1 
ATOM   800   C  CB    . ALA A 1 113 ? 127.298 135.049 102.909 1.00 14.29  ? 113  ALA A CB    1 
ATOM   801   N  N     . HIS A 1 114 ? 128.574 135.679 106.011 1.00 21.33  ? 114  HIS A N     1 
ATOM   802   C  CA    . HIS A 1 114 ? 128.966 135.097 107.297 1.00 19.91  ? 114  HIS A CA    1 
ATOM   803   C  C     . HIS A 1 114 ? 129.081 133.573 107.204 1.00 19.87  ? 114  HIS A C     1 
ATOM   804   O  O     . HIS A 1 114 ? 128.393 132.824 107.899 1.00 20.29  ? 114  HIS A O     1 
ATOM   805   C  CB    . HIS A 1 114 ? 128.000 135.511 108.415 1.00 14.52  ? 114  HIS A CB    1 
ATOM   806   C  CG    . HIS A 1 114 ? 127.990 136.981 108.700 1.00 16.63  ? 114  HIS A CG    1 
ATOM   807   N  ND1   . HIS A 1 114 ? 129.043 137.811 108.385 1.00 15.58  ? 114  HIS A ND1   1 
ATOM   808   C  CD2   . HIS A 1 114 ? 127.051 137.768 109.277 1.00 21.71  ? 114  HIS A CD2   1 
ATOM   809   C  CE1   . HIS A 1 114 ? 128.752 139.047 108.752 1.00 18.57  ? 114  HIS A CE1   1 
ATOM   810   N  NE2   . HIS A 1 114 ? 127.550 139.047 109.296 1.00 18.00  ? 114  HIS A NE2   1 
ATOM   811   N  N     . SER A 1 115 ? 129.982 133.125 106.337 1.00 15.63  ? 115  SER A N     1 
ATOM   812   C  CA    . SER A 1 115 ? 130.171 131.704 106.086 1.00 18.55  ? 115  SER A CA    1 
ATOM   813   C  C     . SER A 1 115 ? 131.266 131.131 106.975 1.00 30.51  ? 115  SER A C     1 
ATOM   814   O  O     . SER A 1 115 ? 132.194 131.833 107.385 1.00 34.47  ? 115  SER A O     1 
ATOM   815   C  CB    . SER A 1 115 ? 130.517 131.458 104.621 1.00 22.32  ? 115  SER A CB    1 
ATOM   816   O  OG    . SER A 1 115 ? 130.428 130.082 104.305 1.00 24.11  ? 115  SER A OG    1 
ATOM   817   N  N     . ASP A 1 116 ? 131.158 129.831 107.255 1.00 24.81  ? 116  ASP A N     1 
ATOM   818   C  CA    . ASP A 1 116 ? 132.092 129.136 108.142 1.00 8.13   ? 116  ASP A CA    1 
ATOM   819   C  C     . ASP A 1 116 ? 133.401 128.906 107.390 1.00 12.93  ? 116  ASP A C     1 
ATOM   820   O  O     . ASP A 1 116 ? 133.694 127.816 106.895 1.00 24.51  ? 116  ASP A O     1 
ATOM   821   C  CB    . ASP A 1 116 ? 131.484 127.829 108.635 1.00 17.79  ? 116  ASP A CB    1 
ATOM   822   C  CG    . ASP A 1 116 ? 132.089 127.358 109.939 1.00 29.83  ? 116  ASP A CG    1 
ATOM   823   O  OD1   . ASP A 1 116 ? 133.272 127.654 110.195 1.00 38.91  ? 116  ASP A OD1   1 
ATOM   824   O  OD2   . ASP A 1 116 ? 131.377 126.685 110.710 1.00 27.81  ? 116  ASP A OD2   1 
ATOM   825   N  N     . VAL A 1 117 ? 134.202 129.970 107.317 1.00 16.23  ? 117  VAL A N     1 
ATOM   826   C  CA    . VAL A 1 117 ? 135.444 129.942 106.547 1.00 13.08  ? 117  VAL A CA    1 
ATOM   827   C  C     . VAL A 1 117 ? 136.438 128.953 107.147 1.00 12.00  ? 117  VAL A C     1 
ATOM   828   O  O     . VAL A 1 117 ? 137.058 128.158 106.428 1.00 20.37  ? 117  VAL A O     1 
ATOM   829   C  CB    . VAL A 1 117 ? 136.030 131.363 106.467 1.00 10.53  ? 117  VAL A CB    1 
ATOM   830   C  CG1   . VAL A 1 117 ? 137.421 131.340 105.893 1.00 12.79  ? 117  VAL A CG1   1 
ATOM   831   C  CG2   . VAL A 1 117 ? 135.127 132.258 105.642 1.00 11.55  ? 117  VAL A CG2   1 
ATOM   832   N  N     . GLN A 1 118 ? 136.588 128.977 108.472 1.00 20.75  ? 118  GLN A N     1 
ATOM   833   C  CA    . GLN A 1 118 ? 137.567 128.132 109.150 1.00 15.42  ? 118  GLN A CA    1 
ATOM   834   C  C     . GLN A 1 118 ? 137.261 126.651 108.954 1.00 12.35  ? 118  GLN A C     1 
ATOM   835   O  O     . GLN A 1 118 ? 138.174 125.842 108.735 1.00 26.69  ? 118  GLN A O     1 
ATOM   836   C  CB    . GLN A 1 118 ? 137.592 128.497 110.634 1.00 15.56  ? 118  GLN A CB    1 
ATOM   837   C  CG    . GLN A 1 118 ? 138.531 127.696 111.498 1.00 24.01  ? 118  GLN A CG    1 
ATOM   838   C  CD    . GLN A 1 118 ? 138.519 128.179 112.934 1.00 15.26  ? 118  GLN A CD    1 
ATOM   839   O  OE1   . GLN A 1 118 ? 138.167 129.322 113.209 1.00 13.87  ? 118  GLN A OE1   1 
ATOM   840   N  NE2   . GLN A 1 118 ? 138.900 127.308 113.856 1.00 12.14  ? 118  GLN A NE2   1 
ATOM   841   N  N     . GLY A 1 119 ? 135.980 126.282 109.009 1.00 15.68  ? 119  GLY A N     1 
ATOM   842   C  CA    . GLY A 1 119 ? 135.613 124.882 108.865 1.00 14.77  ? 119  GLY A CA    1 
ATOM   843   C  C     . GLY A 1 119 ? 135.947 124.316 107.497 1.00 12.97  ? 119  GLY A C     1 
ATOM   844   O  O     . GLY A 1 119 ? 136.513 123.224 107.384 1.00 18.49  ? 119  GLY A O     1 
ATOM   845   N  N     . TYR A 1 120 ? 135.613 125.049 106.432 1.00 15.21  ? 120  TYR A N     1 
ATOM   846   C  CA    . TYR A 1 120 ? 135.919 124.501 105.119 1.00 12.28  ? 120  TYR A CA    1 
ATOM   847   C  C     . TYR A 1 120 ? 137.385 124.672 104.747 1.00 14.52  ? 120  TYR A C     1 
ATOM   848   O  O     . TYR A 1 120 ? 137.885 123.905 103.922 1.00 37.63  ? 120  TYR A O     1 
ATOM   849   C  CB    . TYR A 1 120 ? 134.987 125.068 104.030 1.00 12.70  ? 120  TYR A CB    1 
ATOM   850   C  CG    . TYR A 1 120 ? 135.076 126.538 103.660 1.00 26.72  ? 120  TYR A CG    1 
ATOM   851   C  CD1   . TYR A 1 120 ? 136.198 127.065 103.030 1.00 23.27  ? 120  TYR A CD1   1 
ATOM   852   C  CD2   . TYR A 1 120 ? 133.993 127.378 103.861 1.00 22.29  ? 120  TYR A CD2   1 
ATOM   853   C  CE1   . TYR A 1 120 ? 136.257 128.396 102.671 1.00 10.70  ? 120  TYR A CE1   1 
ATOM   854   C  CE2   . TYR A 1 120 ? 134.042 128.706 103.501 1.00 15.76  ? 120  TYR A CE2   1 
ATOM   855   C  CZ    . TYR A 1 120 ? 135.174 129.209 102.908 1.00 15.17  ? 120  TYR A CZ    1 
ATOM   856   O  OH    . TYR A 1 120 ? 135.217 130.535 102.553 1.00 32.75  ? 120  TYR A OH    1 
ATOM   857   N  N     . LEU A 1 121 ? 138.103 125.613 105.364 1.00 12.24  ? 121  LEU A N     1 
ATOM   858   C  CA    . LEU A 1 121 ? 139.557 125.610 105.227 1.00 9.40   ? 121  LEU A CA    1 
ATOM   859   C  C     . LEU A 1 121 ? 140.164 124.358 105.851 1.00 6.27   ? 121  LEU A C     1 
ATOM   860   O  O     . LEU A 1 121 ? 141.088 123.757 105.288 1.00 18.14  ? 121  LEU A O     1 
ATOM   861   C  CB    . LEU A 1 121 ? 140.152 126.862 105.860 1.00 18.50  ? 121  LEU A CB    1 
ATOM   862   C  CG    . LEU A 1 121 ? 139.966 128.157 105.079 1.00 17.05  ? 121  LEU A CG    1 
ATOM   863   C  CD1   . LEU A 1 121 ? 140.389 129.317 105.938 1.00 7.61   ? 121  LEU A CD1   1 
ATOM   864   C  CD2   . LEU A 1 121 ? 140.759 128.125 103.793 1.00 10.46  ? 121  LEU A CD2   1 
ATOM   865   N  N     . ALA A 1 122 ? 139.655 123.950 107.017 1.00 15.62  ? 122  ALA A N     1 
ATOM   866   C  CA    . ALA A 1 122 ? 140.105 122.701 107.625 1.00 11.50  ? 122  ALA A CA    1 
ATOM   867   C  C     . ALA A 1 122 ? 139.765 121.501 106.746 1.00 21.83  ? 122  ALA A C     1 
ATOM   868   O  O     . ALA A 1 122 ? 140.576 120.576 106.599 1.00 20.75  ? 122  ALA A O     1 
ATOM   869   C  CB    . ALA A 1 122 ? 139.485 122.544 109.012 1.00 11.04  ? 122  ALA A CB    1 
ATOM   870   N  N     . LEU A 1 123 ? 138.567 121.499 106.156 1.00 19.25  ? 123  LEU A N     1 
ATOM   871   C  CA    . LEU A 1 123 ? 138.182 120.415 105.254 1.00 13.95  ? 123  LEU A CA    1 
ATOM   872   C  C     . LEU A 1 123 ? 139.040 120.387 103.994 1.00 14.96  ? 123  LEU A C     1 
ATOM   873   O  O     . LEU A 1 123 ? 139.301 119.310 103.449 1.00 23.30  ? 123  LEU A O     1 
ATOM   874   C  CB    . LEU A 1 123 ? 136.707 120.541 104.882 1.00 13.85  ? 123  LEU A CB    1 
ATOM   875   C  CG    . LEU A 1 123 ? 135.702 120.220 105.984 1.00 12.74  ? 123  LEU A CG    1 
ATOM   876   C  CD1   . LEU A 1 123 ? 134.303 120.568 105.530 1.00 17.66  ? 123  LEU A CD1   1 
ATOM   877   C  CD2   . LEU A 1 123 ? 135.792 118.756 106.365 1.00 22.69  ? 123  LEU A CD2   1 
ATOM   878   N  N     . ILE A 1 124 ? 139.461 121.554 103.506 1.00 19.81  ? 124  ILE A N     1 
ATOM   879   C  CA    . ILE A 1 124 ? 140.366 121.617 102.364 1.00 17.03  ? 124  ILE A CA    1 
ATOM   880   C  C     . ILE A 1 124 ? 141.742 121.085 102.744 1.00 25.43  ? 124  ILE A C     1 
ATOM   881   O  O     . ILE A 1 124 ? 142.396 120.391 101.956 1.00 24.73  ? 124  ILE A O     1 
ATOM   882   C  CB    . ILE A 1 124 ? 140.425 123.062 101.830 1.00 18.29  ? 124  ILE A CB    1 
ATOM   883   C  CG1   . ILE A 1 124 ? 139.182 123.371 100.998 1.00 22.01  ? 124  ILE A CG1   1 
ATOM   884   C  CG2   . ILE A 1 124 ? 141.664 123.302 101.010 1.00 19.81  ? 124  ILE A CG2   1 
ATOM   885   C  CD1   . ILE A 1 124 ? 139.139 124.781 100.471 1.00 16.71  ? 124  ILE A CD1   1 
ATOM   886   N  N     . ALA A 1 125 ? 142.200 121.395 103.959 1.00 31.58  ? 125  ALA A N     1 
ATOM   887   C  CA    . ALA A 1 125 ? 143.479 120.865 104.423 1.00 18.30  ? 125  ALA A CA    1 
ATOM   888   C  C     . ALA A 1 125 ? 143.433 119.348 104.555 1.00 17.86  ? 125  ALA A C     1 
ATOM   889   O  O     . ALA A 1 125 ? 144.420 118.662 104.269 1.00 28.22  ? 125  ALA A O     1 
ATOM   890   C  CB    . ALA A 1 125 ? 143.869 121.511 105.752 1.00 16.23  ? 125  ALA A CB    1 
ATOM   891   N  N     . MET A 1 126 ? 142.297 118.802 104.994 1.00 21.64  ? 126  MET A N     1 
ATOM   892   C  CA    . MET A 1 126 ? 142.175 117.351 105.085 1.00 27.22  ? 126  MET A CA    1 
ATOM   893   C  C     . MET A 1 126 ? 142.048 116.687 103.718 1.00 26.74  ? 126  MET A C     1 
ATOM   894   O  O     . MET A 1 126 ? 142.262 115.475 103.611 1.00 30.60  ? 126  MET A O     1 
ATOM   895   C  CB    . MET A 1 126 ? 140.979 116.972 105.956 1.00 23.59  ? 126  MET A CB    1 
ATOM   896   C  CG    . MET A 1 126 ? 141.156 117.304 107.422 1.00 21.67  ? 126  MET A CG    1 
ATOM   897   S  SD    . MET A 1 126 ? 139.808 116.649 108.414 1.00 51.02  ? 126  MET A SD    1 
ATOM   898   C  CE    . MET A 1 126 ? 139.899 114.916 107.977 1.00 27.46  ? 126  MET A CE    1 
ATOM   899   N  N     . GLY A 1 127 ? 141.719 117.443 102.678 1.00 24.37  ? 127  GLY A N     1 
ATOM   900   C  CA    . GLY A 1 127 ? 141.606 116.898 101.344 1.00 22.66  ? 127  GLY A CA    1 
ATOM   901   C  C     . GLY A 1 127 ? 140.208 116.530 100.907 1.00 26.28  ? 127  GLY A C     1 
ATOM   902   O  O     . GLY A 1 127 ? 140.058 115.876 99.871  1.00 32.92  ? 127  GLY A O     1 
ATOM   903   N  N     . ARG A 1 128 ? 139.184 116.922 101.660 1.00 23.61  ? 128  ARG A N     1 
ATOM   904   C  CA    . ARG A 1 128 ? 137.800 116.596 101.327 1.00 23.96  ? 128  ARG A CA    1 
ATOM   905   C  C     . ARG A 1 128 ? 137.144 117.837 100.730 1.00 26.78  ? 128  ARG A C     1 
ATOM   906   O  O     . ARG A 1 128 ? 136.464 118.607 101.406 1.00 33.12  ? 128  ARG A O     1 
ATOM   907   C  CB    . ARG A 1 128 ? 137.073 116.092 102.564 1.00 27.85  ? 128  ARG A CB    1 
ATOM   908   C  CG    . ARG A 1 128 ? 137.901 115.107 103.358 1.00 23.36  ? 128  ARG A CG    1 
ATOM   909   C  CD    . ARG A 1 128 ? 137.144 114.556 104.536 1.00 25.74  ? 128  ARG A CD    1 
ATOM   910   N  NE    . ARG A 1 128 ? 137.988 113.687 105.346 1.00 30.99  ? 128  ARG A NE    1 
ATOM   911   C  CZ    . ARG A 1 128 ? 138.117 112.383 105.156 1.00 30.64  ? 128  ARG A CZ    1 
ATOM   912   N  NH1   . ARG A 1 128 ? 137.462 111.757 104.193 1.00 32.71  ? 128  ARG A NH1   1 
ATOM   913   N  NH2   . ARG A 1 128 ? 138.923 111.688 105.952 1.00 28.40  ? 128  ARG A NH2   1 
ATOM   914   N  N     . TYR A 1 129 ? 137.357 118.020 99.425  1.00 29.59  ? 129  TYR A N     1 
ATOM   915   C  CA    . TYR A 1 129 ? 136.914 119.239 98.754  1.00 22.02  ? 129  TYR A CA    1 
ATOM   916   C  C     . TYR A 1 129 ? 135.397 119.297 98.606  1.00 23.61  ? 129  TYR A C     1 
ATOM   917   O  O     . TYR A 1 129 ? 134.809 120.385 98.682  1.00 31.81  ? 129  TYR A O     1 
ATOM   918   C  CB    . TYR A 1 129 ? 137.597 119.349 97.394  1.00 19.38  ? 129  TYR A CB    1 
ATOM   919   C  CG    . TYR A 1 129 ? 139.089 119.119 97.460  1.00 24.01  ? 129  TYR A CG    1 
ATOM   920   C  CD1   . TYR A 1 129 ? 139.926 120.041 98.070  1.00 28.56  ? 129  TYR A CD1   1 
ATOM   921   C  CD2   . TYR A 1 129 ? 139.659 117.980 96.914  1.00 28.41  ? 129  TYR A CD2   1 
ATOM   922   C  CE1   . TYR A 1 129 ? 141.289 119.835 98.133  1.00 30.90  ? 129  TYR A CE1   1 
ATOM   923   C  CE2   . TYR A 1 129 ? 141.021 117.766 96.972  1.00 32.84  ? 129  TYR A CE2   1 
ATOM   924   C  CZ    . TYR A 1 129 ? 141.830 118.697 97.583  1.00 34.29  ? 129  TYR A CZ    1 
ATOM   925   O  OH    . TYR A 1 129 ? 143.185 118.487 97.644  1.00 33.55  ? 129  TYR A OH    1 
ATOM   926   N  N     . HIS A 1 130 ? 134.749 118.149 98.400  1.00 32.65  ? 130  HIS A N     1 
ATOM   927   C  CA    . HIS A 1 130 ? 133.291 118.126 98.327  1.00 29.88  ? 130  HIS A CA    1 
ATOM   928   C  C     . HIS A 1 130 ? 132.668 118.571 99.642  1.00 35.04  ? 130  HIS A C     1 
ATOM   929   O  O     . HIS A 1 130 ? 131.663 119.291 99.651  1.00 37.21  ? 130  HIS A O     1 
ATOM   930   C  CB    . HIS A 1 130 ? 132.802 116.727 97.951  1.00 35.47  ? 130  HIS A CB    1 
ATOM   931   C  CG    . HIS A 1 130 ? 132.982 116.390 96.505  1.00 38.96  ? 130  HIS A CG    1 
ATOM   932   N  ND1   . HIS A 1 130 ? 134.210 116.091 95.956  1.00 38.78  ? 130  HIS A ND1   1 
ATOM   933   C  CD2   . HIS A 1 130 ? 132.087 116.302 95.493  1.00 34.69  ? 130  HIS A CD2   1 
ATOM   934   C  CE1   . HIS A 1 130 ? 134.064 115.834 94.669  1.00 36.92  ? 130  HIS A CE1   1 
ATOM   935   N  NE2   . HIS A 1 130 ? 132.785 115.955 94.363  1.00 37.83  ? 130  HIS A NE2   1 
ATOM   936   N  N     . GLU A 1 131 ? 133.260 118.164 100.767 1.00 27.66  ? 131  GLU A N     1 
ATOM   937   C  CA    . GLU A 1 131 ? 132.739 118.570 102.068 1.00 24.34  ? 131  GLU A CA    1 
ATOM   938   C  C     . GLU A 1 131 ? 132.972 120.055 102.320 1.00 24.79  ? 131  GLU A C     1 
ATOM   939   O  O     . GLU A 1 131 ? 132.134 120.728 102.936 1.00 32.12  ? 131  GLU A O     1 
ATOM   940   C  CB    . GLU A 1 131 ? 133.380 117.728 103.168 1.00 29.70  ? 131  GLU A CB    1 
ATOM   941   C  CG    . GLU A 1 131 ? 133.409 116.244 102.864 1.00 30.78  ? 131  GLU A CG    1 
ATOM   942   C  CD    . GLU A 1 131 ? 132.027 115.656 102.672 1.00 39.26  ? 131  GLU A CD    1 
ATOM   943   O  OE1   . GLU A 1 131 ? 131.081 116.111 103.348 1.00 37.35  ? 131  GLU A OE1   1 
ATOM   944   O  OE2   . GLU A 1 131 ? 131.884 114.737 101.840 1.00 39.85  ? 131  GLU A OE2   1 
ATOM   945   N  N     . ALA A 1 132 ? 134.102 120.585 101.847 1.00 20.79  ? 132  ALA A N     1 
ATOM   946   C  CA    . ALA A 1 132 ? 134.337 122.020 101.948 1.00 7.21   ? 132  ALA A CA    1 
ATOM   947   C  C     . ALA A 1 132 ? 133.295 122.799 101.158 1.00 18.51  ? 132  ALA A C     1 
ATOM   948   O  O     . ALA A 1 132 ? 132.757 123.801 101.644 1.00 34.12  ? 132  ALA A O     1 
ATOM   949   C  CB    . ALA A 1 132 ? 135.746 122.360 101.464 1.00 8.70   ? 132  ALA A CB    1 
ATOM   950   N  N     . VAL A 1 133 ? 132.978 122.340 99.946  1.00 24.56  ? 133  VAL A N     1 
ATOM   951   C  CA    . VAL A 1 133 ? 131.952 123.008 99.150  1.00 23.94  ? 133  VAL A CA    1 
ATOM   952   C  C     . VAL A 1 133 ? 130.589 122.888 99.823  1.00 20.48  ? 133  VAL A C     1 
ATOM   953   O  O     . VAL A 1 133 ? 129.784 123.827 99.797  1.00 28.42  ? 133  VAL A O     1 
ATOM   954   C  CB    . VAL A 1 133 ? 131.941 122.445 97.718  1.00 20.02  ? 133  VAL A CB    1 
ATOM   955   C  CG1   . VAL A 1 133 ? 130.795 123.029 96.916  1.00 13.54  ? 133  VAL A CG1   1 
ATOM   956   C  CG2   . VAL A 1 133 ? 133.260 122.743 97.036  1.00 21.30  ? 133  VAL A CG2   1 
ATOM   957   N  N     . LYS A 1 134 ? 130.312 121.739 100.445 1.00 28.78  ? 134  LYS A N     1 
ATOM   958   C  CA    . LYS A 1 134 ? 129.061 121.570 101.176 1.00 24.75  ? 134  LYS A CA    1 
ATOM   959   C  C     . LYS A 1 134 ? 128.948 122.574 102.317 1.00 26.82  ? 134  LYS A C     1 
ATOM   960   O  O     . LYS A 1 134 ? 127.873 123.136 102.558 1.00 29.97  ? 134  LYS A O     1 
ATOM   961   C  CB    . LYS A 1 134 ? 128.954 120.140 101.704 1.00 28.63  ? 134  LYS A CB    1 
ATOM   962   C  CG    . LYS A 1 134 ? 127.834 119.934 102.697 1.00 28.83  ? 134  LYS A CG    1 
ATOM   963   C  CD    . LYS A 1 134 ? 127.551 118.468 102.929 1.00 31.63  ? 134  LYS A CD    1 
ATOM   964   C  CE    . LYS A 1 134 ? 126.281 118.295 103.737 1.00 29.76  ? 134  LYS A CE    1 
ATOM   965   N  NZ    . LYS A 1 134 ? 125.908 116.866 103.890 1.00 34.97  ? 134  LYS A NZ    1 
ATOM   966   N  N     . LEU A 1 135 ? 130.047 122.813 103.030 1.00 22.15  ? 135  LEU A N     1 
ATOM   967   C  CA    . LEU A 1 135 ? 130.024 123.834 104.073 1.00 20.72  ? 135  LEU A CA    1 
ATOM   968   C  C     . LEU A 1 135 ? 129.885 125.236 103.486 1.00 28.37  ? 135  LEU A C     1 
ATOM   969   O  O     . LEU A 1 135 ? 129.272 126.109 104.110 1.00 30.04  ? 135  LEU A O     1 
ATOM   970   C  CB    . LEU A 1 135 ? 131.278 123.731 104.937 1.00 16.80  ? 135  LEU A CB    1 
ATOM   971   C  CG    . LEU A 1 135 ? 131.294 124.585 106.203 1.00 9.74   ? 135  LEU A CG    1 
ATOM   972   C  CD1   . LEU A 1 135 ? 130.000 124.416 106.972 1.00 18.34  ? 135  LEU A CD1   1 
ATOM   973   C  CD2   . LEU A 1 135 ? 132.469 124.200 107.065 1.00 12.09  ? 135  LEU A CD2   1 
ATOM   974   N  N     . MET A 1 136 ? 130.447 125.471 102.297 1.00 31.60  ? 136  MET A N     1 
ATOM   975   C  CA    . MET A 1 136 ? 130.276 126.763 101.633 1.00 18.74  ? 136  MET A CA    1 
ATOM   976   C  C     . MET A 1 136 ? 128.822 127.009 101.245 1.00 13.83  ? 136  MET A C     1 
ATOM   977   O  O     . MET A 1 136 ? 128.342 128.146 101.301 1.00 27.52  ? 136  MET A O     1 
ATOM   978   C  CB    . MET A 1 136 ? 131.159 126.846 100.389 1.00 11.69  ? 136  MET A CB    1 
ATOM   979   C  CG    . MET A 1 136 ? 132.644 126.773 100.645 1.00 10.73  ? 136  MET A CG    1 
ATOM   980   S  SD    . MET A 1 136 ? 133.563 126.598 99.109  1.00 22.91  ? 136  MET A SD    1 
ATOM   981   C  CE    . MET A 1 136 ? 135.157 126.083 99.724  1.00 24.13  ? 136  MET A CE    1 
ATOM   982   N  N     . LYS A 1 137 ? 128.114 125.957 100.827 1.00 20.86  ? 137  LYS A N     1 
ATOM   983   C  CA    . LYS A 1 137 ? 126.752 126.107 100.325 1.00 20.20  ? 137  LYS A CA    1 
ATOM   984   C  C     . LYS A 1 137 ? 125.763 126.536 101.400 1.00 28.54  ? 137  LYS A C     1 
ATOM   985   O  O     . LYS A 1 137 ? 124.675 127.014 101.063 1.00 37.80  ? 137  LYS A O     1 
ATOM   986   C  CB    . LYS A 1 137 ? 126.274 124.798 99.697  1.00 22.13  ? 137  LYS A CB    1 
ATOM   987   C  CG    . LYS A 1 137 ? 126.850 124.504 98.331  1.00 22.42  ? 137  LYS A CG    1 
ATOM   988   C  CD    . LYS A 1 137 ? 126.405 125.537 97.321  1.00 25.89  ? 137  LYS A CD    1 
ATOM   989   C  CE    . LYS A 1 137 ? 126.725 125.085 95.916  1.00 28.31  ? 137  LYS A CE    1 
ATOM   990   N  NZ    . LYS A 1 137 ? 128.166 124.772 95.769  1.00 30.43  ? 137  LYS A NZ    1 
ATOM   991   N  N     . GLU A 1 138 ? 126.101 126.363 102.678 1.00 24.34  ? 138  GLU A N     1 
ATOM   992   C  CA    . GLU A 1 138 ? 125.167 126.699 103.745 1.00 27.35  ? 138  GLU A CA    1 
ATOM   993   C  C     . GLU A 1 138 ? 124.933 128.196 103.873 1.00 28.59  ? 138  GLU A C     1 
ATOM   994   O  O     . GLU A 1 138 ? 123.896 128.603 104.404 1.00 35.89  ? 138  GLU A O     1 
ATOM   995   C  CB    . GLU A 1 138 ? 125.665 126.149 105.080 1.00 23.75  ? 138  GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 138 ? 125.517 124.654 105.228 1.00 29.90  ? 138  GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 138 ? 125.786 124.194 106.639 1.00 34.88  ? 138  GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 138 ? 126.154 125.042 107.476 1.00 33.24  ? 138  GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 138 ? 125.627 122.987 106.914 1.00 36.32  ? 138  GLU A OE2   1 
ATOM   1000  N  N     . LYS A 1 139 ? 125.862 129.019 103.407 1.00 19.22  ? 139  LYS A N     1 
ATOM   1001  C  CA    . LYS A 1 139 ? 125.737 130.461 103.542 1.00 16.12  ? 139  LYS A CA    1 
ATOM   1002  C  C     . LYS A 1 139 ? 125.652 131.206 102.223 1.00 29.92  ? 139  LYS A C     1 
ATOM   1003  O  O     . LYS A 1 139 ? 125.021 132.263 102.177 1.00 36.06  ? 139  LYS A O     1 
ATOM   1004  C  CB    . LYS A 1 139 ? 126.907 131.024 104.354 1.00 15.99  ? 139  LYS A CB    1 
ATOM   1005  C  CG    . LYS A 1 139 ? 126.515 131.463 105.743 1.00 26.46  ? 139  LYS A CG    1 
ATOM   1006  C  CD    . LYS A 1 139 ? 125.844 130.354 106.517 1.00 31.34  ? 139  LYS A CD    1 
ATOM   1007  C  CE    . LYS A 1 139 ? 125.472 130.820 107.906 1.00 30.33  ? 139  LYS A CE    1 
ATOM   1008  N  NZ    . LYS A 1 139 ? 126.671 131.273 108.657 1.00 34.35  ? 139  LYS A NZ    1 
ATOM   1009  N  N     . TYR A 1 140 ? 126.253 130.696 101.152 1.00 24.06  ? 140  TYR A N     1 
ATOM   1010  C  CA    . TYR A 1 140 ? 126.145 131.372 99.870  1.00 18.41  ? 140  TYR A CA    1 
ATOM   1011  C  C     . TYR A 1 140 ? 126.149 130.364 98.733  1.00 16.21  ? 140  TYR A C     1 
ATOM   1012  O  O     . TYR A 1 140 ? 126.688 129.261 98.851  1.00 21.89  ? 140  TYR A O     1 
ATOM   1013  C  CB    . TYR A 1 140 ? 127.262 132.407 99.667  1.00 24.31  ? 140  TYR A CB    1 
ATOM   1014  C  CG    . TYR A 1 140 ? 128.674 131.933 99.928  1.00 18.18  ? 140  TYR A CG    1 
ATOM   1015  C  CD1   . TYR A 1 140 ? 129.316 131.061 99.058  1.00 11.51  ? 140  TYR A CD1   1 
ATOM   1016  C  CD2   . TYR A 1 140 ? 129.384 132.398 101.023 1.00 19.93  ? 140  TYR A CD2   1 
ATOM   1017  C  CE1   . TYR A 1 140 ? 130.612 130.649 99.290  1.00 23.19  ? 140  TYR A CE1   1 
ATOM   1018  C  CE2   . TYR A 1 140 ? 130.677 131.993 101.258 1.00 16.34  ? 140  TYR A CE2   1 
ATOM   1019  C  CZ    . TYR A 1 140 ? 131.287 131.119 100.393 1.00 18.40  ? 140  TYR A CZ    1 
ATOM   1020  O  OH    . TYR A 1 140 ? 132.578 130.720 100.640 1.00 17.21  ? 140  TYR A OH    1 
ATOM   1021  N  N     . ILE A 1 141 ? 125.521 130.762 97.632  1.00 27.37  ? 141  ILE A N     1 
ATOM   1022  C  CA    . ILE A 1 141 ? 125.514 130.006 96.389  1.00 21.71  ? 141  ILE A CA    1 
ATOM   1023  C  C     . ILE A 1 141 ? 126.715 130.409 95.548  1.00 24.44  ? 141  ILE A C     1 
ATOM   1024  O  O     . ILE A 1 141 ? 127.376 131.414 95.834  1.00 36.37  ? 141  ILE A O     1 
ATOM   1025  C  CB    . ILE A 1 141 ? 124.214 130.243 95.611  1.00 18.14  ? 141  ILE A CB    1 
ATOM   1026  C  CG1   . ILE A 1 141 ? 124.133 131.707 95.204  1.00 16.85  ? 141  ILE A CG1   1 
ATOM   1027  C  CG2   . ILE A 1 141 ? 123.030 129.904 96.462  1.00 28.87  ? 141  ILE A CG2   1 
ATOM   1028  C  CD1   . ILE A 1 141 ? 123.073 131.981 94.212  1.00 15.10  ? 141  ILE A CD1   1 
ATOM   1029  N  N     . LEU A 1 142 ? 126.998 129.627 94.510  1.00 13.94  ? 142  LEU A N     1 
ATOM   1030  C  CA    . LEU A 1 142 ? 128.002 129.926 93.495  1.00 16.19  ? 142  LEU A CA    1 
ATOM   1031  C  C     . LEU A 1 142 ? 129.385 130.132 94.100  1.00 19.68  ? 142  LEU A C     1 
ATOM   1032  O  O     . LEU A 1 142 ? 129.918 131.247 94.048  1.00 31.87  ? 142  LEU A O     1 
ATOM   1033  C  CB    . LEU A 1 142 ? 127.598 131.166 92.696  1.00 21.82  ? 142  LEU A CB    1 
ATOM   1034  C  CG    . LEU A 1 142 ? 126.163 131.242 92.176  1.00 25.98  ? 142  LEU A CG    1 
ATOM   1035  C  CD1   . LEU A 1 142 ? 125.843 132.654 91.743  1.00 21.40  ? 142  LEU A CD1   1 
ATOM   1036  C  CD2   . LEU A 1 142 ? 125.936 130.274 91.036  1.00 24.42  ? 142  LEU A CD2   1 
ATOM   1037  N  N     . PRO A 1 143 ? 130.003 129.098 94.676  1.00 21.25  ? 143  PRO A N     1 
ATOM   1038  C  CA    . PRO A 1 143 ? 131.355 129.277 95.221  1.00 19.28  ? 143  PRO A CA    1 
ATOM   1039  C  C     . PRO A 1 143 ? 132.424 129.452 94.157  1.00 23.39  ? 143  PRO A C     1 
ATOM   1040  O  O     . PRO A 1 143 ? 133.455 130.065 94.445  1.00 29.71  ? 143  PRO A O     1 
ATOM   1041  C  CB    . PRO A 1 143 ? 131.576 127.997 96.035  1.00 25.62  ? 143  PRO A CB    1 
ATOM   1042  C  CG    . PRO A 1 143 ? 130.739 126.990 95.356  1.00 27.69  ? 143  PRO A CG    1 
ATOM   1043  C  CD    . PRO A 1 143 ? 129.524 127.716 94.850  1.00 30.34  ? 143  PRO A CD    1 
ATOM   1044  N  N     . ALA A 1 144 ? 132.219 128.940 92.942  1.00 30.66  ? 144  ALA A N     1 
ATOM   1045  C  CA    . ALA A 1 144 ? 133.198 129.153 91.879  1.00 26.25  ? 144  ALA A CA    1 
ATOM   1046  C  C     . ALA A 1 144 ? 133.161 130.590 91.379  1.00 29.69  ? 144  ALA A C     1 
ATOM   1047  O  O     . ALA A 1 144 ? 134.210 131.218 91.177  1.00 36.48  ? 144  ALA A O     1 
ATOM   1048  C  CB    . ALA A 1 144 ? 132.946 128.176 90.732  1.00 25.08  ? 144  ALA A CB    1 
ATOM   1049  N  N     . VAL A 1 145 ? 131.957 131.133 91.195  1.00 33.64  ? 145  VAL A N     1 
ATOM   1050  C  CA    . VAL A 1 145 ? 131.817 132.525 90.784  1.00 27.54  ? 145  VAL A CA    1 
ATOM   1051  C  C     . VAL A 1 145 ? 132.435 133.449 91.823  1.00 21.24  ? 145  VAL A C     1 
ATOM   1052  O  O     . VAL A 1 145 ? 133.169 134.381 91.482  1.00 26.02  ? 145  VAL A O     1 
ATOM   1053  C  CB    . VAL A 1 145 ? 130.335 132.858 90.536  1.00 15.72  ? 145  VAL A CB    1 
ATOM   1054  C  CG1   . VAL A 1 145 ? 130.167 134.329 90.206  1.00 18.52  ? 145  VAL A CG1   1 
ATOM   1055  C  CG2   . VAL A 1 145 ? 129.782 131.986 89.424  1.00 18.94  ? 145  VAL A CG2   1 
ATOM   1056  N  N     . LEU A 1 146 ? 132.164 133.196 93.105  1.00 17.43  ? 146  LEU A N     1 
ATOM   1057  C  CA    . LEU A 1 146 ? 132.733 134.023 94.162  1.00 18.69  ? 146  LEU A CA    1 
ATOM   1058  C  C     . LEU A 1 146 ? 134.237 133.823 94.290  1.00 16.85  ? 146  LEU A C     1 
ATOM   1059  O  O     . LEU A 1 146 ? 134.964 134.777 94.579  1.00 19.35  ? 146  LEU A O     1 
ATOM   1060  C  CB    . LEU A 1 146 ? 132.038 133.729 95.488  1.00 17.96  ? 146  LEU A CB    1 
ATOM   1061  C  CG    . LEU A 1 146 ? 130.561 134.114 95.539  1.00 7.53   ? 146  LEU A CG    1 
ATOM   1062  C  CD1   . LEU A 1 146 ? 129.964 133.742 96.874  1.00 17.01  ? 146  LEU A CD1   1 
ATOM   1063  C  CD2   . LEU A 1 146 ? 130.392 135.596 95.273  1.00 22.68  ? 146  LEU A CD2   1 
ATOM   1064  N  N     . GLY A 1 147 ? 134.726 132.602 94.074  1.00 17.84  ? 147  GLY A N     1 
ATOM   1065  C  CA    . GLY A 1 147 ? 136.158 132.386 94.043  1.00 22.11  ? 147  GLY A CA    1 
ATOM   1066  C  C     . GLY A 1 147 ? 136.842 133.081 92.891  1.00 25.59  ? 147  GLY A C     1 
ATOM   1067  O  O     . GLY A 1 147 ? 138.054 133.308 92.945  1.00 29.98  ? 147  GLY A O     1 
ATOM   1068  N  N     . ARG A 1 148 ? 136.092 133.410 91.843  1.00 23.50  ? 148  ARG A N     1 
ATOM   1069  C  CA    . ARG A 1 148 ? 136.668 134.166 90.739  1.00 17.17  ? 148  ARG A CA    1 
ATOM   1070  C  C     . ARG A 1 148 ? 136.515 135.681 90.890  1.00 22.53  ? 148  ARG A C     1 
ATOM   1071  O  O     . ARG A 1 148 ? 137.421 136.424 90.503  1.00 31.05  ? 148  ARG A O     1 
ATOM   1072  C  CB    . ARG A 1 148 ? 136.054 133.698 89.419  1.00 18.21  ? 148  ARG A CB    1 
ATOM   1073  C  CG    . ARG A 1 148 ? 136.654 132.395 88.924  1.00 20.46  ? 148  ARG A CG    1 
ATOM   1074  C  CD    . ARG A 1 148 ? 135.890 131.809 87.760  1.00 17.47  ? 148  ARG A CD    1 
ATOM   1075  N  NE    . ARG A 1 148 ? 136.620 130.709 87.142  1.00 24.31  ? 148  ARG A NE    1 
ATOM   1076  C  CZ    . ARG A 1 148 ? 136.619 129.462 87.592  1.00 33.02  ? 148  ARG A CZ    1 
ATOM   1077  N  NH1   . ARG A 1 148 ? 135.945 129.120 88.676  1.00 31.44  ? 148  ARG A NH1   1 
ATOM   1078  N  NH2   . ARG A 1 148 ? 137.317 128.538 86.940  1.00 33.48  ? 148  ARG A NH2   1 
ATOM   1079  N  N     . VAL A 1 149 ? 135.409 136.169 91.450  1.00 23.87  ? 149  VAL A N     1 
ATOM   1080  C  CA    . VAL A 1 149 ? 135.110 137.595 91.390  1.00 17.63  ? 149  VAL A CA    1 
ATOM   1081  C  C     . VAL A 1 149 ? 135.000 138.272 92.754  1.00 25.44  ? 149  VAL A C     1 
ATOM   1082  O  O     . VAL A 1 149 ? 135.191 139.496 92.821  1.00 33.23  ? 149  VAL A O     1 
ATOM   1083  C  CB    . VAL A 1 149 ? 133.831 137.870 90.567  1.00 15.34  ? 149  VAL A CB    1 
ATOM   1084  C  CG1   . VAL A 1 149 ? 133.894 137.175 89.218  1.00 15.93  ? 149  VAL A CG1   1 
ATOM   1085  C  CG2   . VAL A 1 149 ? 132.582 137.474 91.338  1.00 13.76  ? 149  VAL A CG2   1 
ATOM   1086  N  N     . CYS A 1 150 ? 134.715 137.554 93.840  1.00 14.92  ? 150  CYS A N     1 
ATOM   1087  C  CA    . CYS A 1 150 ? 134.348 138.218 95.089  1.00 10.25  ? 150  CYS A CA    1 
ATOM   1088  C  C     . CYS A 1 150 ? 135.487 139.102 95.591  1.00 22.68  ? 150  CYS A C     1 
ATOM   1089  O  O     . CYS A 1 150 ? 136.658 138.710 95.520  1.00 33.27  ? 150  CYS A O     1 
ATOM   1090  C  CB    . CYS A 1 150 ? 133.975 137.195 96.163  1.00 28.39  ? 150  CYS A CB    1 
ATOM   1091  S  SG    . CYS A 1 150 ? 133.784 137.857 97.834  1.00 37.95  ? 150  CYS A SG    1 
ATOM   1092  N  N     . PRO A 1 151 ? 135.182 140.303 96.098  1.00 19.55  ? 151  PRO A N     1 
ATOM   1093  C  CA    . PRO A 1 151 ? 136.238 141.218 96.558  1.00 15.59  ? 151  PRO A CA    1 
ATOM   1094  C  C     . PRO A 1 151 ? 137.028 140.714 97.757  1.00 29.49  ? 151  PRO A C     1 
ATOM   1095  O  O     . PRO A 1 151 ? 137.963 141.387 98.200  1.00 29.17  ? 151  PRO A O     1 
ATOM   1096  C  CB    . PRO A 1 151 ? 135.461 142.492 96.911  1.00 8.26   ? 151  PRO A CB    1 
ATOM   1097  C  CG    . PRO A 1 151 ? 134.217 142.413 96.107  1.00 8.32   ? 151  PRO A CG    1 
ATOM   1098  C  CD    . PRO A 1 151 ? 133.867 140.962 96.050  1.00 22.70  ? 151  PRO A CD    1 
ATOM   1099  N  N     . ALA A 1 152 ? 136.655 139.546 98.286  1.00 24.13  ? 152  ALA A N     1 
ATOM   1100  C  CA    . ALA A 1 152 ? 137.340 138.896 99.405  1.00 6.98   ? 152  ALA A CA    1 
ATOM   1101  C  C     . ALA A 1 152 ? 137.327 139.776 100.658 1.00 17.88  ? 152  ALA A C     1 
ATOM   1102  O  O     . ALA A 1 152 ? 138.362 140.227 101.151 1.00 16.79  ? 152  ALA A O     1 
ATOM   1103  C  CB    . ALA A 1 152 ? 138.767 138.494 99.021  1.00 16.41  ? 152  ALA A CB    1 
ATOM   1104  N  N     . PHE A 1 153 ? 136.116 140.015 101.165 1.00 20.32  ? 153  PHE A N     1 
ATOM   1105  C  CA    . PHE A 1 153 ? 135.954 140.724 102.428 1.00 14.51  ? 153  PHE A CA    1 
ATOM   1106  C  C     . PHE A 1 153 ? 136.486 139.927 103.611 1.00 21.79  ? 153  PHE A C     1 
ATOM   1107  O  O     . PHE A 1 153 ? 136.824 140.520 104.640 1.00 27.53  ? 153  PHE A O     1 
ATOM   1108  C  CB    . PHE A 1 153 ? 134.482 141.051 102.670 1.00 15.91  ? 153  PHE A CB    1 
ATOM   1109  C  CG    . PHE A 1 153 ? 133.864 141.911 101.610 1.00 16.25  ? 153  PHE A CG    1 
ATOM   1110  C  CD1   . PHE A 1 153 ? 134.186 143.251 101.512 1.00 19.49  ? 153  PHE A CD1   1 
ATOM   1111  C  CD2   . PHE A 1 153 ? 132.942 141.384 100.726 1.00 15.55  ? 153  PHE A CD2   1 
ATOM   1112  C  CE1   . PHE A 1 153 ? 133.610 144.044 100.545 1.00 27.14  ? 153  PHE A CE1   1 
ATOM   1113  C  CE2   . PHE A 1 153 ? 132.364 142.173 99.759  1.00 18.27  ? 153  PHE A CE2   1 
ATOM   1114  C  CZ    . PHE A 1 153 ? 132.698 143.504 99.668  1.00 23.07  ? 153  PHE A CZ    1 
ATOM   1115  N  N     . CYS A 1 154 ? 136.548 138.600 103.491 1.00 23.46  ? 154  CYS A N     1 
ATOM   1116  C  CA    . CYS A 1 154 ? 137.022 137.760 104.584 1.00 11.48  ? 154  CYS A CA    1 
ATOM   1117  C  C     . CYS A 1 154 ? 138.518 137.921 104.813 1.00 15.87  ? 154  CYS A C     1 
ATOM   1118  O  O     . CYS A 1 154 ? 138.993 137.762 105.942 1.00 27.10  ? 154  CYS A O     1 
ATOM   1119  C  CB    . CYS A 1 154 ? 136.691 136.300 104.291 1.00 14.90  ? 154  CYS A CB    1 
ATOM   1120  S  SG    . CYS A 1 154 ? 137.421 135.700 102.754 1.00 9.96   ? 154  CYS A SG    1 
ATOM   1121  N  N     . GLU A 1 155 ? 139.275 138.219 103.759 1.00 24.44  ? 155  GLU A N     1 
ATOM   1122  C  CA    . GLU A 1 155 ? 140.711 138.408 103.887 1.00 14.87  ? 155  GLU A CA    1 
ATOM   1123  C  C     . GLU A 1 155 ? 141.083 139.810 104.345 1.00 23.88  ? 155  GLU A C     1 
ATOM   1124  O  O     . GLU A 1 155 ? 142.262 140.061 104.613 1.00 35.29  ? 155  GLU A O     1 
ATOM   1125  C  CB    . GLU A 1 155 ? 141.397 138.101 102.555 1.00 19.59  ? 155  GLU A CB    1 
ATOM   1126  C  CG    . GLU A 1 155 ? 141.044 136.740 101.990 1.00 21.55  ? 155  GLU A CG    1 
ATOM   1127  C  CD    . GLU A 1 155 ? 141.677 136.486 100.641 1.00 24.23  ? 155  GLU A CD    1 
ATOM   1128  O  OE1   . GLU A 1 155 ? 142.617 137.218 100.275 1.00 24.54  ? 155  GLU A OE1   1 
ATOM   1129  O  OE2   . GLU A 1 155 ? 141.231 135.554 99.944  1.00 29.86  ? 155  GLU A OE2   1 
ATOM   1130  N  N     . GLU A 1 156 ? 140.116 140.724 104.440 1.00 21.72  ? 156  GLU A N     1 
ATOM   1131  C  CA    . GLU A 1 156 ? 140.419 142.073 104.901 1.00 21.59  ? 156  GLU A CA    1 
ATOM   1132  C  C     . GLU A 1 156 ? 140.748 142.109 106.388 1.00 29.36  ? 156  GLU A C     1 
ATOM   1133  O  O     . GLU A 1 156 ? 141.591 142.905 106.812 1.00 43.03  ? 156  GLU A O     1 
ATOM   1134  C  CB    . GLU A 1 156 ? 139.249 143.007 104.600 1.00 23.40  ? 156  GLU A CB    1 
ATOM   1135  C  CG    . GLU A 1 156 ? 138.949 143.170 103.125 1.00 34.31  ? 156  GLU A CG    1 
ATOM   1136  C  CD    . GLU A 1 156 ? 139.938 144.073 102.424 1.00 38.12  ? 156  GLU A CD    1 
ATOM   1137  O  OE1   . GLU A 1 156 ? 140.694 144.784 103.117 1.00 39.89  ? 156  GLU A OE1   1 
ATOM   1138  O  OE2   . GLU A 1 156 ? 139.959 144.074 101.177 1.00 32.57  ? 156  GLU A OE2   1 
ATOM   1139  N  N     . GLU A 1 157 ? 140.099 141.268 107.195 1.00 26.77  ? 157  GLU A N     1 
ATOM   1140  C  CA    . GLU A 1 157 ? 140.299 141.285 108.641 1.00 32.28  ? 157  GLU A CA    1 
ATOM   1141  C  C     . GLU A 1 157 ? 140.753 139.933 109.184 1.00 26.79  ? 157  GLU A C     1 
ATOM   1142  O  O     . GLU A 1 157 ? 140.620 139.678 110.384 1.00 35.81  ? 157  GLU A O     1 
ATOM   1143  C  CB    . GLU A 1 157 ? 139.030 141.751 109.361 1.00 38.62  ? 157  GLU A CB    1 
ATOM   1144  C  CG    . GLU A 1 157 ? 137.877 140.760 109.348 1.00 38.13  ? 157  GLU A CG    1 
ATOM   1145  C  CD    . GLU A 1 157 ? 137.264 140.600 107.985 1.00 38.41  ? 157  GLU A CD    1 
ATOM   1146  O  OE1   . GLU A 1 157 ? 136.860 141.619 107.392 1.00 36.24  ? 157  GLU A OE1   1 
ATOM   1147  O  OE2   . GLU A 1 157 ? 137.197 139.455 107.498 1.00 39.99  ? 157  GLU A OE2   1 
ATOM   1148  N  N     . CYS A 1 158 ? 141.308 139.076 108.332 1.00 21.34  ? 158  CYS A N     1 
ATOM   1149  C  CA    . CYS A 1 158 ? 141.823 137.790 108.781 1.00 16.75  ? 158  CYS A CA    1 
ATOM   1150  C  C     . CYS A 1 158 ? 142.944 137.989 109.795 1.00 22.47  ? 158  CYS A C     1 
ATOM   1151  O  O     . CYS A 1 158 ? 143.693 138.966 109.745 1.00 28.53  ? 158  CYS A O     1 
ATOM   1152  C  CB    . CYS A 1 158 ? 142.326 136.978 107.585 1.00 17.95  ? 158  CYS A CB    1 
ATOM   1153  S  SG    . CYS A 1 158 ? 143.127 135.411 107.981 1.00 39.08  ? 158  CYS A SG    1 
ATOM   1154  N  N     . ARG A 1 159 ? 143.038 137.060 110.744 1.00 15.74  ? 159  ARG A N     1 
ATOM   1155  C  CA    . ARG A 1 159 ? 144.059 137.150 111.779 1.00 17.82  ? 159  ARG A CA    1 
ATOM   1156  C  C     . ARG A 1 159 ? 145.454 136.824 111.265 1.00 26.38  ? 159  ARG A C     1 
ATOM   1157  O  O     . ARG A 1 159 ? 146.429 137.046 111.989 1.00 33.08  ? 159  ARG A O     1 
ATOM   1158  C  CB    . ARG A 1 159 ? 143.708 136.228 112.942 1.00 13.37  ? 159  ARG A CB    1 
ATOM   1159  C  CG    . ARG A 1 159 ? 142.488 136.664 113.716 1.00 21.22  ? 159  ARG A CG    1 
ATOM   1160  C  CD    . ARG A 1 159 ? 142.794 137.852 114.600 1.00 25.61  ? 159  ARG A CD    1 
ATOM   1161  N  NE    . ARG A 1 159 ? 141.588 138.404 115.200 1.00 23.82  ? 159  ARG A NE    1 
ATOM   1162  C  CZ    . ARG A 1 159 ? 141.003 137.923 116.287 1.00 16.83  ? 159  ARG A CZ    1 
ATOM   1163  N  NH1   . ARG A 1 159 ? 141.489 136.872 116.925 1.00 13.80  ? 159  ARG A NH1   1 
ATOM   1164  N  NH2   . ARG A 1 159 ? 139.906 138.514 116.748 1.00 20.92  ? 159  ARG A NH2   1 
ATOM   1165  N  N     . ARG A 1 160 ? 145.568 136.293 110.050 1.00 21.41  ? 160  ARG A N     1 
ATOM   1166  C  CA    . ARG A 1 160 ? 146.858 136.146 109.394 1.00 20.23  ? 160  ARG A CA    1 
ATOM   1167  C  C     . ARG A 1 160 ? 147.377 137.461 108.830 1.00 19.82  ? 160  ARG A C     1 
ATOM   1168  O  O     . ARG A 1 160 ? 148.561 137.543 108.489 1.00 31.11  ? 160  ARG A O     1 
ATOM   1169  C  CB    . ARG A 1 160 ? 146.764 135.100 108.280 1.00 19.13  ? 160  ARG A CB    1 
ATOM   1170  C  CG    . ARG A 1 160 ? 147.226 133.708 108.679 1.00 27.86  ? 160  ARG A CG    1 
ATOM   1171  C  CD    . ARG A 1 160 ? 148.740 133.615 108.685 1.00 16.27  ? 160  ARG A CD    1 
ATOM   1172  N  NE    . ARG A 1 160 ? 149.216 132.377 109.290 1.00 21.35  ? 160  ARG A NE    1 
ATOM   1173  C  CZ    . ARG A 1 160 ? 150.495 132.081 109.477 1.00 30.07  ? 160  ARG A CZ    1 
ATOM   1174  N  NH1   . ARG A 1 160 ? 151.457 132.901 109.093 1.00 28.15  ? 160  ARG A NH1   1 
ATOM   1175  N  NH2   . ARG A 1 160 ? 150.816 130.935 110.069 1.00 32.94  ? 160  ARG A NH2   1 
ATOM   1176  N  N     . ASN A 1 161 ? 146.522 138.483 108.714 1.00 16.28  ? 161  ASN A N     1 
ATOM   1177  C  CA    . ASN A 1 161 ? 147.008 139.824 108.408 1.00 19.14  ? 161  ASN A CA    1 
ATOM   1178  C  C     . ASN A 1 161 ? 147.906 140.345 109.518 1.00 23.36  ? 161  ASN A C     1 
ATOM   1179  O  O     . ASN A 1 161 ? 148.778 141.185 109.275 1.00 30.41  ? 161  ASN A O     1 
ATOM   1180  C  CB    . ASN A 1 161 ? 145.840 140.788 108.196 1.00 29.27  ? 161  ASN A CB    1 
ATOM   1181  C  CG    . ASN A 1 161 ? 145.074 140.516 106.921 1.00 27.00  ? 161  ASN A CG    1 
ATOM   1182  O  OD1   . ASN A 1 161 ? 145.506 140.890 105.834 1.00 29.36  ? 161  ASN A OD1   1 
ATOM   1183  N  ND2   . ASN A 1 161 ? 143.920 139.884 107.050 1.00 26.43  ? 161  ASN A ND2   1 
ATOM   1184  N  N     . LEU A 1 162 ? 147.698 139.865 110.740 1.00 29.56  ? 162  LEU A N     1 
ATOM   1185  C  CA    . LEU A 1 162 ? 148.530 140.222 111.877 1.00 34.81  ? 162  LEU A CA    1 
ATOM   1186  C  C     . LEU A 1 162 ? 149.810 139.402 111.952 1.00 32.67  ? 162  LEU A C     1 
ATOM   1187  O  O     . LEU A 1 162 ? 150.647 139.676 112.818 1.00 32.25  ? 162  LEU A O     1 
ATOM   1188  C  CB    . LEU A 1 162 ? 147.730 140.059 113.170 1.00 31.58  ? 162  LEU A CB    1 
ATOM   1189  C  CG    . LEU A 1 162 ? 146.379 140.776 113.194 1.00 26.55  ? 162  LEU A CG    1 
ATOM   1190  C  CD1   . LEU A 1 162 ? 145.576 140.379 114.412 1.00 27.97  ? 162  LEU A CD1   1 
ATOM   1191  C  CD2   . LEU A 1 162 ? 146.573 142.278 113.156 1.00 31.36  ? 162  LEU A CD2   1 
ATOM   1192  N  N     . VAL A 1 163 ? 149.988 138.406 111.084 1.00 36.14  ? 163  VAL A N     1 
ATOM   1193  C  CA    . VAL A 1 163 ? 151.225 137.637 111.099 1.00 33.25  ? 163  VAL A CA    1 
ATOM   1194  C  C     . VAL A 1 163 ? 152.040 137.910 109.844 1.00 35.50  ? 163  VAL A C     1 
ATOM   1195  O  O     . VAL A 1 163 ? 153.066 138.595 109.896 1.00 46.50  ? 163  VAL A O     1 
ATOM   1196  C  CB    . VAL A 1 163 ? 150.927 136.131 111.212 1.00 30.72  ? 163  VAL A CB    1 
ATOM   1197  C  CG1   . VAL A 1 163 ? 152.217 135.344 111.334 1.00 34.78  ? 163  VAL A CG1   1 
ATOM   1198  C  CG2   . VAL A 1 163 ? 149.996 135.854 112.372 1.00 33.02  ? 163  VAL A CG2   1 
ATOM   1199  N  N     . GLU A 1 164 ? 151.589 137.385 108.706 1.00 30.60  ? 164  GLU A N     1 
ATOM   1200  C  CA    . GLU A 1 164 ? 152.270 137.653 107.448 1.00 33.16  ? 164  GLU A CA    1 
ATOM   1201  C  C     . GLU A 1 164 ? 151.330 138.175 106.371 1.00 37.43  ? 164  GLU A C     1 
ATOM   1202  O  O     . GLU A 1 164 ? 151.532 139.266 105.828 1.00 42.53  ? 164  GLU A O     1 
ATOM   1203  C  CB    . GLU A 1 164 ? 152.977 136.391 106.953 1.00 33.36  ? 164  GLU A CB    1 
ATOM   1204  C  CG    . GLU A 1 164 ? 153.722 136.580 105.650 1.00 40.23  ? 164  GLU A CG    1 
ATOM   1205  C  CD    . GLU A 1 164 ? 154.584 135.387 105.298 1.00 42.20  ? 164  GLU A CD    1 
ATOM   1206  O  OE1   . GLU A 1 164 ? 154.754 134.502 106.161 1.00 42.81  ? 164  GLU A OE1   1 
ATOM   1207  O  OE2   . GLU A 1 164 ? 155.093 135.336 104.158 1.00 38.82  ? 164  GLU A OE2   1 
ATOM   1208  N  N     . GLU A 1 165 ? 150.280 137.403 106.079 1.00 33.62  ? 165  GLU A N     1 
ATOM   1209  C  CA    . GLU A 1 165 ? 149.466 137.581 104.886 1.00 27.61  ? 165  GLU A CA    1 
ATOM   1210  C  C     . GLU A 1 165 ? 148.176 136.806 105.061 1.00 25.51  ? 165  GLU A C     1 
ATOM   1211  O  O     . GLU A 1 165 ? 148.221 135.663 105.533 1.00 27.73  ? 165  GLU A O     1 
ATOM   1212  C  CB    . GLU A 1 165 ? 150.200 137.091 103.634 1.00 25.44  ? 165  GLU A CB    1 
ATOM   1213  C  CG    . GLU A 1 165 ? 150.954 138.161 102.881 1.00 34.69  ? 165  GLU A CG    1 
ATOM   1214  C  CD    . GLU A 1 165 ? 151.916 137.580 101.874 1.00 43.65  ? 165  GLU A CD    1 
ATOM   1215  O  OE1   . GLU A 1 165 ? 152.375 136.440 102.084 1.00 39.01  ? 165  GLU A OE1   1 
ATOM   1216  O  OE2   . GLU A 1 165 ? 152.214 138.262 100.872 1.00 45.88  ? 165  GLU A OE2   1 
ATOM   1217  N  N     . PRO A 1 166 ? 147.030 137.365 104.676 1.00 20.33  ? 166  PRO A N     1 
ATOM   1218  C  CA    . PRO A 1 166 ? 145.760 136.669 104.897 1.00 18.09  ? 166  PRO A CA    1 
ATOM   1219  C  C     . PRO A 1 166 ? 145.683 135.380 104.098 1.00 23.84  ? 166  PRO A C     1 
ATOM   1220  O  O     . PRO A 1 166 ? 146.293 135.241 103.036 1.00 32.07  ? 166  PRO A O     1 
ATOM   1221  C  CB    . PRO A 1 166 ? 144.714 137.682 104.424 1.00 12.70  ? 166  PRO A CB    1 
ATOM   1222  C  CG    . PRO A 1 166 ? 145.438 138.523 103.440 1.00 18.47  ? 166  PRO A CG    1 
ATOM   1223  C  CD    . PRO A 1 166 ? 146.846 138.627 103.943 1.00 23.34  ? 166  PRO A CD    1 
ATOM   1224  N  N     . LEU A 1 167 ? 144.930 134.427 104.634 1.00 17.46  ? 167  LEU A N     1 
ATOM   1225  C  CA    . LEU A 1 167 ? 144.813 133.126 103.995 1.00 13.79  ? 167  LEU A CA    1 
ATOM   1226  C  C     . LEU A 1 167 ? 144.116 133.255 102.647 1.00 30.69  ? 167  LEU A C     1 
ATOM   1227  O  O     . LEU A 1 167 ? 143.207 134.070 102.473 1.00 37.96  ? 167  LEU A O     1 
ATOM   1228  C  CB    . LEU A 1 167 ? 144.050 132.165 104.904 1.00 9.71   ? 167  LEU A CB    1 
ATOM   1229  C  CG    . LEU A 1 167 ? 144.511 130.713 104.826 1.00 13.28  ? 167  LEU A CG    1 
ATOM   1230  C  CD1   . LEU A 1 167 ? 146.004 130.666 104.966 1.00 32.37  ? 167  LEU A CD1   1 
ATOM   1231  C  CD2   . LEU A 1 167 ? 143.880 129.899 105.915 1.00 20.08  ? 167  LEU A CD2   1 
ATOM   1232  N  N     . ALA A 1 168 ? 144.556 132.446 101.685 1.00 29.98  ? 168  ALA A N     1 
ATOM   1233  C  CA    . ALA A 1 168 ? 143.982 132.475 100.346 1.00 19.26  ? 168  ALA A CA    1 
ATOM   1234  C  C     . ALA A 1 168 ? 142.616 131.808 100.346 1.00 15.41  ? 168  ALA A C     1 
ATOM   1235  O  O     . ALA A 1 168 ? 142.430 130.755 99.729  1.00 25.45  ? 168  ALA A O     1 
ATOM   1236  C  CB    . ALA A 1 168 ? 144.908 131.787 99.344  1.00 21.92  ? 168  ALA A CB    1 
ATOM   1237  N  N     . ILE A 1 169 ? 141.658 132.419 101.041 1.00 17.63  ? 169  ILE A N     1 
ATOM   1238  C  CA    . ILE A 1 169 ? 140.335 131.824 101.177 1.00 16.37  ? 169  ILE A CA    1 
ATOM   1239  C  C     . ILE A 1 169 ? 139.625 131.785 99.832  1.00 17.34  ? 169  ILE A C     1 
ATOM   1240  O  O     . ILE A 1 169 ? 138.995 130.784 99.477  1.00 25.74  ? 169  ILE A O     1 
ATOM   1241  C  CB    . ILE A 1 169 ? 139.525 132.591 102.233 1.00 22.84  ? 169  ILE A CB    1 
ATOM   1242  C  CG1   . ILE A 1 169 ? 140.277 132.589 103.565 1.00 11.30  ? 169  ILE A CG1   1 
ATOM   1243  C  CG2   . ILE A 1 169 ? 138.149 131.980 102.386 1.00 26.54  ? 169  ILE A CG2   1 
ATOM   1244  C  CD1   . ILE A 1 169 ? 139.901 133.710 104.488 1.00 19.82  ? 169  ILE A CD1   1 
ATOM   1245  N  N     . ARG A 1 170 ? 139.725 132.866 99.058  1.00 17.98  ? 170  ARG A N     1 
ATOM   1246  C  CA    . ARG A 1 170 ? 139.071 132.903 97.756  1.00 23.09  ? 170  ARG A CA    1 
ATOM   1247  C  C     . ARG A 1 170 ? 139.690 131.897 96.791  1.00 34.66  ? 170  ARG A C     1 
ATOM   1248  O  O     . ARG A 1 170 ? 138.973 131.220 96.049  1.00 36.80  ? 170  ARG A O     1 
ATOM   1249  C  CB    . ARG A 1 170 ? 139.134 134.316 97.183  1.00 27.47  ? 170  ARG A CB    1 
ATOM   1250  C  CG    . ARG A 1 170 ? 138.268 134.522 95.963  1.00 29.09  ? 170  ARG A CG    1 
ATOM   1251  C  CD    . ARG A 1 170 ? 138.463 135.899 95.373  1.00 24.91  ? 170  ARG A CD    1 
ATOM   1252  N  NE    . ARG A 1 170 ? 139.870 136.179 95.124  1.00 17.52  ? 170  ARG A NE    1 
ATOM   1253  C  CZ    . ARG A 1 170 ? 140.528 135.792 94.040  1.00 28.68  ? 170  ARG A CZ    1 
ATOM   1254  N  NH1   . ARG A 1 170 ? 139.933 135.106 93.079  1.00 29.53  ? 170  ARG A NH1   1 
ATOM   1255  N  NH2   . ARG A 1 170 ? 141.816 136.099 93.920  1.00 31.65  ? 170  ARG A NH2   1 
ATOM   1256  N  N     . GLN A 1 171 ? 141.018 131.766 96.802  1.00 26.32  ? 171  GLN A N     1 
ATOM   1257  C  CA    . GLN A 1 171 ? 141.677 130.857 95.867  1.00 15.45  ? 171  GLN A CA    1 
ATOM   1258  C  C     . GLN A 1 171 ? 141.456 129.396 96.245  1.00 28.70  ? 171  GLN A C     1 
ATOM   1259  O  O     . GLN A 1 171 ? 141.233 128.550 95.371  1.00 33.31  ? 171  GLN A O     1 
ATOM   1260  C  CB    . GLN A 1 171 ? 143.168 131.176 95.789  1.00 17.33  ? 171  GLN A CB    1 
ATOM   1261  C  CG    . GLN A 1 171 ? 143.542 132.144 94.681  1.00 28.76  ? 171  GLN A CG    1 
ATOM   1262  C  CD    . GLN A 1 171 ? 143.973 133.493 95.205  1.00 35.79  ? 171  GLN A CD    1 
ATOM   1263  O  OE1   . GLN A 1 171 ? 143.520 133.936 96.257  1.00 35.71  ? 171  GLN A OE1   1 
ATOM   1264  N  NE2   . GLN A 1 171 ? 144.859 134.154 94.475  1.00 30.86  ? 171  GLN A NE2   1 
ATOM   1265  N  N     . LEU A 1 172 ? 141.521 129.075 97.539  1.00 25.89  ? 172  LEU A N     1 
ATOM   1266  C  CA    . LEU A 1 172 ? 141.226 127.711 97.972  1.00 15.30  ? 172  LEU A CA    1 
ATOM   1267  C  C     . LEU A 1 172 ? 139.759 127.368 97.741  1.00 18.18  ? 172  LEU A C     1 
ATOM   1268  O  O     . LEU A 1 172 ? 139.429 126.232 97.382  1.00 31.92  ? 172  LEU A O     1 
ATOM   1269  C  CB    . LEU A 1 172 ? 141.600 127.532 99.442  1.00 20.42  ? 172  LEU A CB    1 
ATOM   1270  C  CG    . LEU A 1 172 ? 143.096 127.552 99.760  1.00 20.78  ? 172  LEU A CG    1 
ATOM   1271  C  CD1   . LEU A 1 172 ? 143.330 127.703 101.245 1.00 16.95  ? 172  LEU A CD1   1 
ATOM   1272  C  CD2   . LEU A 1 172 ? 143.768 126.295 99.248  1.00 22.37  ? 172  LEU A CD2   1 
ATOM   1273  N  N     . LYS A 1 173 ? 138.868 128.341 97.943  1.00 23.95  ? 173  LYS A N     1 
ATOM   1274  C  CA    . LYS A 1 173 ? 137.458 128.140 97.632  1.00 24.90  ? 173  LYS A CA    1 
ATOM   1275  C  C     . LYS A 1 173 ? 137.256 127.897 96.144  1.00 28.28  ? 173  LYS A C     1 
ATOM   1276  O  O     . LYS A 1 173 ? 136.447 127.051 95.752  1.00 34.59  ? 173  LYS A O     1 
ATOM   1277  C  CB    . LYS A 1 173 ? 136.647 129.349 98.099  1.00 26.75  ? 173  LYS A CB    1 
ATOM   1278  C  CG    . LYS A 1 173 ? 135.207 129.368 97.624  1.00 20.88  ? 173  LYS A CG    1 
ATOM   1279  C  CD    . LYS A 1 173 ? 134.521 130.669 97.994  1.00 17.23  ? 173  LYS A CD    1 
ATOM   1280  C  CE    . LYS A 1 173 ? 135.372 131.854 97.581  1.00 21.55  ? 173  LYS A CE    1 
ATOM   1281  N  NZ    . LYS A 1 173 ? 134.601 133.119 97.513  1.00 24.60  ? 173  LYS A NZ    1 
ATOM   1282  N  N     . ARG A 1 174 ? 137.990 128.626 95.301  1.00 28.05  ? 174  ARG A N     1 
ATOM   1283  C  CA    . ARG A 1 174 ? 137.923 128.396 93.864  1.00 29.22  ? 174  ARG A CA    1 
ATOM   1284  C  C     . ARG A 1 174 ? 138.412 127.001 93.502  1.00 31.69  ? 174  ARG A C     1 
ATOM   1285  O  O     . ARG A 1 174 ? 137.798 126.320 92.674  1.00 32.94  ? 174  ARG A O     1 
ATOM   1286  C  CB    . ARG A 1 174 ? 138.740 129.457 93.130  1.00 27.31  ? 174  ARG A CB    1 
ATOM   1287  C  CG    . ARG A 1 174 ? 138.824 129.252 91.637  1.00 23.68  ? 174  ARG A CG    1 
ATOM   1288  C  CD    . ARG A 1 174 ? 139.604 130.372 90.985  1.00 30.28  ? 174  ARG A CD    1 
ATOM   1289  N  NE    . ARG A 1 174 ? 139.674 130.209 89.540  1.00 29.29  ? 174  ARG A NE    1 
ATOM   1290  C  CZ    . ARG A 1 174 ? 140.103 131.143 88.704  1.00 29.19  ? 174  ARG A CZ    1 
ATOM   1291  N  NH1   . ARG A 1 174 ? 140.507 132.324 89.138  1.00 28.75  ? 174  ARG A NH1   1 
ATOM   1292  N  NH2   . ARG A 1 174 ? 140.126 130.885 87.401  1.00 30.83  ? 174  ARG A NH2   1 
ATOM   1293  N  N     . PHE A 1 175 ? 139.513 126.559 94.114  1.00 31.62  ? 175  PHE A N     1 
ATOM   1294  C  CA    . PHE A 1 175 ? 140.022 125.218 93.835  1.00 31.20  ? 175  PHE A CA    1 
ATOM   1295  C  C     . PHE A 1 175 ? 139.011 124.154 94.242  1.00 26.18  ? 175  PHE A C     1 
ATOM   1296  O  O     . PHE A 1 175 ? 138.746 123.212 93.487  1.00 33.26  ? 175  PHE A O     1 
ATOM   1297  C  CB    . PHE A 1 175 ? 141.355 124.982 94.550  1.00 31.89  ? 175  PHE A CB    1 
ATOM   1298  C  CG    . PHE A 1 175 ? 141.916 123.598 94.337  1.00 32.03  ? 175  PHE A CG    1 
ATOM   1299  C  CD1   . PHE A 1 175 ? 142.748 123.336 93.265  1.00 33.00  ? 175  PHE A CD1   1 
ATOM   1300  C  CD2   . PHE A 1 175 ? 141.596 122.557 95.196  1.00 30.47  ? 175  PHE A CD2   1 
ATOM   1301  C  CE1   . PHE A 1 175 ? 143.252 122.071 93.056  1.00 37.27  ? 175  PHE A CE1   1 
ATOM   1302  C  CE2   . PHE A 1 175 ? 142.096 121.290 94.987  1.00 33.99  ? 175  PHE A CE2   1 
ATOM   1303  C  CZ    . PHE A 1 175 ? 142.926 121.048 93.916  1.00 36.87  ? 175  PHE A CZ    1 
ATOM   1304  N  N     . ALA A 1 176 ? 138.444 124.286 95.443  1.00 15.21  ? 176  ALA A N     1 
ATOM   1305  C  CA    . ALA A 1 176 ? 137.477 123.303 95.922  1.00 17.33  ? 176  ALA A CA    1 
ATOM   1306  C  C     . ALA A 1 176 ? 136.212 123.309 95.074  1.00 25.43  ? 176  ALA A C     1 
ATOM   1307  O  O     . ALA A 1 176 ? 135.656 122.247 94.773  1.00 28.26  ? 176  ALA A O     1 
ATOM   1308  C  CB    . ALA A 1 176 ? 137.146 123.567 97.389  1.00 23.91  ? 176  ALA A CB    1 
ATOM   1309  N  N     . ALA A 1 177 ? 135.751 124.493 94.668  1.00 29.18  ? 177  ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 177 ? 134.561 124.586 93.834  1.00 23.88  ? 177  ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 177 ? 134.802 123.995 92.452  1.00 34.02  ? 177  ALA A C     1 
ATOM   1312  O  O     . ALA A 1 177 ? 133.923 123.329 91.902  1.00 40.76  ? 177  ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 177 ? 134.108 126.040 93.729  1.00 24.89  ? 177  ALA A CB    1 
ATOM   1314  N  N     . ASP A 1 178 ? 135.983 124.226 91.873  1.00 32.75  ? 178  ASP A N     1 
ATOM   1315  C  CA    . ASP A 1 178 ? 136.311 123.614 90.588  1.00 30.69  ? 178  ASP A CA    1 
ATOM   1316  C  C     . ASP A 1 178 ? 136.404 122.098 90.703  1.00 33.68  ? 178  ASP A C     1 
ATOM   1317  O  O     . ASP A 1 178 ? 135.923 121.372 89.823  1.00 34.64  ? 178  ASP A O     1 
ATOM   1318  C  CB    . ASP A 1 178 ? 137.620 124.189 90.051  1.00 36.19  ? 178  ASP A CB    1 
ATOM   1319  C  CG    . ASP A 1 178 ? 137.464 125.596 89.520  1.00 42.96  ? 178  ASP A CG    1 
ATOM   1320  O  OD1   . ASP A 1 178 ? 136.315 126.064 89.402  1.00 40.44  ? 178  ASP A OD1   1 
ATOM   1321  O  OD2   . ASP A 1 178 ? 138.494 126.233 89.220  1.00 44.84  ? 178  ASP A OD2   1 
ATOM   1322  N  N     . TYR A 1 179 ? 137.016 121.605 91.784  1.00 38.26  ? 179  TYR A N     1 
ATOM   1323  C  CA    . TYR A 1 179 ? 137.088 120.167 92.021  1.00 35.17  ? 179  TYR A CA    1 
ATOM   1324  C  C     . TYR A 1 179 ? 135.695 119.565 92.145  1.00 32.58  ? 179  TYR A C     1 
ATOM   1325  O  O     . TYR A 1 179 ? 135.435 118.467 91.642  1.00 40.85  ? 179  TYR A O     1 
ATOM   1326  C  CB    . TYR A 1 179 ? 137.909 119.895 93.285  1.00 30.42  ? 179  TYR A CB    1 
ATOM   1327  C  CG    . TYR A 1 179 ? 138.296 118.448 93.508  1.00 31.45  ? 179  TYR A CG    1 
ATOM   1328  C  CD1   . TYR A 1 179 ? 137.399 117.543 94.059  1.00 33.57  ? 179  TYR A CD1   1 
ATOM   1329  C  CD2   . TYR A 1 179 ? 139.567 117.994 93.189  1.00 33.27  ? 179  TYR A CD2   1 
ATOM   1330  C  CE1   . TYR A 1 179 ? 137.749 116.227 94.268  1.00 37.17  ? 179  TYR A CE1   1 
ATOM   1331  C  CE2   . TYR A 1 179 ? 139.927 116.679 93.399  1.00 35.88  ? 179  TYR A CE2   1 
ATOM   1332  C  CZ    . TYR A 1 179 ? 139.012 115.801 93.938  1.00 38.35  ? 179  TYR A CZ    1 
ATOM   1333  O  OH    . TYR A 1 179 ? 139.360 114.489 94.149  1.00 37.61  ? 179  TYR A OH    1 
ATOM   1334  N  N     . ASP A 1 180 ? 134.790 120.270 92.823  1.00 31.22  ? 180  ASP A N     1 
ATOM   1335  C  CA    . ASP A 1 180 ? 133.425 119.781 92.972  1.00 29.87  ? 180  ASP A CA    1 
ATOM   1336  C  C     . ASP A 1 180 ? 132.663 119.841 91.652  1.00 36.29  ? 180  ASP A C     1 
ATOM   1337  O  O     . ASP A 1 180 ? 131.854 118.957 91.358  1.00 47.62  ? 180  ASP A O     1 
ATOM   1338  C  CB    . ASP A 1 180 ? 132.710 120.585 94.057  1.00 36.47  ? 180  ASP A CB    1 
ATOM   1339  C  CG    . ASP A 1 180 ? 131.321 120.070 94.348  1.00 44.92  ? 180  ASP A CG    1 
ATOM   1340  O  OD1   . ASP A 1 180 ? 130.398 120.359 93.559  1.00 40.02  ? 180  ASP A OD1   1 
ATOM   1341  O  OD2   . ASP A 1 180 ? 131.152 119.371 95.368  1.00 52.98  ? 180  ASP A OD2   1 
ATOM   1342  N  N     . LEU A 1 181 ? 132.905 120.877 90.848  1.00 36.05  ? 181  LEU A N     1 
ATOM   1343  C  CA    . LEU A 1 181 ? 132.228 120.992 89.560  1.00 41.33  ? 181  LEU A CA    1 
ATOM   1344  C  C     . LEU A 1 181 ? 132.674 119.901 88.596  1.00 42.97  ? 181  LEU A C     1 
ATOM   1345  O  O     . LEU A 1 181 ? 131.861 119.377 87.826  1.00 39.97  ? 181  LEU A O     1 
ATOM   1346  C  CB    . LEU A 1 181 ? 132.480 122.371 88.954  1.00 38.99  ? 181  LEU A CB    1 
ATOM   1347  C  CG    . LEU A 1 181 ? 131.767 123.575 89.569  1.00 39.61  ? 181  LEU A CG    1 
ATOM   1348  C  CD1   . LEU A 1 181 ? 132.216 124.855 88.889  1.00 37.34  ? 181  LEU A CD1   1 
ATOM   1349  C  CD2   . LEU A 1 181 ? 130.261 123.414 89.480  1.00 38.76  ? 181  LEU A CD2   1 
ATOM   1350  N  N     . GLU A 1 182 ? 133.960 119.545 88.622  1.00 45.40  ? 182  GLU A N     1 
ATOM   1351  C  CA    . GLU A 1 182 ? 134.471 118.578 87.656  1.00 41.81  ? 182  GLU A CA    1 
ATOM   1352  C  C     . GLU A 1 182 ? 134.256 117.139 88.109  1.00 43.69  ? 182  GLU A C     1 
ATOM   1353  O  O     . GLU A 1 182 ? 133.943 116.271 87.288  1.00 52.65  ? 182  GLU A O     1 
ATOM   1354  C  CB    . GLU A 1 182 ? 135.955 118.832 87.399  1.00 43.29  ? 182  GLU A CB    1 
ATOM   1355  C  CG    . GLU A 1 182 ? 136.248 120.196 86.811  1.00 48.35  ? 182  GLU A CG    1 
ATOM   1356  C  CD    . GLU A 1 182 ? 137.703 120.368 86.448  1.00 52.03  ? 182  GLU A CD    1 
ATOM   1357  O  OE1   . GLU A 1 182 ? 138.403 119.345 86.302  1.00 52.10  ? 182  GLU A OE1   1 
ATOM   1358  O  OE2   . GLU A 1 182 ? 138.148 121.526 86.310  1.00 49.54  ? 182  GLU A OE2   1 
ATOM   1359  N  N     . ASN A 1 183 ? 134.421 116.863 89.400  1.00 36.04  ? 183  ASN A N     1 
ATOM   1360  C  CA    . ASN A 1 183 ? 134.405 115.497 89.921  1.00 35.10  ? 183  ASN A CA    1 
ATOM   1361  C  C     . ASN A 1 183 ? 133.060 115.132 90.531  1.00 35.02  ? 183  ASN A C     1 
ATOM   1362  O  O     . ASN A 1 183 ? 132.995 114.405 91.524  1.00 38.21  ? 183  ASN A O     1 
ATOM   1363  C  CB    . ASN A 1 183 ? 135.527 115.306 90.936  1.00 40.77  ? 183  ASN A CB    1 
ATOM   1364  C  CG    . ASN A 1 183 ? 136.904 115.401 90.307  1.00 40.23  ? 183  ASN A CG    1 
ATOM   1365  O  OD1   . ASN A 1 183 ? 137.472 114.399 89.879  1.00 42.20  ? 183  ASN A OD1   1 
ATOM   1366  N  ND2   . ASN A 1 183 ? 137.448 116.608 90.252  1.00 35.81  ? 183  ASN A ND2   1 
ATOM   1367  N  N     . GLY A 1 184 ? 131.970 115.629 89.957  1.00 40.67  ? 184  GLY A N     1 
ATOM   1368  C  CA    . GLY A 1 184 ? 130.650 115.329 90.451  1.00 44.48  ? 184  GLY A CA    1 
ATOM   1369  C  C     . GLY A 1 184 ? 130.168 116.404 91.397  1.00 47.89  ? 184  GLY A C     1 
ATOM   1370  O  O     . GLY A 1 184 ? 130.682 116.558 92.509  1.00 53.12  ? 184  GLY A O     1 
ATOM   1371  N  N     . PRO A 1 185 ? 129.177 117.179 90.968  1.00 47.45  ? 185  PRO A N     1 
ATOM   1372  C  CA    . PRO A 1 185 ? 128.710 118.297 91.792  1.00 46.60  ? 185  PRO A CA    1 
ATOM   1373  C  C     . PRO A 1 185 ? 128.039 117.814 93.066  1.00 47.47  ? 185  PRO A C     1 
ATOM   1374  O  O     . PRO A 1 185 ? 127.469 116.723 93.122  1.00 48.91  ? 185  PRO A O     1 
ATOM   1375  C  CB    . PRO A 1 185 ? 127.717 119.018 90.877  1.00 47.60  ? 185  PRO A CB    1 
ATOM   1376  C  CG    . PRO A 1 185 ? 127.229 117.955 89.959  1.00 49.98  ? 185  PRO A CG    1 
ATOM   1377  C  CD    . PRO A 1 185 ? 128.389 117.031 89.734  1.00 48.40  ? 185  PRO A CD    1 
ATOM   1378  N  N     . TRP A 1 186 ? 128.120 118.640 94.103  1.00 46.19  ? 186  TRP A N     1 
ATOM   1379  C  CA    . TRP A 1 186 ? 127.412 118.368 95.345  1.00 44.68  ? 186  TRP A CA    1 
ATOM   1380  C  C     . TRP A 1 186 ? 126.051 119.049 95.293  1.00 46.22  ? 186  TRP A C     1 
ATOM   1381  O  O     . TRP A 1 186 ? 125.968 120.272 95.146  1.00 50.51  ? 186  TRP A O     1 
ATOM   1382  C  CB    . TRP A 1 186 ? 128.198 118.843 96.566  1.00 41.14  ? 186  TRP A CB    1 
ATOM   1383  C  CG    . TRP A 1 186 ? 127.449 118.581 97.827  1.00 40.17  ? 186  TRP A CG    1 
ATOM   1384  C  CD1   . TRP A 1 186 ? 127.439 117.425 98.546  1.00 45.05  ? 186  TRP A CD1   1 
ATOM   1385  C  CD2   . TRP A 1 186 ? 126.564 119.481 98.502  1.00 47.38  ? 186  TRP A CD2   1 
ATOM   1386  N  NE1   . TRP A 1 186 ? 126.612 117.551 99.634  1.00 47.31  ? 186  TRP A NE1   1 
ATOM   1387  C  CE2   . TRP A 1 186 ? 126.062 118.805 99.628  1.00 45.34  ? 186  TRP A CE2   1 
ATOM   1388  C  CE3   . TRP A 1 186 ? 126.151 120.794 98.266  1.00 50.25  ? 186  TRP A CE3   1 
ATOM   1389  C  CZ2   . TRP A 1 186 ? 125.169 119.396 100.513 1.00 44.75  ? 186  TRP A CZ2   1 
ATOM   1390  C  CZ3   . TRP A 1 186 ? 125.268 121.378 99.147  1.00 43.87  ? 186  TRP A CZ3   1 
ATOM   1391  C  CH2   . TRP A 1 186 ? 124.789 120.682 100.259 1.00 45.10  ? 186  TRP A CH2   1 
ATOM   1392  N  N     . MET A 1 187 ? 124.992 118.259 95.415  1.00 50.06  ? 187  MET A N     1 
ATOM   1393  C  CA    . MET A 1 187 ? 123.642 118.787 95.402  1.00 47.09  ? 187  MET A CA    1 
ATOM   1394  C  C     . MET A 1 187 ? 122.993 118.577 96.757  1.00 49.27  ? 187  MET A C     1 
ATOM   1395  O  O     . MET A 1 187 ? 123.073 117.473 97.310  1.00 56.30  ? 187  MET A O     1 
ATOM   1396  C  CB    . MET A 1 187 ? 122.806 118.111 94.315  1.00 50.23  ? 187  MET A CB    1 
ATOM   1397  C  CG    . MET A 1 187 ? 123.298 118.379 92.909  1.00 52.53  ? 187  MET A CG    1 
ATOM   1398  S  SD    . MET A 1 187 ? 123.267 120.128 92.489  1.00 60.55  ? 187  MET A SD    1 
ATOM   1399  C  CE    . MET A 1 187 ? 123.756 120.060 90.772  1.00 51.87  ? 187  MET A CE    1 
ATOM   1400  N  N     . PRO A 1 188 ? 122.354 119.597 97.321  1.00 46.17  ? 188  PRO A N     1 
ATOM   1401  C  CA    . PRO A 1 188 ? 121.750 119.444 98.649  1.00 50.06  ? 188  PRO A CA    1 
ATOM   1402  C  C     . PRO A 1 188 ? 120.504 118.576 98.637  1.00 53.48  ? 188  PRO A C     1 
ATOM   1403  O  O     . PRO A 1 188 ? 120.043 118.145 97.577  1.00 52.64  ? 188  PRO A O     1 
ATOM   1404  C  CB    . PRO A 1 188 ? 121.423 120.888 99.049  1.00 46.75  ? 188  PRO A CB    1 
ATOM   1405  C  CG    . PRO A 1 188 ? 121.261 121.602 97.758  1.00 48.21  ? 188  PRO A CG    1 
ATOM   1406  C  CD    . PRO A 1 188 ? 122.246 120.976 96.819  1.00 48.92  ? 188  PRO A CD    1 
ATOM   1407  N  N     . GLU A 1 189 ? 119.959 118.311 99.818  1.00 61.14  ? 189  GLU A N     1 
ATOM   1408  C  CA    . GLU A 1 189 ? 118.731 117.546 99.966  1.00 59.25  ? 189  GLU A CA    1 
ATOM   1409  C  C     . GLU A 1 189 ? 117.560 118.506 100.104 1.00 58.10  ? 189  GLU A C     1 
ATOM   1410  O  O     . GLU A 1 189 ? 117.610 119.442 100.908 1.00 61.35  ? 189  GLU A O     1 
ATOM   1411  C  CB    . GLU A 1 189 ? 118.808 116.621 101.181 1.00 58.83  ? 189  GLU A CB    1 
ATOM   1412  C  CG    . GLU A 1 189 ? 119.955 115.627 101.129 1.00 62.41  ? 189  GLU A CG    1 
ATOM   1413  C  CD    . GLU A 1 189 ? 119.782 114.589 100.037 1.00 62.74  ? 189  GLU A CD    1 
ATOM   1414  O  OE1   . GLU A 1 189 ? 118.626 114.310 99.653  1.00 64.32  ? 189  GLU A OE1   1 
ATOM   1415  O  OE2   . GLU A 1 189 ? 120.803 114.051 99.561  1.00 60.81  ? 189  GLU A OE2   1 
ATOM   1416  N  N     . ILE A 1 190 ? 116.515 118.277 99.321  1.00 53.43  ? 190  ILE A N     1 
ATOM   1417  C  CA    . ILE A 1 190 ? 115.349 119.154 99.281  1.00 54.21  ? 190  ILE A CA    1 
ATOM   1418  C  C     . ILE A 1 190 ? 114.289 118.581 100.214 1.00 55.76  ? 190  ILE A C     1 
ATOM   1419  O  O     . ILE A 1 190 ? 113.836 117.448 99.994  1.00 57.98  ? 190  ILE A O     1 
ATOM   1420  C  CB    . ILE A 1 190 ? 114.806 119.308 97.855  1.00 52.52  ? 190  ILE A CB    1 
ATOM   1421  C  CG1   . ILE A 1 190 ? 115.919 119.764 96.913  1.00 51.82  ? 190  ILE A CG1   1 
ATOM   1422  C  CG2   . ILE A 1 190 ? 113.665 120.304 97.832  1.00 50.77  ? 190  ILE A CG2   1 
ATOM   1423  C  CD1   . ILE A 1 190 ? 116.550 121.074 97.306  1.00 51.68  ? 190  ILE A CD1   1 
ATOM   1424  N  N     . PRO A 1 191 ? 113.883 119.303 101.253 1.00 54.85  ? 191  PRO A N     1 
ATOM   1425  C  CA    . PRO A 1 191 ? 112.838 118.813 102.155 1.00 57.37  ? 191  PRO A CA    1 
ATOM   1426  C  C     . PRO A 1 191 ? 111.511 118.669 101.433 1.00 60.70  ? 191  PRO A C     1 
ATOM   1427  O  O     . PRO A 1 191 ? 111.322 119.242 100.349 1.00 57.69  ? 191  PRO A O     1 
ATOM   1428  C  CB    . PRO A 1 191 ? 112.772 119.906 103.232 1.00 55.62  ? 191  PRO A CB    1 
ATOM   1429  C  CG    . PRO A 1 191 ? 114.115 120.528 103.209 1.00 53.01  ? 191  PRO A CG    1 
ATOM   1430  C  CD    . PRO A 1 191 ? 114.539 120.510 101.775 1.00 53.12  ? 191  PRO A CD    1 
ATOM   1431  N  N     . PRO A 1 192 ? 110.573 117.904 101.994 1.00 74.10  ? 192  PRO A N     1 
ATOM   1432  C  CA    . PRO A 1 192 ? 109.278 117.710 101.333 1.00 72.45  ? 192  PRO A CA    1 
ATOM   1433  C  C     . PRO A 1 192 ? 108.545 119.024 101.112 1.00 72.12  ? 192  PRO A C     1 
ATOM   1434  O  O     . PRO A 1 192 ? 108.774 120.022 101.798 1.00 72.75  ? 192  PRO A O     1 
ATOM   1435  C  CB    . PRO A 1 192 ? 108.515 116.806 102.307 1.00 70.65  ? 192  PRO A CB    1 
ATOM   1436  C  CG    . PRO A 1 192 ? 109.577 116.083 103.045 1.00 72.35  ? 192  PRO A CG    1 
ATOM   1437  C  CD    . PRO A 1 192 ? 110.704 117.059 103.194 1.00 71.35  ? 192  PRO A CD    1 
ATOM   1438  N  N     . SER A 1 193 ? 107.656 119.006 100.121 1.00 75.22  ? 193  SER A N     1 
ATOM   1439  C  CA    . SER A 1 193 ? 107.008 120.226 99.658  1.00 75.04  ? 193  SER A CA    1 
ATOM   1440  C  C     . SER A 1 193 ? 106.174 120.864 100.760 1.00 73.13  ? 193  SER A C     1 
ATOM   1441  O  O     . SER A 1 193 ? 105.372 120.198 101.419 1.00 71.38  ? 193  SER A O     1 
ATOM   1442  C  CB    . SER A 1 193 ? 106.129 119.920 98.445  1.00 75.57  ? 193  SER A CB    1 
ATOM   1443  O  OG    . SER A 1 193 ? 105.447 121.081 98.004  1.00 76.00  ? 193  SER A OG    1 
ATOM   1444  N  N     . THR A 1 194 ? 106.369 122.165 100.949 1.00 73.35  ? 194  THR A N     1 
ATOM   1445  C  CA    . THR A 1 194 ? 105.589 122.952 101.891 1.00 78.82  ? 194  THR A CA    1 
ATOM   1446  C  C     . THR A 1 194 ? 104.290 123.467 101.289 1.00 78.49  ? 194  THR A C     1 
ATOM   1447  O  O     . THR A 1 194 ? 103.505 124.106 101.996 1.00 77.03  ? 194  THR A O     1 
ATOM   1448  C  CB    . THR A 1 194 ? 106.421 124.128 102.412 1.00 77.37  ? 194  THR A CB    1 
ATOM   1449  O  OG1   . THR A 1 194 ? 107.031 124.812 101.311 1.00 77.32  ? 194  THR A OG1   1 
ATOM   1450  C  CG2   . THR A 1 194 ? 107.506 123.634 103.350 1.00 69.82  ? 194  THR A CG2   1 
ATOM   1451  N  N     . GLY A 1 195 ? 104.046 123.210 100.007 1.00 80.01  ? 195  GLY A N     1 
ATOM   1452  C  CA    . GLY A 1 195 ? 102.818 123.618 99.365  1.00 80.73  ? 195  GLY A CA    1 
ATOM   1453  C  C     . GLY A 1 195 ? 102.755 125.071 98.959  1.00 83.38  ? 195  GLY A C     1 
ATOM   1454  O  O     . GLY A 1 195 ? 101.709 125.512 98.467  1.00 84.92  ? 195  GLY A O     1 
ATOM   1455  N  N     . LYS A 1 196 ? 103.829 125.830 99.147  1.00 67.26  ? 196  LYS A N     1 
ATOM   1456  C  CA    . LYS A 1 196 ? 103.867 127.242 98.800  1.00 65.03  ? 196  LYS A CA    1 
ATOM   1457  C  C     . LYS A 1 196 ? 104.799 127.457 97.618  1.00 65.60  ? 196  LYS A C     1 
ATOM   1458  O  O     . LYS A 1 196 ? 105.867 126.844 97.539  1.00 64.34  ? 196  LYS A O     1 
ATOM   1459  C  CB    . LYS A 1 196 ? 104.328 128.093 99.985  1.00 64.87  ? 196  LYS A CB    1 
ATOM   1460  C  CG    . LYS A 1 196 ? 103.214 128.549 100.915 1.00 65.17  ? 196  LYS A CG    1 
ATOM   1461  C  CD    . LYS A 1 196 ? 102.650 127.405 101.739 1.00 62.67  ? 196  LYS A CD    1 
ATOM   1462  C  CE    . LYS A 1 196 ? 101.546 127.886 102.665 1.00 66.23  ? 196  LYS A CE    1 
ATOM   1463  N  NZ    . LYS A 1 196 ? 100.981 126.775 103.479 1.00 69.49  ? 196  LYS A NZ    1 
ATOM   1464  N  N     . ARG A 1 197 ? 104.390 128.321 96.696  1.00 59.87  ? 197  ARG A N     1 
ATOM   1465  C  CA    . ARG A 1 197 ? 105.205 128.680 95.547  1.00 54.23  ? 197  ARG A CA    1 
ATOM   1466  C  C     . ARG A 1 197 ? 105.645 130.132 95.670  1.00 51.26  ? 197  ARG A C     1 
ATOM   1467  O  O     . ARG A 1 197 ? 104.870 130.993 96.096  1.00 54.42  ? 197  ARG A O     1 
ATOM   1468  C  CB    . ARG A 1 197 ? 104.448 128.457 94.234  1.00 50.98  ? 197  ARG A CB    1 
ATOM   1469  C  CG    . ARG A 1 197 ? 103.156 129.237 94.100  1.00 53.07  ? 197  ARG A CG    1 
ATOM   1470  C  CD    . ARG A 1 197 ? 102.594 129.123 92.696  1.00 54.80  ? 197  ARG A CD    1 
ATOM   1471  N  NE    . ARG A 1 197 ? 101.449 130.002 92.492  1.00 53.94  ? 197  ARG A NE    1 
ATOM   1472  C  CZ    . ARG A 1 197 ? 100.188 129.658 92.716  1.00 56.65  ? 197  ARG A CZ    1 
ATOM   1473  N  NH1   . ARG A 1 197 ? 99.869  128.455 93.164  1.00 53.34  ? 197  ARG A NH1   1 
ATOM   1474  N  NH2   . ARG A 1 197 ? 99.223  130.543 92.482  1.00 54.30  ? 197  ARG A NH2   1 
ATOM   1475  N  N     . ILE A 1 198 ? 106.897 130.400 95.312  1.00 40.60  ? 198  ILE A N     1 
ATOM   1476  C  CA    . ILE A 1 198 ? 107.478 131.730 95.431  1.00 42.35  ? 198  ILE A CA    1 
ATOM   1477  C  C     . ILE A 1 198 ? 107.880 132.217 94.048  1.00 44.33  ? 198  ILE A C     1 
ATOM   1478  O  O     . ILE A 1 198 ? 108.413 131.451 93.238  1.00 40.62  ? 198  ILE A O     1 
ATOM   1479  C  CB    . ILE A 1 198 ? 108.691 131.751 96.384  1.00 37.23  ? 198  ILE A CB    1 
ATOM   1480  C  CG1   . ILE A 1 198 ? 108.349 131.066 97.705  1.00 41.92  ? 198  ILE A CG1   1 
ATOM   1481  C  CG2   . ILE A 1 198 ? 109.128 133.179 96.646  1.00 36.05  ? 198  ILE A CG2   1 
ATOM   1482  C  CD1   . ILE A 1 198 ? 107.263 131.758 98.482  1.00 44.30  ? 198  ILE A CD1   1 
ATOM   1483  N  N     . ALA A 1 199 ? 107.619 133.491 93.782  1.00 38.76  ? 199  ALA A N     1 
ATOM   1484  C  CA    . ALA A 1 199 ? 107.996 134.133 92.534  1.00 36.02  ? 199  ALA A CA    1 
ATOM   1485  C  C     . ALA A 1 199 ? 109.171 135.066 92.788  1.00 33.38  ? 199  ALA A C     1 
ATOM   1486  O  O     . ALA A 1 199 ? 109.148 135.857 93.735  1.00 40.27  ? 199  ALA A O     1 
ATOM   1487  C  CB    . ALA A 1 199 ? 106.818 134.905 91.940  1.00 36.12  ? 199  ALA A CB    1 
ATOM   1488  N  N     . VAL A 1 200 ? 110.199 134.964 91.955  1.00 24.82  ? 200  VAL A N     1 
ATOM   1489  C  CA    . VAL A 1 200 ? 111.370 135.824 92.043  1.00 18.07  ? 200  VAL A CA    1 
ATOM   1490  C  C     . VAL A 1 200 ? 111.504 136.576 90.729  1.00 29.13  ? 200  VAL A C     1 
ATOM   1491  O  O     . VAL A 1 200 ? 111.504 135.963 89.656  1.00 38.72  ? 200  VAL A O     1 
ATOM   1492  C  CB    . VAL A 1 200 ? 112.647 135.024 92.351  1.00 23.01  ? 200  VAL A CB    1 
ATOM   1493  C  CG1   . VAL A 1 200 ? 113.849 135.935 92.316  1.00 20.58  ? 200  VAL A CG1   1 
ATOM   1494  C  CG2   . VAL A 1 200 ? 112.535 134.351 93.702  1.00 26.52  ? 200  VAL A CG2   1 
ATOM   1495  N  N     . VAL A 1 201 ? 111.613 137.895 90.814  1.00 30.22  ? 201  VAL A N     1 
ATOM   1496  C  CA    . VAL A 1 201 ? 111.738 138.759 89.648  1.00 31.06  ? 201  VAL A CA    1 
ATOM   1497  C  C     . VAL A 1 201 ? 113.186 139.229 89.601  1.00 30.18  ? 201  VAL A C     1 
ATOM   1498  O  O     . VAL A 1 201 ? 113.584 140.138 90.337  1.00 31.77  ? 201  VAL A O     1 
ATOM   1499  C  CB    . VAL A 1 201 ? 110.762 139.937 89.701  1.00 26.07  ? 201  VAL A CB    1 
ATOM   1500  C  CG1   . VAL A 1 201 ? 110.717 140.643 88.361  1.00 30.16  ? 201  VAL A CG1   1 
ATOM   1501  C  CG2   . VAL A 1 201 ? 109.379 139.457 90.106  1.00 24.37  ? 201  VAL A CG2   1 
ATOM   1502  N  N     . GLY A 1 202 ? 113.978 138.614 88.729  1.00 27.77  ? 202  GLY A N     1 
ATOM   1503  C  CA    . GLY A 1 202 ? 115.393 138.910 88.641  1.00 26.00  ? 202  GLY A CA    1 
ATOM   1504  C  C     . GLY A 1 202 ? 116.238 137.656 88.699  1.00 34.71  ? 202  GLY A C     1 
ATOM   1505  O  O     . GLY A 1 202 ? 116.140 136.878 89.653  1.00 45.47  ? 202  GLY A O     1 
ATOM   1506  N  N     . GLY A 1 203 ? 117.073 137.448 87.686  1.00 26.80  ? 203  GLY A N     1 
ATOM   1507  C  CA    . GLY A 1 203 ? 117.854 136.231 87.593  1.00 27.52  ? 203  GLY A CA    1 
ATOM   1508  C  C     . GLY A 1 203 ? 119.291 136.390 88.037  1.00 26.86  ? 203  GLY A C     1 
ATOM   1509  O  O     . GLY A 1 203 ? 120.138 135.550 87.723  1.00 31.50  ? 203  GLY A O     1 
ATOM   1510  N  N     . GLY A 1 204 ? 119.579 137.458 88.772  1.00 23.00  ? 204  GLY A N     1 
ATOM   1511  C  CA    . GLY A 1 204 ? 120.923 137.730 89.216  1.00 19.32  ? 204  GLY A CA    1 
ATOM   1512  C  C     . GLY A 1 204 ? 121.300 136.943 90.452  1.00 27.05  ? 204  GLY A C     1 
ATOM   1513  O  O     . GLY A 1 204 ? 120.607 136.006 90.858  1.00 34.19  ? 204  GLY A O     1 
ATOM   1514  N  N     . PRO A 1 205 ? 122.431 137.304 91.064  1.00 29.35  ? 205  PRO A N     1 
ATOM   1515  C  CA    . PRO A 1 205 ? 122.847 136.618 92.299  1.00 19.70  ? 205  PRO A CA    1 
ATOM   1516  C  C     . PRO A 1 205 ? 121.823 136.678 93.419  1.00 20.85  ? 205  PRO A C     1 
ATOM   1517  O  O     . PRO A 1 205 ? 121.654 135.689 94.139  1.00 32.41  ? 205  PRO A O     1 
ATOM   1518  C  CB    . PRO A 1 205 ? 124.139 137.352 92.674  1.00 22.76  ? 205  PRO A CB    1 
ATOM   1519  C  CG    . PRO A 1 205 ? 124.675 137.821 91.376  1.00 25.15  ? 205  PRO A CG    1 
ATOM   1520  C  CD    . PRO A 1 205 ? 123.486 138.186 90.541  1.00 27.42  ? 205  PRO A CD    1 
ATOM   1521  N  N     . ALA A 1 206 ? 121.132 137.807 93.587  1.00 23.33  ? 206  ALA A N     1 
ATOM   1522  C  CA    . ALA A 1 206 ? 120.139 137.910 94.653  1.00 24.13  ? 206  ALA A CA    1 
ATOM   1523  C  C     . ALA A 1 206 ? 118.949 136.998 94.385  1.00 22.50  ? 206  ALA A C     1 
ATOM   1524  O  O     . ALA A 1 206 ? 118.480 136.289 95.285  1.00 38.62  ? 206  ALA A O     1 
ATOM   1525  C  CB    . ALA A 1 206 ? 119.684 139.359 94.813  1.00 21.85  ? 206  ALA A CB    1 
ATOM   1526  N  N     . GLY A 1 207 ? 118.445 137.006 93.151  1.00 14.54  ? 207  GLY A N     1 
ATOM   1527  C  CA    . GLY A 1 207 ? 117.344 136.125 92.809  1.00 18.05  ? 207  GLY A CA    1 
ATOM   1528  C  C     . GLY A 1 207 ? 117.719 134.661 92.912  1.00 24.19  ? 207  GLY A C     1 
ATOM   1529  O  O     . GLY A 1 207 ? 116.945 133.845 93.416  1.00 26.48  ? 207  GLY A O     1 
ATOM   1530  N  N     . LEU A 1 208 ? 118.922 134.315 92.453  1.00 28.29  ? 208  LEU A N     1 
ATOM   1531  C  CA    . LEU A 1 208 ? 119.385 132.936 92.542  1.00 21.89  ? 208  LEU A CA    1 
ATOM   1532  C  C     . LEU A 1 208 ? 119.553 132.499 93.992  1.00 19.15  ? 208  LEU A C     1 
ATOM   1533  O  O     . LEU A 1 208 ? 119.222 131.364 94.345  1.00 22.76  ? 208  LEU A O     1 
ATOM   1534  C  CB    . LEU A 1 208 ? 120.694 132.776 91.772  1.00 23.42  ? 208  LEU A CB    1 
ATOM   1535  C  CG    . LEU A 1 208 ? 120.643 132.810 90.247  1.00 21.04  ? 208  LEU A CG    1 
ATOM   1536  C  CD1   . LEU A 1 208 ? 122.051 132.778 89.684  1.00 20.58  ? 208  LEU A CD1   1 
ATOM   1537  C  CD2   . LEU A 1 208 ? 119.824 131.652 89.709  1.00 21.73  ? 208  LEU A CD2   1 
ATOM   1538  N  N     . ALA A 1 209 ? 120.060 133.388 94.850  1.00 23.33  ? 209  ALA A N     1 
ATOM   1539  C  CA    . ALA A 1 209 ? 120.214 133.054 96.262  1.00 21.13  ? 209  ALA A CA    1 
ATOM   1540  C  C     . ALA A 1 209 ? 118.863 132.872 96.944  1.00 26.51  ? 209  ALA A C     1 
ATOM   1541  O  O     . ALA A 1 209 ? 118.669 131.914 97.704  1.00 33.82  ? 209  ALA A O     1 
ATOM   1542  C  CB    . ALA A 1 209 ? 121.030 134.133 96.968  1.00 15.72  ? 209  ALA A CB    1 
ATOM   1543  N  N     . CYS A 1 210 ? 117.918 133.779 96.683  1.00 26.93  ? 210  CYS A N     1 
ATOM   1544  C  CA    . CYS A 1 210 ? 116.580 133.639 97.248  1.00 18.57  ? 210  CYS A CA    1 
ATOM   1545  C  C     . CYS A 1 210 ? 115.923 132.348 96.779  1.00 27.35  ? 210  CYS A C     1 
ATOM   1546  O  O     . CYS A 1 210 ? 115.327 131.618 97.580  1.00 34.75  ? 210  CYS A O     1 
ATOM   1547  C  CB    . CYS A 1 210 ? 115.728 134.851 96.870  1.00 21.73  ? 210  CYS A CB    1 
ATOM   1548  S  SG    . CYS A 1 210 ? 114.042 134.844 97.511  1.00 31.73  ? 210  CYS A SG    1 
ATOM   1549  N  N     . ALA A 1 211 ? 116.055 132.035 95.488  1.00 25.57  ? 211  ALA A N     1 
ATOM   1550  C  CA    . ALA A 1 211 ? 115.472 130.814 94.946  1.00 19.11  ? 211  ALA A CA    1 
ATOM   1551  C  C     . ALA A 1 211 ? 116.111 129.571 95.551  1.00 17.94  ? 211  ALA A C     1 
ATOM   1552  O  O     . ALA A 1 211 ? 115.408 128.627 95.920  1.00 30.38  ? 211  ALA A O     1 
ATOM   1553  C  CB    . ALA A 1 211 ? 115.617 130.805 93.427  1.00 26.69  ? 211  ALA A CB    1 
ATOM   1554  N  N     . TYR A 1 212 ? 117.441 129.554 95.662  1.00 23.97  ? 212  TYR A N     1 
ATOM   1555  C  CA    . TYR A 1 212 ? 118.129 128.393 96.214  1.00 25.98  ? 212  TYR A CA    1 
ATOM   1556  C  C     . TYR A 1 212 ? 117.744 128.161 97.666  1.00 28.70  ? 212  TYR A C     1 
ATOM   1557  O  O     . TYR A 1 212 ? 117.486 127.023 98.073  1.00 31.14  ? 212  TYR A O     1 
ATOM   1558  C  CB    . TYR A 1 212 ? 119.642 128.575 96.079  1.00 22.49  ? 212  TYR A CB    1 
ATOM   1559  C  CG    . TYR A 1 212 ? 120.473 127.470 96.695  1.00 23.97  ? 212  TYR A CG    1 
ATOM   1560  C  CD1   . TYR A 1 212 ? 120.756 126.311 95.988  1.00 31.66  ? 212  TYR A CD1   1 
ATOM   1561  C  CD2   . TYR A 1 212 ? 120.989 127.594 97.978  1.00 24.30  ? 212  TYR A CD2   1 
ATOM   1562  C  CE1   . TYR A 1 212 ? 121.519 125.306 96.544  1.00 32.06  ? 212  TYR A CE1   1 
ATOM   1563  C  CE2   . TYR A 1 212 ? 121.753 126.596 98.538  1.00 23.92  ? 212  TYR A CE2   1 
ATOM   1564  C  CZ    . TYR A 1 212 ? 122.014 125.454 97.818  1.00 24.81  ? 212  TYR A CZ    1 
ATOM   1565  O  OH    . TYR A 1 212 ? 122.774 124.457 98.378  1.00 28.82  ? 212  TYR A OH    1 
ATOM   1566  N  N     . TYR A 1 213 ? 117.681 129.227 98.463  1.00 28.55  ? 213  TYR A N     1 
ATOM   1567  C  CA    . TYR A 1 213 ? 117.401 129.037 99.878  1.00 18.86  ? 213  TYR A CA    1 
ATOM   1568  C  C     . TYR A 1 213 ? 115.916 128.899 100.187 1.00 26.03  ? 213  TYR A C     1 
ATOM   1569  O  O     . TYR A 1 213 ? 115.575 128.454 101.286 1.00 38.74  ? 213  TYR A O     1 
ATOM   1570  C  CB    . TYR A 1 213 ? 118.034 130.169 100.685 1.00 19.86  ? 213  TYR A CB    1 
ATOM   1571  C  CG    . TYR A 1 213 ? 119.533 130.014 100.739 1.00 22.49  ? 213  TYR A CG    1 
ATOM   1572  C  CD1   . TYR A 1 213 ? 120.107 128.966 101.440 1.00 25.36  ? 213  TYR A CD1   1 
ATOM   1573  C  CD2   . TYR A 1 213 ? 120.370 130.887 100.064 1.00 26.58  ? 213  TYR A CD2   1 
ATOM   1574  C  CE1   . TYR A 1 213 ? 121.469 128.799 101.481 1.00 24.19  ? 213  TYR A CE1   1 
ATOM   1575  C  CE2   . TYR A 1 213 ? 121.738 130.729 100.101 1.00 21.70  ? 213  TYR A CE2   1 
ATOM   1576  C  CZ    . TYR A 1 213 ? 122.279 129.681 100.812 1.00 25.07  ? 213  TYR A CZ    1 
ATOM   1577  O  OH    . TYR A 1 213 ? 123.639 129.509 100.858 1.00 29.87  ? 213  TYR A OH    1 
ATOM   1578  N  N     . LEU A 1 214 ? 115.027 129.237 99.254  1.00 27.10  ? 214  LEU A N     1 
ATOM   1579  C  CA    . LEU A 1 214 ? 113.631 128.850 99.397  1.00 31.76  ? 214  LEU A CA    1 
ATOM   1580  C  C     . LEU A 1 214 ? 113.346 127.469 98.829  1.00 35.00  ? 214  LEU A C     1 
ATOM   1581  O  O     . LEU A 1 214 ? 112.361 126.839 99.229  1.00 44.35  ? 214  LEU A O     1 
ATOM   1582  C  CB    . LEU A 1 214 ? 112.720 129.880 98.727  1.00 33.31  ? 214  LEU A CB    1 
ATOM   1583  C  CG    . LEU A 1 214 ? 112.654 131.211 99.471  1.00 32.77  ? 214  LEU A CG    1 
ATOM   1584  C  CD1   . LEU A 1 214 ? 111.849 132.209 98.693  1.00 31.31  ? 214  LEU A CD1   1 
ATOM   1585  C  CD2   . LEU A 1 214 ? 112.066 131.014 100.855 1.00 34.32  ? 214  LEU A CD2   1 
ATOM   1586  N  N     . ARG A 1 215 ? 114.182 126.990 97.909  1.00 36.23  ? 215  ARG A N     1 
ATOM   1587  C  CA    . ARG A 1 215 ? 114.074 125.622 97.424  1.00 32.39  ? 215  ARG A CA    1 
ATOM   1588  C  C     . ARG A 1 215 ? 114.612 124.634 98.450  1.00 36.92  ? 215  ARG A C     1 
ATOM   1589  O  O     . ARG A 1 215 ? 114.063 123.539 98.608  1.00 38.96  ? 215  ARG A O     1 
ATOM   1590  C  CB    . ARG A 1 215 ? 114.817 125.487 96.093  1.00 33.08  ? 215  ARG A CB    1 
ATOM   1591  C  CG    . ARG A 1 215 ? 114.705 124.126 95.447  1.00 38.04  ? 215  ARG A CG    1 
ATOM   1592  C  CD    . ARG A 1 215 ? 113.260 123.731 95.256  1.00 37.71  ? 215  ARG A CD    1 
ATOM   1593  N  NE    . ARG A 1 215 ? 113.138 122.342 94.835  1.00 40.25  ? 215  ARG A NE    1 
ATOM   1594  C  CZ    . ARG A 1 215 ? 112.002 121.662 94.825  1.00 43.28  ? 215  ARG A CZ    1 
ATOM   1595  N  NH1   . ARG A 1 215 ? 110.866 122.211 95.219  1.00 40.90  ? 215  ARG A NH1   1 
ATOM   1596  N  NH2   . ARG A 1 215 ? 112.006 120.399 94.412  1.00 44.19  ? 215  ARG A NH2   1 
ATOM   1597  N  N     . THR A 1 216 ? 115.678 125.007 99.162  1.00 38.70  ? 216  THR A N     1 
ATOM   1598  C  CA    . THR A 1 216 ? 116.216 124.150 100.210 1.00 35.62  ? 216  THR A CA    1 
ATOM   1599  C  C     . THR A 1 216 ? 115.366 124.152 101.472 1.00 43.23  ? 216  THR A C     1 
ATOM   1600  O  O     . THR A 1 216 ? 115.663 123.389 102.396 1.00 46.89  ? 216  THR A O     1 
ATOM   1601  C  CB    . THR A 1 216 ? 117.648 124.556 100.566 1.00 33.64  ? 216  THR A CB    1 
ATOM   1602  O  OG1   . THR A 1 216 ? 117.683 125.938 100.935 1.00 42.08  ? 216  THR A OG1   1 
ATOM   1603  C  CG2   . THR A 1 216 ? 118.575 124.316 99.389  1.00 32.78  ? 216  THR A CG2   1 
ATOM   1604  N  N     . MET A 1 217 ? 114.341 124.999 101.549 1.00 36.92  ? 217  MET A N     1 
ATOM   1605  C  CA    . MET A 1 217 ? 113.386 124.944 102.645 1.00 38.75  ? 217  MET A CA    1 
ATOM   1606  C  C     . MET A 1 217 ? 112.109 124.200 102.283 1.00 42.44  ? 217  MET A C     1 
ATOM   1607  O  O     . MET A 1 217 ? 111.419 123.714 103.184 1.00 49.00  ? 217  MET A O     1 
ATOM   1608  C  CB    . MET A 1 217 ? 113.031 126.357 103.119 1.00 37.84  ? 217  MET A CB    1 
ATOM   1609  C  CG    . MET A 1 217 ? 114.171 127.086 103.806 1.00 37.69  ? 217  MET A CG    1 
ATOM   1610  S  SD    . MET A 1 217 ? 113.814 128.831 104.085 1.00 51.77  ? 217  MET A SD    1 
ATOM   1611  C  CE    . MET A 1 217 ? 115.351 129.380 104.811 1.00 39.54  ? 217  MET A CE    1 
ATOM   1612  N  N     . GLY A 1 218 ? 111.782 124.097 100.997 1.00 40.01  ? 218  GLY A N     1 
ATOM   1613  C  CA    . GLY A 1 218 ? 110.632 123.322 100.577 1.00 45.42  ? 218  GLY A CA    1 
ATOM   1614  C  C     . GLY A 1 218 ? 109.761 123.998 99.539  1.00 42.95  ? 218  GLY A C     1 
ATOM   1615  O  O     . GLY A 1 218 ? 109.164 123.328 98.692  1.00 45.61  ? 218  GLY A O     1 
ATOM   1616  N  N     . HIS A 1 219 ? 109.683 125.324 99.590  1.00 38.90  ? 219  HIS A N     1 
ATOM   1617  C  CA    . HIS A 1 219 ? 108.804 126.058 98.692  1.00 40.96  ? 219  HIS A CA    1 
ATOM   1618  C  C     . HIS A 1 219 ? 109.360 126.056 97.273  1.00 43.74  ? 219  HIS A C     1 
ATOM   1619  O  O     . HIS A 1 219 ? 110.538 126.351 97.056  1.00 46.39  ? 219  HIS A O     1 
ATOM   1620  C  CB    . HIS A 1 219 ? 108.628 127.491 99.187  1.00 41.12  ? 219  HIS A CB    1 
ATOM   1621  C  CG    . HIS A 1 219 ? 108.865 127.652 100.655 1.00 45.12  ? 219  HIS A CG    1 
ATOM   1622  N  ND1   . HIS A 1 219 ? 108.098 127.017 101.606 1.00 49.73  ? 219  HIS A ND1   1 
ATOM   1623  C  CD2   . HIS A 1 219 ? 109.789 128.371 101.335 1.00 43.21  ? 219  HIS A CD2   1 
ATOM   1624  C  CE1   . HIS A 1 219 ? 108.537 127.341 102.809 1.00 44.99  ? 219  HIS A CE1   1 
ATOM   1625  N  NE2   . HIS A 1 219 ? 109.562 128.162 102.672 1.00 42.31  ? 219  HIS A NE2   1 
ATOM   1626  N  N     . ASP A 1 220 ? 108.509 125.719 96.308  1.00 43.64  ? 220  ASP A N     1 
ATOM   1627  C  CA    . ASP A 1 220 ? 108.909 125.773 94.910  1.00 42.12  ? 220  ASP A CA    1 
ATOM   1628  C  C     . ASP A 1 220 ? 109.066 127.221 94.470  1.00 46.78  ? 220  ASP A C     1 
ATOM   1629  O  O     . ASP A 1 220 ? 108.263 128.085 94.830  1.00 49.85  ? 220  ASP A O     1 
ATOM   1630  C  CB    . ASP A 1 220 ? 107.881 125.061 94.033  1.00 44.63  ? 220  ASP A CB    1 
ATOM   1631  C  CG    . ASP A 1 220 ? 107.724 123.600 94.392  1.00 51.72  ? 220  ASP A CG    1 
ATOM   1632  O  OD1   . ASP A 1 220 ? 108.658 123.032 94.991  1.00 50.56  ? 220  ASP A OD1   1 
ATOM   1633  O  OD2   . ASP A 1 220 ? 106.668 123.017 94.072  1.00 52.11  ? 220  ASP A OD2   1 
ATOM   1634  N  N     . VAL A 1 221 ? 110.109 127.491 93.693  1.00 38.33  ? 221  VAL A N     1 
ATOM   1635  C  CA    . VAL A 1 221 ? 110.459 128.852 93.314  1.00 35.39  ? 221  VAL A CA    1 
ATOM   1636  C  C     . VAL A 1 221 ? 110.399 128.989 91.801  1.00 39.27  ? 221  VAL A C     1 
ATOM   1637  O  O     . VAL A 1 221 ? 110.833 128.095 91.067  1.00 45.37  ? 221  VAL A O     1 
ATOM   1638  C  CB    . VAL A 1 221 ? 111.854 129.250 93.835  1.00 30.34  ? 221  VAL A CB    1 
ATOM   1639  C  CG1   . VAL A 1 221 ? 112.023 130.747 93.752  1.00 30.96  ? 221  VAL A CG1   1 
ATOM   1640  C  CG2   . VAL A 1 221 ? 112.049 128.766 95.258  1.00 35.62  ? 221  VAL A CG2   1 
ATOM   1641  N  N     . THR A 1 222 ? 109.856 130.112 91.341  1.00 39.27  ? 222  THR A N     1 
ATOM   1642  C  CA    . THR A 1 222 ? 109.836 130.474 89.932  1.00 36.96  ? 222  THR A CA    1 
ATOM   1643  C  C     . THR A 1 222 ? 110.606 131.773 89.750  1.00 36.99  ? 222  THR A C     1 
ATOM   1644  O  O     . THR A 1 222 ? 110.317 132.768 90.423  1.00 47.83  ? 222  THR A O     1 
ATOM   1645  C  CB    . THR A 1 222 ? 108.403 130.636 89.425  1.00 45.37  ? 222  THR A CB    1 
ATOM   1646  O  OG1   . THR A 1 222 ? 107.647 129.464 89.748  1.00 46.61  ? 222  THR A OG1   1 
ATOM   1647  C  CG2   . THR A 1 222 ? 108.391 130.842 87.922  1.00 42.73  ? 222  THR A CG2   1 
ATOM   1648  N  N     . ILE A 1 223 ? 111.575 131.767 88.842  1.00 23.29  ? 223  ILE A N     1 
ATOM   1649  C  CA    . ILE A 1 223 ? 112.426 132.924 88.592  1.00 23.08  ? 223  ILE A CA    1 
ATOM   1650  C  C     . ILE A 1 223 ? 111.947 133.623 87.329  1.00 34.47  ? 223  ILE A C     1 
ATOM   1651  O  O     . ILE A 1 223 ? 111.780 132.986 86.282  1.00 41.16  ? 223  ILE A O     1 
ATOM   1652  C  CB    . ILE A 1 223 ? 113.904 132.517 88.470  1.00 26.98  ? 223  ILE A CB    1 
ATOM   1653  C  CG1   . ILE A 1 223 ? 114.415 131.949 89.792  1.00 30.63  ? 223  ILE A CG1   1 
ATOM   1654  C  CG2   . ILE A 1 223 ? 114.758 133.702 88.049  1.00 27.64  ? 223  ILE A CG2   1 
ATOM   1655  C  CD1   . ILE A 1 223 ? 115.895 131.660 89.791  1.00 31.79  ? 223  ILE A CD1   1 
ATOM   1656  N  N     . PHE A 1 224 ? 111.725 134.929 87.427  1.00 37.27  ? 224  PHE A N     1 
ATOM   1657  C  CA    . PHE A 1 224 ? 111.351 135.762 86.292  1.00 32.43  ? 224  PHE A CA    1 
ATOM   1658  C  C     . PHE A 1 224 ? 112.541 136.635 85.923  1.00 36.29  ? 224  PHE A C     1 
ATOM   1659  O  O     . PHE A 1 224 ? 113.025 137.412 86.753  1.00 37.47  ? 224  PHE A O     1 
ATOM   1660  C  CB    . PHE A 1 224 ? 110.133 136.625 86.619  1.00 34.82  ? 224  PHE A CB    1 
ATOM   1661  C  CG    . PHE A 1 224 ? 108.880 135.838 86.851  1.00 36.91  ? 224  PHE A CG    1 
ATOM   1662  C  CD1   . PHE A 1 224 ? 108.625 135.261 88.081  1.00 35.37  ? 224  PHE A CD1   1 
ATOM   1663  C  CD2   . PHE A 1 224 ? 107.952 135.681 85.840  1.00 36.74  ? 224  PHE A CD2   1 
ATOM   1664  C  CE1   . PHE A 1 224 ? 107.475 134.537 88.294  1.00 35.36  ? 224  PHE A CE1   1 
ATOM   1665  C  CE2   . PHE A 1 224 ? 106.800 134.959 86.050  1.00 39.28  ? 224  PHE A CE2   1 
ATOM   1666  C  CZ    . PHE A 1 224 ? 106.561 134.386 87.277  1.00 38.51  ? 224  PHE A CZ    1 
ATOM   1667  N  N     . ASP A 1 225 ? 113.008 136.506 84.686  1.00 35.30  ? 225  ASP A N     1 
ATOM   1668  C  CA    . ASP A 1 225 ? 114.144 137.274 84.205  1.00 38.31  ? 225  ASP A CA    1 
ATOM   1669  C  C     . ASP A 1 225 ? 113.839 137.787 82.807  1.00 38.62  ? 225  ASP A C     1 
ATOM   1670  O  O     . ASP A 1 225 ? 113.303 137.055 81.972  1.00 41.12  ? 225  ASP A O     1 
ATOM   1671  C  CB    . ASP A 1 225 ? 115.423 136.426 84.202  1.00 35.61  ? 225  ASP A CB    1 
ATOM   1672  C  CG    . ASP A 1 225 ? 116.677 137.260 84.055  1.00 37.56  ? 225  ASP A CG    1 
ATOM   1673  O  OD1   . ASP A 1 225 ? 116.565 138.494 83.921  1.00 36.68  ? 225  ASP A OD1   1 
ATOM   1674  O  OD2   . ASP A 1 225 ? 117.783 136.683 84.075  1.00 35.90  ? 225  ASP A OD2   1 
ATOM   1675  N  N     . ALA A 1 226 ? 114.174 139.054 82.562  1.00 39.58  ? 226  ALA A N     1 
ATOM   1676  C  CA    . ALA A 1 226 ? 113.928 139.645 81.252  1.00 44.47  ? 226  ALA A CA    1 
ATOM   1677  C  C     . ALA A 1 226 ? 114.843 139.040 80.195  1.00 48.53  ? 226  ALA A C     1 
ATOM   1678  O  O     . ALA A 1 226 ? 114.390 138.659 79.110  1.00 50.44  ? 226  ALA A O     1 
ATOM   1679  C  CB    . ALA A 1 226 ? 114.112 141.160 81.319  1.00 43.96  ? 226  ALA A CB    1 
ATOM   1680  N  N     . MET A 1 227 ? 116.135 138.943 80.497  1.00 47.30  ? 227  MET A N     1 
ATOM   1681  C  CA    . MET A 1 227 ? 117.101 138.420 79.549  1.00 46.56  ? 227  MET A CA    1 
ATOM   1682  C  C     . MET A 1 227 ? 116.927 136.912 79.371  1.00 48.88  ? 227  MET A C     1 
ATOM   1683  O  O     . MET A 1 227 ? 116.415 136.226 80.259  1.00 52.81  ? 227  MET A O     1 
ATOM   1684  C  CB    . MET A 1 227 ? 118.512 138.749 80.018  1.00 46.97  ? 227  MET A CB    1 
ATOM   1685  C  CG    . MET A 1 227 ? 118.916 140.183 79.752  1.00 46.81  ? 227  MET A CG    1 
ATOM   1686  S  SD    . MET A 1 227 ? 118.796 140.598 78.004  1.00 65.88  ? 227  MET A SD    1 
ATOM   1687  C  CE    . MET A 1 227 ? 119.467 142.256 77.996  1.00 50.55  ? 227  MET A CE    1 
ATOM   1688  N  N     . PRO A 1 228 ? 117.334 136.372 78.216  1.00 43.53  ? 228  PRO A N     1 
ATOM   1689  C  CA    . PRO A 1 228 ? 117.134 134.935 77.970  1.00 43.56  ? 228  PRO A CA    1 
ATOM   1690  C  C     . PRO A 1 228 ? 117.959 134.023 78.863  1.00 47.01  ? 228  PRO A C     1 
ATOM   1691  O  O     . PRO A 1 228 ? 117.623 132.838 78.977  1.00 47.40  ? 228  PRO A O     1 
ATOM   1692  C  CB    . PRO A 1 228 ? 117.531 134.774 76.497  1.00 43.64  ? 228  PRO A CB    1 
ATOM   1693  C  CG    . PRO A 1 228 ? 118.445 135.915 76.229  1.00 45.45  ? 228  PRO A CG    1 
ATOM   1694  C  CD    . PRO A 1 228 ? 117.925 137.049 77.049  1.00 41.57  ? 228  PRO A CD    1 
ATOM   1695  N  N     . HIS A 1 229 ? 119.022 134.519 79.488  1.00 47.61  ? 229  HIS A N     1 
ATOM   1696  C  CA    . HIS A 1 229 ? 119.899 133.697 80.306  1.00 40.95  ? 229  HIS A CA    1 
ATOM   1697  C  C     . HIS A 1 229 ? 119.834 134.135 81.762  1.00 41.67  ? 229  HIS A C     1 
ATOM   1698  O  O     . HIS A 1 229 ? 119.348 135.220 82.089  1.00 43.41  ? 229  HIS A O     1 
ATOM   1699  C  CB    . HIS A 1 229 ? 121.351 133.765 79.818  1.00 36.86  ? 229  HIS A CB    1 
ATOM   1700  C  CG    . HIS A 1 229 ? 121.586 133.073 78.513  1.00 41.33  ? 229  HIS A CG    1 
ATOM   1701  N  ND1   . HIS A 1 229 ? 120.777 132.058 78.051  1.00 44.68  ? 229  HIS A ND1   1 
ATOM   1702  C  CD2   . HIS A 1 229 ? 122.546 133.246 77.574  1.00 40.38  ? 229  HIS A CD2   1 
ATOM   1703  C  CE1   . HIS A 1 229 ? 121.226 131.637 76.883  1.00 43.36  ? 229  HIS A CE1   1 
ATOM   1704  N  NE2   . HIS A 1 229 ? 122.299 132.341 76.571  1.00 45.11  ? 229  HIS A NE2   1 
ATOM   1705  N  N     . LEU A 1 230 ? 120.336 133.270 82.634  1.00 39.51  ? 230  LEU A N     1 
ATOM   1706  C  CA    . LEU A 1 230 ? 120.409 133.553 84.055  1.00 37.93  ? 230  LEU A CA    1 
ATOM   1707  C  C     . LEU A 1 230 ? 121.763 134.149 84.418  1.00 34.19  ? 230  LEU A C     1 
ATOM   1708  O  O     . LEU A 1 230 ? 122.713 134.141 83.633  1.00 38.89  ? 230  LEU A O     1 
ATOM   1709  C  CB    . LEU A 1 230 ? 120.158 132.288 84.868  1.00 35.37  ? 230  LEU A CB    1 
ATOM   1710  C  CG    . LEU A 1 230 ? 118.720 131.787 84.875  1.00 39.45  ? 230  LEU A CG    1 
ATOM   1711  C  CD1   . LEU A 1 230 ? 118.656 130.471 85.601  1.00 37.28  ? 230  LEU A CD1   1 
ATOM   1712  C  CD2   . LEU A 1 230 ? 117.816 132.808 85.534  1.00 38.98  ? 230  LEU A CD2   1 
ATOM   1713  N  N     . GLY A 1 231 ? 121.845 134.664 85.641  1.00 26.22  ? 231  GLY A N     1 
ATOM   1714  C  CA    . GLY A 1 231 ? 123.016 135.326 86.141  1.00 31.14  ? 231  GLY A CA    1 
ATOM   1715  C  C     . GLY A 1 231 ? 122.919 136.836 86.122  1.00 30.16  ? 231  GLY A C     1 
ATOM   1716  O  O     . GLY A 1 231 ? 123.594 137.500 86.916  1.00 32.93  ? 231  GLY A O     1 
ATOM   1717  N  N     . GLY A 1 232 ? 122.081 137.389 85.250  1.00 25.40  ? 232  GLY A N     1 
ATOM   1718  C  CA    . GLY A 1 232 ? 121.923 138.824 85.154  1.00 30.14  ? 232  GLY A CA    1 
ATOM   1719  C  C     . GLY A 1 232 ? 123.207 139.531 84.782  1.00 24.71  ? 232  GLY A C     1 
ATOM   1720  O  O     . GLY A 1 232 ? 123.714 139.374 83.668  1.00 37.95  ? 232  GLY A O     1 
ATOM   1721  N  N     . MET A 1 233 ? 123.749 140.306 85.716  1.00 22.27  ? 233  MET A N     1 
ATOM   1722  C  CA    . MET A 1 233 ? 125.006 141.001 85.485  1.00 24.38  ? 233  MET A CA    1 
ATOM   1723  C  C     . MET A 1 233 ? 126.220 140.117 85.731  1.00 31.51  ? 233  MET A C     1 
ATOM   1724  O  O     . MET A 1 233 ? 127.350 140.599 85.612  1.00 30.49  ? 233  MET A O     1 
ATOM   1725  C  CB    . MET A 1 233 ? 125.090 142.251 86.359  1.00 29.71  ? 233  MET A CB    1 
ATOM   1726  C  CG    . MET A 1 233 ? 124.123 143.353 85.972  1.00 31.75  ? 233  MET A CG    1 
ATOM   1727  S  SD    . MET A 1 233 ? 124.401 143.992 84.313  1.00 35.83  ? 233  MET A SD    1 
ATOM   1728  C  CE    . MET A 1 233 ? 123.281 145.385 84.304  1.00 30.82  ? 233  MET A CE    1 
ATOM   1729  N  N     . MET A 1 234 ? 126.023 138.855 86.105  1.00 38.29  ? 234  MET A N     1 
ATOM   1730  C  CA    . MET A 1 234 ? 127.124 137.904 86.047  1.00 29.48  ? 234  MET A CA    1 
ATOM   1731  C  C     . MET A 1 234 ? 127.385 137.449 84.618  1.00 32.01  ? 234  MET A C     1 
ATOM   1732  O  O     . MET A 1 234 ? 128.521 137.108 84.276  1.00 38.73  ? 234  MET A O     1 
ATOM   1733  C  CB    . MET A 1 234 ? 126.836 136.702 86.944  1.00 22.72  ? 234  MET A CB    1 
ATOM   1734  C  CG    . MET A 1 234 ? 126.808 137.036 88.420  1.00 25.11  ? 234  MET A CG    1 
ATOM   1735  S  SD    . MET A 1 234 ? 126.801 135.567 89.453  1.00 39.53  ? 234  MET A SD    1 
ATOM   1736  C  CE    . MET A 1 234 ? 125.417 134.685 88.755  1.00 28.32  ? 234  MET A CE    1 
ATOM   1737  N  N     . ARG A 1 235 ? 126.351 137.448 83.780  1.00 33.39  ? 235  ARG A N     1 
ATOM   1738  C  CA    . ARG A 1 235 ? 126.451 137.067 82.378  1.00 25.57  ? 235  ARG A CA    1 
ATOM   1739  C  C     . ARG A 1 235 ? 126.602 138.262 81.447  1.00 31.83  ? 235  ARG A C     1 
ATOM   1740  O  O     . ARG A 1 235 ? 127.429 138.226 80.534  1.00 46.28  ? 235  ARG A O     1 
ATOM   1741  C  CB    . ARG A 1 235 ? 125.216 136.257 81.972  1.00 30.24  ? 235  ARG A CB    1 
ATOM   1742  C  CG    . ARG A 1 235 ? 125.188 135.838 80.519  1.00 31.84  ? 235  ARG A CG    1 
ATOM   1743  C  CD    . ARG A 1 235 ? 125.494 134.367 80.368  1.00 34.77  ? 235  ARG A CD    1 
ATOM   1744  N  NE    . ARG A 1 235 ? 124.575 133.544 81.144  1.00 34.56  ? 235  ARG A NE    1 
ATOM   1745  C  CZ    . ARG A 1 235 ? 124.580 132.219 81.145  1.00 37.38  ? 235  ARG A CZ    1 
ATOM   1746  N  NH1   . ARG A 1 235 ? 125.437 131.531 80.410  1.00 36.46  ? 235  ARG A NH1   1 
ATOM   1747  N  NH2   . ARG A 1 235 ? 123.705 131.567 81.903  1.00 42.04  ? 235  ARG A NH2   1 
ATOM   1748  N  N     . TYR A 1 236 ? 125.828 139.324 81.661  1.00 36.56  ? 236  TYR A N     1 
ATOM   1749  C  CA    . TYR A 1 236 ? 125.852 140.496 80.797  1.00 37.76  ? 236  TYR A CA    1 
ATOM   1750  C  C     . TYR A 1 236 ? 126.622 141.658 81.405  1.00 36.65  ? 236  TYR A C     1 
ATOM   1751  O  O     . TYR A 1 236 ? 126.638 142.750 80.832  1.00 42.71  ? 236  TYR A O     1 
ATOM   1752  C  CB    . TYR A 1 236 ? 124.424 140.920 80.466  1.00 38.16  ? 236  TYR A CB    1 
ATOM   1753  C  CG    . TYR A 1 236 ? 123.591 139.775 79.959  1.00 37.45  ? 236  TYR A CG    1 
ATOM   1754  C  CD1   . TYR A 1 236 ? 123.774 139.281 78.680  1.00 42.54  ? 236  TYR A CD1   1 
ATOM   1755  C  CD2   . TYR A 1 236 ? 122.636 139.172 80.765  1.00 36.82  ? 236  TYR A CD2   1 
ATOM   1756  C  CE1   . TYR A 1 236 ? 123.029 138.232 78.211  1.00 47.42  ? 236  TYR A CE1   1 
ATOM   1757  C  CE2   . TYR A 1 236 ? 121.887 138.117 80.305  1.00 40.57  ? 236  TYR A CE2   1 
ATOM   1758  C  CZ    . TYR A 1 236 ? 122.086 137.653 79.024  1.00 47.50  ? 236  TYR A CZ    1 
ATOM   1759  O  OH    . TYR A 1 236 ? 121.341 136.607 78.544  1.00 43.93  ? 236  TYR A OH    1 
ATOM   1760  N  N     . GLY A 1 237 ? 127.248 141.444 82.554  1.00 38.75  ? 237  GLY A N     1 
ATOM   1761  C  CA    . GLY A 1 237 ? 128.034 142.449 83.235  1.00 36.41  ? 237  GLY A CA    1 
ATOM   1762  C  C     . GLY A 1 237 ? 129.501 142.089 83.232  1.00 39.20  ? 237  GLY A C     1 
ATOM   1763  O  O     . GLY A 1 237 ? 130.234 142.445 82.305  1.00 40.09  ? 237  GLY A O     1 
ATOM   1764  N  N     . ILE A 1 238 ? 129.936 141.444 84.312  1.00 36.44  ? 238  ILE A N     1 
ATOM   1765  C  CA    . ILE A 1 238 ? 131.290 140.923 84.495  1.00 34.35  ? 238  ILE A CA    1 
ATOM   1766  C  C     . ILE A 1 238 ? 131.791 140.273 83.210  1.00 37.94  ? 238  ILE A C     1 
ATOM   1767  O  O     . ILE A 1 238 ? 131.177 139.322 82.707  1.00 40.83  ? 238  ILE A O     1 
ATOM   1768  C  CB    . ILE A 1 238 ? 131.341 139.928 85.664  1.00 27.95  ? 238  ILE A CB    1 
ATOM   1769  C  CG1   . ILE A 1 238 ? 130.578 140.481 86.866  1.00 29.26  ? 238  ILE A CG1   1 
ATOM   1770  C  CG2   . ILE A 1 238 ? 132.778 139.640 86.050  1.00 30.59  ? 238  ILE A CG2   1 
ATOM   1771  C  CD1   . ILE A 1 238 ? 130.489 139.520 88.019  1.00 31.55  ? 238  ILE A CD1   1 
ATOM   1772  N  N     . PRO A 1 239 ? 132.891 140.761 82.651  1.00 31.80  ? 239  PRO A N     1 
ATOM   1773  C  CA    . PRO A 1 239 ? 133.348 140.291 81.342  1.00 35.88  ? 239  PRO A CA    1 
ATOM   1774  C  C     . PRO A 1 239 ? 133.925 138.889 81.424  1.00 37.86  ? 239  PRO A C     1 
ATOM   1775  O  O     . PRO A 1 239 ? 134.255 138.409 82.519  1.00 40.18  ? 239  PRO A O     1 
ATOM   1776  C  CB    . PRO A 1 239 ? 134.419 141.323 80.965  1.00 35.23  ? 239  PRO A CB    1 
ATOM   1777  C  CG    . PRO A 1 239 ? 134.887 141.857 82.261  1.00 31.15  ? 239  PRO A CG    1 
ATOM   1778  C  CD    . PRO A 1 239 ? 133.712 141.866 83.165  1.00 27.46  ? 239  PRO A CD    1 
ATOM   1779  N  N     . PRO A 1 240 ? 134.050 138.192 80.288  1.00 38.68  ? 240  PRO A N     1 
ATOM   1780  C  CA    . PRO A 1 240 ? 134.446 136.775 80.330  1.00 36.77  ? 240  PRO A CA    1 
ATOM   1781  C  C     . PRO A 1 240 ? 135.908 136.519 80.682  1.00 42.36  ? 240  PRO A C     1 
ATOM   1782  O  O     . PRO A 1 240 ? 136.238 135.374 81.013  1.00 47.98  ? 240  PRO A O     1 
ATOM   1783  C  CB    . PRO A 1 240 ? 134.124 136.280 78.914  1.00 40.44  ? 240  PRO A CB    1 
ATOM   1784  C  CG    . PRO A 1 240 ? 134.150 137.495 78.074  1.00 42.09  ? 240  PRO A CG    1 
ATOM   1785  C  CD    . PRO A 1 240 ? 133.632 138.600 78.936  1.00 42.01  ? 240  PRO A CD    1 
ATOM   1786  N  N     . TYR A 1 241 ? 136.794 137.514 80.626  1.00 37.24  ? 241  TYR A N     1 
ATOM   1787  C  CA    . TYR A 1 241 ? 138.169 137.261 81.048  1.00 35.66  ? 241  TYR A CA    1 
ATOM   1788  C  C     . TYR A 1 241 ? 138.320 137.204 82.562  1.00 43.10  ? 241  TYR A C     1 
ATOM   1789  O  O     . TYR A 1 241 ? 139.371 136.777 83.049  1.00 47.54  ? 241  TYR A O     1 
ATOM   1790  C  CB    . TYR A 1 241 ? 139.124 138.313 80.475  1.00 41.85  ? 241  TYR A CB    1 
ATOM   1791  C  CG    . TYR A 1 241 ? 138.701 139.740 80.700  1.00 44.39  ? 241  TYR A CG    1 
ATOM   1792  C  CD1   . TYR A 1 241 ? 139.023 140.407 81.874  1.00 41.93  ? 241  TYR A CD1   1 
ATOM   1793  C  CD2   . TYR A 1 241 ? 137.998 140.427 79.728  1.00 44.87  ? 241  TYR A CD2   1 
ATOM   1794  C  CE1   . TYR A 1 241 ? 138.636 141.713 82.074  1.00 38.98  ? 241  TYR A CE1   1 
ATOM   1795  C  CE2   . TYR A 1 241 ? 137.618 141.726 79.915  1.00 44.62  ? 241  TYR A CE2   1 
ATOM   1796  C  CZ    . TYR A 1 241 ? 137.937 142.365 81.087  1.00 44.13  ? 241  TYR A CZ    1 
ATOM   1797  O  OH    . TYR A 1 241 ? 137.532 143.662 81.264  1.00 48.48  ? 241  TYR A OH    1 
ATOM   1798  N  N     . ARG A 1 242 ? 137.304 137.621 83.311  1.00 44.13  ? 242  ARG A N     1 
ATOM   1799  C  CA    . ARG A 1 242 ? 137.258 137.442 84.755  1.00 40.22  ? 242  ARG A CA    1 
ATOM   1800  C  C     . ARG A 1 242 ? 136.379 136.274 85.163  1.00 40.50  ? 242  ARG A C     1 
ATOM   1801  O  O     . ARG A 1 242 ? 136.702 135.555 86.112  1.00 40.85  ? 242  ARG A O     1 
ATOM   1802  C  CB    . ARG A 1 242 ? 136.733 138.709 85.428  1.00 34.25  ? 242  ARG A CB    1 
ATOM   1803  C  CG    . ARG A 1 242 ? 137.238 139.983 84.814  1.00 41.71  ? 242  ARG A CG    1 
ATOM   1804  C  CD    . ARG A 1 242 ? 136.611 141.162 85.501  1.00 40.43  ? 242  ARG A CD    1 
ATOM   1805  N  NE    . ARG A 1 242 ? 136.654 140.977 86.942  1.00 39.36  ? 242  ARG A NE    1 
ATOM   1806  C  CZ    . ARG A 1 242 ? 136.215 141.859 87.825  1.00 42.79  ? 242  ARG A CZ    1 
ATOM   1807  N  NH1   . ARG A 1 242 ? 135.680 143.008 87.447  1.00 42.27  ? 242  ARG A NH1   1 
ATOM   1808  N  NH2   . ARG A 1 242 ? 136.320 141.584 89.119  1.00 38.60  ? 242  ARG A NH2   1 
ATOM   1809  N  N     . LEU A 1 243 ? 135.270 136.079 84.459  1.00 38.39  ? 243  LEU A N     1 
ATOM   1810  C  CA    . LEU A 1 243 ? 134.313 135.018 84.758  1.00 36.89  ? 243  LEU A CA    1 
ATOM   1811  C  C     . LEU A 1 243 ? 133.942 134.344 83.445  1.00 43.56  ? 243  LEU A C     1 
ATOM   1812  O  O     . LEU A 1 243 ? 133.092 134.862 82.700  1.00 49.55  ? 243  LEU A O     1 
ATOM   1813  C  CB    . LEU A 1 243 ? 133.083 135.578 85.460  1.00 32.09  ? 243  LEU A CB    1 
ATOM   1814  C  CG    . LEU A 1 243 ? 132.048 134.592 85.992  1.00 31.94  ? 243  LEU A CG    1 
ATOM   1815  C  CD1   . LEU A 1 243 ? 132.678 133.644 86.991  1.00 37.27  ? 243  LEU A CD1   1 
ATOM   1816  C  CD2   . LEU A 1 243 ? 130.894 135.346 86.622  1.00 36.03  ? 243  LEU A CD2   1 
ATOM   1817  N  N     . PRO A 1 244 ? 134.581 133.226 83.107  1.00 34.75  ? 244  PRO A N     1 
ATOM   1818  C  CA    . PRO A 1 244 ? 134.180 132.484 81.907  1.00 32.37  ? 244  PRO A CA    1 
ATOM   1819  C  C     . PRO A 1 244 ? 132.739 132.010 82.011  1.00 36.40  ? 244  PRO A C     1 
ATOM   1820  O  O     . PRO A 1 244 ? 132.258 131.652 83.088  1.00 44.41  ? 244  PRO A O     1 
ATOM   1821  C  CB    . PRO A 1 244 ? 135.163 131.311 81.876  1.00 34.57  ? 244  PRO A CB    1 
ATOM   1822  C  CG    . PRO A 1 244 ? 136.351 131.806 82.621  1.00 33.76  ? 244  PRO A CG    1 
ATOM   1823  C  CD    . PRO A 1 244 ? 135.806 132.677 83.709  1.00 31.97  ? 244  PRO A CD    1 
ATOM   1824  N  N     . LYS A 1 245 ? 132.046 132.015 80.874  1.00 35.92  ? 245  LYS A N     1 
ATOM   1825  C  CA    . LYS A 1 245 ? 130.618 131.736 80.883  1.00 35.28  ? 245  LYS A CA    1 
ATOM   1826  C  C     . LYS A 1 245 ? 130.299 130.250 80.961  1.00 40.24  ? 245  LYS A C     1 
ATOM   1827  O  O     . LYS A 1 245 ? 129.167 129.898 81.298  1.00 43.77  ? 245  LYS A O     1 
ATOM   1828  C  CB    . LYS A 1 245 ? 129.952 132.350 79.651  1.00 35.24  ? 245  LYS A CB    1 
ATOM   1829  C  CG    . LYS A 1 245 ? 130.210 133.839 79.494  1.00 35.50  ? 245  LYS A CG    1 
ATOM   1830  C  CD    . LYS A 1 245 ? 129.956 134.593 80.789  1.00 35.69  ? 245  LYS A CD    1 
ATOM   1831  C  CE    . LYS A 1 245 ? 130.396 136.041 80.673  1.00 34.95  ? 245  LYS A CE    1 
ATOM   1832  N  NZ    . LYS A 1 245 ? 130.314 136.762 81.971  1.00 27.53  ? 245  LYS A NZ    1 
ATOM   1833  N  N     . ASP A 1 246 ? 131.258 129.370 80.665  1.00 34.82  ? 246  ASP A N     1 
ATOM   1834  C  CA    . ASP A 1 246 ? 131.030 127.949 80.908  1.00 34.12  ? 246  ASP A CA    1 
ATOM   1835  C  C     . ASP A 1 246 ? 131.073 127.640 82.399  1.00 42.40  ? 246  ASP A C     1 
ATOM   1836  O  O     . ASP A 1 246 ? 130.294 126.815 82.893  1.00 47.38  ? 246  ASP A O     1 
ATOM   1837  C  CB    . ASP A 1 246 ? 132.053 127.108 80.146  1.00 42.73  ? 246  ASP A CB    1 
ATOM   1838  C  CG    . ASP A 1 246 ? 133.477 127.500 80.459  1.00 47.93  ? 246  ASP A CG    1 
ATOM   1839  O  OD1   . ASP A 1 246 ? 133.727 128.702 80.674  1.00 45.06  ? 246  ASP A OD1   1 
ATOM   1840  O  OD2   . ASP A 1 246 ? 134.348 126.607 80.492  1.00 50.75  ? 246  ASP A OD2   1 
ATOM   1841  N  N     . VAL A 1 247 ? 131.965 128.310 83.132  1.00 42.33  ? 247  VAL A N     1 
ATOM   1842  C  CA    . VAL A 1 247 ? 131.975 128.213 84.589  1.00 40.77  ? 247  VAL A CA    1 
ATOM   1843  C  C     . VAL A 1 247 ? 130.659 128.724 85.158  1.00 36.31  ? 247  VAL A C     1 
ATOM   1844  O  O     . VAL A 1 247 ? 130.082 128.125 86.075  1.00 38.69  ? 247  VAL A O     1 
ATOM   1845  C  CB    . VAL A 1 247 ? 133.179 128.984 85.161  1.00 35.74  ? 247  VAL A CB    1 
ATOM   1846  C  CG1   . VAL A 1 247 ? 133.116 129.039 86.675  1.00 38.90  ? 247  VAL A CG1   1 
ATOM   1847  C  CG2   . VAL A 1 247 ? 134.476 128.347 84.705  1.00 32.82  ? 247  VAL A CG2   1 
ATOM   1848  N  N     . LEU A 1 248 ? 130.164 129.840 84.621  1.00 37.02  ? 248  LEU A N     1 
ATOM   1849  C  CA    . LEU A 1 248 ? 128.885 130.374 85.069  1.00 40.89  ? 248  LEU A CA    1 
ATOM   1850  C  C     . LEU A 1 248 ? 127.743 129.424 84.739  1.00 36.27  ? 248  LEU A C     1 
ATOM   1851  O  O     . LEU A 1 248 ? 126.820 129.261 85.541  1.00 42.19  ? 248  LEU A O     1 
ATOM   1852  C  CB    . LEU A 1 248 ? 128.641 131.745 84.443  1.00 38.94  ? 248  LEU A CB    1 
ATOM   1853  C  CG    . LEU A 1 248 ? 127.413 132.492 84.955  1.00 29.21  ? 248  LEU A CG    1 
ATOM   1854  C  CD1   . LEU A 1 248 ? 127.512 132.694 86.453  1.00 32.98  ? 248  LEU A CD1   1 
ATOM   1855  C  CD2   . LEU A 1 248 ? 127.262 133.821 84.243  1.00 35.18  ? 248  LEU A CD2   1 
ATOM   1856  N  N     . ASP A 1 249 ? 127.781 128.795 83.563  1.00 26.85  ? 249  ASP A N     1 
ATOM   1857  C  CA    . ASP A 1 249 ? 126.746 127.828 83.217  1.00 29.94  ? 249  ASP A CA    1 
ATOM   1858  C  C     . ASP A 1 249 ? 126.763 126.640 84.167  1.00 34.86  ? 249  ASP A C     1 
ATOM   1859  O  O     . ASP A 1 249 ? 125.707 126.180 84.606  1.00 40.55  ? 249  ASP A O     1 
ATOM   1860  C  CB    . ASP A 1 249 ? 126.912 127.367 81.770  1.00 33.68  ? 249  ASP A CB    1 
ATOM   1861  C  CG    . ASP A 1 249 ? 126.285 128.324 80.779  1.00 43.25  ? 249  ASP A CG    1 
ATOM   1862  O  OD1   . ASP A 1 249 ? 125.366 129.070 81.171  1.00 40.81  ? 249  ASP A OD1   1 
ATOM   1863  O  OD2   . ASP A 1 249 ? 126.706 128.327 79.604  1.00 41.04  ? 249  ASP A OD2   1 
ATOM   1864  N  N     . LYS A 1 250 ? 127.953 126.149 84.522  1.00 42.21  ? 250  LYS A N     1 
ATOM   1865  C  CA    . LYS A 1 250 ? 128.045 125.040 85.471  1.00 43.59  ? 250  LYS A CA    1 
ATOM   1866  C  C     . LYS A 1 250 ? 127.552 125.439 86.863  1.00 42.35  ? 250  LYS A C     1 
ATOM   1867  O  O     . LYS A 1 250 ? 126.841 124.669 87.520  1.00 44.10  ? 250  LYS A O     1 
ATOM   1868  C  CB    . LYS A 1 250 ? 129.483 124.526 85.529  1.00 38.55  ? 250  LYS A CB    1 
ATOM   1869  C  CG    . LYS A 1 250 ? 129.941 123.860 84.244  1.00 41.49  ? 250  LYS A CG    1 
ATOM   1870  C  CD    . LYS A 1 250 ? 131.442 123.644 84.222  1.00 42.83  ? 250  LYS A CD    1 
ATOM   1871  C  CE    . LYS A 1 250 ? 131.886 122.716 85.333  1.00 43.90  ? 250  LYS A CE    1 
ATOM   1872  N  NZ    . LYS A 1 250 ? 133.364 122.538 85.343  1.00 48.58  ? 250  LYS A NZ    1 
ATOM   1873  N  N     . ASP A 1 251 ? 127.898 126.644 87.323  1.00 34.10  ? 251  ASP A N     1 
ATOM   1874  C  CA    . ASP A 1 251 ? 127.483 127.074 88.659  1.00 34.23  ? 251  ASP A CA    1 
ATOM   1875  C  C     . ASP A 1 251 ? 125.980 127.352 88.724  1.00 38.83  ? 251  ASP A C     1 
ATOM   1876  O  O     . ASP A 1 251 ? 125.297 126.952 89.681  1.00 45.79  ? 251  ASP A O     1 
ATOM   1877  C  CB    . ASP A 1 251 ? 128.282 128.309 89.069  1.00 35.99  ? 251  ASP A CB    1 
ATOM   1878  C  CG    . ASP A 1 251 ? 128.804 128.220 90.485  1.00 45.34  ? 251  ASP A CG    1 
ATOM   1879  O  OD1   . ASP A 1 251 ? 128.235 127.444 91.281  1.00 42.18  ? 251  ASP A OD1   1 
ATOM   1880  O  OD2   . ASP A 1 251 ? 129.781 128.927 90.804  1.00 50.19  ? 251  ASP A OD2   1 
ATOM   1881  N  N     . ILE A 1 252 ? 125.444 128.039 87.716  1.00 38.52  ? 252  ILE A N     1 
ATOM   1882  C  CA    . ILE A 1 252 ? 124.007 128.260 87.655  1.00 31.11  ? 252  ILE A CA    1 
ATOM   1883  C  C     . ILE A 1 252 ? 123.275 126.940 87.469  1.00 37.59  ? 252  ILE A C     1 
ATOM   1884  O  O     . ILE A 1 252 ? 122.161 126.775 87.964  1.00 36.83  ? 252  ILE A O     1 
ATOM   1885  C  CB    . ILE A 1 252 ? 123.673 129.274 86.544  1.00 32.52  ? 252  ILE A CB    1 
ATOM   1886  C  CG1   . ILE A 1 252 ? 124.242 130.646 86.898  1.00 31.80  ? 252  ILE A CG1   1 
ATOM   1887  C  CG2   . ILE A 1 252 ? 122.174 129.389 86.332  1.00 37.58  ? 252  ILE A CG2   1 
ATOM   1888  C  CD1   . ILE A 1 252 ? 123.905 131.716 85.894  1.00 35.53  ? 252  ILE A CD1   1 
ATOM   1889  N  N     . ALA A 1 253 ? 123.880 125.974 86.774  1.00 33.65  ? 253  ALA A N     1 
ATOM   1890  C  CA    . ALA A 1 253 ? 123.292 124.643 86.709  1.00 33.49  ? 253  ALA A CA    1 
ATOM   1891  C  C     . ALA A 1 253 ? 123.241 124.009 88.088  1.00 36.83  ? 253  ALA A C     1 
ATOM   1892  O  O     . ALA A 1 253 ? 122.248 123.372 88.447  1.00 38.31  ? 253  ALA A O     1 
ATOM   1893  C  CB    . ALA A 1 253 ? 124.079 123.764 85.740  1.00 33.24  ? 253  ALA A CB    1 
ATOM   1894  N  N     . THR A 1 254 ? 124.301 124.184 88.879  1.00 33.52  ? 254  THR A N     1 
ATOM   1895  C  CA    . THR A 1 254 ? 124.291 123.687 90.252  1.00 30.53  ? 254  THR A CA    1 
ATOM   1896  C  C     . THR A 1 254 ? 123.127 124.276 91.040  1.00 37.70  ? 254  THR A C     1 
ATOM   1897  O  O     . THR A 1 254 ? 122.453 123.566 91.794  1.00 41.25  ? 254  THR A O     1 
ATOM   1898  C  CB    . THR A 1 254 ? 125.623 124.004 90.936  1.00 30.66  ? 254  THR A CB    1 
ATOM   1899  O  OG1   . THR A 1 254 ? 126.690 123.372 90.220  1.00 36.51  ? 254  THR A OG1   1 
ATOM   1900  C  CG2   . THR A 1 254 ? 125.627 123.507 92.370  1.00 33.71  ? 254  THR A CG2   1 
ATOM   1901  N  N     . VAL A 1 255 ? 122.869 125.572 90.865  1.00 43.30  ? 255  VAL A N     1 
ATOM   1902  C  CA    . VAL A 1 255 ? 121.744 126.200 91.562  1.00 37.38  ? 255  VAL A CA    1 
ATOM   1903  C  C     . VAL A 1 255 ? 120.406 125.690 91.022  1.00 37.57  ? 255  VAL A C     1 
ATOM   1904  O  O     . VAL A 1 255 ? 119.509 125.318 91.788  1.00 38.94  ? 255  VAL A O     1 
ATOM   1905  C  CB    . VAL A 1 255 ? 121.838 127.733 91.467  1.00 35.54  ? 255  VAL A CB    1 
ATOM   1906  C  CG1   . VAL A 1 255 ? 120.533 128.371 91.915  1.00 32.84  ? 255  VAL A CG1   1 
ATOM   1907  C  CG2   . VAL A 1 255 ? 122.994 128.244 92.306  1.00 30.10  ? 255  VAL A CG2   1 
ATOM   1908  N  N     . ILE A 1 256 ? 120.256 125.654 89.697  1.00 39.17  ? 256  ILE A N     1 
ATOM   1909  C  CA    . ILE A 1 256 ? 118.957 125.438 89.063  1.00 39.97  ? 256  ILE A CA    1 
ATOM   1910  C  C     . ILE A 1 256 ? 118.539 123.970 89.057  1.00 41.17  ? 256  ILE A C     1 
ATOM   1911  O  O     . ILE A 1 256 ? 117.337 123.674 89.014  1.00 42.92  ? 256  ILE A O     1 
ATOM   1912  C  CB    . ILE A 1 256 ? 118.997 126.041 87.645  1.00 36.79  ? 256  ILE A CB    1 
ATOM   1913  C  CG1   . ILE A 1 256 ? 119.140 127.560 87.728  1.00 36.48  ? 256  ILE A CG1   1 
ATOM   1914  C  CG2   . ILE A 1 256 ? 117.751 125.718 86.840  1.00 34.81  ? 256  ILE A CG2   1 
ATOM   1915  C  CD1   . ILE A 1 256 ? 118.025 128.235 88.480  1.00 42.65  ? 256  ILE A CD1   1 
ATOM   1916  N  N     . ASN A 1 257 ? 119.485 123.035 89.153  1.00 43.09  ? 257  ASN A N     1 
ATOM   1917  C  CA    . ASN A 1 257 ? 119.133 121.623 89.216  1.00 43.94  ? 257  ASN A CA    1 
ATOM   1918  C  C     . ASN A 1 257 ? 118.414 121.252 90.505  1.00 46.61  ? 257  ASN A C     1 
ATOM   1919  O  O     . ASN A 1 257 ? 117.888 120.139 90.601  1.00 49.44  ? 257  ASN A O     1 
ATOM   1920  C  CB    . ASN A 1 257 ? 120.385 120.761 89.053  1.00 44.59  ? 257  ASN A CB    1 
ATOM   1921  C  CG    . ASN A 1 257 ? 120.922 120.777 87.639  1.00 44.63  ? 257  ASN A CG    1 
ATOM   1922  O  OD1   . ASN A 1 257 ? 122.132 120.825 87.421  1.00 42.10  ? 257  ASN A OD1   1 
ATOM   1923  N  ND2   . ASN A 1 257 ? 120.022 120.739 86.666  1.00 40.55  ? 257  ASN A ND2   1 
ATOM   1924  N  N     . THR A 1 258 ? 118.386 122.147 91.494  1.00 38.37  ? 258  THR A N     1 
ATOM   1925  C  CA    . THR A 1 258 ? 117.620 121.918 92.711  1.00 40.87  ? 258  THR A CA    1 
ATOM   1926  C  C     . THR A 1 258 ? 116.115 121.932 92.475  1.00 46.36  ? 258  THR A C     1 
ATOM   1927  O  O     . THR A 1 258 ? 115.368 121.478 93.347  1.00 50.70  ? 258  THR A O     1 
ATOM   1928  C  CB    . THR A 1 258 ? 117.987 122.962 93.766  1.00 42.37  ? 258  THR A CB    1 
ATOM   1929  O  OG1   . THR A 1 258 ? 117.719 124.274 93.258  1.00 44.58  ? 258  THR A OG1   1 
ATOM   1930  C  CG2   . THR A 1 258 ? 119.457 122.860 94.120  1.00 41.70  ? 258  THR A CG2   1 
ATOM   1931  N  N     . GLY A 1 259 ? 115.652 122.438 91.334  1.00 38.52  ? 259  GLY A N     1 
ATOM   1932  C  CA    . GLY A 1 259 ? 114.246 122.353 90.992  1.00 38.33  ? 259  GLY A CA    1 
ATOM   1933  C  C     . GLY A 1 259 ? 113.562 123.689 90.799  1.00 42.45  ? 259  GLY A C     1 
ATOM   1934  O  O     . GLY A 1 259 ? 112.347 123.802 90.983  1.00 45.30  ? 259  GLY A O     1 
ATOM   1935  N  N     . ILE A 1 260 ? 114.325 124.708 90.424  1.00 43.83  ? 260  ILE A N     1 
ATOM   1936  C  CA    . ILE A 1 260 ? 113.796 126.055 90.252  1.00 37.70  ? 260  ILE A CA    1 
ATOM   1937  C  C     . ILE A 1 260 ? 113.409 126.232 88.791  1.00 41.16  ? 260  ILE A C     1 
ATOM   1938  O  O     . ILE A 1 260 ? 114.264 126.159 87.902  1.00 43.56  ? 260  ILE A O     1 
ATOM   1939  C  CB    . ILE A 1 260 ? 114.823 127.112 90.680  1.00 33.85  ? 260  ILE A CB    1 
ATOM   1940  C  CG1   . ILE A 1 260 ? 115.489 126.704 91.992  1.00 39.77  ? 260  ILE A CG1   1 
ATOM   1941  C  CG2   . ILE A 1 260 ? 114.155 128.460 90.839  1.00 34.26  ? 260  ILE A CG2   1 
ATOM   1942  C  CD1   . ILE A 1 260 ? 116.712 127.512 92.322  1.00 39.23  ? 260  ILE A CD1   1 
ATOM   1943  N  N     . GLU A 1 261 ? 112.124 126.461 88.536  1.00 44.00  ? 261  GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 261 ? 111.673 126.676 87.171  1.00 45.38  ? 261  GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 261 ? 112.047 128.084 86.731  1.00 39.98  ? 261  GLU A C     1 
ATOM   1946  O  O     . GLU A 1 261 ? 111.780 129.062 87.435  1.00 42.59  ? 261  GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 261 ? 110.167 126.442 87.040  1.00 44.95  ? 261  GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 261 ? 109.299 127.224 88.002  1.00 42.59  ? 261  GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 261 ? 107.887 127.408 87.483  1.00 46.47  ? 261  GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 261 ? 107.661 127.181 86.276  1.00 47.68  ? 261  GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 261 ? 107.002 127.783 88.280  1.00 43.79  ? 261  GLU A OE2   1 
ATOM   1952  N  N     . VAL A 1 262 ? 112.683 128.180 85.573  1.00 40.31  ? 262  VAL A N     1 
ATOM   1953  C  CA    . VAL A 1 262 ? 113.253 129.429 85.094  1.00 40.43  ? 262  VAL A CA    1 
ATOM   1954  C  C     . VAL A 1 262 ? 112.358 129.971 83.993  1.00 42.29  ? 262  VAL A C     1 
ATOM   1955  O  O     . VAL A 1 262 ? 112.111 129.293 82.988  1.00 48.86  ? 262  VAL A O     1 
ATOM   1956  C  CB    . VAL A 1 262 ? 114.689 129.230 84.591  1.00 37.59  ? 262  VAL A CB    1 
ATOM   1957  C  CG1   . VAL A 1 262 ? 115.265 130.545 84.116  1.00 33.69  ? 262  VAL A CG1   1 
ATOM   1958  C  CG2   . VAL A 1 262 ? 115.542 128.632 85.689  1.00 41.60  ? 262  VAL A CG2   1 
ATOM   1959  N  N     . LYS A 1 263 ? 111.867 131.185 84.183  1.00 38.69  ? 263  LYS A N     1 
ATOM   1960  C  CA    . LYS A 1 263 ? 111.080 131.880 83.176  1.00 42.77  ? 263  LYS A CA    1 
ATOM   1961  C  C     . LYS A 1 263 ? 111.914 133.050 82.673  1.00 45.13  ? 263  LYS A C     1 
ATOM   1962  O  O     . LYS A 1 263 ? 112.125 134.028 83.397  1.00 43.37  ? 263  LYS A O     1 
ATOM   1963  C  CB    . LYS A 1 263 ? 109.745 132.343 83.748  1.00 43.83  ? 263  LYS A CB    1 
ATOM   1964  C  CG    . LYS A 1 263 ? 108.626 132.388 82.731  1.00 46.73  ? 263  LYS A CG    1 
ATOM   1965  C  CD    . LYS A 1 263 ? 107.297 132.662 83.398  1.00 45.42  ? 263  LYS A CD    1 
ATOM   1966  C  CE    . LYS A 1 263 ? 107.028 131.669 84.516  1.00 46.96  ? 263  LYS A CE    1 
ATOM   1967  N  NZ    . LYS A 1 263 ? 106.997 130.265 84.025  1.00 47.40  ? 263  LYS A NZ    1 
ATOM   1968  N  N     . THR A 1 264 ? 112.400 132.937 81.444  1.00 47.72  ? 264  THR A N     1 
ATOM   1969  C  CA    . THR A 1 264 ? 113.164 133.988 80.794  1.00 48.31  ? 264  THR A CA    1 
ATOM   1970  C  C     . THR A 1 264 ? 112.330 134.617 79.686  1.00 52.81  ? 264  THR A C     1 
ATOM   1971  O  O     . THR A 1 264 ? 111.391 134.009 79.165  1.00 55.16  ? 264  THR A O     1 
ATOM   1972  C  CB    . THR A 1 264 ? 114.476 133.444 80.226  1.00 45.65  ? 264  THR A CB    1 
ATOM   1973  O  OG1   . THR A 1 264 ? 114.201 132.319 79.384  1.00 52.88  ? 264  THR A OG1   1 
ATOM   1974  C  CG2   . THR A 1 264 ? 115.394 133.016 81.353  1.00 44.21  ? 264  THR A CG2   1 
ATOM   1975  N  N     . ASN A 1 265 ? 112.687 135.857 79.341  1.00 51.59  ? 265  ASN A N     1 
ATOM   1976  C  CA    . ASN A 1 265 ? 111.904 136.696 78.434  1.00 52.24  ? 265  ASN A CA    1 
ATOM   1977  C  C     . ASN A 1 265 ? 110.477 136.881 78.939  1.00 54.56  ? 265  ASN A C     1 
ATOM   1978  O  O     . ASN A 1 265 ? 109.538 137.020 78.152  1.00 56.66  ? 265  ASN A O     1 
ATOM   1979  C  CB    . ASN A 1 265 ? 111.903 136.145 77.005  1.00 51.56  ? 265  ASN A CB    1 
ATOM   1980  C  CG    . ASN A 1 265 ? 113.286 136.106 76.399  1.00 55.00  ? 265  ASN A CG    1 
ATOM   1981  O  OD1   . ASN A 1 265 ? 113.717 135.081 75.873  1.00 54.55  ? 265  ASN A OD1   1 
ATOM   1982  N  ND2   . ASN A 1 265 ? 113.994 137.225 76.471  1.00 51.95  ? 265  ASN A ND2   1 
ATOM   1983  N  N     . THR A 1 266 ? 110.310 136.882 80.261  1.00 50.15  ? 266  THR A N     1 
ATOM   1984  C  CA    . THR A 1 266 ? 109.030 137.135 80.919  1.00 50.65  ? 266  THR A CA    1 
ATOM   1985  C  C     . THR A 1 266 ? 109.296 138.211 81.966  1.00 50.86  ? 266  THR A C     1 
ATOM   1986  O  O     . THR A 1 266 ? 109.633 137.905 83.112  1.00 52.51  ? 266  THR A O     1 
ATOM   1987  C  CB    . THR A 1 266 ? 108.462 135.866 81.539  1.00 50.26  ? 266  THR A CB    1 
ATOM   1988  O  OG1   . THR A 1 266 ? 108.425 134.828 80.552  1.00 48.96  ? 266  THR A OG1   1 
ATOM   1989  C  CG2   . THR A 1 266 ? 107.054 136.113 82.057  1.00 54.85  ? 266  THR A CG2   1 
ATOM   1990  N  N     . ALA A 1 267 ? 109.146 139.470 81.570  1.00 56.26  ? 267  ALA A N     1 
ATOM   1991  C  CA    . ALA A 1 267 ? 109.553 140.599 82.390  1.00 59.89  ? 267  ALA A CA    1 
ATOM   1992  C  C     . ALA A 1 267 ? 108.364 141.191 83.135  1.00 64.87  ? 267  ALA A C     1 
ATOM   1993  O  O     . ALA A 1 267 ? 107.239 141.203 82.627  1.00 66.66  ? 267  ALA A O     1 
ATOM   1994  C  CB    . ALA A 1 267 ? 110.217 141.678 81.534  1.00 57.75  ? 267  ALA A CB    1 
ATOM   1995  N  N     . LEU A 1 268 ? 108.625 141.676 84.346  1.00 65.50  ? 268  LEU A N     1 
ATOM   1996  C  CA    . LEU A 1 268 ? 107.626 142.401 85.118  1.00 61.02  ? 268  LEU A CA    1 
ATOM   1997  C  C     . LEU A 1 268 ? 107.478 143.813 84.567  1.00 65.50  ? 268  LEU A C     1 
ATOM   1998  O  O     . LEU A 1 268 ? 108.472 144.514 84.357  1.00 64.53  ? 268  LEU A O     1 
ATOM   1999  C  CB    . LEU A 1 268 ? 108.024 142.444 86.592  1.00 58.06  ? 268  LEU A CB    1 
ATOM   2000  C  CG    . LEU A 1 268 ? 107.191 143.315 87.532  1.00 62.17  ? 268  LEU A CG    1 
ATOM   2001  C  CD1   . LEU A 1 268 ? 105.759 142.820 87.607  1.00 65.66  ? 268  LEU A CD1   1 
ATOM   2002  C  CD2   . LEU A 1 268 ? 107.821 143.348 88.911  1.00 60.89  ? 268  LEU A CD2   1 
ATOM   2003  N  N     . GLY A 1 269 ? 106.235 144.229 84.340  1.00 77.46  ? 269  GLY A N     1 
ATOM   2004  C  CA    . GLY A 1 269 ? 105.935 145.502 83.732  1.00 76.69  ? 269  GLY A CA    1 
ATOM   2005  C  C     . GLY A 1 269 ? 105.668 145.435 82.244  1.00 77.85  ? 269  GLY A C     1 
ATOM   2006  O  O     . GLY A 1 269 ? 105.073 146.366 81.692  1.00 79.30  ? 269  GLY A O     1 
ATOM   2007  N  N     . LYS A 1 270 ? 106.087 144.358 81.585  1.00 75.75  ? 270  LYS A N     1 
ATOM   2008  C  CA    . LYS A 1 270 ? 105.841 144.159 80.166  1.00 76.01  ? 270  LYS A CA    1 
ATOM   2009  C  C     . LYS A 1 270 ? 105.017 142.921 79.857  1.00 76.65  ? 270  LYS A C     1 
ATOM   2010  O  O     . LYS A 1 270 ? 104.259 142.933 78.886  1.00 76.59  ? 270  LYS A O     1 
ATOM   2011  C  CB    . LYS A 1 270 ? 107.168 144.075 79.395  1.00 76.34  ? 270  LYS A CB    1 
ATOM   2012  C  CG    . LYS A 1 270 ? 107.893 145.404 79.275  1.00 76.78  ? 270  LYS A CG    1 
ATOM   2013  C  CD    . LYS A 1 270 ? 109.137 145.285 78.410  1.00 76.38  ? 270  LYS A CD    1 
ATOM   2014  C  CE    . LYS A 1 270 ? 110.229 144.502 79.114  1.00 77.19  ? 270  LYS A CE    1 
ATOM   2015  N  NZ    . LYS A 1 270 ? 110.671 145.179 80.364  1.00 77.91  ? 270  LYS A NZ    1 
ATOM   2016  N  N     . ASP A 1 271 ? 105.140 141.859 80.648  1.00 71.73  ? 271  ASP A N     1 
ATOM   2017  C  CA    . ASP A 1 271 ? 104.362 140.645 80.449  1.00 72.08  ? 271  ASP A CA    1 
ATOM   2018  C  C     . ASP A 1 271 ? 103.305 140.443 81.523  1.00 72.60  ? 271  ASP A C     1 
ATOM   2019  O  O     . ASP A 1 271 ? 102.142 140.179 81.203  1.00 75.30  ? 271  ASP A O     1 
ATOM   2020  C  CB    . ASP A 1 271 ? 105.291 139.426 80.400  1.00 70.90  ? 271  ASP A CB    1 
ATOM   2021  C  CG    . ASP A 1 271 ? 104.575 138.170 79.961  1.00 71.08  ? 271  ASP A CG    1 
ATOM   2022  O  OD1   . ASP A 1 271 ? 104.392 137.988 78.740  1.00 70.27  ? 271  ASP A OD1   1 
ATOM   2023  O  OD2   . ASP A 1 271 ? 104.188 137.368 80.835  1.00 70.70  ? 271  ASP A OD2   1 
ATOM   2024  N  N     . ILE A 1 272 ? 103.678 140.561 82.797  1.00 71.11  ? 272  ILE A N     1 
ATOM   2025  C  CA    . ILE A 1 272 ? 102.741 140.427 83.902  1.00 72.11  ? 272  ILE A CA    1 
ATOM   2026  C  C     . ILE A 1 272 ? 102.896 141.631 84.820  1.00 74.10  ? 272  ILE A C     1 
ATOM   2027  O  O     . ILE A 1 272 ? 103.933 142.298 84.842  1.00 73.33  ? 272  ILE A O     1 
ATOM   2028  C  CB    . ILE A 1 272 ? 102.944 139.118 84.696  1.00 70.98  ? 272  ILE A CB    1 
ATOM   2029  C  CG1   . ILE A 1 272 ? 104.363 139.046 85.258  1.00 71.28  ? 272  ILE A CG1   1 
ATOM   2030  C  CG2   . ILE A 1 272 ? 102.653 137.908 83.823  1.00 72.98  ? 272  ILE A CG2   1 
ATOM   2031  C  CD1   . ILE A 1 272 ? 104.623 137.810 86.084  1.00 70.06  ? 272  ILE A CD1   1 
ATOM   2032  N  N     . ALA A 1 273 ? 101.843 141.905 85.579  1.00 77.28  ? 273  ALA A N     1 
ATOM   2033  C  CA    . ALA A 1 273 ? 101.817 143.026 86.504  1.00 75.37  ? 273  ALA A CA    1 
ATOM   2034  C  C     . ALA A 1 273 ? 102.084 142.549 87.926  1.00 78.30  ? 273  ALA A C     1 
ATOM   2035  O  O     . ALA A 1 273 ? 101.870 141.383 88.265  1.00 76.94  ? 273  ALA A O     1 
ATOM   2036  C  CB    . ALA A 1 273 ? 100.473 143.755 86.437  1.00 74.64  ? 273  ALA A CB    1 
ATOM   2037  N  N     . LEU A 1 274 ? 102.558 143.477 88.760  1.00 75.17  ? 274  LEU A N     1 
ATOM   2038  C  CA    . LEU A 1 274 ? 102.906 143.123 90.132  1.00 72.37  ? 274  LEU A CA    1 
ATOM   2039  C  C     . LEU A 1 274 ? 101.673 142.775 90.956  1.00 73.01  ? 274  LEU A C     1 
ATOM   2040  O  O     . LEU A 1 274 ? 101.751 141.924 91.848  1.00 75.30  ? 274  LEU A O     1 
ATOM   2041  C  CB    . LEU A 1 274 ? 103.690 144.260 90.787  1.00 72.56  ? 274  LEU A CB    1 
ATOM   2042  C  CG    . LEU A 1 274 ? 104.863 143.832 91.674  1.00 71.95  ? 274  LEU A CG    1 
ATOM   2043  C  CD1   . LEU A 1 274 ? 105.884 144.946 91.797  1.00 72.75  ? 274  LEU A CD1   1 
ATOM   2044  C  CD2   . LEU A 1 274 ? 104.384 143.406 93.049  1.00 71.96  ? 274  LEU A CD2   1 
ATOM   2045  N  N     . GLU A 1 275 ? 100.533 143.413 90.679  1.00 77.93  ? 275  GLU A N     1 
ATOM   2046  C  CA    . GLU A 1 275 ? 99.298  143.042 91.365  1.00 78.82  ? 275  GLU A CA    1 
ATOM   2047  C  C     . GLU A 1 275 ? 98.889  141.616 91.018  1.00 77.92  ? 275  GLU A C     1 
ATOM   2048  O  O     . GLU A 1 275 ? 98.572  140.813 91.904  1.00 75.80  ? 275  GLU A O     1 
ATOM   2049  C  CB    . GLU A 1 275 ? 98.184  144.026 91.010  1.00 79.55  ? 275  GLU A CB    1 
ATOM   2050  C  CG    . GLU A 1 275 ? 98.353  145.403 91.628  1.00 80.30  ? 275  GLU A CG    1 
ATOM   2051  C  CD    . GLU A 1 275 ? 98.163  145.395 93.133  1.00 80.91  ? 275  GLU A CD    1 
ATOM   2052  O  OE1   . GLU A 1 275 ? 97.507  144.466 93.650  1.00 78.55  ? 275  GLU A OE1   1 
ATOM   2053  O  OE2   . GLU A 1 275 ? 98.671  146.321 93.801  1.00 80.03  ? 275  GLU A OE2   1 
ATOM   2054  N  N     . GLU A 1 276 ? 98.909  141.277 89.728  1.00 78.20  ? 276  GLU A N     1 
ATOM   2055  C  CA    . GLU A 1 276 ? 98.650  139.900 89.328  1.00 78.45  ? 276  GLU A CA    1 
ATOM   2056  C  C     . GLU A 1 276 ? 99.736  138.962 89.834  1.00 77.91  ? 276  GLU A C     1 
ATOM   2057  O  O     . GLU A 1 276 ? 99.452  137.801 90.149  1.00 77.31  ? 276  GLU A O     1 
ATOM   2058  C  CB    . GLU A 1 276 ? 98.532  139.804 87.807  1.00 77.97  ? 276  GLU A CB    1 
ATOM   2059  C  CG    . GLU A 1 276 ? 97.380  140.606 87.220  1.00 79.56  ? 276  GLU A CG    1 
ATOM   2060  C  CD    . GLU A 1 276 ? 96.022  140.022 87.564  1.00 79.27  ? 276  GLU A CD    1 
ATOM   2061  O  OE1   . GLU A 1 276 ? 95.948  138.811 87.862  1.00 75.47  ? 276  GLU A OE1   1 
ATOM   2062  O  OE2   . GLU A 1 276 ? 95.027  140.776 87.535  1.00 78.69  ? 276  GLU A OE2   1 
ATOM   2063  N  N     . LEU A 1 277 ? 100.977 139.446 89.922  1.00 70.99  ? 277  LEU A N     1 
ATOM   2064  C  CA    . LEU A 1 277 ? 102.060 138.623 90.450  1.00 70.35  ? 277  LEU A CA    1 
ATOM   2065  C  C     . LEU A 1 277 ? 101.804 138.246 91.904  1.00 72.07  ? 277  LEU A C     1 
ATOM   2066  O  O     . LEU A 1 277 ? 102.023 137.096 92.303  1.00 72.09  ? 277  LEU A O     1 
ATOM   2067  C  CB    . LEU A 1 277 ? 103.390 139.363 90.302  1.00 68.67  ? 277  LEU A CB    1 
ATOM   2068  C  CG    . LEU A 1 277 ? 104.664 138.533 90.155  1.00 65.73  ? 277  LEU A CG    1 
ATOM   2069  C  CD1   . LEU A 1 277 ? 105.714 139.316 89.392  1.00 65.30  ? 277  LEU A CD1   1 
ATOM   2070  C  CD2   . LEU A 1 277 ? 105.198 138.133 91.511  1.00 67.98  ? 277  LEU A CD2   1 
ATOM   2071  N  N     . ARG A 1 278 ? 101.339 139.200 92.710  1.00 68.95  ? 278  ARG A N     1 
ATOM   2072  C  CA    . ARG A 1 278 ? 100.985 138.896 94.092  1.00 66.98  ? 278  ARG A CA    1 
ATOM   2073  C  C     . ARG A 1 278 ? 99.745  138.016 94.166  1.00 70.71  ? 278  ARG A C     1 
ATOM   2074  O  O     . ARG A 1 278 ? 99.648  137.142 95.034  1.00 70.90  ? 278  ARG A O     1 
ATOM   2075  C  CB    . ARG A 1 278 ? 100.767 140.189 94.872  1.00 68.37  ? 278  ARG A CB    1 
ATOM   2076  C  CG    . ARG A 1 278 ? 102.006 141.040 95.000  1.00 69.73  ? 278  ARG A CG    1 
ATOM   2077  C  CD    . ARG A 1 278 ? 101.662 142.461 95.392  1.00 69.94  ? 278  ARG A CD    1 
ATOM   2078  N  NE    . ARG A 1 278 ? 100.874 142.529 96.616  1.00 71.70  ? 278  ARG A NE    1 
ATOM   2079  C  CZ    . ARG A 1 278 ? 99.596  142.876 96.664  1.00 74.30  ? 278  ARG A CZ    1 
ATOM   2080  N  NH1   . ARG A 1 278 ? 98.929  143.210 95.572  1.00 73.23  ? 278  ARG A NH1   1 
ATOM   2081  N  NH2   . ARG A 1 278 ? 98.972  142.891 97.838  1.00 70.87  ? 278  ARG A NH2   1 
ATOM   2082  N  N     . GLU A 1 279 ? 98.781  138.240 93.272  1.00 75.27  ? 279  GLU A N     1 
ATOM   2083  C  CA    . GLU A 1 279 ? 97.554  137.452 93.296  1.00 74.74  ? 279  GLU A CA    1 
ATOM   2084  C  C     . GLU A 1 279 ? 97.809  135.995 92.930  1.00 75.55  ? 279  GLU A C     1 
ATOM   2085  O  O     . GLU A 1 279 ? 97.102  135.104 93.412  1.00 75.72  ? 279  GLU A O     1 
ATOM   2086  C  CB    . GLU A 1 279 ? 96.523  138.066 92.349  1.00 73.43  ? 279  GLU A CB    1 
ATOM   2087  C  CG    . GLU A 1 279 ? 95.130  137.477 92.467  1.00 75.57  ? 279  GLU A CG    1 
ATOM   2088  C  CD    . GLU A 1 279 ? 94.441  137.864 93.760  1.00 76.99  ? 279  GLU A CD    1 
ATOM   2089  O  OE1   . GLU A 1 279 ? 94.822  138.893 94.355  1.00 75.45  ? 279  GLU A OE1   1 
ATOM   2090  O  OE2   . GLU A 1 279 ? 93.516  137.138 94.182  1.00 77.33  ? 279  GLU A OE2   1 
ATOM   2091  N  N     . GLN A 1 280 ? 98.807  135.731 92.090  1.00 69.58  ? 280  GLN A N     1 
ATOM   2092  C  CA    . GLN A 1 280 ? 99.074  134.388 91.598  1.00 69.52  ? 280  GLN A CA    1 
ATOM   2093  C  C     . GLN A 1 280 ? 100.224 133.697 92.322  1.00 70.56  ? 280  GLN A C     1 
ATOM   2094  O  O     . GLN A 1 280 ? 100.608 132.592 91.928  1.00 71.01  ? 280  GLN A O     1 
ATOM   2095  C  CB    . GLN A 1 280 ? 99.360  134.432 90.096  1.00 67.79  ? 280  GLN A CB    1 
ATOM   2096  C  CG    . GLN A 1 280 ? 98.216  135.000 89.279  1.00 68.50  ? 280  GLN A CG    1 
ATOM   2097  C  CD    . GLN A 1 280 ? 98.614  135.298 87.852  1.00 70.49  ? 280  GLN A CD    1 
ATOM   2098  O  OE1   . GLN A 1 280 ? 99.433  134.593 87.265  1.00 68.26  ? 280  GLN A OE1   1 
ATOM   2099  N  NE2   . GLN A 1 280 ? 98.039  136.352 87.287  1.00 69.40  ? 280  GLN A NE2   1 
ATOM   2100  N  N     . TYR A 1 281 ? 100.783 134.310 93.364  1.00 60.86  ? 281  TYR A N     1 
ATOM   2101  C  CA    . TYR A 1 281 ? 101.918 133.715 94.056  1.00 60.74  ? 281  TYR A CA    1 
ATOM   2102  C  C     . TYR A 1 281 ? 101.839 134.028 95.543  1.00 63.82  ? 281  TYR A C     1 
ATOM   2103  O  O     . TYR A 1 281 ? 101.197 134.992 95.963  1.00 61.17  ? 281  TYR A O     1 
ATOM   2104  C  CB    . TYR A 1 281 ? 103.248 134.202 93.470  1.00 57.44  ? 281  TYR A CB    1 
ATOM   2105  C  CG    . TYR A 1 281 ? 103.521 133.673 92.081  1.00 59.52  ? 281  TYR A CG    1 
ATOM   2106  C  CD1   . TYR A 1 281 ? 104.061 132.407 91.895  1.00 59.16  ? 281  TYR A CD1   1 
ATOM   2107  C  CD2   . TYR A 1 281 ? 103.235 134.435 90.955  1.00 59.19  ? 281  TYR A CD2   1 
ATOM   2108  C  CE1   . TYR A 1 281 ? 104.310 131.915 90.628  1.00 58.94  ? 281  TYR A CE1   1 
ATOM   2109  C  CE2   . TYR A 1 281 ? 103.481 133.951 89.685  1.00 57.74  ? 281  TYR A CE2   1 
ATOM   2110  C  CZ    . TYR A 1 281 ? 104.019 132.690 89.528  1.00 59.82  ? 281  TYR A CZ    1 
ATOM   2111  O  OH    . TYR A 1 281 ? 104.268 132.200 88.268  1.00 61.57  ? 281  TYR A OH    1 
ATOM   2112  N  N     . ASP A 1 282 ? 102.504 133.186 96.339  1.00 59.70  ? 282  ASP A N     1 
ATOM   2113  C  CA    . ASP A 1 282 ? 102.481 133.342 97.790  1.00 56.20  ? 282  ASP A CA    1 
ATOM   2114  C  C     . ASP A 1 282 ? 103.391 134.472 98.263  1.00 55.88  ? 282  ASP A C     1 
ATOM   2115  O  O     . ASP A 1 282 ? 103.031 135.213 99.184  1.00 57.14  ? 282  ASP A O     1 
ATOM   2116  C  CB    . ASP A 1 282 ? 102.866 132.026 98.459  1.00 53.13  ? 282  ASP A CB    1 
ATOM   2117  C  CG    . ASP A 1 282 ? 101.792 130.970 98.316  1.00 58.17  ? 282  ASP A CG    1 
ATOM   2118  O  OD1   . ASP A 1 282 ? 100.613 131.285 98.569  1.00 57.63  ? 282  ASP A OD1   1 
ATOM   2119  O  OD2   . ASP A 1 282 ? 102.121 129.828 97.941  1.00 61.25  ? 282  ASP A OD2   1 
ATOM   2120  N  N     . ALA A 1 283 ? 104.565 134.621 97.656  1.00 44.72  ? 283  ALA A N     1 
ATOM   2121  C  CA    . ALA A 1 283 ? 105.471 135.703 98.011  1.00 39.60  ? 283  ALA A CA    1 
ATOM   2122  C  C     . ALA A 1 283 ? 106.290 136.078 96.787  1.00 42.00  ? 283  ALA A C     1 
ATOM   2123  O  O     . ALA A 1 283 ? 106.427 135.293 95.846  1.00 44.86  ? 283  ALA A O     1 
ATOM   2124  C  CB    . ALA A 1 283 ? 106.385 135.317 99.178  1.00 43.29  ? 283  ALA A CB    1 
ATOM   2125  N  N     . VAL A 1 284 ? 106.831 137.294 96.806  1.00 34.95  ? 284  VAL A N     1 
ATOM   2126  C  CA    . VAL A 1 284 ? 107.561 137.843 95.668  1.00 34.84  ? 284  VAL A CA    1 
ATOM   2127  C  C     . VAL A 1 284 ? 108.801 138.576 96.167  1.00 31.73  ? 284  VAL A C     1 
ATOM   2128  O  O     . VAL A 1 284 ? 108.742 139.331 97.142  1.00 37.54  ? 284  VAL A O     1 
ATOM   2129  C  CB    . VAL A 1 284 ? 106.656 138.762 94.812  1.00 29.84  ? 284  VAL A CB    1 
ATOM   2130  C  CG1   . VAL A 1 284 ? 105.588 139.413 95.664  1.00 29.09  ? 284  VAL A CG1   1 
ATOM   2131  C  CG2   . VAL A 1 284 ? 107.469 139.817 94.078  1.00 30.55  ? 284  VAL A CG2   1 
ATOM   2132  N  N     . PHE A 1 285 ? 109.929 138.335 95.499  1.00 22.57  ? 285  PHE A N     1 
ATOM   2133  C  CA    . PHE A 1 285 ? 111.189 139.015 95.764  1.00 15.78  ? 285  PHE A CA    1 
ATOM   2134  C  C     . PHE A 1 285 ? 111.585 139.804 94.525  1.00 23.14  ? 285  PHE A C     1 
ATOM   2135  O  O     . PHE A 1 285 ? 111.571 139.266 93.414  1.00 29.29  ? 285  PHE A O     1 
ATOM   2136  C  CB    . PHE A 1 285 ? 112.282 138.007 96.136  1.00 25.11  ? 285  PHE A CB    1 
ATOM   2137  C  CG    . PHE A 1 285 ? 113.656 138.605 96.274  1.00 23.30  ? 285  PHE A CG    1 
ATOM   2138  C  CD1   . PHE A 1 285 ? 114.034 139.242 97.441  1.00 30.41  ? 285  PHE A CD1   1 
ATOM   2139  C  CD2   . PHE A 1 285 ? 114.580 138.501 95.247  1.00 24.73  ? 285  PHE A CD2   1 
ATOM   2140  C  CE1   . PHE A 1 285 ? 115.299 139.781 97.574  1.00 27.77  ? 285  PHE A CE1   1 
ATOM   2141  C  CE2   . PHE A 1 285 ? 115.843 139.039 95.376  1.00 24.29  ? 285  PHE A CE2   1 
ATOM   2142  C  CZ    . PHE A 1 285 ? 116.203 139.678 96.541  1.00 26.61  ? 285  PHE A CZ    1 
ATOM   2143  N  N     . LEU A 1 286 ? 111.933 141.075 94.713  1.00 37.90  ? 286  LEU A N     1 
ATOM   2144  C  CA    . LEU A 1 286 ? 112.303 141.959 93.608  1.00 33.81  ? 286  LEU A CA    1 
ATOM   2145  C  C     . LEU A 1 286 ? 113.823 142.067 93.567  1.00 29.15  ? 286  LEU A C     1 
ATOM   2146  O  O     . LEU A 1 286 ? 114.425 142.922 94.215  1.00 33.99  ? 286  LEU A O     1 
ATOM   2147  C  CB    . LEU A 1 286 ? 111.648 143.327 93.755  1.00 30.37  ? 286  LEU A CB    1 
ATOM   2148  C  CG    . LEU A 1 286 ? 110.131 143.391 93.568  1.00 28.06  ? 286  LEU A CG    1 
ATOM   2149  C  CD1   . LEU A 1 286 ? 109.650 144.828 93.624  1.00 35.32  ? 286  LEU A CD1   1 
ATOM   2150  C  CD2   . LEU A 1 286 ? 109.722 142.739 92.259  1.00 28.69  ? 286  LEU A CD2   1 
ATOM   2151  N  N     . GLY A 1 287 ? 114.445 141.182 92.797  1.00 27.24  ? 287  GLY A N     1 
ATOM   2152  C  CA    . GLY A 1 287 ? 115.871 141.248 92.559  1.00 28.56  ? 287  GLY A CA    1 
ATOM   2153  C  C     . GLY A 1 287 ? 116.154 141.729 91.153  1.00 36.30  ? 287  GLY A C     1 
ATOM   2154  O  O     . GLY A 1 287 ? 117.036 141.201 90.470  1.00 39.98  ? 287  GLY A O     1 
ATOM   2155  N  N     . VAL A 1 288 ? 115.406 142.741 90.713  1.00 38.33  ? 288  VAL A N     1 
ATOM   2156  C  CA    . VAL A 1 288 ? 115.460 143.224 89.337  1.00 32.22  ? 288  VAL A CA    1 
ATOM   2157  C  C     . VAL A 1 288 ? 116.737 144.017 89.099  1.00 26.14  ? 288  VAL A C     1 
ATOM   2158  O  O     . VAL A 1 288 ? 116.973 144.514 87.994  1.00 35.11  ? 288  VAL A O     1 
ATOM   2159  C  CB    . VAL A 1 288 ? 114.222 144.075 89.001  1.00 28.81  ? 288  VAL A CB    1 
ATOM   2160  C  CG1   . VAL A 1 288 ? 112.962 143.355 89.424  1.00 29.93  ? 288  VAL A CG1   1 
ATOM   2161  C  CG2   . VAL A 1 288 ? 114.313 145.432 89.667  1.00 25.36  ? 288  VAL A CG2   1 
ATOM   2162  N  N     . GLY A 1 289 ? 117.564 144.145 90.129  1.00 24.59  ? 289  GLY A N     1 
ATOM   2163  C  CA    . GLY A 1 289 ? 118.809 144.848 89.953  1.00 29.79  ? 289  GLY A CA    1 
ATOM   2164  C  C     . GLY A 1 289 ? 118.594 146.340 89.773  1.00 33.80  ? 289  GLY A C     1 
ATOM   2165  O  O     . GLY A 1 289 ? 117.583 146.918 90.177  1.00 38.16  ? 289  GLY A O     1 
ATOM   2166  N  N     . ALA A 1 290 ? 119.582 146.962 89.144  1.00 40.46  ? 290  ALA A N     1 
ATOM   2167  C  CA    . ALA A 1 290 ? 119.616 148.400 88.918  1.00 42.12  ? 290  ALA A CA    1 
ATOM   2168  C  C     . ALA A 1 290 ? 120.019 148.690 87.479  1.00 45.30  ? 290  ALA A C     1 
ATOM   2169  O  O     . ALA A 1 290 ? 120.927 149.475 87.203  1.00 43.89  ? 290  ALA A O     1 
ATOM   2170  C  CB    . ALA A 1 290 ? 120.555 149.070 89.913  1.00 41.36  ? 290  ALA A CB    1 
ATOM   2171  N  N     . TRP A 1 291 ? 119.329 148.045 86.536  1.00 39.71  ? 291  TRP A N     1 
ATOM   2172  C  CA    . TRP A 1 291 ? 119.802 147.971 85.157  1.00 36.96  ? 291  TRP A CA    1 
ATOM   2173  C  C     . TRP A 1 291 ? 119.846 149.318 84.450  1.00 39.76  ? 291  TRP A C     1 
ATOM   2174  O  O     . TRP A 1 291 ? 120.459 149.417 83.382  1.00 48.06  ? 291  TRP A O     1 
ATOM   2175  C  CB    . TRP A 1 291 ? 118.926 147.003 84.367  1.00 38.33  ? 291  TRP A CB    1 
ATOM   2176  C  CG    . TRP A 1 291 ? 119.429 145.612 84.429  1.00 31.18  ? 291  TRP A CG    1 
ATOM   2177  C  CD1   . TRP A 1 291 ? 119.693 144.890 85.550  1.00 31.64  ? 291  TRP A CD1   1 
ATOM   2178  C  CD2   . TRP A 1 291 ? 119.742 144.764 83.321  1.00 35.47  ? 291  TRP A CD2   1 
ATOM   2179  N  NE1   . TRP A 1 291 ? 120.152 143.643 85.212  1.00 39.79  ? 291  TRP A NE1   1 
ATOM   2180  C  CE2   . TRP A 1 291 ? 120.191 143.541 83.847  1.00 39.81  ? 291  TRP A CE2   1 
ATOM   2181  C  CE3   . TRP A 1 291 ? 119.688 144.921 81.934  1.00 41.32  ? 291  TRP A CE3   1 
ATOM   2182  C  CZ2   . TRP A 1 291 ? 120.578 142.478 83.037  1.00 38.98  ? 291  TRP A CZ2   1 
ATOM   2183  C  CZ3   . TRP A 1 291 ? 120.074 143.867 81.134  1.00 42.62  ? 291  TRP A CZ3   1 
ATOM   2184  C  CH2   . TRP A 1 291 ? 120.513 142.661 81.687  1.00 41.54  ? 291  TRP A CH2   1 
ATOM   2185  N  N     . LYS A 1 292 ? 119.222 150.352 85.000  1.00 52.09  ? 292  LYS A N     1 
ATOM   2186  C  CA    . LYS A 1 292 ? 119.263 151.668 84.381  1.00 56.19  ? 292  LYS A CA    1 
ATOM   2187  C  C     . LYS A 1 292 ? 120.494 152.423 84.865  1.00 54.93  ? 292  LYS A C     1 
ATOM   2188  O  O     . LYS A 1 292 ? 120.780 152.455 86.066  1.00 60.76  ? 292  LYS A O     1 
ATOM   2189  C  CB    . LYS A 1 292 ? 117.991 152.456 84.690  1.00 56.95  ? 292  LYS A CB    1 
ATOM   2190  C  CG    . LYS A 1 292 ? 117.584 153.402 83.583  1.00 58.67  ? 292  LYS A CG    1 
ATOM   2191  C  CD    . LYS A 1 292 ? 116.216 153.995 83.836  1.00 58.45  ? 292  LYS A CD    1 
ATOM   2192  C  CE    . LYS A 1 292 ? 115.695 154.693 82.597  1.00 60.60  ? 292  LYS A CE    1 
ATOM   2193  N  NZ    . LYS A 1 292 ? 115.573 153.746 81.457  1.00 59.99  ? 292  LYS A NZ    1 
ATOM   2194  N  N     . SER A 1 293 ? 121.223 153.018 83.928  1.00 58.14  ? 293  SER A N     1 
ATOM   2195  C  CA    . SER A 1 293 ? 122.435 153.755 84.246  1.00 61.05  ? 293  SER A CA    1 
ATOM   2196  C  C     . SER A 1 293 ? 122.102 155.206 84.560  1.00 64.66  ? 293  SER A C     1 
ATOM   2197  O  O     . SER A 1 293 ? 121.292 155.833 83.872  1.00 67.79  ? 293  SER A O     1 
ATOM   2198  C  CB    . SER A 1 293 ? 123.429 153.687 83.089  1.00 62.92  ? 293  SER A CB    1 
ATOM   2199  O  OG    . SER A 1 293 ? 124.609 154.406 83.396  1.00 64.47  ? 293  SER A OG    1 
ATOM   2200  N  N     . ARG A 1 294 ? 122.735 155.735 85.600  1.00 69.15  ? 294  ARG A N     1 
ATOM   2201  C  CA    . ARG A 1 294 ? 122.451 157.089 86.052  1.00 69.87  ? 294  ARG A CA    1 
ATOM   2202  C  C     . ARG A 1 294 ? 123.190 158.092 85.176  1.00 73.50  ? 294  ARG A C     1 
ATOM   2203  O  O     . ARG A 1 294 ? 124.417 158.036 85.055  1.00 74.48  ? 294  ARG A O     1 
ATOM   2204  C  CB    . ARG A 1 294 ? 122.843 157.257 87.517  1.00 70.71  ? 294  ARG A CB    1 
ATOM   2205  C  CG    . ARG A 1 294 ? 122.406 158.577 88.122  1.00 71.69  ? 294  ARG A CG    1 
ATOM   2206  C  CD    . ARG A 1 294 ? 122.963 158.745 89.518  1.00 72.93  ? 294  ARG A CD    1 
ATOM   2207  N  NE    . ARG A 1 294 ? 122.548 157.662 90.399  1.00 76.10  ? 294  ARG A NE    1 
ATOM   2208  C  CZ    . ARG A 1 294 ? 123.078 157.424 91.591  1.00 75.52  ? 294  ARG A CZ    1 
ATOM   2209  N  NH1   . ARG A 1 294 ? 124.059 158.170 92.071  1.00 71.98  ? 294  ARG A NH1   1 
ATOM   2210  N  NH2   . ARG A 1 294 ? 122.615 156.410 92.316  1.00 74.06  ? 294  ARG A NH2   1 
ATOM   2211  N  N     . LYS A 1 295 ? 122.439 159.002 84.565  1.00 87.41  ? 295  LYS A N     1 
ATOM   2212  C  CA    . LYS A 1 295 ? 123.036 160.045 83.747  1.00 86.73  ? 295  LYS A CA    1 
ATOM   2213  C  C     . LYS A 1 295 ? 123.809 161.020 84.624  1.00 87.91  ? 295  LYS A C     1 
ATOM   2214  O  O     . LYS A 1 295 ? 123.394 161.339 85.741  1.00 87.65  ? 295  LYS A O     1 
ATOM   2215  C  CB    . LYS A 1 295 ? 121.954 160.780 82.960  1.00 88.44  ? 295  LYS A CB    1 
ATOM   2216  C  CG    . LYS A 1 295 ? 122.482 161.761 81.938  1.00 88.19  ? 295  LYS A CG    1 
ATOM   2217  C  CD    . LYS A 1 295 ? 123.105 161.047 80.756  1.00 88.27  ? 295  LYS A CD    1 
ATOM   2218  C  CE    . LYS A 1 295 ? 122.058 160.286 79.965  1.00 89.24  ? 295  LYS A CE    1 
ATOM   2219  N  NZ    . LYS A 1 295 ? 122.610 159.749 78.692  1.00 87.34  ? 295  LYS A NZ    1 
ATOM   2220  N  N     . MET A 1 296 ? 124.947 161.488 84.111  1.00 95.83  ? 296  MET A N     1 
ATOM   2221  C  CA    . MET A 1 296 ? 125.821 162.346 84.904  1.00 96.88  ? 296  MET A CA    1 
ATOM   2222  C  C     . MET A 1 296 ? 125.146 163.667 85.247  1.00 95.92  ? 296  MET A C     1 
ATOM   2223  O  O     . MET A 1 296 ? 125.273 164.163 86.373  1.00 94.82  ? 296  MET A O     1 
ATOM   2224  C  CB    . MET A 1 296 ? 127.126 162.589 84.153  1.00 96.95  ? 296  MET A CB    1 
ATOM   2225  C  CG    . MET A 1 296 ? 128.168 163.322 84.958  1.00 96.34  ? 296  MET A CG    1 
ATOM   2226  S  SD    . MET A 1 296 ? 129.585 163.721 83.935  1.00 96.76  ? 296  MET A SD    1 
ATOM   2227  C  CE    . MET A 1 296 ? 129.832 162.162 83.089  1.00 96.06  ? 296  MET A CE    1 
ATOM   2228  N  N     . GLY A 1 297 ? 124.429 164.253 84.295  1.00 102.56 ? 297  GLY A N     1 
ATOM   2229  C  CA    . GLY A 1 297 ? 123.702 165.477 84.559  1.00 104.21 ? 297  GLY A CA    1 
ATOM   2230  C  C     . GLY A 1 297 ? 124.485 166.725 84.220  1.00 104.90 ? 297  GLY A C     1 
ATOM   2231  O  O     . GLY A 1 297 ? 124.569 167.651 85.030  1.00 104.89 ? 297  GLY A O     1 
ATOM   2232  N  N     . ILE A 1 298 ? 125.068 166.759 83.023  1.00 102.83 ? 298  ILE A N     1 
ATOM   2233  C  CA    . ILE A 1 298 ? 125.796 167.919 82.532  1.00 102.55 ? 298  ILE A CA    1 
ATOM   2234  C  C     . ILE A 1 298 ? 125.283 168.258 81.139  1.00 102.96 ? 298  ILE A C     1 
ATOM   2235  O  O     . ILE A 1 298 ? 124.577 167.477 80.502  1.00 103.18 ? 298  ILE A O     1 
ATOM   2236  C  CB    . ILE A 1 298 ? 127.321 167.699 82.508  1.00 100.88 ? 298  ILE A CB    1 
ATOM   2237  C  CG1   . ILE A 1 298 ? 127.684 166.523 81.602  1.00 102.01 ? 298  ILE A CG1   1 
ATOM   2238  C  CG2   . ILE A 1 298 ? 127.860 167.494 83.916  1.00 100.55 ? 298  ILE A CG2   1 
ATOM   2239  C  CD1   . ILE A 1 298 ? 129.174 166.340 81.413  1.00 101.93 ? 298  ILE A CD1   1 
ATOM   2240  N  N     . GLU A 1 299 ? 125.644 169.449 80.675  1.00 101.09 ? 299  GLU A N     1 
ATOM   2241  C  CA    . GLU A 1 299 ? 125.184 169.908 79.373  1.00 101.47 ? 299  GLU A CA    1 
ATOM   2242  C  C     . GLU A 1 299 ? 125.931 169.182 78.262  1.00 100.85 ? 299  GLU A C     1 
ATOM   2243  O  O     . GLU A 1 299 ? 127.143 168.967 78.342  1.00 100.77 ? 299  GLU A O     1 
ATOM   2244  C  CB    . GLU A 1 299 ? 125.379 171.419 79.246  1.00 101.68 ? 299  GLU A CB    1 
ATOM   2245  C  CG    . GLU A 1 299 ? 124.426 172.101 78.270  1.00 101.24 ? 299  GLU A CG    1 
ATOM   2246  C  CD    . GLU A 1 299 ? 124.838 171.932 76.820  1.00 102.21 ? 299  GLU A CD    1 
ATOM   2247  O  OE1   . GLU A 1 299 ? 126.045 171.747 76.559  1.00 102.22 ? 299  GLU A OE1   1 
ATOM   2248  O  OE2   . GLU A 1 299 ? 123.952 171.984 75.941  1.00 102.41 ? 299  GLU A OE2   1 
ATOM   2249  N  N     . GLY A 1 300 ? 125.198 168.807 77.219  1.00 103.91 ? 300  GLY A N     1 
ATOM   2250  C  CA    . GLY A 1 300 ? 125.794 168.154 76.073  1.00 105.24 ? 300  GLY A CA    1 
ATOM   2251  C  C     . GLY A 1 300 ? 125.918 166.654 76.171  1.00 105.95 ? 300  GLY A C     1 
ATOM   2252  O  O     . GLY A 1 300 ? 126.711 166.064 75.430  1.00 106.65 ? 300  GLY A O     1 
ATOM   2253  N  N     . GLU A 1 301 ? 125.161 166.011 77.060  1.00 103.83 ? 301  GLU A N     1 
ATOM   2254  C  CA    . GLU A 1 301 ? 125.236 164.563 77.197  1.00 104.71 ? 301  GLU A CA    1 
ATOM   2255  C  C     . GLU A 1 301 ? 124.590 163.821 76.038  1.00 105.23 ? 301  GLU A C     1 
ATOM   2256  O  O     . GLU A 1 301 ? 124.793 162.609 75.915  1.00 104.07 ? 301  GLU A O     1 
ATOM   2257  C  CB    . GLU A 1 301 ? 124.583 164.128 78.505  1.00 104.11 ? 301  GLU A CB    1 
ATOM   2258  C  CG    . GLU A 1 301 ? 125.414 164.430 79.727  1.00 104.19 ? 301  GLU A CG    1 
ATOM   2259  C  CD    . GLU A 1 301 ? 124.600 164.404 81.000  1.00 104.72 ? 301  GLU A CD    1 
ATOM   2260  O  OE1   . GLU A 1 301 ? 123.391 164.713 80.941  1.00 104.67 ? 301  GLU A OE1   1 
ATOM   2261  O  OE2   . GLU A 1 301 ? 125.167 164.076 82.061  1.00 104.81 ? 301  GLU A OE2   1 
ATOM   2262  N  N     . ASP A 1 302 ? 123.824 164.505 75.196  1.00 110.55 ? 302  ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 302 ? 123.112 163.862 74.101  1.00 110.75 ? 302  ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 302 ? 123.957 163.717 72.845  1.00 110.91 ? 302  ASP A C     1 
ATOM   2265  O  O     . ASP A 1 302 ? 123.456 163.207 71.838  1.00 110.87 ? 302  ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 302 ? 121.837 164.645 73.775  1.00 111.89 ? 302  ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 302 ? 120.897 164.746 74.959  1.00 111.74 ? 302  ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 302 ? 120.892 163.819 75.796  1.00 111.08 ? 302  ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 302 ? 120.164 165.752 75.054  1.00 111.97 ? 302  ASP A OD2   1 
ATOM   2270  N  N     . LEU A 1 303 ? 125.212 164.155 72.874  1.00 110.01 ? 303  LEU A N     1 
ATOM   2271  C  CA    . LEU A 1 303 ? 126.058 164.092 71.693  1.00 109.23 ? 303  LEU A CA    1 
ATOM   2272  C  C     . LEU A 1 303 ? 126.343 162.648 71.300  1.00 108.63 ? 303  LEU A C     1 
ATOM   2273  O  O     . LEU A 1 303 ? 126.431 161.754 72.146  1.00 109.26 ? 303  LEU A O     1 
ATOM   2274  C  CB    . LEU A 1 303 ? 127.371 164.832 71.937  1.00 108.28 ? 303  LEU A CB    1 
ATOM   2275  C  CG    . LEU A 1 303 ? 127.261 166.342 72.139  1.00 109.17 ? 303  LEU A CG    1 
ATOM   2276  C  CD1   . LEU A 1 303 ? 128.642 166.969 72.212  1.00 109.63 ? 303  LEU A CD1   1 
ATOM   2277  C  CD2   . LEU A 1 303 ? 126.441 166.971 71.027  1.00 109.73 ? 303  LEU A CD2   1 
ATOM   2278  N  N     . ASP A 1 304 ? 126.472 162.426 69.994  1.00 107.80 ? 304  ASP A N     1 
ATOM   2279  C  CA    . ASP A 1 304 ? 126.839 161.110 69.492  1.00 108.73 ? 304  ASP A CA    1 
ATOM   2280  C  C     . ASP A 1 304 ? 128.234 160.739 69.977  1.00 109.79 ? 304  ASP A C     1 
ATOM   2281  O  O     . ASP A 1 304 ? 129.157 161.556 69.955  1.00 109.52 ? 304  ASP A O     1 
ATOM   2282  C  CB    . ASP A 1 304 ? 126.785 161.091 67.965  1.00 109.64 ? 304  ASP A CB    1 
ATOM   2283  C  CG    . ASP A 1 304 ? 126.896 159.690 67.395  1.00 110.67 ? 304  ASP A CG    1 
ATOM   2284  O  OD1   . ASP A 1 304 ? 126.822 158.717 68.175  1.00 110.19 ? 304  ASP A OD1   1 
ATOM   2285  O  OD2   . ASP A 1 304 ? 127.058 159.562 66.163  1.00 109.50 ? 304  ASP A OD2   1 
ATOM   2286  N  N     . GLY A 1 305 ? 128.386 159.496 70.417  1.00 99.68  ? 305  GLY A N     1 
ATOM   2287  C  CA    . GLY A 1 305 ? 129.608 159.062 71.052  1.00 97.04  ? 305  GLY A CA    1 
ATOM   2288  C  C     . GLY A 1 305 ? 129.591 159.110 72.562  1.00 96.14  ? 305  GLY A C     1 
ATOM   2289  O  O     . GLY A 1 305 ? 130.653 158.978 73.180  1.00 95.67  ? 305  GLY A O     1 
ATOM   2290  N  N     . VAL A 1 306 ? 128.430 159.317 73.171  1.00 87.43  ? 306  VAL A N     1 
ATOM   2291  C  CA    . VAL A 1 306 ? 128.249 159.202 74.611  1.00 85.77  ? 306  VAL A CA    1 
ATOM   2292  C  C     . VAL A 1 306 ? 127.375 157.981 74.850  1.00 85.77  ? 306  VAL A C     1 
ATOM   2293  O  O     . VAL A 1 306 ? 126.194 157.965 74.481  1.00 86.97  ? 306  VAL A O     1 
ATOM   2294  C  CB    . VAL A 1 306 ? 127.624 160.465 75.215  1.00 85.93  ? 306  VAL A CB    1 
ATOM   2295  C  CG1   . VAL A 1 306 ? 127.277 160.234 76.672  1.00 84.71  ? 306  VAL A CG1   1 
ATOM   2296  C  CG2   . VAL A 1 306 ? 128.576 161.635 75.073  1.00 87.46  ? 306  VAL A CG2   1 
ATOM   2297  N  N     . ILE A 1 307 ? 127.954 156.953 75.464  1.00 74.39  ? 307  ILE A N     1 
ATOM   2298  C  CA    . ILE A 1 307 ? 127.273 155.690 75.696  1.00 72.38  ? 307  ILE A CA    1 
ATOM   2299  C  C     . ILE A 1 307 ? 127.405 155.355 77.174  1.00 71.48  ? 307  ILE A C     1 
ATOM   2300  O  O     . ILE A 1 307 ? 128.273 155.873 77.877  1.00 74.10  ? 307  ILE A O     1 
ATOM   2301  C  CB    . ILE A 1 307 ? 127.844 154.557 74.809  1.00 74.69  ? 307  ILE A CB    1 
ATOM   2302  C  CG1   . ILE A 1 307 ? 126.807 153.460 74.573  1.00 74.99  ? 307  ILE A CG1   1 
ATOM   2303  C  CG2   . ILE A 1 307 ? 129.101 153.971 75.422  1.00 72.60  ? 307  ILE A CG2   1 
ATOM   2304  C  CD1   . ILE A 1 307 ? 127.297 152.355 73.662  1.00 73.61  ? 307  ILE A CD1   1 
ATOM   2305  N  N     . HIS A 1 308 ? 126.508 154.504 77.652  1.00 68.96  ? 308  HIS A N     1 
ATOM   2306  C  CA    . HIS A 1 308 ? 126.523 154.089 79.044  1.00 71.59  ? 308  HIS A CA    1 
ATOM   2307  C  C     . HIS A 1 308 ? 127.398 152.855 79.221  1.00 72.09  ? 308  HIS A C     1 
ATOM   2308  O  O     . HIS A 1 308 ? 127.512 152.018 78.322  1.00 73.67  ? 308  HIS A O     1 
ATOM   2309  C  CB    . HIS A 1 308 ? 125.104 153.809 79.536  1.00 73.06  ? 308  HIS A CB    1 
ATOM   2310  C  CG    . HIS A 1 308 ? 124.237 155.027 79.588  1.00 72.35  ? 308  HIS A CG    1 
ATOM   2311  N  ND1   . HIS A 1 308 ? 122.895 155.000 79.280  1.00 71.55  ? 308  HIS A ND1   1 
ATOM   2312  C  CD2   . HIS A 1 308 ? 124.522 156.308 79.918  1.00 71.67  ? 308  HIS A CD2   1 
ATOM   2313  C  CE1   . HIS A 1 308 ? 122.391 156.214 79.413  1.00 72.22  ? 308  HIS A CE1   1 
ATOM   2314  N  NE2   . HIS A 1 308 ? 123.357 157.026 79.801  1.00 72.73  ? 308  HIS A NE2   1 
ATOM   2315  N  N     . GLY A 1 309 ? 128.023 152.757 80.395  1.00 64.57  ? 309  GLY A N     1 
ATOM   2316  C  CA    . GLY A 1 309 ? 128.947 151.661 80.642  1.00 63.33  ? 309  GLY A CA    1 
ATOM   2317  C  C     . GLY A 1 309 ? 128.273 150.305 80.649  1.00 60.26  ? 309  GLY A C     1 
ATOM   2318  O  O     . GLY A 1 309 ? 128.789 149.341 80.076  1.00 63.53  ? 309  GLY A O     1 
ATOM   2319  N  N     . THR A 1 310 ? 127.115 150.209 81.302  1.00 56.89  ? 310  THR A N     1 
ATOM   2320  C  CA    . THR A 1 310 ? 126.396 148.941 81.349  1.00 58.82  ? 310  THR A CA    1 
ATOM   2321  C  C     . THR A 1 310 ? 125.914 148.529 79.965  1.00 61.52  ? 310  THR A C     1 
ATOM   2322  O  O     . THR A 1 310 ? 125.961 147.345 79.614  1.00 61.87  ? 310  THR A O     1 
ATOM   2323  C  CB    . THR A 1 310 ? 125.223 149.040 82.322  1.00 62.09  ? 310  THR A CB    1 
ATOM   2324  O  OG1   . THR A 1 310 ? 124.323 150.065 81.885  1.00 65.26  ? 310  THR A OG1   1 
ATOM   2325  C  CG2   . THR A 1 310 ? 125.721 149.378 83.712  1.00 59.07  ? 310  THR A CG2   1 
ATOM   2326  N  N     . GLU A 1 311 ? 125.444 149.491 79.168  1.00 62.92  ? 311  GLU A N     1 
ATOM   2327  C  CA    . GLU A 1 311 ? 125.007 149.179 77.811  1.00 61.49  ? 311  GLU A CA    1 
ATOM   2328  C  C     . GLU A 1 311 ? 126.176 148.701 76.959  1.00 64.18  ? 311  GLU A C     1 
ATOM   2329  O  O     . GLU A 1 311 ? 126.043 147.745 76.186  1.00 67.78  ? 311  GLU A O     1 
ATOM   2330  C  CB    . GLU A 1 311 ? 124.337 150.402 77.187  1.00 60.55  ? 311  GLU A CB    1 
ATOM   2331  C  CG    . GLU A 1 311 ? 123.570 150.107 75.916  1.00 63.91  ? 311  GLU A CG    1 
ATOM   2332  C  CD    . GLU A 1 311 ? 122.727 151.280 75.463  1.00 68.49  ? 311  GLU A CD    1 
ATOM   2333  O  OE1   . GLU A 1 311 ? 122.654 152.281 76.206  1.00 69.87  ? 311  GLU A OE1   1 
ATOM   2334  O  OE2   . GLU A 1 311 ? 122.136 151.202 74.367  1.00 65.56  ? 311  GLU A OE2   1 
ATOM   2335  N  N     . PHE A 1 312 ? 127.335 149.342 77.107  1.00 57.19  ? 312  PHE A N     1 
ATOM   2336  C  CA    . PHE A 1 312 ? 128.539 148.909 76.407  1.00 54.29  ? 312  PHE A CA    1 
ATOM   2337  C  C     . PHE A 1 312 ? 128.927 147.487 76.803  1.00 59.02  ? 312  PHE A C     1 
ATOM   2338  O  O     . PHE A 1 312 ? 129.235 146.650 75.945  1.00 63.74  ? 312  PHE A O     1 
ATOM   2339  C  CB    . PHE A 1 312 ? 129.668 149.898 76.706  1.00 55.32  ? 312  PHE A CB    1 
ATOM   2340  C  CG    . PHE A 1 312 ? 131.033 149.413 76.326  1.00 55.94  ? 312  PHE A CG    1 
ATOM   2341  C  CD1   . PHE A 1 312 ? 131.452 149.445 75.011  1.00 60.40  ? 312  PHE A CD1   1 
ATOM   2342  C  CD2   . PHE A 1 312 ? 131.913 148.963 77.293  1.00 55.33  ? 312  PHE A CD2   1 
ATOM   2343  C  CE1   . PHE A 1 312 ? 132.713 149.013 74.664  1.00 62.27  ? 312  PHE A CE1   1 
ATOM   2344  C  CE2   . PHE A 1 312 ? 133.173 148.529 76.952  1.00 54.20  ? 312  PHE A CE2   1 
ATOM   2345  C  CZ    . PHE A 1 312 ? 133.574 148.555 75.636  1.00 56.65  ? 312  PHE A CZ    1 
ATOM   2346  N  N     . LEU A 1 313 ? 128.895 147.191 78.105  1.00 52.25  ? 313  LEU A N     1 
ATOM   2347  C  CA    . LEU A 1 313 ? 129.281 145.862 78.571  1.00 45.38  ? 313  LEU A CA    1 
ATOM   2348  C  C     . LEU A 1 313 ? 128.309 144.791 78.099  1.00 44.30  ? 313  LEU A C     1 
ATOM   2349  O  O     . LEU A 1 313 ? 128.731 143.694 77.720  1.00 47.18  ? 313  LEU A O     1 
ATOM   2350  C  CB    . LEU A 1 313 ? 129.389 145.843 80.093  1.00 48.59  ? 313  LEU A CB    1 
ATOM   2351  C  CG    . LEU A 1 313 ? 130.703 146.383 80.648  1.00 48.44  ? 313  LEU A CG    1 
ATOM   2352  C  CD1   . LEU A 1 313 ? 130.758 146.214 82.155  1.00 52.66  ? 313  LEU A CD1   1 
ATOM   2353  C  CD2   . LEU A 1 313 ? 131.887 145.709 79.984  1.00 46.17  ? 313  LEU A CD2   1 
ATOM   2354  N  N     . ARG A 1 314 ? 127.005 145.073 78.129  1.00 49.35  ? 314  ARG A N     1 
ATOM   2355  C  CA    . ARG A 1 314 ? 126.056 144.067 77.668  1.00 49.19  ? 314  ARG A CA    1 
ATOM   2356  C  C     . ARG A 1 314 ? 126.118 143.898 76.157  1.00 54.23  ? 314  ARG A C     1 
ATOM   2357  O  O     . ARG A 1 314 ? 125.856 142.804 75.652  1.00 58.41  ? 314  ARG A O     1 
ATOM   2358  C  CB    . ARG A 1 314 ? 124.634 144.404 78.118  1.00 50.63  ? 314  ARG A CB    1 
ATOM   2359  C  CG    . ARG A 1 314 ? 124.078 145.693 77.575  1.00 56.08  ? 314  ARG A CG    1 
ATOM   2360  C  CD    . ARG A 1 314 ? 122.571 145.741 77.708  1.00 56.15  ? 314  ARG A CD    1 
ATOM   2361  N  NE    . ARG A 1 314 ? 121.919 144.942 76.680  1.00 57.71  ? 314  ARG A NE    1 
ATOM   2362  C  CZ    . ARG A 1 314 ? 121.606 145.394 75.475  1.00 56.98  ? 314  ARG A CZ    1 
ATOM   2363  N  NH1   . ARG A 1 314 ? 121.861 146.641 75.118  1.00 59.64  ? 314  ARG A NH1   1 
ATOM   2364  N  NH2   . ARG A 1 314 ? 121.021 144.575 74.607  1.00 50.58  ? 314  ARG A NH2   1 
ATOM   2365  N  N     . LYS A 1 315 ? 126.472 144.955 75.420  1.00 63.27  ? 315  LYS A N     1 
ATOM   2366  C  CA    . LYS A 1 315 ? 126.694 144.797 73.987  1.00 65.93  ? 315  LYS A CA    1 
ATOM   2367  C  C     . LYS A 1 315 ? 127.911 143.923 73.711  1.00 66.72  ? 315  LYS A C     1 
ATOM   2368  O  O     . LYS A 1 315 ? 127.890 143.098 72.792  1.00 67.23  ? 315  LYS A O     1 
ATOM   2369  C  CB    . LYS A 1 315 ? 126.853 146.162 73.321  1.00 64.74  ? 315  LYS A CB    1 
ATOM   2370  C  CG    . LYS A 1 315 ? 125.552 146.907 73.105  1.00 66.60  ? 315  LYS A CG    1 
ATOM   2371  C  CD    . LYS A 1 315 ? 125.797 148.241 72.428  1.00 67.45  ? 315  LYS A CD    1 
ATOM   2372  C  CE    . LYS A 1 315 ? 124.517 149.040 72.305  1.00 67.19  ? 315  LYS A CE    1 
ATOM   2373  N  NZ    . LYS A 1 315 ? 123.491 148.313 71.514  1.00 65.30  ? 315  LYS A NZ    1 
ATOM   2374  N  N     . VAL A 1 316 ? 128.981 144.093 74.490  1.00 55.88  ? 316  VAL A N     1 
ATOM   2375  C  CA    . VAL A 1 316 ? 130.182 143.289 74.271  1.00 55.83  ? 316  VAL A CA    1 
ATOM   2376  C  C     . VAL A 1 316 ? 129.946 141.834 74.670  1.00 60.01  ? 316  VAL A C     1 
ATOM   2377  O  O     . VAL A 1 316 ? 130.363 140.908 73.964  1.00 58.90  ? 316  VAL A O     1 
ATOM   2378  C  CB    . VAL A 1 316 ? 131.380 143.899 75.020  1.00 52.24  ? 316  VAL A CB    1 
ATOM   2379  C  CG1   . VAL A 1 316 ? 132.578 142.979 74.931  1.00 52.04  ? 316  VAL A CG1   1 
ATOM   2380  C  CG2   . VAL A 1 316 ? 131.724 145.254 74.439  1.00 54.82  ? 316  VAL A CG2   1 
ATOM   2381  N  N     . ASN A 1 317 ? 129.280 141.607 75.805  1.00 59.51  ? 317  ASN A N     1 
ATOM   2382  C  CA    . ASN A 1 317 ? 129.056 140.243 76.276  1.00 53.70  ? 317  ASN A CA    1 
ATOM   2383  C  C     . ASN A 1 317 ? 128.114 139.475 75.358  1.00 54.74  ? 317  ASN A C     1 
ATOM   2384  O  O     . ASN A 1 317 ? 128.340 138.292 75.080  1.00 57.26  ? 317  ASN A O     1 
ATOM   2385  C  CB    . ASN A 1 317 ? 128.505 140.258 77.702  1.00 53.93  ? 317  ASN A CB    1 
ATOM   2386  C  CG    . ASN A 1 317 ? 129.555 140.612 78.732  1.00 48.61  ? 317  ASN A CG    1 
ATOM   2387  O  OD1   . ASN A 1 317 ? 130.191 139.735 79.310  1.00 48.62  ? 317  ASN A OD1   1 
ATOM   2388  N  ND2   . ASN A 1 317 ? 129.741 141.903 78.968  1.00 46.88  ? 317  ASN A ND2   1 
ATOM   2389  N  N     . MET A 1 318 ? 127.051 140.124 74.881  1.00 61.33  ? 318  MET A N     1 
ATOM   2390  C  CA    . MET A 1 318 ? 126.041 139.417 74.103  1.00 67.97  ? 318  MET A CA    1 
ATOM   2391  C  C     . MET A 1 318 ? 126.511 139.053 72.701  1.00 67.25  ? 318  MET A C     1 
ATOM   2392  O  O     . MET A 1 318 ? 125.831 138.275 72.026  1.00 64.94  ? 318  MET A O     1 
ATOM   2393  C  CB    . MET A 1 318 ? 124.758 140.244 74.018  1.00 67.08  ? 318  MET A CB    1 
ATOM   2394  C  CG    . MET A 1 318 ? 123.972 140.291 75.316  1.00 64.33  ? 318  MET A CG    1 
ATOM   2395  S  SD    . MET A 1 318 ? 122.312 140.964 75.129  1.00 66.50  ? 318  MET A SD    1 
ATOM   2396  C  CE    . MET A 1 318 ? 121.542 139.676 74.157  1.00 66.27  ? 318  MET A CE    1 
ATOM   2397  N  N     . GLY A 1 319 ? 127.642 139.582 72.250  1.00 77.21  ? 319  GLY A N     1 
ATOM   2398  C  CA    . GLY A 1 319 ? 128.140 139.246 70.933  1.00 79.03  ? 319  GLY A CA    1 
ATOM   2399  C  C     . GLY A 1 319 ? 127.642 140.188 69.860  1.00 79.12  ? 319  GLY A C     1 
ATOM   2400  O  O     . GLY A 1 319 ? 127.247 139.756 68.774  1.00 79.18  ? 319  GLY A O     1 
ATOM   2401  N  N     . GLU A 1 320 ? 127.655 141.482 70.155  1.00 85.64  ? 320  GLU A N     1 
ATOM   2402  C  CA    . GLU A 1 320 ? 127.219 142.505 69.222  1.00 87.66  ? 320  GLU A CA    1 
ATOM   2403  C  C     . GLU A 1 320 ? 128.375 143.446 68.909  1.00 89.33  ? 320  GLU A C     1 
ATOM   2404  O  O     . GLU A 1 320 ? 129.404 143.457 69.589  1.00 86.40  ? 320  GLU A O     1 
ATOM   2405  C  CB    . GLU A 1 320 ? 126.024 143.286 69.780  1.00 87.25  ? 320  GLU A CB    1 
ATOM   2406  C  CG    . GLU A 1 320 ? 124.817 142.419 70.076  1.00 86.98  ? 320  GLU A CG    1 
ATOM   2407  C  CD    . GLU A 1 320 ? 123.612 143.227 70.498  1.00 88.52  ? 320  GLU A CD    1 
ATOM   2408  O  OE1   . GLU A 1 320 ? 123.662 144.469 70.390  1.00 87.65  ? 320  GLU A OE1   1 
ATOM   2409  O  OE2   . GLU A 1 320 ? 122.615 142.620 70.939  1.00 88.04  ? 320  GLU A OE2   1 
ATOM   2410  N  N     . LYS A 1 321 ? 128.192 144.235 67.856  1.00 107.03 ? 321  LYS A N     1 
ATOM   2411  C  CA    . LYS A 1 321 ? 129.215 145.159 67.390  1.00 106.25 ? 321  LYS A CA    1 
ATOM   2412  C  C     . LYS A 1 321 ? 128.995 146.520 68.035  1.00 105.57 ? 321  LYS A C     1 
ATOM   2413  O  O     . LYS A 1 321 ? 127.921 147.113 67.895  1.00 104.14 ? 321  LYS A O     1 
ATOM   2414  C  CB    . LYS A 1 321 ? 129.183 145.277 65.868  1.00 107.02 ? 321  LYS A CB    1 
ATOM   2415  C  CG    . LYS A 1 321 ? 129.438 143.970 65.136  1.00 107.11 ? 321  LYS A CG    1 
ATOM   2416  C  CD    . LYS A 1 321 ? 129.363 144.135 63.620  1.00 105.78 ? 321  LYS A CD    1 
ATOM   2417  C  CE    . LYS A 1 321 ? 130.587 144.848 63.053  1.00 105.30 ? 321  LYS A CE    1 
ATOM   2418  N  NZ    . LYS A 1 321 ? 130.490 146.335 63.114  1.00 106.01 ? 321  LYS A NZ    1 
ATOM   2419  N  N     . VAL A 1 322 ? 130.008 147.009 68.741  1.00 107.13 ? 322  VAL A N     1 
ATOM   2420  C  CA    . VAL A 1 322 ? 129.981 148.328 69.357  1.00 107.40 ? 322  VAL A CA    1 
ATOM   2421  C  C     . VAL A 1 322 ? 131.090 149.154 68.723  1.00 107.28 ? 322  VAL A C     1 
ATOM   2422  O  O     . VAL A 1 322 ? 132.259 148.751 68.738  1.00 107.26 ? 322  VAL A O     1 
ATOM   2423  C  CB    . VAL A 1 322 ? 130.136 148.252 70.885  1.00 108.02 ? 322  VAL A CB    1 
ATOM   2424  C  CG1   . VAL A 1 322 ? 131.184 147.220 71.268  1.00 107.40 ? 322  VAL A CG1   1 
ATOM   2425  C  CG2   . VAL A 1 322 ? 130.488 149.616 71.454  1.00 107.98 ? 322  VAL A CG2   1 
ATOM   2426  N  N     . GLU A 1 323 ? 130.723 150.294 68.149  1.00 106.16 ? 323  GLU A N     1 
ATOM   2427  C  CA    . GLU A 1 323 ? 131.685 151.139 67.452  1.00 106.93 ? 323  GLU A CA    1 
ATOM   2428  C  C     . GLU A 1 323 ? 132.466 151.940 68.483  1.00 105.62 ? 323  GLU A C     1 
ATOM   2429  O  O     . GLU A 1 323 ? 131.934 152.874 69.090  1.00 103.97 ? 323  GLU A O     1 
ATOM   2430  C  CB    . GLU A 1 323 ? 130.975 152.056 66.461  1.00 106.63 ? 323  GLU A CB    1 
ATOM   2431  C  CG    . GLU A 1 323 ? 131.916 152.883 65.605  1.00 106.03 ? 323  GLU A CG    1 
ATOM   2432  C  CD    . GLU A 1 323 ? 132.754 152.035 64.669  1.00 107.14 ? 323  GLU A CD    1 
ATOM   2433  O  OE1   . GLU A 1 323 ? 132.291 150.944 64.275  1.00 107.32 ? 323  GLU A OE1   1 
ATOM   2434  O  OE2   . GLU A 1 323 ? 133.877 152.459 64.329  1.00 108.10 ? 323  GLU A OE2   1 
ATOM   2435  N  N     . LEU A 1 324 ? 133.728 151.578 68.683  1.00 95.91  ? 324  LEU A N     1 
ATOM   2436  C  CA    . LEU A 1 324 ? 134.571 152.204 69.689  1.00 94.51  ? 324  LEU A CA    1 
ATOM   2437  C  C     . LEU A 1 324 ? 135.796 152.809 69.022  1.00 94.71  ? 324  LEU A C     1 
ATOM   2438  O  O     . LEU A 1 324 ? 136.486 152.134 68.252  1.00 94.23  ? 324  LEU A O     1 
ATOM   2439  C  CB    . LEU A 1 324 ? 134.989 151.190 70.750  1.00 93.45  ? 324  LEU A CB    1 
ATOM   2440  C  CG    . LEU A 1 324 ? 135.476 151.773 72.069  1.00 92.92  ? 324  LEU A CG    1 
ATOM   2441  C  CD1   . LEU A 1 324 ? 134.347 152.512 72.761  1.00 93.87  ? 324  LEU A CD1   1 
ATOM   2442  C  CD2   . LEU A 1 324 ? 136.013 150.668 72.946  1.00 93.44  ? 324  LEU A CD2   1 
ATOM   2443  N  N     . GLY A 1 325 ? 136.066 154.073 69.325  1.00 99.08  ? 325  GLY A N     1 
ATOM   2444  C  CA    . GLY A 1 325 ? 137.206 154.765 68.771  1.00 99.05  ? 325  GLY A CA    1 
ATOM   2445  C  C     . GLY A 1 325 ? 138.483 154.473 69.533  1.00 99.30  ? 325  GLY A C     1 
ATOM   2446  O  O     . GLY A 1 325 ? 138.534 153.656 70.453  1.00 98.54  ? 325  GLY A O     1 
ATOM   2447  N  N     . LYS A 1 326 ? 139.544 155.169 69.124  1.00 94.36  ? 326  LYS A N     1 
ATOM   2448  C  CA    . LYS A 1 326 ? 140.852 154.955 69.732  1.00 92.73  ? 326  LYS A CA    1 
ATOM   2449  C  C     . LYS A 1 326 ? 140.918 155.535 71.139  1.00 92.70  ? 326  LYS A C     1 
ATOM   2450  O  O     . LYS A 1 326 ? 141.452 154.897 72.054  1.00 92.38  ? 326  LYS A O     1 
ATOM   2451  C  CB    . LYS A 1 326 ? 141.938 155.563 68.848  1.00 92.17  ? 326  LYS A CB    1 
ATOM   2452  C  CG    . LYS A 1 326 ? 143.348 155.374 69.368  1.00 92.18  ? 326  LYS A CG    1 
ATOM   2453  C  CD    . LYS A 1 326 ? 143.718 153.907 69.431  1.00 91.73  ? 326  LYS A CD    1 
ATOM   2454  C  CE    . LYS A 1 326 ? 145.194 153.731 69.741  1.00 92.70  ? 326  LYS A CE    1 
ATOM   2455  N  NZ    . LYS A 1 326 ? 145.575 154.388 71.021  1.00 92.62  ? 326  LYS A NZ    1 
ATOM   2456  N  N     . ARG A 1 327 ? 140.385 156.738 71.336  1.00 92.82  ? 327  ARG A N     1 
ATOM   2457  C  CA    . ARG A 1 327 ? 140.488 157.446 72.608  1.00 90.70  ? 327  ARG A CA    1 
ATOM   2458  C  C     . ARG A 1 327 ? 139.148 157.375 73.327  1.00 91.21  ? 327  ARG A C     1 
ATOM   2459  O  O     . ARG A 1 327 ? 138.161 157.964 72.878  1.00 94.22  ? 327  ARG A O     1 
ATOM   2460  C  CB    . ARG A 1 327 ? 140.915 158.894 72.387  1.00 91.72  ? 327  ARG A CB    1 
ATOM   2461  C  CG    . ARG A 1 327 ? 142.319 159.047 71.848  1.00 91.90  ? 327  ARG A CG    1 
ATOM   2462  C  CD    . ARG A 1 327 ? 142.623 160.496 71.535  1.00 92.19  ? 327  ARG A CD    1 
ATOM   2463  N  NE    . ARG A 1 327 ? 144.024 160.692 71.188  1.00 92.06  ? 327  ARG A NE    1 
ATOM   2464  C  CZ    . ARG A 1 327 ? 144.982 160.949 72.069  1.00 93.59  ? 327  ARG A CZ    1 
ATOM   2465  N  NH1   . ARG A 1 327 ? 144.723 161.049 73.362  1.00 93.79  ? 327  ARG A NH1   1 
ATOM   2466  N  NH2   . ARG A 1 327 ? 146.231 161.109 71.641  1.00 93.06  ? 327  ARG A NH2   1 
ATOM   2467  N  N     . VAL A 1 328 ? 139.121 156.669 74.451  1.00 80.96  ? 328  VAL A N     1 
ATOM   2468  C  CA    . VAL A 1 328 ? 137.912 156.466 75.236  1.00 81.59  ? 328  VAL A CA    1 
ATOM   2469  C  C     . VAL A 1 328 ? 138.152 157.014 76.633  1.00 82.87  ? 328  VAL A C     1 
ATOM   2470  O  O     . VAL A 1 328 ? 139.180 156.719 77.251  1.00 85.86  ? 328  VAL A O     1 
ATOM   2471  C  CB    . VAL A 1 328 ? 137.519 154.978 75.292  1.00 82.91  ? 328  VAL A CB    1 
ATOM   2472  C  CG1   . VAL A 1 328 ? 136.282 154.778 76.149  1.00 79.35  ? 328  VAL A CG1   1 
ATOM   2473  C  CG2   . VAL A 1 328 ? 137.297 154.444 73.893  1.00 85.83  ? 328  VAL A CG2   1 
ATOM   2474  N  N     . ILE A 1 329 ? 137.217 157.821 77.120  1.00 81.43  ? 329  ILE A N     1 
ATOM   2475  C  CA    . ILE A 1 329 ? 137.212 158.273 78.504  1.00 79.09  ? 329  ILE A CA    1 
ATOM   2476  C  C     . ILE A 1 329 ? 136.038 157.605 79.205  1.00 78.45  ? 329  ILE A C     1 
ATOM   2477  O  O     . ILE A 1 329 ? 134.930 157.543 78.660  1.00 83.82  ? 329  ILE A O     1 
ATOM   2478  C  CB    . ILE A 1 329 ? 137.142 159.807 78.612  1.00 79.86  ? 329  ILE A CB    1 
ATOM   2479  C  CG1   . ILE A 1 329 ? 136.937 160.239 80.064  1.00 78.94  ? 329  ILE A CG1   1 
ATOM   2480  C  CG2   . ILE A 1 329 ? 136.047 160.369 77.735  1.00 82.54  ? 329  ILE A CG2   1 
ATOM   2481  C  CD1   . ILE A 1 329 ? 136.724 161.722 80.235  1.00 81.41  ? 329  ILE A CD1   1 
ATOM   2482  N  N     . VAL A 1 330 ? 136.294 157.071 80.393  1.00 69.95  ? 330  VAL A N     1 
ATOM   2483  C  CA    . VAL A 1 330 ? 135.291 156.386 81.194  1.00 69.72  ? 330  VAL A CA    1 
ATOM   2484  C  C     . VAL A 1 330 ? 135.113 157.157 82.492  1.00 72.69  ? 330  VAL A C     1 
ATOM   2485  O  O     . VAL A 1 330 ? 136.097 157.497 83.157  1.00 74.33  ? 330  VAL A O     1 
ATOM   2486  C  CB    . VAL A 1 330 ? 135.694 154.927 81.472  1.00 71.43  ? 330  VAL A CB    1 
ATOM   2487  C  CG1   . VAL A 1 330 ? 134.888 154.367 82.624  1.00 71.29  ? 330  VAL A CG1   1 
ATOM   2488  C  CG2   . VAL A 1 330 ? 135.512 154.087 80.222  1.00 71.37  ? 330  VAL A CG2   1 
ATOM   2489  N  N     . VAL A 1 331 ? 133.865 157.438 82.846  1.00 76.79  ? 331  VAL A N     1 
ATOM   2490  C  CA    . VAL A 1 331 ? 133.536 158.144 84.077  1.00 77.56  ? 331  VAL A CA    1 
ATOM   2491  C  C     . VAL A 1 331 ? 132.986 157.139 85.077  1.00 76.59  ? 331  VAL A C     1 
ATOM   2492  O  O     . VAL A 1 331 ? 132.025 156.420 84.780  1.00 78.00  ? 331  VAL A O     1 
ATOM   2493  C  CB    . VAL A 1 331 ? 132.526 159.273 83.814  1.00 76.95  ? 331  VAL A CB    1 
ATOM   2494  C  CG1   . VAL A 1 331 ? 132.310 160.091 85.072  1.00 78.08  ? 331  VAL A CG1   1 
ATOM   2495  C  CG2   . VAL A 1 331 ? 133.007 160.146 82.673  1.00 76.80  ? 331  VAL A CG2   1 
ATOM   2496  N  N     . GLY A 1 332 ? 133.592 157.079 86.248  1.00 69.80  ? 332  GLY A N     1 
ATOM   2497  C  CA    . GLY A 1 332 ? 133.145 156.167 87.283  1.00 68.05  ? 332  GLY A CA    1 
ATOM   2498  C  C     . GLY A 1 332 ? 134.309 155.664 88.107  1.00 69.48  ? 332  GLY A C     1 
ATOM   2499  O  O     . GLY A 1 332 ? 135.474 155.799 87.744  1.00 69.60  ? 332  GLY A O     1 
ATOM   2500  N  N     . GLY A 1 333 ? 133.966 155.069 89.244  1.00 67.66  ? 333  GLY A N     1 
ATOM   2501  C  CA    . GLY A 1 333 ? 134.964 154.511 90.130  1.00 66.78  ? 333  GLY A CA    1 
ATOM   2502  C  C     . GLY A 1 333 ? 134.591 153.135 90.632  1.00 65.28  ? 333  GLY A C     1 
ATOM   2503  O  O     . GLY A 1 333 ? 135.360 152.498 91.355  1.00 64.59  ? 333  GLY A O     1 
ATOM   2504  N  N     . GLY A 1 334 ? 133.411 152.661 90.251  1.00 56.28  ? 334  GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 334 ? 132.943 151.363 90.678  1.00 54.05  ? 334  GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 334 ? 133.574 150.243 89.878  1.00 53.90  ? 334  GLY A C     1 
ATOM   2507  O  O     . GLY A 1 334 ? 134.494 150.436 89.083  1.00 60.59  ? 334  GLY A O     1 
ATOM   2508  N  N     . ASN A 1 335 ? 133.064 149.034 90.117  1.00 44.64  ? 335  ASN A N     1 
ATOM   2509  C  CA    . ASN A 1 335 ? 133.496 147.883 89.332  1.00 38.07  ? 335  ASN A CA    1 
ATOM   2510  C  C     . ASN A 1 335 ? 133.087 148.017 87.872  1.00 41.01  ? 335  ASN A C     1 
ATOM   2511  O  O     . ASN A 1 335 ? 133.748 147.456 86.988  1.00 48.96  ? 335  ASN A O     1 
ATOM   2512  C  CB    . ASN A 1 335 ? 132.923 146.600 89.932  1.00 35.54  ? 335  ASN A CB    1 
ATOM   2513  C  CG    . ASN A 1 335 ? 133.634 146.182 91.200  1.00 43.69  ? 335  ASN A CG    1 
ATOM   2514  O  OD1   . ASN A 1 335 ? 134.860 146.213 91.275  1.00 46.32  ? 335  ASN A OD1   1 
ATOM   2515  N  ND2   . ASN A 1 335 ? 132.867 145.788 92.207  1.00 42.81  ? 335  ASN A ND2   1 
ATOM   2516  N  N     . THR A 1 336 ? 132.005 148.755 87.606  1.00 37.84  ? 336  THR A N     1 
ATOM   2517  C  CA    . THR A 1 336 ? 131.556 148.958 86.233  1.00 37.30  ? 336  THR A CA    1 
ATOM   2518  C  C     . THR A 1 336 ? 132.606 149.696 85.417  1.00 39.34  ? 336  THR A C     1 
ATOM   2519  O  O     . THR A 1 336 ? 132.877 149.333 84.267  1.00 42.49  ? 336  THR A O     1 
ATOM   2520  C  CB    . THR A 1 336 ? 130.236 149.732 86.220  1.00 44.08  ? 336  THR A CB    1 
ATOM   2521  O  OG1   . THR A 1 336 ? 129.304 149.115 87.115  1.00 45.87  ? 336  THR A OG1   1 
ATOM   2522  C  CG2   . THR A 1 336 ? 129.644 149.748 84.824  1.00 41.27  ? 336  THR A CG2   1 
ATOM   2523  N  N     . ALA A 1 337 ? 133.206 150.737 85.999  1.00 52.17  ? 337  ALA A N     1 
ATOM   2524  C  CA    . ALA A 1 337 ? 134.236 151.491 85.295  1.00 48.96  ? 337  ALA A CA    1 
ATOM   2525  C  C     . ALA A 1 337 ? 135.448 150.619 85.002  1.00 49.95  ? 337  ALA A C     1 
ATOM   2526  O  O     . ALA A 1 337 ? 136.028 150.694 83.915  1.00 58.46  ? 337  ALA A O     1 
ATOM   2527  C  CB    . ALA A 1 337 ? 134.637 152.718 86.111  1.00 52.27  ? 337  ALA A CB    1 
ATOM   2528  N  N     . MET A 1 338 ? 135.832 149.772 85.955  1.00 48.34  ? 338  MET A N     1 
ATOM   2529  C  CA    . MET A 1 338 ? 136.963 148.879 85.735  1.00 51.28  ? 338  MET A CA    1 
ATOM   2530  C  C     . MET A 1 338 ? 136.680 147.884 84.621  1.00 57.30  ? 338  MET A C     1 
ATOM   2531  O  O     . MET A 1 338 ? 137.546 147.620 83.777  1.00 61.91  ? 338  MET A O     1 
ATOM   2532  C  CB    . MET A 1 338 ? 137.303 148.147 87.027  1.00 51.37  ? 338  MET A CB    1 
ATOM   2533  C  CG    . MET A 1 338 ? 137.614 149.082 88.157  1.00 56.40  ? 338  MET A CG    1 
ATOM   2534  S  SD    . MET A 1 338 ? 138.941 150.200 87.706  1.00 65.35  ? 338  MET A SD    1 
ATOM   2535  C  CE    . MET A 1 338 ? 140.187 149.004 87.258  1.00 55.84  ? 338  MET A CE    1 
ATOM   2536  N  N     . ASP A 1 339 ? 135.474 147.318 84.601  1.00 49.17  ? 339  ASP A N     1 
ATOM   2537  C  CA    . ASP A 1 339 ? 135.168 146.326 83.579  1.00 41.22  ? 339  ASP A CA    1 
ATOM   2538  C  C     . ASP A 1 339 ? 135.041 146.965 82.201  1.00 45.52  ? 339  ASP A C     1 
ATOM   2539  O  O     . ASP A 1 339 ? 135.525 146.403 81.212  1.00 50.17  ? 339  ASP A O     1 
ATOM   2540  C  CB    . ASP A 1 339 ? 133.910 145.554 83.961  1.00 40.26  ? 339  ASP A CB    1 
ATOM   2541  C  CG    . ASP A 1 339 ? 134.151 144.616 85.128  1.00 45.33  ? 339  ASP A CG    1 
ATOM   2542  O  OD1   . ASP A 1 339 ? 135.302 144.554 85.605  1.00 48.34  ? 339  ASP A OD1   1 
ATOM   2543  O  OD2   . ASP A 1 339 ? 133.203 143.935 85.566  1.00 44.15  ? 339  ASP A OD2   1 
ATOM   2544  N  N     . VAL A 1 340 ? 134.438 148.155 82.110  1.00 48.69  ? 340  VAL A N     1 
ATOM   2545  C  CA    . VAL A 1 340 ? 134.392 148.817 80.809  1.00 48.56  ? 340  VAL A CA    1 
ATOM   2546  C  C     . VAL A 1 340 ? 135.794 149.220 80.367  1.00 46.46  ? 340  VAL A C     1 
ATOM   2547  O  O     . VAL A 1 340 ? 136.113 149.146 79.179  1.00 50.89  ? 340  VAL A O     1 
ATOM   2548  C  CB    . VAL A 1 340 ? 133.424 150.021 80.796  1.00 47.40  ? 340  VAL A CB    1 
ATOM   2549  C  CG1   . VAL A 1 340 ? 132.030 149.605 81.197  1.00 49.30  ? 340  VAL A CG1   1 
ATOM   2550  C  CG2   . VAL A 1 340 ? 133.898 151.125 81.680  1.00 47.49  ? 340  VAL A CG2   1 
ATOM   2551  N  N     . ALA A 1 341 ? 136.667 149.608 81.303  1.00 45.85  ? 341  ALA A N     1 
ATOM   2552  C  CA    . ALA A 1 341 ? 138.025 149.992 80.938  1.00 48.48  ? 341  ALA A CA    1 
ATOM   2553  C  C     . ALA A 1 341 ? 138.816 148.805 80.406  1.00 50.21  ? 341  ALA A C     1 
ATOM   2554  O  O     . ALA A 1 341 ? 139.428 148.883 79.335  1.00 57.93  ? 341  ALA A O     1 
ATOM   2555  C  CB    . ALA A 1 341 ? 138.734 150.608 82.141  1.00 49.39  ? 341  ALA A CB    1 
ATOM   2556  N  N     . ARG A 1 342 ? 138.810 147.692 81.138  1.00 48.72  ? 342  ARG A N     1 
ATOM   2557  C  CA    . ARG A 1 342 ? 139.583 146.536 80.711  1.00 51.51  ? 342  ARG A CA    1 
ATOM   2558  C  C     . ARG A 1 342 ? 138.939 145.795 79.544  1.00 51.25  ? 342  ARG A C     1 
ATOM   2559  O  O     . ARG A 1 342 ? 139.620 145.009 78.879  1.00 50.87  ? 342  ARG A O     1 
ATOM   2560  C  CB    . ARG A 1 342 ? 139.811 145.586 81.889  1.00 51.14  ? 342  ARG A CB    1 
ATOM   2561  C  CG    . ARG A 1 342 ? 140.645 146.170 83.021  1.00 54.03  ? 342  ARG A CG    1 
ATOM   2562  C  CD    . ARG A 1 342 ? 141.408 145.079 83.755  1.00 53.54  ? 342  ARG A CD    1 
ATOM   2563  N  NE    . ARG A 1 342 ? 140.525 144.137 84.430  1.00 53.34  ? 342  ARG A NE    1 
ATOM   2564  C  CZ    . ARG A 1 342 ? 140.881 142.918 84.809  1.00 54.18  ? 342  ARG A CZ    1 
ATOM   2565  N  NH1   . ARG A 1 342 ? 142.094 142.448 84.574  1.00 53.05  ? 342  ARG A NH1   1 
ATOM   2566  N  NH2   . ARG A 1 342 ? 139.996 142.148 85.433  1.00 50.88  ? 342  ARG A NH2   1 
ATOM   2567  N  N     . THR A 1 343 ? 137.655 146.034 79.267  1.00 51.14  ? 343  THR A N     1 
ATOM   2568  C  CA    . THR A 1 343 ? 137.032 145.478 78.074  1.00 47.49  ? 343  THR A CA    1 
ATOM   2569  C  C     . THR A 1 343 ? 137.266 146.350 76.845  1.00 51.39  ? 343  THR A C     1 
ATOM   2570  O  O     . THR A 1 343 ? 137.448 145.827 75.740  1.00 54.00  ? 343  THR A O     1 
ATOM   2571  C  CB    . THR A 1 343 ? 135.531 145.294 78.306  1.00 46.88  ? 343  THR A CB    1 
ATOM   2572  O  OG1   . THR A 1 343 ? 135.318 144.627 79.555  1.00 49.92  ? 343  THR A OG1   1 
ATOM   2573  C  CG2   . THR A 1 343 ? 134.928 144.461 77.205  1.00 49.23  ? 343  THR A CG2   1 
ATOM   2574  N  N     . ALA A 1 344 ? 137.270 147.674 77.016  1.00 49.82  ? 344  ALA A N     1 
ATOM   2575  C  CA    . ALA A 1 344 ? 137.587 148.573 75.915  1.00 52.16  ? 344  ALA A CA    1 
ATOM   2576  C  C     . ALA A 1 344 ? 139.064 148.517 75.558  1.00 56.90  ? 344  ALA A C     1 
ATOM   2577  O  O     . ALA A 1 344 ? 139.431 148.763 74.405  1.00 58.25  ? 344  ALA A O     1 
ATOM   2578  C  CB    . ALA A 1 344 ? 137.182 150.000 76.276  1.00 55.04  ? 344  ALA A CB    1 
ATOM   2579  N  N     . LEU A 1 345 ? 139.921 148.212 76.534  1.00 52.11  ? 345  LEU A N     1 
ATOM   2580  C  CA    . LEU A 1 345 ? 141.339 148.031 76.249  1.00 49.33  ? 345  LEU A CA    1 
ATOM   2581  C  C     . LEU A 1 345 ? 141.571 146.831 75.341  1.00 52.14  ? 345  LEU A C     1 
ATOM   2582  O  O     . LEU A 1 345 ? 142.431 146.872 74.455  1.00 54.82  ? 345  LEU A O     1 
ATOM   2583  C  CB    . LEU A 1 345 ? 142.106 147.874 77.558  1.00 50.62  ? 345  LEU A CB    1 
ATOM   2584  C  CG    . LEU A 1 345 ? 143.620 147.753 77.470  1.00 56.43  ? 345  LEU A CG    1 
ATOM   2585  C  CD1   . LEU A 1 345 ? 144.221 149.040 76.941  1.00 53.79  ? 345  LEU A CD1   1 
ATOM   2586  C  CD2   . LEU A 1 345 ? 144.170 147.421 78.835  1.00 59.06  ? 345  LEU A CD2   1 
ATOM   2587  N  N     . ARG A 1 346 ? 140.816 145.751 75.548  1.00 50.86  ? 346  ARG A N     1 
ATOM   2588  C  CA    . ARG A 1 346 ? 140.953 144.571 74.703  1.00 49.75  ? 346  ARG A CA    1 
ATOM   2589  C  C     . ARG A 1 346 ? 140.369 144.779 73.313  1.00 47.78  ? 346  ARG A C     1 
ATOM   2590  O  O     . ARG A 1 346 ? 140.760 144.072 72.381  1.00 51.12  ? 346  ARG A O     1 
ATOM   2591  C  CB    . ARG A 1 346 ? 140.293 143.368 75.376  1.00 54.10  ? 346  ARG A CB    1 
ATOM   2592  C  CG    . ARG A 1 346 ? 141.118 142.771 76.499  1.00 50.56  ? 346  ARG A CG    1 
ATOM   2593  C  CD    . ARG A 1 346 ? 140.293 141.842 77.364  1.00 49.45  ? 346  ARG A CD    1 
ATOM   2594  N  NE    . ARG A 1 346 ? 141.114 141.097 78.309  1.00 51.79  ? 346  ARG A NE    1 
ATOM   2595  C  CZ    . ARG A 1 346 ? 141.588 141.588 79.445  1.00 51.26  ? 346  ARG A CZ    1 
ATOM   2596  N  NH1   . ARG A 1 346 ? 141.361 142.840 79.805  1.00 49.77  ? 346  ARG A NH1   1 
ATOM   2597  N  NH2   . ARG A 1 346 ? 142.309 140.804 80.240  1.00 51.91  ? 346  ARG A NH2   1 
ATOM   2598  N  N     . LEU A 1 347 ? 139.446 145.725 73.153  1.00 53.45  ? 347  LEU A N     1 
ATOM   2599  C  CA    . LEU A 1 347 ? 138.873 146.005 71.844  1.00 56.34  ? 347  LEU A CA    1 
ATOM   2600  C  C     . LEU A 1 347 ? 139.757 146.901 70.987  1.00 55.33  ? 347  LEU A C     1 
ATOM   2601  O  O     . LEU A 1 347 ? 139.466 147.074 69.799  1.00 58.18  ? 347  LEU A O     1 
ATOM   2602  C  CB    . LEU A 1 347 ? 137.491 146.643 71.999  1.00 56.17  ? 347  LEU A CB    1 
ATOM   2603  C  CG    . LEU A 1 347 ? 136.374 145.725 72.493  1.00 55.11  ? 347  LEU A CG    1 
ATOM   2604  C  CD1   . LEU A 1 347 ? 135.067 146.486 72.584  1.00 54.58  ? 347  LEU A CD1   1 
ATOM   2605  C  CD2   . LEU A 1 347 ? 136.226 144.519 71.584  1.00 56.96  ? 347  LEU A CD2   1 
ATOM   2606  N  N     . GLY A 1 348 ? 140.822 147.463 71.548  1.00 56.91  ? 348  GLY A N     1 
ATOM   2607  C  CA    . GLY A 1 348 ? 141.741 148.262 70.764  1.00 58.83  ? 348  GLY A CA    1 
ATOM   2608  C  C     . GLY A 1 348 ? 141.613 149.754 70.983  1.00 59.32  ? 348  GLY A C     1 
ATOM   2609  O  O     . GLY A 1 348 ? 141.679 150.532 70.028  1.00 59.61  ? 348  GLY A O     1 
ATOM   2610  N  N     . ALA A 1 349 ? 141.435 150.168 72.232  1.00 64.96  ? 349  ALA A N     1 
ATOM   2611  C  CA    . ALA A 1 349 ? 141.275 151.572 72.571  1.00 65.83  ? 349  ALA A CA    1 
ATOM   2612  C  C     . ALA A 1 349 ? 142.320 151.996 73.595  1.00 64.77  ? 349  ALA A C     1 
ATOM   2613  O  O     . ALA A 1 349 ? 143.023 151.173 74.186  1.00 64.29  ? 349  ALA A O     1 
ATOM   2614  C  CB    . ALA A 1 349 ? 139.865 151.848 73.107  1.00 64.62  ? 349  ALA A CB    1 
ATOM   2615  N  N     . ASP A 1 350 ? 142.422 153.307 73.788  1.00 71.90  ? 350  ASP A N     1 
ATOM   2616  C  CA    . ASP A 1 350 ? 143.259 153.909 74.823  1.00 71.13  ? 350  ASP A CA    1 
ATOM   2617  C  C     . ASP A 1 350 ? 142.307 154.519 75.844  1.00 71.89  ? 350  ASP A C     1 
ATOM   2618  O  O     . ASP A 1 350 ? 141.804 155.630 75.654  1.00 71.86  ? 350  ASP A O     1 
ATOM   2619  C  CB    . ASP A 1 350 ? 144.203 154.951 74.233  1.00 75.58  ? 350  ASP A CB    1 
ATOM   2620  C  CG    . ASP A 1 350 ? 145.243 155.422 75.227  1.00 76.79  ? 350  ASP A CG    1 
ATOM   2621  O  OD1   . ASP A 1 350 ? 145.322 154.837 76.327  1.00 75.82  ? 350  ASP A OD1   1 
ATOM   2622  O  OD2   . ASP A 1 350 ? 145.983 156.377 74.909  1.00 76.55  ? 350  ASP A OD2   1 
ATOM   2623  N  N     . VAL A 1 351 ? 142.065 153.792 76.929  1.00 66.76  ? 351  VAL A N     1 
ATOM   2624  C  CA    . VAL A 1 351 ? 140.948 154.066 77.823  1.00 66.92  ? 351  VAL A CA    1 
ATOM   2625  C  C     . VAL A 1 351 ? 141.454 154.763 79.078  1.00 65.84  ? 351  VAL A C     1 
ATOM   2626  O  O     . VAL A 1 351 ? 142.428 154.322 79.700  1.00 70.91  ? 351  VAL A O     1 
ATOM   2627  C  CB    . VAL A 1 351 ? 140.189 152.773 78.168  1.00 63.67  ? 351  VAL A CB    1 
ATOM   2628  C  CG1   . VAL A 1 351 ? 141.158 151.650 78.489  1.00 65.84  ? 351  VAL A CG1   1 
ATOM   2629  C  CG2   . VAL A 1 351 ? 139.232 153.012 79.320  1.00 65.51  ? 351  VAL A CG2   1 
ATOM   2630  N  N     . THR A 1 352 ? 140.799 155.860 79.439  1.00 71.21  ? 352  THR A N     1 
ATOM   2631  C  CA    . THR A 1 352 ? 141.055 156.576 80.678  1.00 70.73  ? 352  THR A CA    1 
ATOM   2632  C  C     . THR A 1 352 ? 139.821 156.492 81.566  1.00 70.52  ? 352  THR A C     1 
ATOM   2633  O  O     . THR A 1 352 ? 138.689 156.492 81.074  1.00 76.78  ? 352  THR A O     1 
ATOM   2634  C  CB    . THR A 1 352 ? 141.414 158.040 80.407  1.00 75.04  ? 352  THR A CB    1 
ATOM   2635  O  OG1   . THR A 1 352 ? 140.287 158.712 79.835  1.00 74.77  ? 352  THR A OG1   1 
ATOM   2636  C  CG2   . THR A 1 352 ? 142.586 158.132 79.444  1.00 75.51  ? 352  THR A CG2   1 
ATOM   2637  N  N     . VAL A 1 353 ? 140.041 156.414 82.874  1.00 69.74  ? 353  VAL A N     1 
ATOM   2638  C  CA    . VAL A 1 353 ? 138.969 156.278 83.853  1.00 72.94  ? 353  VAL A CA    1 
ATOM   2639  C  C     . VAL A 1 353 ? 138.997 157.493 84.767  1.00 74.21  ? 353  VAL A C     1 
ATOM   2640  O  O     . VAL A 1 353 ? 140.050 157.843 85.308  1.00 74.75  ? 353  VAL A O     1 
ATOM   2641  C  CB    . VAL A 1 353 ? 139.104 154.976 84.662  1.00 70.76  ? 353  VAL A CB    1 
ATOM   2642  C  CG1   . VAL A 1 353 ? 138.070 154.923 85.770  1.00 70.25  ? 353  VAL A CG1   1 
ATOM   2643  C  CG2   . VAL A 1 353 ? 138.956 153.787 83.749  1.00 67.35  ? 353  VAL A CG2   1 
ATOM   2644  N  N     . VAL A 1 354 ? 137.843 158.132 84.936  1.00 75.16  ? 354  VAL A N     1 
ATOM   2645  C  CA    . VAL A 1 354 ? 137.724 159.362 85.707  1.00 75.25  ? 354  VAL A CA    1 
ATOM   2646  C  C     . VAL A 1 354 ? 136.860 159.095 86.931  1.00 77.78  ? 354  VAL A C     1 
ATOM   2647  O  O     . VAL A 1 354 ? 135.807 158.457 86.834  1.00 79.77  ? 354  VAL A O     1 
ATOM   2648  C  CB    . VAL A 1 354 ? 137.140 160.506 84.854  1.00 75.41  ? 354  VAL A CB    1 
ATOM   2649  C  CG1   . VAL A 1 354 ? 137.126 161.801 85.637  1.00 78.20  ? 354  VAL A CG1   1 
ATOM   2650  C  CG2   . VAL A 1 354 ? 137.945 160.669 83.584  1.00 75.77  ? 354  VAL A CG2   1 
ATOM   2651  N  N     . TYR A 1 355 ? 137.313 159.584 88.084  1.00 76.01  ? 355  TYR A N     1 
ATOM   2652  C  CA    . TYR A 1 355 ? 136.658 159.326 89.357  1.00 74.61  ? 355  TYR A CA    1 
ATOM   2653  C  C     . TYR A 1 355 ? 136.732 160.573 90.225  1.00 78.46  ? 355  TYR A C     1 
ATOM   2654  O  O     . TYR A 1 355 ? 137.736 161.291 90.209  1.00 78.93  ? 355  TYR A O     1 
ATOM   2655  C  CB    . TYR A 1 355 ? 137.312 158.131 90.062  1.00 75.50  ? 355  TYR A CB    1 
ATOM   2656  C  CG    . TYR A 1 355 ? 136.658 157.718 91.357  1.00 76.05  ? 355  TYR A CG    1 
ATOM   2657  C  CD1   . TYR A 1 355 ? 135.280 157.704 91.490  1.00 74.72  ? 355  TYR A CD1   1 
ATOM   2658  C  CD2   . TYR A 1 355 ? 137.425 157.318 92.441  1.00 76.49  ? 355  TYR A CD2   1 
ATOM   2659  C  CE1   . TYR A 1 355 ? 134.684 157.320 92.669  1.00 75.90  ? 355  TYR A CE1   1 
ATOM   2660  C  CE2   . TYR A 1 355 ? 136.838 156.930 93.624  1.00 75.91  ? 355  TYR A CE2   1 
ATOM   2661  C  CZ    . TYR A 1 355 ? 135.467 156.933 93.732  1.00 77.08  ? 355  TYR A CZ    1 
ATOM   2662  O  OH    . TYR A 1 355 ? 134.875 156.548 94.911  1.00 78.61  ? 355  TYR A OH    1 
ATOM   2663  N  N     . ARG A 1 356 ? 135.663 160.827 90.983  1.00 84.76  ? 356  ARG A N     1 
ATOM   2664  C  CA    . ARG A 1 356 ? 135.604 162.028 91.810  1.00 82.83  ? 356  ARG A CA    1 
ATOM   2665  C  C     . ARG A 1 356 ? 136.545 161.958 93.005  1.00 83.59  ? 356  ARG A C     1 
ATOM   2666  O  O     . ARG A 1 356 ? 137.080 162.990 93.425  1.00 86.72  ? 356  ARG A O     1 
ATOM   2667  C  CB    . ARG A 1 356 ? 134.176 162.266 92.299  1.00 84.12  ? 356  ARG A CB    1 
ATOM   2668  C  CG    . ARG A 1 356 ? 133.253 162.883 91.273  1.00 86.06  ? 356  ARG A CG    1 
ATOM   2669  C  CD    . ARG A 1 356 ? 132.057 163.518 91.952  1.00 86.70  ? 356  ARG A CD    1 
ATOM   2670  N  NE    . ARG A 1 356 ? 131.300 164.371 91.045  1.00 86.71  ? 356  ARG A NE    1 
ATOM   2671  C  CZ    . ARG A 1 356 ? 130.293 163.953 90.290  1.00 86.14  ? 356  ARG A CZ    1 
ATOM   2672  N  NH1   . ARG A 1 356 ? 129.896 162.692 90.304  1.00 85.32  ? 356  ARG A NH1   1 
ATOM   2673  N  NH2   . ARG A 1 356 ? 129.670 164.823 89.500  1.00 86.24  ? 356  ARG A NH2   1 
ATOM   2674  N  N     . ARG A 1 357 ? 136.751 160.777 93.572  1.00 87.56  ? 357  ARG A N     1 
ATOM   2675  C  CA    . ARG A 1 357 ? 137.450 160.633 94.838  1.00 87.38  ? 357  ARG A CA    1 
ATOM   2676  C  C     . ARG A 1 357 ? 138.849 160.057 94.622  1.00 89.26  ? 357  ARG A C     1 
ATOM   2677  O  O     . ARG A 1 357 ? 139.305 159.875 93.488  1.00 91.19  ? 357  ARG A O     1 
ATOM   2678  C  CB    . ARG A 1 357 ? 136.613 159.777 95.787  1.00 87.36  ? 357  ARG A CB    1 
ATOM   2679  C  CG    . ARG A 1 357 ? 135.216 160.324 96.000  1.00 89.41  ? 357  ARG A CG    1 
ATOM   2680  C  CD    . ARG A 1 357 ? 134.343 159.366 96.780  1.00 89.27  ? 357  ARG A CD    1 
ATOM   2681  N  NE    . ARG A 1 357 ? 132.963 159.831 96.837  1.00 91.15  ? 357  ARG A NE    1 
ATOM   2682  C  CZ    . ARG A 1 357 ? 131.964 159.150 97.379  1.00 91.81  ? 357  ARG A CZ    1 
ATOM   2683  N  NH1   . ARG A 1 357 ? 132.156 157.964 97.931  1.00 90.87  ? 357  ARG A NH1   1 
ATOM   2684  N  NH2   . ARG A 1 357 ? 130.741 159.672 97.364  1.00 90.53  ? 357  ARG A NH2   1 
ATOM   2685  N  N     . SER A 1 358 ? 139.537 159.778 95.726  1.00 86.71  ? 358  SER A N     1 
ATOM   2686  C  CA    . SER A 1 358 ? 140.921 159.327 95.689  1.00 87.38  ? 358  SER A CA    1 
ATOM   2687  C  C     . SER A 1 358 ? 140.981 157.832 95.380  1.00 89.31  ? 358  SER A C     1 
ATOM   2688  O  O     . SER A 1 358 ? 139.969 157.184 95.098  1.00 86.94  ? 358  SER A O     1 
ATOM   2689  C  CB    . SER A 1 358 ? 141.617 159.656 97.005  1.00 86.28  ? 358  SER A CB    1 
ATOM   2690  O  OG    . SER A 1 358 ? 140.977 159.008 98.089  1.00 86.23  ? 358  SER A OG    1 
ATOM   2691  N  N     . LYS A 1 359 ? 142.190 157.266 95.433  1.00 90.81  ? 359  LYS A N     1 
ATOM   2692  C  CA    . LYS A 1 359 ? 142.369 155.856 95.100  1.00 89.01  ? 359  LYS A CA    1 
ATOM   2693  C  C     . LYS A 1 359 ? 141.807 154.949 96.186  1.00 87.15  ? 359  LYS A C     1 
ATOM   2694  O  O     . LYS A 1 359 ? 141.147 153.948 95.886  1.00 86.48  ? 359  LYS A O     1 
ATOM   2695  C  CB    . LYS A 1 359 ? 143.850 155.557 94.873  1.00 88.64  ? 359  LYS A CB    1 
ATOM   2696  C  CG    . LYS A 1 359 ? 144.523 156.466 93.861  1.00 89.29  ? 359  LYS A CG    1 
ATOM   2697  C  CD    . LYS A 1 359 ? 145.964 156.049 93.619  1.00 87.90  ? 359  LYS A CD    1 
ATOM   2698  C  CE    . LYS A 1 359 ? 146.043 154.630 93.079  1.00 87.73  ? 359  LYS A CE    1 
ATOM   2699  N  NZ    . LYS A 1 359 ? 147.448 154.203 92.836  1.00 89.84  ? 359  LYS A NZ    1 
ATOM   2700  N  N     . SER A 1 360 ? 142.063 155.279 97.453  1.00 85.13  ? 360  SER A N     1 
ATOM   2701  C  CA    . SER A 1 360 ? 141.642 154.419 98.551  1.00 84.87  ? 360  SER A CA    1 
ATOM   2702  C  C     . SER A 1 360 ? 140.128 154.350 98.695  1.00 85.64  ? 360  SER A C     1 
ATOM   2703  O  O     . SER A 1 360 ? 139.614 153.359 99.223  1.00 86.69  ? 360  SER A O     1 
ATOM   2704  C  CB    . SER A 1 360 ? 142.267 154.898 99.860  1.00 86.87  ? 360  SER A CB    1 
ATOM   2705  O  OG    . SER A 1 360 ? 141.861 156.220 100.161 1.00 88.04  ? 360  SER A OG    1 
ATOM   2706  N  N     . GLU A 1 361 ? 139.406 155.369 98.240  1.00 85.22  ? 361  GLU A N     1 
ATOM   2707  C  CA    . GLU A 1 361 ? 137.955 155.395 98.336  1.00 84.25  ? 361  GLU A CA    1 
ATOM   2708  C  C     . GLU A 1 361 ? 137.281 154.757 97.132  1.00 85.33  ? 361  GLU A C     1 
ATOM   2709  O  O     . GLU A 1 361 ? 136.054 154.821 97.018  1.00 85.65  ? 361  GLU A O     1 
ATOM   2710  C  CB    . GLU A 1 361 ? 137.463 156.833 98.511  1.00 86.67  ? 361  GLU A CB    1 
ATOM   2711  C  CG    . GLU A 1 361 ? 137.971 157.503 99.778  1.00 85.97  ? 361  GLU A CG    1 
ATOM   2712  C  CD    . GLU A 1 361 ? 137.455 158.919 99.942  1.00 86.72  ? 361  GLU A CD    1 
ATOM   2713  O  OE1   . GLU A 1 361 ? 136.757 159.410 99.030  1.00 86.68  ? 361  GLU A OE1   1 
ATOM   2714  O  OE2   . GLU A 1 361 ? 137.746 159.541 100.984 1.00 87.96  ? 361  GLU A OE2   1 
ATOM   2715  N  N     . MET A 1 362 ? 138.051 154.151 96.241  1.00 78.80  ? 362  MET A N     1 
ATOM   2716  C  CA    . MET A 1 362 ? 137.494 153.533 95.047  1.00 72.65  ? 362  MET A CA    1 
ATOM   2717  C  C     . MET A 1 362 ? 136.691 152.300 95.433  1.00 70.75  ? 362  MET A C     1 
ATOM   2718  O  O     . MET A 1 362 ? 137.251 151.369 96.024  1.00 71.59  ? 362  MET A O     1 
ATOM   2719  C  CB    . MET A 1 362 ? 138.615 153.159 94.085  1.00 70.03  ? 362  MET A CB    1 
ATOM   2720  C  CG    . MET A 1 362 ? 138.204 153.135 92.632  1.00 70.82  ? 362  MET A CG    1 
ATOM   2721  S  SD    . MET A 1 362 ? 139.575 152.767 91.528  1.00 76.22  ? 362  MET A SD    1 
ATOM   2722  C  CE    . MET A 1 362 ? 138.814 153.098 89.945  1.00 71.32  ? 362  MET A CE    1 
ATOM   2723  N  N     . PRO A 1 363 ? 135.393 152.242 95.120  1.00 59.90  ? 363  PRO A N     1 
ATOM   2724  C  CA    . PRO A 1 363 ? 134.599 151.057 95.478  1.00 62.13  ? 363  PRO A CA    1 
ATOM   2725  C  C     . PRO A 1 363 ? 134.963 149.818 94.684  1.00 63.92  ? 363  PRO A C     1 
ATOM   2726  O  O     . PRO A 1 363 ? 134.447 148.736 94.990  1.00 60.18  ? 363  PRO A O     1 
ATOM   2727  C  CB    . PRO A 1 363 ? 133.158 151.495 95.178  1.00 60.64  ? 363  PRO A CB    1 
ATOM   2728  C  CG    . PRO A 1 363 ? 133.213 152.989 95.067  1.00 61.71  ? 363  PRO A CG    1 
ATOM   2729  C  CD    . PRO A 1 363 ? 134.564 153.298 94.524  1.00 60.69  ? 363  PRO A CD    1 
ATOM   2730  N  N     . ALA A 1 364 ? 135.821 149.942 93.680  1.00 61.67  ? 364  ALA A N     1 
ATOM   2731  C  CA    . ALA A 1 364 ? 136.164 148.822 92.826  1.00 53.65  ? 364  ALA A CA    1 
ATOM   2732  C  C     . ALA A 1 364 ? 137.034 147.812 93.565  1.00 53.78  ? 364  ALA A C     1 
ATOM   2733  O  O     . ALA A 1 364 ? 137.693 148.122 94.561  1.00 55.79  ? 364  ALA A O     1 
ATOM   2734  C  CB    . ALA A 1 364 ? 136.891 149.309 91.579  1.00 53.09  ? 364  ALA A CB    1 
ATOM   2735  N  N     . ASN A 1 365 ? 137.015 146.582 93.060  1.00 51.85  ? 365  ASN A N     1 
ATOM   2736  C  CA    . ASN A 1 365 ? 137.892 145.539 93.567  1.00 48.35  ? 365  ASN A CA    1 
ATOM   2737  C  C     . ASN A 1 365 ? 139.346 145.944 93.361  1.00 52.08  ? 365  ASN A C     1 
ATOM   2738  O  O     . ASN A 1 365 ? 139.738 146.353 92.265  1.00 58.92  ? 365  ASN A O     1 
ATOM   2739  C  CB    . ASN A 1 365 ? 137.586 144.229 92.846  1.00 44.12  ? 365  ASN A CB    1 
ATOM   2740  C  CG    . ASN A 1 365 ? 137.931 143.014 93.666  1.00 52.58  ? 365  ASN A CG    1 
ATOM   2741  O  OD1   . ASN A 1 365 ? 138.778 143.068 94.556  1.00 55.59  ? 365  ASN A OD1   1 
ATOM   2742  N  ND2   . ASN A 1 365 ? 137.274 141.900 93.367  1.00 55.12  ? 365  ASN A ND2   1 
ATOM   2743  N  N     . SER A 1 366 ? 140.148 145.836 94.423  1.00 43.62  ? 366  SER A N     1 
ATOM   2744  C  CA    . SER A 1 366 ? 141.495 146.401 94.394  1.00 43.56  ? 366  SER A CA    1 
ATOM   2745  C  C     . SER A 1 366 ? 142.420 145.612 93.476  1.00 45.30  ? 366  SER A C     1 
ATOM   2746  O  O     . SER A 1 366 ? 143.244 146.199 92.761  1.00 50.32  ? 366  SER A O     1 
ATOM   2747  C  CB    . SER A 1 366 ? 142.068 146.462 95.809  1.00 51.22  ? 366  SER A CB    1 
ATOM   2748  O  OG    . SER A 1 366 ? 142.154 145.170 96.377  1.00 52.31  ? 366  SER A OG    1 
ATOM   2749  N  N     . ARG A 1 367 ? 142.305 144.282 93.483  1.00 42.44  ? 367  ARG A N     1 
ATOM   2750  C  CA    . ARG A 1 367 ? 143.144 143.478 92.603  1.00 43.54  ? 367  ARG A CA    1 
ATOM   2751  C  C     . ARG A 1 367 ? 142.831 143.747 91.140  1.00 45.94  ? 367  ARG A C     1 
ATOM   2752  O  O     . ARG A 1 367 ? 143.730 143.700 90.297  1.00 49.93  ? 367  ARG A O     1 
ATOM   2753  C  CB    . ARG A 1 367 ? 142.989 141.991 92.923  1.00 42.16  ? 367  ARG A CB    1 
ATOM   2754  C  CG    . ARG A 1 367 ? 141.564 141.497 92.999  1.00 42.98  ? 367  ARG A CG    1 
ATOM   2755  C  CD    . ARG A 1 367 ? 141.535 140.012 93.305  1.00 43.76  ? 367  ARG A CD    1 
ATOM   2756  N  NE    . ARG A 1 367 ? 140.235 139.583 93.805  1.00 46.14  ? 367  ARG A NE    1 
ATOM   2757  C  CZ    . ARG A 1 367 ? 139.262 139.105 93.045  1.00 43.30  ? 367  ARG A CZ    1 
ATOM   2758  N  NH1   . ARG A 1 367 ? 139.407 138.973 91.738  1.00 38.58  ? 367  ARG A NH1   1 
ATOM   2759  N  NH2   . ARG A 1 367 ? 138.112 138.752 93.611  1.00 40.68  ? 367  ARG A NH2   1 
ATOM   2760  N  N     . GLU A 1 368 ? 141.573 144.052 90.820  1.00 51.19  ? 368  GLU A N     1 
ATOM   2761  C  CA    . GLU A 1 368 ? 141.235 144.400 89.445  1.00 48.74  ? 368  GLU A CA    1 
ATOM   2762  C  C     . GLU A 1 368 ? 141.834 145.744 89.053  1.00 49.78  ? 368  GLU A C     1 
ATOM   2763  O  O     . GLU A 1 368 ? 142.250 145.929 87.905  1.00 61.01  ? 368  GLU A O     1 
ATOM   2764  C  CB    . GLU A 1 368 ? 139.721 144.403 89.267  1.00 50.16  ? 368  GLU A CB    1 
ATOM   2765  C  CG    . GLU A 1 368 ? 139.072 143.124 89.746  1.00 57.42  ? 368  GLU A CG    1 
ATOM   2766  C  CD    . GLU A 1 368 ? 139.635 141.890 89.073  1.00 58.73  ? 368  GLU A CD    1 
ATOM   2767  O  OE1   . GLU A 1 368 ? 139.907 141.941 87.857  1.00 59.03  ? 368  GLU A OE1   1 
ATOM   2768  O  OE2   . GLU A 1 368 ? 139.808 140.865 89.761  1.00 54.99  ? 368  GLU A OE2   1 
ATOM   2769  N  N     . VAL A 1 369 ? 141.904 146.687 89.995  1.00 52.06  ? 369  VAL A N     1 
ATOM   2770  C  CA    . VAL A 1 369 ? 142.575 147.959 89.734  1.00 53.98  ? 369  VAL A CA    1 
ATOM   2771  C  C     . VAL A 1 369 ? 144.059 147.737 89.465  1.00 57.46  ? 369  VAL A C     1 
ATOM   2772  O  O     . VAL A 1 369 ? 144.631 148.310 88.527  1.00 61.00  ? 369  VAL A O     1 
ATOM   2773  C  CB    . VAL A 1 369 ? 142.349 148.928 90.909  1.00 53.89  ? 369  VAL A CB    1 
ATOM   2774  C  CG1   . VAL A 1 369 ? 143.115 150.220 90.692  1.00 54.71  ? 369  VAL A CG1   1 
ATOM   2775  C  CG2   . VAL A 1 369 ? 140.869 149.205 91.080  1.00 54.99  ? 369  VAL A CG2   1 
ATOM   2776  N  N     . GLU A 1 370 ? 144.704 146.897 90.279  1.00 58.11  ? 370  GLU A N     1 
ATOM   2777  C  CA    . GLU A 1 370 ? 146.117 146.598 90.060  1.00 58.15  ? 370  GLU A CA    1 
ATOM   2778  C  C     . GLU A 1 370 ? 146.340 145.899 88.721  1.00 59.65  ? 370  GLU A C     1 
ATOM   2779  O  O     . GLU A 1 370 ? 147.284 146.227 87.989  1.00 61.68  ? 370  GLU A O     1 
ATOM   2780  C  CB    . GLU A 1 370 ? 146.654 145.750 91.213  1.00 60.49  ? 370  GLU A CB    1 
ATOM   2781  C  CG    . GLU A 1 370 ? 147.898 144.934 90.881  1.00 63.79  ? 370  GLU A CG    1 
ATOM   2782  C  CD    . GLU A 1 370 ? 149.112 145.790 90.575  1.00 62.76  ? 370  GLU A CD    1 
ATOM   2783  O  OE1   . GLU A 1 370 ? 149.155 146.956 91.021  1.00 60.82  ? 370  GLU A OE1   1 
ATOM   2784  O  OE2   . GLU A 1 370 ? 150.027 145.293 89.888  1.00 58.45  ? 370  GLU A OE2   1 
ATOM   2785  N  N     . GLU A 1 371 ? 145.474 144.941 88.380  1.00 58.80  ? 371  GLU A N     1 
ATOM   2786  C  CA    . GLU A 1 371 ? 145.587 144.255 87.097  1.00 57.71  ? 371  GLU A CA    1 
ATOM   2787  C  C     . GLU A 1 371 ? 145.397 145.218 85.935  1.00 62.81  ? 371  GLU A C     1 
ATOM   2788  O  O     . GLU A 1 371 ? 146.105 145.127 84.927  1.00 70.53  ? 371  GLU A O     1 
ATOM   2789  C  CB    . GLU A 1 371 ? 144.571 143.118 87.010  1.00 58.58  ? 371  GLU A CB    1 
ATOM   2790  C  CG    . GLU A 1 371 ? 144.904 141.913 87.861  1.00 64.47  ? 371  GLU A CG    1 
ATOM   2791  C  CD    . GLU A 1 371 ? 143.922 140.779 87.660  1.00 64.38  ? 371  GLU A CD    1 
ATOM   2792  O  OE1   . GLU A 1 371 ? 143.080 140.879 86.745  1.00 60.13  ? 371  GLU A OE1   1 
ATOM   2793  O  OE2   . GLU A 1 371 ? 143.991 139.788 88.416  1.00 66.54  ? 371  GLU A OE2   1 
ATOM   2794  N  N     . ALA A 1 372 ? 144.440 146.141 86.052  1.00 57.35  ? 372  ALA A N     1 
ATOM   2795  C  CA    . ALA A 1 372 ? 144.230 147.125 84.997  1.00 56.74  ? 372  ALA A CA    1 
ATOM   2796  C  C     . ALA A 1 372 ? 145.440 148.032 84.847  1.00 56.88  ? 372  ALA A C     1 
ATOM   2797  O  O     . ALA A 1 372 ? 145.789 148.432 83.730  1.00 61.83  ? 372  ALA A O     1 
ATOM   2798  C  CB    . ALA A 1 372 ? 142.978 147.949 85.283  1.00 59.50  ? 372  ALA A CB    1 
ATOM   2799  N  N     . GLU A 1 373 ? 146.085 148.378 85.963  1.00 61.51  ? 373  GLU A N     1 
ATOM   2800  C  CA    . GLU A 1 373 ? 147.347 149.103 85.877  1.00 66.87  ? 373  GLU A CA    1 
ATOM   2801  C  C     . GLU A 1 373 ? 148.396 148.284 85.138  1.00 67.42  ? 373  GLU A C     1 
ATOM   2802  O  O     . GLU A 1 373 ? 149.189 148.830 84.364  1.00 65.18  ? 373  GLU A O     1 
ATOM   2803  C  CB    . GLU A 1 373 ? 147.842 149.478 87.273  1.00 67.72  ? 373  GLU A CB    1 
ATOM   2804  C  CG    . GLU A 1 373 ? 147.070 150.609 87.930  1.00 66.80  ? 373  GLU A CG    1 
ATOM   2805  C  CD    . GLU A 1 373 ? 147.498 151.978 87.440  1.00 67.68  ? 373  GLU A CD    1 
ATOM   2806  O  OE1   . GLU A 1 373 ? 148.348 152.055 86.530  1.00 67.74  ? 373  GLU A OE1   1 
ATOM   2807  O  OE2   . GLU A 1 373 ? 146.989 152.984 87.975  1.00 68.46  ? 373  GLU A OE2   1 
ATOM   2808  N  N     . GLU A 1 374 ? 148.414 146.968 85.366  1.00 69.70  ? 374  GLU A N     1 
ATOM   2809  C  CA    . GLU A 1 374 ? 149.334 146.103 84.633  1.00 67.34  ? 374  GLU A CA    1 
ATOM   2810  C  C     . GLU A 1 374 ? 148.994 146.031 83.149  1.00 66.57  ? 374  GLU A C     1 
ATOM   2811  O  O     . GLU A 1 374 ? 149.897 145.920 82.313  1.00 66.33  ? 374  GLU A O     1 
ATOM   2812  C  CB    . GLU A 1 374 ? 149.330 144.698 85.232  1.00 65.84  ? 374  GLU A CB    1 
ATOM   2813  C  CG    . GLU A 1 374 ? 149.868 144.615 86.641  1.00 67.16  ? 374  GLU A CG    1 
ATOM   2814  C  CD    . GLU A 1 374 ? 149.868 143.198 87.171  1.00 70.15  ? 374  GLU A CD    1 
ATOM   2815  O  OE1   . GLU A 1 374 ? 149.289 142.316 86.504  1.00 71.77  ? 374  GLU A OE1   1 
ATOM   2816  O  OE2   . GLU A 1 374 ? 150.448 142.964 88.251  1.00 70.80  ? 374  GLU A OE2   1 
ATOM   2817  N  N     . GLU A 1 375 ? 147.708 146.074 82.802  1.00 65.20  ? 375  GLU A N     1 
ATOM   2818  C  CA    . GLU A 1 375 ? 147.297 145.957 81.410  1.00 67.52  ? 375  GLU A CA    1 
ATOM   2819  C  C     . GLU A 1 375 ? 147.384 147.269 80.643  1.00 67.69  ? 375  GLU A C     1 
ATOM   2820  O  O     . GLU A 1 375 ? 147.331 147.247 79.410  1.00 64.14  ? 375  GLU A O     1 
ATOM   2821  C  CB    . GLU A 1 375 ? 145.871 145.415 81.329  1.00 66.08  ? 375  GLU A CB    1 
ATOM   2822  C  CG    . GLU A 1 375 ? 145.690 144.061 81.972  1.00 62.90  ? 375  GLU A CG    1 
ATOM   2823  C  CD    . GLU A 1 375 ? 144.251 143.604 81.951  1.00 66.39  ? 375  GLU A CD    1 
ATOM   2824  O  OE1   . GLU A 1 375 ? 143.547 143.906 80.968  1.00 67.19  ? 375  GLU A OE1   1 
ATOM   2825  O  OE2   . GLU A 1 375 ? 143.821 142.949 82.921  1.00 67.02  ? 375  GLU A OE2   1 
ATOM   2826  N  N     . GLY A 1 376 ? 147.519 148.401 81.326  1.00 69.71  ? 376  GLY A N     1 
ATOM   2827  C  CA    . GLY A 1 376 ? 147.682 149.666 80.638  1.00 66.99  ? 376  GLY A CA    1 
ATOM   2828  C  C     . GLY A 1 376 ? 146.434 150.522 80.593  1.00 69.73  ? 376  GLY A C     1 
ATOM   2829  O  O     . GLY A 1 376 ? 146.099 151.086 79.548  1.00 73.60  ? 376  GLY A O     1 
ATOM   2830  N  N     . VAL A 1 377 ? 145.732 150.622 81.715  1.00 70.14  ? 377  VAL A N     1 
ATOM   2831  C  CA    . VAL A 1 377 ? 144.563 151.483 81.838  1.00 68.82  ? 377  VAL A CA    1 
ATOM   2832  C  C     . VAL A 1 377 ? 144.972 152.732 82.602  1.00 68.77  ? 377  VAL A C     1 
ATOM   2833  O  O     . VAL A 1 377 ? 145.503 152.643 83.715  1.00 71.20  ? 377  VAL A O     1 
ATOM   2834  C  CB    . VAL A 1 377 ? 143.404 150.758 82.541  1.00 67.08  ? 377  VAL A CB    1 
ATOM   2835  C  CG1   . VAL A 1 377 ? 142.266 151.722 82.804  1.00 66.53  ? 377  VAL A CG1   1 
ATOM   2836  C  CG2   . VAL A 1 377 ? 142.924 149.592 81.700  1.00 67.48  ? 377  VAL A CG2   1 
ATOM   2837  N  N     . LYS A 1 378 ? 144.736 153.894 82.002  1.00 64.64  ? 378  LYS A N     1 
ATOM   2838  C  CA    . LYS A 1 378 ? 145.095 155.166 82.612  1.00 63.90  ? 378  LYS A CA    1 
ATOM   2839  C  C     . LYS A 1 378 ? 143.985 155.608 83.554  1.00 66.19  ? 378  LYS A C     1 
ATOM   2840  O  O     . LYS A 1 378 ? 142.808 155.605 83.183  1.00 67.78  ? 378  LYS A O     1 
ATOM   2841  C  CB    . LYS A 1 378 ? 145.346 156.232 81.545  1.00 63.21  ? 378  LYS A CB    1 
ATOM   2842  C  CG    . LYS A 1 378 ? 146.585 155.995 80.695  1.00 66.38  ? 378  LYS A CG    1 
ATOM   2843  C  CD    . LYS A 1 378 ? 146.296 155.103 79.500  1.00 67.14  ? 378  LYS A CD    1 
ATOM   2844  C  CE    . LYS A 1 378 ? 147.552 154.841 78.694  1.00 67.18  ? 378  LYS A CE    1 
ATOM   2845  N  NZ    . LYS A 1 378 ? 147.270 153.970 77.521  1.00 64.23  ? 378  LYS A NZ    1 
ATOM   2846  N  N     . PHE A 1 379 ? 144.360 155.983 84.770  1.00 68.76  ? 379  PHE A N     1 
ATOM   2847  C  CA    . PHE A 1 379 ? 143.403 156.358 85.799  1.00 68.36  ? 379  PHE A CA    1 
ATOM   2848  C  C     . PHE A 1 379 ? 143.506 157.844 86.096  1.00 68.45  ? 379  PHE A C     1 
ATOM   2849  O  O     . PHE A 1 379 ? 144.597 158.358 86.356  1.00 70.15  ? 379  PHE A O     1 
ATOM   2850  C  CB    . PHE A 1 379 ? 143.634 155.561 87.081  1.00 70.81  ? 379  PHE A CB    1 
ATOM   2851  C  CG    . PHE A 1 379 ? 143.242 154.128 86.975  1.00 70.32  ? 379  PHE A CG    1 
ATOM   2852  C  CD1   . PHE A 1 379 ? 141.947 153.733 87.243  1.00 68.66  ? 379  PHE A CD1   1 
ATOM   2853  C  CD2   . PHE A 1 379 ? 144.168 153.172 86.610  1.00 69.70  ? 379  PHE A CD2   1 
ATOM   2854  C  CE1   . PHE A 1 379 ? 141.588 152.412 87.147  1.00 69.94  ? 379  PHE A CE1   1 
ATOM   2855  C  CE2   . PHE A 1 379 ? 143.811 151.851 86.513  1.00 68.37  ? 379  PHE A CE2   1 
ATOM   2856  C  CZ    . PHE A 1 379 ? 142.522 151.472 86.781  1.00 68.47  ? 379  PHE A CZ    1 
ATOM   2857  N  N     . MET A 1 380 ? 142.367 158.521 86.057  1.00 74.90  ? 380  MET A N     1 
ATOM   2858  C  CA    . MET A 1 380 ? 142.238 159.890 86.528  1.00 76.92  ? 380  MET A CA    1 
ATOM   2859  C  C     . MET A 1 380 ? 141.403 159.863 87.800  1.00 79.13  ? 380  MET A C     1 
ATOM   2860  O  O     . MET A 1 380 ? 140.232 159.472 87.768  1.00 78.04  ? 380  MET A O     1 
ATOM   2861  C  CB    . MET A 1 380 ? 141.581 160.776 85.470  1.00 77.26  ? 380  MET A CB    1 
ATOM   2862  C  CG    . MET A 1 380 ? 142.193 160.666 84.086  1.00 76.90  ? 380  MET A CG    1 
ATOM   2863  S  SD    . MET A 1 380 ? 143.794 161.474 83.971  1.00 78.69  ? 380  MET A SD    1 
ATOM   2864  C  CE    . MET A 1 380 ? 143.345 163.149 84.412  1.00 77.16  ? 380  MET A CE    1 
ATOM   2865  N  N     . PHE A 1 381 ? 142.003 160.262 88.913  1.00 87.93  ? 381  PHE A N     1 
ATOM   2866  C  CA    . PHE A 1 381 ? 141.294 160.376 90.176  1.00 86.66  ? 381  PHE A CA    1 
ATOM   2867  C  C     . PHE A 1 381 ? 141.183 161.841 90.571  1.00 88.47  ? 381  PHE A C     1 
ATOM   2868  O  O     . PHE A 1 381 ? 142.001 162.672 90.164  1.00 88.93  ? 381  PHE A O     1 
ATOM   2869  C  CB    . PHE A 1 381 ? 141.995 159.587 91.281  1.00 87.28  ? 381  PHE A CB    1 
ATOM   2870  C  CG    . PHE A 1 381 ? 141.945 158.103 91.086  1.00 87.65  ? 381  PHE A CG    1 
ATOM   2871  C  CD1   . PHE A 1 381 ? 140.759 157.414 91.246  1.00 84.77  ? 381  PHE A CD1   1 
ATOM   2872  C  CD2   . PHE A 1 381 ? 143.084 157.396 90.751  1.00 87.56  ? 381  PHE A CD2   1 
ATOM   2873  C  CE1   . PHE A 1 381 ? 140.709 156.053 91.071  1.00 85.94  ? 381  PHE A CE1   1 
ATOM   2874  C  CE2   . PHE A 1 381 ? 143.039 156.033 90.575  1.00 86.61  ? 381  PHE A CE2   1 
ATOM   2875  C  CZ    . PHE A 1 381 ? 141.850 155.360 90.734  1.00 87.08  ? 381  PHE A CZ    1 
ATOM   2876  N  N     . LEU A 1 382 ? 140.153 162.144 91.362  1.00 90.14  ? 382  LEU A N     1 
ATOM   2877  C  CA    . LEU A 1 382 ? 139.852 163.509 91.796  1.00 93.20  ? 382  LEU A CA    1 
ATOM   2878  C  C     . LEU A 1 382 ? 139.624 164.437 90.601  1.00 92.86  ? 382  LEU A C     1 
ATOM   2879  O  O     . LEU A 1 382 ? 140.192 165.526 90.511  1.00 93.24  ? 382  LEU A O     1 
ATOM   2880  C  CB    . LEU A 1 382 ? 140.952 164.051 92.714  1.00 92.82  ? 382  LEU A CB    1 
ATOM   2881  C  CG    . LEU A 1 382 ? 141.164 163.309 94.032  1.00 91.91  ? 382  LEU A CG    1 
ATOM   2882  C  CD1   . LEU A 1 382 ? 142.407 163.822 94.734  1.00 91.25  ? 382  LEU A CD1   1 
ATOM   2883  C  CD2   . LEU A 1 382 ? 139.951 163.463 94.928  1.00 92.74  ? 382  LEU A CD2   1 
ATOM   2884  N  N     . THR A 1 383 ? 138.782 163.988 89.671  1.00 89.79  ? 383  THR A N     1 
ATOM   2885  C  CA    . THR A 1 383 ? 138.376 164.798 88.530  1.00 89.71  ? 383  THR A CA    1 
ATOM   2886  C  C     . THR A 1 383 ? 136.957 164.400 88.143  1.00 90.85  ? 383  THR A C     1 
ATOM   2887  O  O     . THR A 1 383 ? 136.503 163.296 88.453  1.00 91.96  ? 383  THR A O     1 
ATOM   2888  C  CB    . THR A 1 383 ? 139.329 164.625 87.339  1.00 89.01  ? 383  THR A CB    1 
ATOM   2889  O  OG1   . THR A 1 383 ? 140.651 164.334 87.811  1.00 87.25  ? 383  THR A OG1   1 
ATOM   2890  C  CG2   . THR A 1 383 ? 139.378 165.897 86.512  1.00 91.70  ? 383  THR A CG2   1 
ATOM   2891  N  N     . ASN A 1 384 ? 136.252 165.308 87.467  1.00 97.36  ? 384  ASN A N     1 
ATOM   2892  C  CA    . ASN A 1 384 ? 134.881 165.030 87.055  1.00 98.79  ? 384  ASN A CA    1 
ATOM   2893  C  C     . ASN A 1 384 ? 134.523 165.881 85.847  1.00 100.27 ? 384  ASN A C     1 
ATOM   2894  O  O     . ASN A 1 384 ? 135.000 167.015 85.727  1.00 100.78 ? 384  ASN A O     1 
ATOM   2895  C  CB    . ASN A 1 384 ? 133.885 165.291 88.193  1.00 98.18  ? 384  ASN A CB    1 
ATOM   2896  C  CG    . ASN A 1 384 ? 133.515 166.751 88.319  1.00 99.54  ? 384  ASN A CG    1 
ATOM   2897  O  OD1   . ASN A 1 384 ? 134.273 167.548 88.865  1.00 99.35  ? 384  ASN A OD1   1 
ATOM   2898  N  ND2   . ASN A 1 384 ? 132.342 167.110 87.814  1.00 100.70 ? 384  ASN A ND2   1 
ATOM   2899  N  N     . PRO A 1 385 ? 133.685 165.372 84.946  1.00 99.58  ? 385  PRO A N     1 
ATOM   2900  C  CA    . PRO A 1 385 ? 133.325 166.136 83.745  1.00 98.80  ? 385  PRO A CA    1 
ATOM   2901  C  C     . PRO A 1 385 ? 132.372 167.286 84.028  1.00 96.61  ? 385  PRO A C     1 
ATOM   2902  O  O     . PRO A 1 385 ? 131.569 167.255 84.963  1.00 96.47  ? 385  PRO A O     1 
ATOM   2903  C  CB    . PRO A 1 385 ? 132.658 165.085 82.847  1.00 96.25  ? 385  PRO A CB    1 
ATOM   2904  C  CG    . PRO A 1 385 ? 133.089 163.764 83.406  1.00 94.09  ? 385  PRO A CG    1 
ATOM   2905  C  CD    . PRO A 1 385 ? 133.196 163.987 84.875  1.00 93.79  ? 385  PRO A CD    1 
ATOM   2906  N  N     . VAL A 1 386 ? 132.465 168.310 83.181  1.00 99.46  ? 386  VAL A N     1 
ATOM   2907  C  CA    . VAL A 1 386 ? 131.654 169.516 83.291  1.00 101.13 ? 386  VAL A CA    1 
ATOM   2908  C  C     . VAL A 1 386 ? 130.703 169.655 82.110  1.00 101.91 ? 386  VAL A C     1 
ATOM   2909  O  O     . VAL A 1 386 ? 129.517 169.932 82.288  1.00 103.62 ? 386  VAL A O     1 
ATOM   2910  C  CB    . VAL A 1 386 ? 132.543 170.772 83.428  1.00 102.05 ? 386  VAL A CB    1 
ATOM   2911  C  CG1   . VAL A 1 386 ? 131.696 171.982 83.783  1.00 101.42 ? 386  VAL A CG1   1 
ATOM   2912  C  CG2   . VAL A 1 386 ? 133.627 170.547 84.458  1.00 101.72 ? 386  VAL A CG2   1 
ATOM   2913  N  N     . LYS A 1 387 ? 131.215 169.500 80.891  1.00 102.47 ? 387  LYS A N     1 
ATOM   2914  C  CA    . LYS A 1 387 ? 130.369 169.494 79.706  1.00 102.17 ? 387  LYS A CA    1 
ATOM   2915  C  C     . LYS A 1 387 ? 131.096 168.751 78.597  1.00 101.88 ? 387  LYS A C     1 
ATOM   2916  O  O     . LYS A 1 387 ? 132.322 168.615 78.614  1.00 101.45 ? 387  LYS A O     1 
ATOM   2917  C  CB    . LYS A 1 387 ? 129.997 170.911 79.256  1.00 102.70 ? 387  LYS A CB    1 
ATOM   2918  C  CG    . LYS A 1 387 ? 130.977 171.540 78.286  1.00 103.13 ? 387  LYS A CG    1 
ATOM   2919  C  CD    . LYS A 1 387 ? 130.497 172.901 77.819  1.00 103.45 ? 387  LYS A CD    1 
ATOM   2920  C  CE    . LYS A 1 387 ? 129.170 172.793 77.089  1.00 103.42 ? 387  LYS A CE    1 
ATOM   2921  N  NZ    . LYS A 1 387 ? 128.684 174.120 76.621  1.00 103.40 ? 387  LYS A NZ    1 
ATOM   2922  N  N     . ILE A 1 388 ? 130.320 168.275 77.631  1.00 103.96 ? 388  ILE A N     1 
ATOM   2923  C  CA    . ILE A 1 388 ? 130.829 167.486 76.516  1.00 104.22 ? 388  ILE A CA    1 
ATOM   2924  C  C     . ILE A 1 388 ? 130.742 168.347 75.265  1.00 105.74 ? 388  ILE A C     1 
ATOM   2925  O  O     . ILE A 1 388 ? 129.646 168.736 74.844  1.00 104.76 ? 388  ILE A O     1 
ATOM   2926  C  CB    . ILE A 1 388 ? 130.048 166.175 76.358  1.00 102.85 ? 388  ILE A CB    1 
ATOM   2927  C  CG1   . ILE A 1 388 ? 130.068 165.402 77.677  1.00 102.58 ? 388  ILE A CG1   1 
ATOM   2928  C  CG2   . ILE A 1 388 ? 130.631 165.341 75.237  1.00 103.19 ? 388  ILE A CG2   1 
ATOM   2929  C  CD1   . ILE A 1 388 ? 129.220 164.161 77.675  1.00 103.87 ? 388  ILE A CD1   1 
ATOM   2930  N  N     . ILE A 1 389 ? 131.893 168.642 74.669  1.00 112.60 ? 389  ILE A N     1 
ATOM   2931  C  CA    . ILE A 1 389 ? 132.004 169.648 73.620  1.00 113.05 ? 389  ILE A CA    1 
ATOM   2932  C  C     . ILE A 1 389 ? 132.102 168.954 72.271  1.00 112.98 ? 389  ILE A C     1 
ATOM   2933  O  O     . ILE A 1 389 ? 132.879 168.007 72.103  1.00 112.19 ? 389  ILE A O     1 
ATOM   2934  C  CB    . ILE A 1 389 ? 133.216 170.568 73.853  1.00 113.17 ? 389  ILE A CB    1 
ATOM   2935  C  CG1   . ILE A 1 389 ? 133.155 171.211 75.240  1.00 112.67 ? 389  ILE A CG1   1 
ATOM   2936  C  CG2   . ILE A 1 389 ? 133.290 171.642 72.779  1.00 112.81 ? 389  ILE A CG2   1 
ATOM   2937  C  CD1   . ILE A 1 389 ? 134.032 170.533 76.273  1.00 112.35 ? 389  ILE A CD1   1 
ATOM   2938  N  N     . GLY A 1 390 ? 131.314 169.428 71.311  1.00 118.27 ? 390  GLY A N     1 
ATOM   2939  C  CA    . GLY A 1 390 ? 131.318 168.892 69.967  1.00 117.58 ? 390  GLY A CA    1 
ATOM   2940  C  C     . GLY A 1 390 ? 130.103 169.345 69.189  1.00 118.32 ? 390  GLY A C     1 
ATOM   2941  O  O     . GLY A 1 390 ? 129.061 169.641 69.780  1.00 118.13 ? 390  GLY A O     1 
ATOM   2942  N  N     . LYS A 1 391 ? 130.227 169.424 67.863  1.00 116.41 ? 391  LYS A N     1 
ATOM   2943  C  CA    . LYS A 1 391 ? 129.094 169.824 67.035  1.00 116.62 ? 391  LYS A CA    1 
ATOM   2944  C  C     . LYS A 1 391 ? 127.960 168.813 67.142  1.00 116.74 ? 391  LYS A C     1 
ATOM   2945  O  O     . LYS A 1 391 ? 126.870 169.126 67.635  1.00 116.60 ? 391  LYS A O     1 
ATOM   2946  C  CB    . LYS A 1 391 ? 129.544 169.984 65.582  1.00 116.32 ? 391  LYS A CB    1 
ATOM   2947  C  CG    . LYS A 1 391 ? 130.708 170.943 65.392  1.00 116.38 ? 391  LYS A CG    1 
ATOM   2948  C  CD    . LYS A 1 391 ? 131.151 170.990 63.939  1.00 115.51 ? 391  LYS A CD    1 
ATOM   2949  C  CE    . LYS A 1 391 ? 132.345 171.912 63.754  1.00 115.77 ? 391  LYS A CE    1 
ATOM   2950  N  NZ    . LYS A 1 391 ? 132.807 171.946 62.338  1.00 115.87 ? 391  LYS A NZ    1 
ATOM   2951  N  N     . GLU A 1 392 ? 128.202 167.599 66.694  1.00 122.70 ? 392  GLU A N     1 
ATOM   2952  C  CA    . GLU A 1 392 ? 127.243 166.508 66.809  1.00 122.68 ? 392  GLU A CA    1 
ATOM   2953  C  C     . GLU A 1 392 ? 127.845 165.277 67.464  1.00 122.09 ? 392  GLU A C     1 
ATOM   2954  O  O     . GLU A 1 392 ? 127.151 164.584 68.210  1.00 121.49 ? 392  GLU A O     1 
ATOM   2955  C  CB    . GLU A 1 392 ? 126.684 166.143 65.426  1.00 122.14 ? 392  GLU A CB    1 
ATOM   2956  C  CG    . GLU A 1 392 ? 125.889 167.256 64.767  1.00 122.14 ? 392  GLU A CG    1 
ATOM   2957  C  CD    . GLU A 1 392 ? 125.360 166.864 63.403  1.00 122.46 ? 392  GLU A CD    1 
ATOM   2958  O  OE1   . GLU A 1 392 ? 125.613 165.719 62.973  1.00 122.79 ? 392  GLU A OE1   1 
ATOM   2959  O  OE2   . GLU A 1 392 ? 124.692 167.700 62.760  1.00 121.88 ? 392  GLU A OE2   1 
ATOM   2960  N  N     . LYS A 1 393 ? 129.113 164.990 67.205  1.00 118.15 ? 393  LYS A N     1 
ATOM   2961  C  CA    . LYS A 1 393 ? 129.830 163.922 67.880  1.00 117.65 ? 393  LYS A CA    1 
ATOM   2962  C  C     . LYS A 1 393 ? 130.752 164.508 68.941  1.00 117.66 ? 393  LYS A C     1 
ATOM   2963  O  O     . LYS A 1 393 ? 131.110 165.687 68.904  1.00 117.96 ? 393  LYS A O     1 
ATOM   2964  C  CB    . LYS A 1 393 ? 130.637 163.088 66.882  1.00 116.18 ? 393  LYS A CB    1 
ATOM   2965  C  CG    . LYS A 1 393 ? 131.771 163.844 66.215  1.00 116.22 ? 393  LYS A CG    1 
ATOM   2966  C  CD    . LYS A 1 393 ? 132.594 162.926 65.327  1.00 117.67 ? 393  LYS A CD    1 
ATOM   2967  C  CE    . LYS A 1 393 ? 133.771 163.663 64.711  1.00 117.77 ? 393  LYS A CE    1 
ATOM   2968  N  NZ    . LYS A 1 393 ? 134.603 162.767 63.860  1.00 116.33 ? 393  LYS A NZ    1 
ATOM   2969  N  N     . VAL A 1 394 ? 131.127 163.670 69.899  1.00 111.57 ? 394  VAL A N     1 
ATOM   2970  C  CA    . VAL A 1 394 ? 131.983 164.111 70.994  1.00 111.62 ? 394  VAL A CA    1 
ATOM   2971  C  C     . VAL A 1 394 ? 133.418 164.217 70.498  1.00 112.74 ? 394  VAL A C     1 
ATOM   2972  O  O     . VAL A 1 394 ? 133.948 163.288 69.878  1.00 111.47 ? 394  VAL A O     1 
ATOM   2973  C  CB    . VAL A 1 394 ? 131.872 163.158 72.194  1.00 109.97 ? 394  VAL A CB    1 
ATOM   2974  C  CG1   . VAL A 1 394 ? 131.907 161.718 71.733  1.00 110.26 ? 394  VAL A CG1   1 
ATOM   2975  C  CG2   . VAL A 1 394 ? 132.993 163.423 73.180  1.00 109.66 ? 394  VAL A CG2   1 
ATOM   2976  N  N     . GLU A 1 395 ? 134.042 165.357 70.753  1.00 113.45 ? 395  GLU A N     1 
ATOM   2977  C  CA    . GLU A 1 395 ? 135.434 165.583 70.393  1.00 111.63 ? 395  GLU A CA    1 
ATOM   2978  C  C     . GLU A 1 395 ? 136.303 165.946 71.583  1.00 111.26 ? 395  GLU A C     1 
ATOM   2979  O  O     . GLU A 1 395 ? 137.465 165.540 71.636  1.00 110.88 ? 395  GLU A O     1 
ATOM   2980  C  CB    . GLU A 1 395 ? 135.532 166.683 69.328  1.00 112.01 ? 395  GLU A CB    1 
ATOM   2981  C  CG    . GLU A 1 395 ? 134.841 166.334 68.021  1.00 112.15 ? 395  GLU A CG    1 
ATOM   2982  C  CD    . GLU A 1 395 ? 134.949 167.441 66.991  1.00 113.81 ? 395  GLU A CD    1 
ATOM   2983  O  OE1   . GLU A 1 395 ? 135.543 168.493 67.308  1.00 114.06 ? 395  GLU A OE1   1 
ATOM   2984  O  OE2   . GLU A 1 395 ? 134.441 167.259 65.865  1.00 112.90 ? 395  GLU A OE2   1 
ATOM   2985  N  N     . GLU A 1 396 ? 135.776 166.706 72.539  1.00 112.94 ? 396  GLU A N     1 
ATOM   2986  C  CA    . GLU A 1 396 ? 136.503 166.990 73.765  1.00 112.49 ? 396  GLU A CA    1 
ATOM   2987  C  C     . GLU A 1 396 ? 135.509 167.165 74.902  1.00 112.63 ? 396  GLU A C     1 
ATOM   2988  O  O     . GLU A 1 396 ? 134.355 167.544 74.688  1.00 112.89 ? 396  GLU A O     1 
ATOM   2989  C  CB    . GLU A 1 396 ? 137.385 168.235 73.638  1.00 111.08 ? 396  GLU A CB    1 
ATOM   2990  C  CG    . GLU A 1 396 ? 136.615 169.525 73.477  1.00 111.27 ? 396  GLU A CG    1 
ATOM   2991  C  CD    . GLU A 1 396 ? 137.470 170.747 73.717  1.00 112.44 ? 396  GLU A CD    1 
ATOM   2992  O  OE1   . GLU A 1 396 ? 138.677 170.586 73.992  1.00 112.89 ? 396  GLU A OE1   1 
ATOM   2993  O  OE2   . GLU A 1 396 ? 136.935 171.872 73.632  1.00 112.77 ? 396  GLU A OE2   1 
ATOM   2994  N  N     . VAL A 1 397 ? 135.969 166.877 76.115  1.00 108.11 ? 397  VAL A N     1 
ATOM   2995  C  CA    . VAL A 1 397 ? 135.164 167.017 77.320  1.00 107.77 ? 397  VAL A CA    1 
ATOM   2996  C  C     . VAL A 1 397 ? 135.984 167.793 78.340  1.00 107.11 ? 397  VAL A C     1 
ATOM   2997  O  O     . VAL A 1 397 ? 137.164 167.494 78.553  1.00 108.00 ? 397  VAL A O     1 
ATOM   2998  C  CB    . VAL A 1 397 ? 134.720 165.647 77.874  1.00 107.01 ? 397  VAL A CB    1 
ATOM   2999  C  CG1   . VAL A 1 397 ? 135.897 164.695 77.995  1.00 105.89 ? 397  VAL A CG1   1 
ATOM   3000  C  CG2   . VAL A 1 397 ? 134.010 165.806 79.208  1.00 107.36 ? 397  VAL A CG2   1 
ATOM   3001  N  N     . GLU A 1 398 ? 135.378 168.810 78.940  1.00 104.67 ? 398  GLU A N     1 
ATOM   3002  C  CA    . GLU A 1 398 ? 136.068 169.643 79.911  1.00 105.20 ? 398  GLU A CA    1 
ATOM   3003  C  C     . GLU A 1 398 ? 135.785 169.124 81.313  1.00 106.73 ? 398  GLU A C     1 
ATOM   3004  O  O     . GLU A 1 398 ? 134.628 168.900 81.681  1.00 107.83 ? 398  GLU A O     1 
ATOM   3005  C  CB    . GLU A 1 398 ? 135.659 171.113 79.780  1.00 106.24 ? 398  GLU A CB    1 
ATOM   3006  C  CG    . GLU A 1 398 ? 134.178 171.391 79.909  1.00 106.84 ? 398  GLU A CG    1 
ATOM   3007  C  CD    . GLU A 1 398 ? 133.865 172.873 79.892  1.00 107.89 ? 398  GLU A CD    1 
ATOM   3008  O  OE1   . GLU A 1 398 ? 134.704 173.653 79.396  1.00 108.53 ? 398  GLU A OE1   1 
ATOM   3009  O  OE2   . GLU A 1 398 ? 132.783 173.260 80.380  1.00 107.38 ? 398  GLU A OE2   1 
ATOM   3010  N  N     . LEU A 1 399 ? 136.845 168.904 82.077  1.00 102.39 ? 399  LEU A N     1 
ATOM   3011  C  CA    . LEU A 1 399 ? 136.730 168.443 83.448  1.00 101.73 ? 399  LEU A CA    1 
ATOM   3012  C  C     . LEU A 1 399 ? 137.300 169.501 84.381  1.00 101.86 ? 399  LEU A C     1 
ATOM   3013  O  O     . LEU A 1 399 ? 137.927 170.473 83.954  1.00 102.78 ? 399  LEU A O     1 
ATOM   3014  C  CB    . LEU A 1 399 ? 137.452 167.104 83.659  1.00 101.79 ? 399  LEU A CB    1 
ATOM   3015  C  CG    . LEU A 1 399 ? 137.676 166.118 82.509  1.00 101.94 ? 399  LEU A CG    1 
ATOM   3016  C  CD1   . LEU A 1 399 ? 138.524 164.951 82.981  1.00 101.08 ? 399  LEU A CD1   1 
ATOM   3017  C  CD2   . LEU A 1 399 ? 136.374 165.608 81.944  1.00 101.31 ? 399  LEU A CD2   1 
ATOM   3018  N  N     . ILE A 1 400 ? 137.058 169.309 85.672  1.00 107.14 ? 400  ILE A N     1 
ATOM   3019  C  CA    . ILE A 1 400 ? 137.617 170.152 86.718  1.00 106.77 ? 400  ILE A CA    1 
ATOM   3020  C  C     . ILE A 1 400 ? 138.234 169.239 87.766  1.00 105.89 ? 400  ILE A C     1 
ATOM   3021  O  O     . ILE A 1 400 ? 137.618 168.245 88.168  1.00 107.80 ? 400  ILE A O     1 
ATOM   3022  C  CB    . ILE A 1 400 ? 136.553 171.081 87.339  1.00 107.05 ? 400  ILE A CB    1 
ATOM   3023  C  CG1   . ILE A 1 400 ? 137.072 171.742 88.616  1.00 107.32 ? 400  ILE A CG1   1 
ATOM   3024  C  CG2   . ILE A 1 400 ? 135.278 170.324 87.634  1.00 107.27 ? 400  ILE A CG2   1 
ATOM   3025  C  CD1   . ILE A 1 400 ? 138.233 172.675 88.397  1.00 106.92 ? 400  ILE A CD1   1 
ATOM   3026  N  N     . LYS A 1 401 ? 139.460 169.548 88.175  1.00 100.01 ? 401  LYS A N     1 
ATOM   3027  C  CA    . LYS A 1 401 ? 140.085 168.803 89.256  1.00 101.19 ? 401  LYS A CA    1 
ATOM   3028  C  C     . LYS A 1 401 ? 139.287 168.996 90.540  1.00 103.11 ? 401  LYS A C     1 
ATOM   3029  O  O     . LYS A 1 401 ? 138.772 170.082 90.811  1.00 103.96 ? 401  LYS A O     1 
ATOM   3030  C  CB    . LYS A 1 401 ? 141.531 169.260 89.441  1.00 102.15 ? 401  LYS A CB    1 
ATOM   3031  C  CG    . LYS A 1 401 ? 142.311 168.471 90.472  1.00 102.38 ? 401  LYS A CG    1 
ATOM   3032  C  CD    . LYS A 1 401 ? 143.776 168.858 90.461  1.00 102.07 ? 401  LYS A CD    1 
ATOM   3033  C  CE    . LYS A 1 401 ? 144.405 168.572 89.110  1.00 101.56 ? 401  LYS A CE    1 
ATOM   3034  N  NZ    . LYS A 1 401 ? 145.851 168.922 89.089  1.00 101.47 ? 401  LYS A NZ    1 
ATOM   3035  N  N     . MET A 1 402 ? 139.166 167.931 91.324  1.00 99.65  ? 402  MET A N     1 
ATOM   3036  C  CA    . MET A 1 402 ? 138.350 167.950 92.526  1.00 100.61 ? 402  MET A CA    1 
ATOM   3037  C  C     . MET A 1 402 ? 139.209 167.786 93.771  1.00 100.80 ? 402  MET A C     1 
ATOM   3038  O  O     . MET A 1 402 ? 140.281 167.176 93.734  1.00 100.29 ? 402  MET A O     1 
ATOM   3039  C  CB    . MET A 1 402 ? 137.289 166.850 92.491  1.00 99.40  ? 402  MET A CB    1 
ATOM   3040  C  CG    . MET A 1 402 ? 136.368 166.923 91.296  1.00 99.53  ? 402  MET A CG    1 
ATOM   3041  S  SD    . MET A 1 402 ? 134.816 166.065 91.600  1.00 100.43 ? 402  MET A SD    1 
ATOM   3042  C  CE    . MET A 1 402 ? 134.000 167.222 92.694  1.00 101.02 ? 402  MET A CE    1 
ATOM   3043  N  N     . LYS A 1 403 ? 138.723 168.348 94.875  1.00 105.34 ? 403  LYS A N     1 
ATOM   3044  C  CA    . LYS A 1 403 ? 139.363 168.213 96.177  1.00 105.46 ? 403  LYS A CA    1 
ATOM   3045  C  C     . LYS A 1 403 ? 138.278 168.214 97.241  1.00 106.32 ? 403  LYS A C     1 
ATOM   3046  O  O     . LYS A 1 403 ? 137.576 169.214 97.410  1.00 106.78 ? 403  LYS A O     1 
ATOM   3047  C  CB    . LYS A 1 403 ? 140.365 169.343 96.427  1.00 105.64 ? 403  LYS A CB    1 
ATOM   3048  C  CG    . LYS A 1 403 ? 140.938 169.359 97.834  1.00 105.86 ? 403  LYS A CG    1 
ATOM   3049  C  CD    . LYS A 1 403 ? 141.676 168.068 98.149  1.00 105.11 ? 403  LYS A CD    1 
ATOM   3050  C  CE    . LYS A 1 403 ? 142.889 167.888 97.251  1.00 105.63 ? 403  LYS A CE    1 
ATOM   3051  N  NZ    . LYS A 1 403 ? 143.620 166.627 97.554  1.00 106.18 ? 403  LYS A NZ    1 
ATOM   3052  N  N     . LEU A 1 404 ? 138.146 167.099 97.956  1.00 108.01 ? 404  LEU A N     1 
ATOM   3053  C  CA    . LEU A 1 404 ? 137.106 166.926 98.965  1.00 107.81 ? 404  LEU A CA    1 
ATOM   3054  C  C     . LEU A 1 404 ? 137.649 167.361 100.321 1.00 108.16 ? 404  LEU A C     1 
ATOM   3055  O  O     . LEU A 1 404 ? 138.577 166.744 100.854 1.00 107.48 ? 404  LEU A O     1 
ATOM   3056  C  CB    . LEU A 1 404 ? 136.624 165.477 99.003  1.00 107.53 ? 404  LEU A CB    1 
ATOM   3057  C  CG    . LEU A 1 404 ? 137.478 164.413 98.308  1.00 107.64 ? 404  LEU A CG    1 
ATOM   3058  C  CD1   . LEU A 1 404 ? 138.694 164.032 99.140  1.00 107.34 ? 404  LEU A CD1   1 
ATOM   3059  C  CD2   . LEU A 1 404 ? 136.639 163.184 97.988  1.00 108.09 ? 404  LEU A CD2   1 
ATOM   3060  N  N     . GLY A 1 405 ? 137.070 168.426 100.876 1.00 115.07 ? 405  GLY A N     1 
ATOM   3061  C  CA    . GLY A 1 405 ? 137.460 168.914 102.180 1.00 115.13 ? 405  GLY A CA    1 
ATOM   3062  C  C     . GLY A 1 405 ? 136.689 168.246 103.305 1.00 115.95 ? 405  GLY A C     1 
ATOM   3063  O  O     . GLY A 1 405 ? 135.795 167.428 103.094 1.00 116.78 ? 405  GLY A O     1 
ATOM   3064  N  N     . GLU A 1 406 ? 137.060 168.612 104.529 1.00 117.69 ? 406  GLU A N     1 
ATOM   3065  C  CA    . GLU A 1 406 ? 136.383 168.087 105.701 1.00 118.09 ? 406  GLU A CA    1 
ATOM   3066  C  C     . GLU A 1 406 ? 134.965 168.652 105.793 1.00 118.66 ? 406  GLU A C     1 
ATOM   3067  O  O     . GLU A 1 406 ? 134.710 169.783 105.369 1.00 118.08 ? 406  GLU A O     1 
ATOM   3068  C  CB    . GLU A 1 406 ? 137.164 168.430 106.966 1.00 118.01 ? 406  GLU A CB    1 
ATOM   3069  C  CG    . GLU A 1 406 ? 138.540 167.786 107.041 1.00 118.36 ? 406  GLU A CG    1 
ATOM   3070  C  CD    . GLU A 1 406 ? 138.475 166.280 107.214 1.00 118.28 ? 406  GLU A CD    1 
ATOM   3071  O  OE1   . GLU A 1 406 ? 137.452 165.779 107.727 1.00 118.89 ? 406  GLU A OE1   1 
ATOM   3072  O  OE2   . GLU A 1 406 ? 139.450 165.596 106.837 1.00 117.90 ? 406  GLU A OE2   1 
ATOM   3073  N  N     . PRO A 1 407 ? 134.014 167.873 106.337 1.00 30.00  ? 407  PRO A N     1 
ATOM   3074  C  CA    . PRO A 1 407 ? 132.625 168.317 106.503 1.00 30.00  ? 407  PRO A CA    1 
ATOM   3075  C  C     . PRO A 1 407 ? 132.494 169.545 107.401 1.00 30.00  ? 407  PRO A C     1 
ATOM   3076  O  O     . PRO A 1 407 ? 132.038 170.585 106.924 1.00 30.00  ? 407  PRO A O     1 
ATOM   3077  C  CB    . PRO A 1 407 ? 131.944 167.105 107.148 1.00 30.00  ? 407  PRO A CB    1 
ATOM   3078  C  CG    . PRO A 1 407 ? 132.784 165.945 106.749 1.00 30.00  ? 407  PRO A CG    1 
ATOM   3079  C  CD    . PRO A 1 407 ? 134.188 166.463 106.726 1.00 30.00  ? 407  PRO A CD    1 
ATOM   3080  N  N     . ARG A 1 412 ? 132.487 162.596 106.186 1.00 120.10 ? 412  ARG A N     1 
ATOM   3081  C  CA    . ARG A 1 412 ? 131.920 162.263 104.885 1.00 120.49 ? 412  ARG A CA    1 
ATOM   3082  C  C     . ARG A 1 412 ? 132.870 162.667 103.764 1.00 120.09 ? 412  ARG A C     1 
ATOM   3083  O  O     . ARG A 1 412 ? 133.184 161.860 102.889 1.00 119.61 ? 412  ARG A O     1 
ATOM   3084  C  CB    . ARG A 1 412 ? 130.561 162.942 104.694 1.00 120.73 ? 412  ARG A CB    1 
ATOM   3085  C  CG    . ARG A 1 412 ? 129.376 162.206 105.315 1.00 120.55 ? 412  ARG A CG    1 
ATOM   3086  C  CD    . ARG A 1 412 ? 129.194 162.524 106.795 1.00 119.97 ? 412  ARG A CD    1 
ATOM   3087  N  NE    . ARG A 1 412 ? 130.085 161.747 107.648 1.00 120.08 ? 412  ARG A NE    1 
ATOM   3088  C  CZ    . ARG A 1 412 ? 129.806 160.540 108.121 1.00 120.21 ? 412  ARG A CZ    1 
ATOM   3089  N  NH1   . ARG A 1 412 ? 128.663 159.935 107.841 1.00 120.51 ? 412  ARG A NH1   1 
ATOM   3090  N  NH2   . ARG A 1 412 ? 130.696 159.924 108.894 1.00 119.56 ? 412  ARG A NH2   1 
ATOM   3091  N  N     . ARG A 1 413 ? 133.320 163.924 103.811 1.00 116.80 ? 413  ARG A N     1 
ATOM   3092  C  CA    . ARG A 1 413 ? 134.236 164.488 102.817 1.00 117.00 ? 413  ARG A CA    1 
ATOM   3093  C  C     . ARG A 1 413 ? 133.668 164.356 101.405 1.00 116.60 ? 413  ARG A C     1 
ATOM   3094  O  O     . ARG A 1 413 ? 134.285 163.771 100.513 1.00 116.18 ? 413  ARG A O     1 
ATOM   3095  C  CB    . ARG A 1 413 ? 135.622 163.846 102.915 1.00 116.47 ? 413  ARG A CB    1 
ATOM   3096  C  CG    . ARG A 1 413 ? 136.235 163.904 104.302 1.00 115.81 ? 413  ARG A CG    1 
ATOM   3097  C  CD    . ARG A 1 413 ? 137.598 163.236 104.327 1.00 116.10 ? 413  ARG A CD    1 
ATOM   3098  N  NE    . ARG A 1 413 ? 138.120 163.117 105.683 1.00 115.94 ? 413  ARG A NE    1 
ATOM   3099  C  CZ    . ARG A 1 413 ? 137.902 162.080 106.480 1.00 116.44 ? 413  ARG A CZ    1 
ATOM   3100  N  NH1   . ARG A 1 413 ? 137.173 161.048 106.088 1.00 115.51 ? 413  ARG A NH1   1 
ATOM   3101  N  NH2   . ARG A 1 413 ? 138.428 162.079 107.702 1.00 116.36 ? 413  ARG A NH2   1 
ATOM   3102  N  N     . ARG A 1 414 ? 132.468 164.893 101.216 1.00 117.60 ? 414  ARG A N     1 
ATOM   3103  C  CA    . ARG A 1 414 ? 131.850 164.872 99.901  1.00 118.16 ? 414  ARG A CA    1 
ATOM   3104  C  C     . ARG A 1 414 ? 132.667 165.733 98.940  1.00 118.57 ? 414  ARG A C     1 
ATOM   3105  O  O     . ARG A 1 414 ? 133.088 166.838 99.303  1.00 118.92 ? 414  ARG A O     1 
ATOM   3106  C  CB    . ARG A 1 414 ? 130.410 165.379 99.981  1.00 117.71 ? 414  ARG A CB    1 
ATOM   3107  C  CG    . ARG A 1 414 ? 129.461 164.733 98.984  1.00 117.20 ? 414  ARG A CG    1 
ATOM   3108  C  CD    . ARG A 1 414 ? 129.484 163.217 99.110  1.00 117.58 ? 414  ARG A CD    1 
ATOM   3109  N  NE    . ARG A 1 414 ? 129.175 162.771 100.463 1.00 118.64 ? 414  ARG A NE    1 
ATOM   3110  C  CZ    . ARG A 1 414 ? 129.193 161.505 100.857 1.00 118.39 ? 414  ARG A CZ    1 
ATOM   3111  N  NH1   . ARG A 1 414 ? 129.504 160.526 100.024 1.00 118.33 ? 414  ARG A NH1   1 
ATOM   3112  N  NH2   . ARG A 1 414 ? 128.892 161.214 102.120 1.00 118.45 ? 414  ARG A NH2   1 
ATOM   3113  N  N     . PRO A 1 415 ? 132.928 165.256 97.723  1.00 113.85 ? 415  PRO A N     1 
ATOM   3114  C  CA    . PRO A 1 415 ? 133.793 166.009 96.808  1.00 113.13 ? 415  PRO A CA    1 
ATOM   3115  C  C     . PRO A 1 415 ? 133.172 167.333 96.386  1.00 112.67 ? 415  PRO A C     1 
ATOM   3116  O  O     . PRO A 1 415 ? 131.981 167.418 96.081  1.00 113.27 ? 415  PRO A O     1 
ATOM   3117  C  CB    . PRO A 1 415 ? 133.957 165.059 95.617  1.00 112.49 ? 415  PRO A CB    1 
ATOM   3118  C  CG    . PRO A 1 415 ? 132.757 164.176 95.674  1.00 111.77 ? 415  PRO A CG    1 
ATOM   3119  C  CD    . PRO A 1 415 ? 132.473 163.987 97.132  1.00 112.08 ? 415  PRO A CD    1 
ATOM   3120  N  N     . MET A 1 416 ? 134.003 168.373 96.371  1.00 108.92 ? 416  MET A N     1 
ATOM   3121  C  CA    . MET A 1 416 ? 133.612 169.698 95.903  1.00 109.18 ? 416  MET A CA    1 
ATOM   3122  C  C     . MET A 1 416 ? 134.695 170.174 94.947  1.00 109.29 ? 416  MET A C     1 
ATOM   3123  O  O     . MET A 1 416 ? 135.884 170.195 95.325  1.00 108.30 ? 416  MET A O     1 
ATOM   3124  C  CB    . MET A 1 416 ? 133.432 170.676 97.066  1.00 109.69 ? 416  MET A CB    1 
ATOM   3125  C  CG    . MET A 1 416 ? 132.332 170.290 98.040  1.00 108.97 ? 416  MET A CG    1 
ATOM   3126  S  SD    . MET A 1 416 ? 132.159 171.467 99.395  1.00 112.44 ? 416  MET A SD    1 
ATOM   3127  C  CE    . MET A 1 416 ? 131.771 172.965 98.494  1.00 109.15 ? 416  MET A CE    1 
ATOM   3128  N  N     . PRO A 1 417 ? 134.354 170.552 93.719  1.00 109.36 ? 417  PRO A N     1 
ATOM   3129  C  CA    . PRO A 1 417 ? 135.390 170.879 92.736  1.00 109.65 ? 417  PRO A CA    1 
ATOM   3130  C  C     . PRO A 1 417 ? 136.128 172.161 93.081  1.00 109.35 ? 417  PRO A C     1 
ATOM   3131  O  O     . PRO A 1 417 ? 135.600 173.054 93.747  1.00 109.54 ? 417  PRO A O     1 
ATOM   3132  C  CB    . PRO A 1 417 ? 134.600 171.029 91.431  1.00 108.90 ? 417  PRO A CB    1 
ATOM   3133  C  CG    . PRO A 1 417 ? 133.240 171.431 91.871  1.00 108.62 ? 417  PRO A CG    1 
ATOM   3134  C  CD    . PRO A 1 417 ? 132.998 170.718 93.171  1.00 108.90 ? 417  PRO A CD    1 
ATOM   3135  N  N     . ILE A 1 418 ? 137.376 172.238 92.617  1.00 107.71 ? 418  ILE A N     1 
ATOM   3136  C  CA    . ILE A 1 418 ? 138.124 173.482 92.724  1.00 108.39 ? 418  ILE A CA    1 
ATOM   3137  C  C     . ILE A 1 418 ? 137.506 174.525 91.793  1.00 108.47 ? 418  ILE A C     1 
ATOM   3138  O  O     . ILE A 1 418 ? 136.724 174.210 90.889  1.00 107.79 ? 418  ILE A O     1 
ATOM   3139  C  CB    . ILE A 1 418 ? 139.612 173.246 92.414  1.00 107.98 ? 418  ILE A CB    1 
ATOM   3140  C  CG1   . ILE A 1 418 ? 140.072 171.930 93.037  1.00 107.65 ? 418  ILE A CG1   1 
ATOM   3141  C  CG2   . ILE A 1 418 ? 140.482 174.359 92.981  1.00 107.79 ? 418  ILE A CG2   1 
ATOM   3142  C  CD1   . ILE A 1 418 ? 141.540 171.635 92.826  1.00 108.72 ? 418  ILE A CD1   1 
ATOM   3143  N  N     . GLU A 1 419 ? 137.856 175.792 92.034  1.00 103.86 ? 419  GLU A N     1 
ATOM   3144  C  CA    . GLU A 1 419 ? 137.195 176.899 91.347  1.00 103.79 ? 419  GLU A CA    1 
ATOM   3145  C  C     . GLU A 1 419 ? 137.386 176.820 89.837  1.00 104.78 ? 419  GLU A C     1 
ATOM   3146  O  O     . GLU A 1 419 ? 136.438 177.041 89.075  1.00 105.28 ? 419  GLU A O     1 
ATOM   3147  C  CB    . GLU A 1 419 ? 137.712 178.231 91.892  1.00 102.72 ? 419  GLU A CB    1 
ATOM   3148  C  CG    . GLU A 1 419 ? 136.938 179.453 91.417  1.00 103.18 ? 419  GLU A CG    1 
ATOM   3149  C  CD    . GLU A 1 419 ? 137.495 180.046 90.135  1.00 103.56 ? 419  GLU A CD    1 
ATOM   3150  O  OE1   . GLU A 1 419 ? 138.618 179.667 89.740  1.00 103.39 ? 419  GLU A OE1   1 
ATOM   3151  O  OE2   . GLU A 1 419 ? 136.808 180.891 89.523  1.00 103.85 ? 419  GLU A OE2   1 
ATOM   3152  N  N     . GLY A 1 420 ? 138.596 176.510 89.382  1.00 104.70 ? 420  GLY A N     1 
ATOM   3153  C  CA    . GLY A 1 420 ? 138.808 176.364 87.956  1.00 104.44 ? 420  GLY A CA    1 
ATOM   3154  C  C     . GLY A 1 420 ? 140.145 175.774 87.563  1.00 105.33 ? 420  GLY A C     1 
ATOM   3155  O  O     . GLY A 1 420 ? 141.197 176.233 88.019  1.00 104.62 ? 420  GLY A O     1 
ATOM   3156  N  N     . SER A 1 421 ? 140.111 174.749 86.712  1.00 106.93 ? 421  SER A N     1 
ATOM   3157  C  CA    . SER A 1 421 ? 141.318 174.159 86.148  1.00 106.92 ? 421  SER A CA    1 
ATOM   3158  C  C     . SER A 1 421 ? 141.225 173.869 84.659  1.00 105.70 ? 421  SER A C     1 
ATOM   3159  O  O     . SER A 1 421 ? 142.274 173.781 84.008  1.00 106.53 ? 421  SER A O     1 
ATOM   3160  C  CB    . SER A 1 421 ? 141.678 172.858 86.880  1.00 107.08 ? 421  SER A CB    1 
ATOM   3161  O  OG    . SER A 1 421 ? 142.895 172.321 86.391  1.00 106.32 ? 421  SER A OG    1 
ATOM   3162  N  N     . GLU A 1 422 ? 140.021 173.716 84.103  1.00 103.95 ? 422  GLU A N     1 
ATOM   3163  C  CA    . GLU A 1 422 ? 139.799 173.512 82.670  1.00 105.11 ? 422  GLU A CA    1 
ATOM   3164  C  C     . GLU A 1 422 ? 140.557 172.287 82.153  1.00 104.78 ? 422  GLU A C     1 
ATOM   3165  O  O     . GLU A 1 422 ? 141.438 172.376 81.297  1.00 103.91 ? 422  GLU A O     1 
ATOM   3166  C  CB    . GLU A 1 422 ? 140.167 174.769 81.874  1.00 104.89 ? 422  GLU A CB    1 
ATOM   3167  C  CG    . GLU A 1 422 ? 139.325 175.986 82.221  1.00 105.18 ? 422  GLU A CG    1 
ATOM   3168  C  CD    . GLU A 1 422 ? 139.663 177.192 81.369  1.00 105.91 ? 422  GLU A CD    1 
ATOM   3169  O  OE1   . GLU A 1 422 ? 140.563 177.082 80.509  1.00 106.41 ? 422  GLU A OE1   1 
ATOM   3170  O  OE2   . GLU A 1 422 ? 139.029 178.252 81.557  1.00 105.28 ? 422  GLU A OE2   1 
ATOM   3171  N  N     . PHE A 1 423 ? 140.192 171.127 82.697  1.00 105.03 ? 423  PHE A N     1 
ATOM   3172  C  CA    . PHE A 1 423 ? 140.734 169.848 82.243  1.00 104.71 ? 423  PHE A CA    1 
ATOM   3173  C  C     . PHE A 1 423 ? 140.029 169.469 80.945  1.00 104.76 ? 423  PHE A C     1 
ATOM   3174  O  O     . PHE A 1 423 ? 139.069 168.695 80.917  1.00 103.83 ? 423  PHE A O     1 
ATOM   3175  C  CB    . PHE A 1 423 ? 140.552 168.776 83.309  1.00 104.82 ? 423  PHE A CB    1 
ATOM   3176  C  CG    . PHE A 1 423 ? 141.833 168.255 83.875  1.00 104.35 ? 423  PHE A CG    1 
ATOM   3177  C  CD1   . PHE A 1 423 ? 142.394 168.838 84.998  1.00 103.94 ? 423  PHE A CD1   1 
ATOM   3178  C  CD2   . PHE A 1 423 ? 142.471 167.175 83.294  1.00 105.54 ? 423  PHE A CD2   1 
ATOM   3179  C  CE1   . PHE A 1 423 ? 143.575 168.358 85.527  1.00 104.20 ? 423  PHE A CE1   1 
ATOM   3180  C  CE2   . PHE A 1 423 ? 143.653 166.690 83.817  1.00 105.58 ? 423  PHE A CE2   1 
ATOM   3181  C  CZ    . PHE A 1 423 ? 144.207 167.282 84.936  1.00 104.74 ? 423  PHE A CZ    1 
ATOM   3182  N  N     . ARG A 1 424 ? 140.516 170.034 79.847  1.00 109.47 ? 424  ARG A N     1 
ATOM   3183  C  CA    . ARG A 1 424 ? 139.974 169.763 78.523  1.00 109.39 ? 424  ARG A CA    1 
ATOM   3184  C  C     . ARG A 1 424 ? 140.858 168.734 77.834  1.00 109.89 ? 424  ARG A C     1 
ATOM   3185  O  O     . ARG A 1 424 ? 142.065 168.950 77.682  1.00 109.82 ? 424  ARG A O     1 
ATOM   3186  C  CB    . ARG A 1 424 ? 139.890 171.044 77.696  1.00 108.29 ? 424  ARG A CB    1 
ATOM   3187  C  CG    . ARG A 1 424 ? 139.252 172.204 78.432  1.00 109.11 ? 424  ARG A CG    1 
ATOM   3188  C  CD    . ARG A 1 424 ? 139.098 173.406 77.529  1.00 109.44 ? 424  ARG A CD    1 
ATOM   3189  N  NE    . ARG A 1 424 ? 138.156 173.146 76.449  1.00 109.91 ? 424  ARG A NE    1 
ATOM   3190  C  CZ    . ARG A 1 424 ? 136.853 173.378 76.524  1.00 110.50 ? 424  ARG A CZ    1 
ATOM   3191  N  NH1   . ARG A 1 424 ? 136.302 173.877 77.618  1.00 109.99 ? 424  ARG A NH1   1 
ATOM   3192  N  NH2   . ARG A 1 424 ? 136.083 173.103 75.475  1.00 109.70 ? 424  ARG A NH2   1 
ATOM   3193  N  N     . VAL A 1 425 ? 140.261 167.619 77.424  1.00 111.62 ? 425  VAL A N     1 
ATOM   3194  C  CA    . VAL A 1 425 ? 140.982 166.533 76.775  1.00 110.90 ? 425  VAL A CA    1 
ATOM   3195  C  C     . VAL A 1 425 ? 140.229 166.145 75.510  1.00 110.40 ? 425  VAL A C     1 
ATOM   3196  O  O     . VAL A 1 425 ? 139.000 166.027 75.527  1.00 110.61 ? 425  VAL A O     1 
ATOM   3197  C  CB    . VAL A 1 425 ? 141.156 165.326 77.720  1.00 109.87 ? 425  VAL A CB    1 
ATOM   3198  C  CG1   . VAL A 1 425 ? 139.837 164.956 78.379  1.00 110.72 ? 425  VAL A CG1   1 
ATOM   3199  C  CG2   . VAL A 1 425 ? 141.754 164.136 76.983  1.00 109.76 ? 425  VAL A CG2   1 
ATOM   3200  N  N     . LYS A 1 426 ? 140.961 165.973 74.410  1.00 110.15 ? 426  LYS A N     1 
ATOM   3201  C  CA    . LYS A 1 426 ? 140.358 165.578 73.141  1.00 111.49 ? 426  LYS A CA    1 
ATOM   3202  C  C     . LYS A 1 426 ? 140.179 164.065 73.124  1.00 111.23 ? 426  LYS A C     1 
ATOM   3203  O  O     . LYS A 1 426 ? 141.161 163.315 73.112  1.00 110.62 ? 426  LYS A O     1 
ATOM   3204  C  CB    . LYS A 1 426 ? 141.217 166.038 71.968  1.00 109.82 ? 426  LYS A CB    1 
ATOM   3205  C  CG    . LYS A 1 426 ? 140.680 165.605 70.614  1.00 109.51 ? 426  LYS A CG    1 
ATOM   3206  C  CD    . LYS A 1 426 ? 141.591 166.059 69.487  1.00 110.87 ? 426  LYS A CD    1 
ATOM   3207  C  CE    . LYS A 1 426 ? 141.730 167.571 69.467  1.00 110.88 ? 426  LYS A CE    1 
ATOM   3208  N  NZ    . LYS A 1 426 ? 140.418 168.246 69.265  1.00 109.53 ? 426  LYS A NZ    1 
ATOM   3209  N  N     . VAL A 1 427 ? 138.926 163.612 73.121  1.00 103.24 ? 427  VAL A N     1 
ATOM   3210  C  CA    . VAL A 1 427 ? 138.604 162.195 73.192  1.00 101.23 ? 427  VAL A CA    1 
ATOM   3211  C  C     . VAL A 1 427 ? 137.558 161.864 72.139  1.00 101.70 ? 427  VAL A C     1 
ATOM   3212  O  O     . VAL A 1 427 ? 136.820 162.729 71.662  1.00 102.80 ? 427  VAL A O     1 
ATOM   3213  C  CB    . VAL A 1 427 ? 138.103 161.786 74.590  1.00 102.01 ? 427  VAL A CB    1 
ATOM   3214  C  CG1   . VAL A 1 427 ? 139.238 161.838 75.595  1.00 102.49 ? 427  VAL A CG1   1 
ATOM   3215  C  CG2   . VAL A 1 427 ? 136.964 162.691 75.019  1.00 103.60 ? 427  VAL A CG2   1 
ATOM   3216  N  N     . ASP A 1 428 ? 137.495 160.583 71.786  1.00 100.30 ? 428  ASP A N     1 
ATOM   3217  C  CA    . ASP A 1 428 ? 136.601 160.118 70.736  1.00 100.45 ? 428  ASP A CA    1 
ATOM   3218  C  C     . ASP A 1 428 ? 135.293 159.555 71.267  1.00 100.90 ? 428  ASP A C     1 
ATOM   3219  O  O     . ASP A 1 428 ? 134.254 159.721 70.622  1.00 101.11 ? 428  ASP A O     1 
ATOM   3220  C  CB    . ASP A 1 428 ? 137.301 159.055 69.883  1.00 99.86  ? 428  ASP A CB    1 
ATOM   3221  C  CG    . ASP A 1 428 ? 136.678 158.905 68.513  1.00 100.85 ? 428  ASP A CG    1 
ATOM   3222  O  OD1   . ASP A 1 428 ? 135.771 159.696 68.180  1.00 101.57 ? 428  ASP A OD1   1 
ATOM   3223  O  OD2   . ASP A 1 428 ? 137.096 157.996 67.766  1.00 100.02 ? 428  ASP A OD2   1 
ATOM   3224  N  N     . ASN A 1 429 ? 135.313 158.897 72.422  1.00 93.76  ? 429  ASN A N     1 
ATOM   3225  C  CA    . ASN A 1 429 ? 134.113 158.348 73.031  1.00 91.06  ? 429  ASN A CA    1 
ATOM   3226  C  C     . ASN A 1 429 ? 134.085 158.684 74.513  1.00 91.48  ? 429  ASN A C     1 
ATOM   3227  O  O     . ASN A 1 429 ? 135.124 158.754 75.172  1.00 91.05  ? 429  ASN A O     1 
ATOM   3228  C  CB    . ASN A 1 429 ? 134.031 156.828 72.852  1.00 90.34  ? 429  ASN A CB    1 
ATOM   3229  C  CG    . ASN A 1 429 ? 133.572 156.429 71.470  1.00 92.05  ? 429  ASN A CG    1 
ATOM   3230  O  OD1   . ASN A 1 429 ? 134.305 156.572 70.493  1.00 93.03  ? 429  ASN A OD1   1 
ATOM   3231  N  ND2   . ASN A 1 429 ? 132.355 155.909 71.380  1.00 92.51  ? 429  ASN A ND2   1 
ATOM   3232  N  N     . VAL A 1 430 ? 132.878 158.890 75.031  1.00 85.97  ? 430  VAL A N     1 
ATOM   3233  C  CA    . VAL A 1 430 ? 132.639 159.070 76.456  1.00 85.11  ? 430  VAL A CA    1 
ATOM   3234  C  C     . VAL A 1 430 ? 131.727 157.945 76.917  1.00 84.87  ? 430  VAL A C     1 
ATOM   3235  O  O     . VAL A 1 430 ? 130.698 157.677 76.287  1.00 87.33  ? 430  VAL A O     1 
ATOM   3236  C  CB    . VAL A 1 430 ? 132.017 160.444 76.766  1.00 87.31  ? 430  VAL A CB    1 
ATOM   3237  C  CG1   . VAL A 1 430 ? 131.751 160.586 78.253  1.00 86.30  ? 430  VAL A CG1   1 
ATOM   3238  C  CG2   . VAL A 1 430 ? 132.926 161.553 76.288  1.00 87.41  ? 430  VAL A CG2   1 
ATOM   3239  N  N     . ILE A 1 431 ? 132.112 157.276 77.998  1.00 71.35  ? 431  ILE A N     1 
ATOM   3240  C  CA    . ILE A 1 431 ? 131.350 156.165 78.552  1.00 71.53  ? 431  ILE A CA    1 
ATOM   3241  C  C     . ILE A 1 431 ? 131.016 156.497 80.000  1.00 74.50  ? 431  ILE A C     1 
ATOM   3242  O  O     . ILE A 1 431 ? 131.915 156.783 80.801  1.00 74.23  ? 431  ILE A O     1 
ATOM   3243  C  CB    . ILE A 1 431 ? 132.116 154.839 78.441  1.00 71.74  ? 431  ILE A CB    1 
ATOM   3244  C  CG1   . ILE A 1 431 ? 132.368 154.498 76.973  1.00 70.87  ? 431  ILE A CG1   1 
ATOM   3245  C  CG2   . ILE A 1 431 ? 131.346 153.726 79.098  1.00 72.60  ? 431  ILE A CG2   1 
ATOM   3246  C  CD1   . ILE A 1 431 ? 132.977 153.134 76.755  1.00 71.14  ? 431  ILE A CD1   1 
ATOM   3247  N  N     . LEU A 1 432 ? 129.730 156.460 80.334  1.00 78.30  ? 432  LEU A N     1 
ATOM   3248  C  CA    . LEU A 1 432 ? 129.241 156.860 81.648  1.00 78.71  ? 432  LEU A CA    1 
ATOM   3249  C  C     . LEU A 1 432 ? 128.971 155.625 82.498  1.00 78.19  ? 432  LEU A C     1 
ATOM   3250  O  O     . LEU A 1 432 ? 128.172 154.764 82.117  1.00 77.17  ? 432  LEU A O     1 
ATOM   3251  C  CB    . LEU A 1 432 ? 127.971 157.702 81.529  1.00 76.90  ? 432  LEU A CB    1 
ATOM   3252  C  CG    . LEU A 1 432 ? 128.110 159.216 81.368  1.00 77.30  ? 432  LEU A CG    1 
ATOM   3253  C  CD1   . LEU A 1 432 ? 128.715 159.576 80.026  1.00 77.86  ? 432  LEU A CD1   1 
ATOM   3254  C  CD2   . LEU A 1 432 ? 126.761 159.888 81.541  1.00 77.06  ? 432  LEU A CD2   1 
ATOM   3255  N  N     . ALA A 1 433 ? 129.633 155.548 83.646  1.00 69.96  ? 433  ALA A N     1 
ATOM   3256  C  CA    . ALA A 1 433 ? 129.415 154.509 84.644  1.00 66.95  ? 433  ALA A CA    1 
ATOM   3257  C  C     . ALA A 1 433 ? 129.325 155.138 86.026  1.00 69.19  ? 433  ALA A C     1 
ATOM   3258  O  O     . ALA A 1 433 ? 129.976 154.711 86.982  1.00 69.02  ? 433  ALA A O     1 
ATOM   3259  C  CB    . ALA A 1 433 ? 130.515 153.456 84.588  1.00 64.91  ? 433  ALA A CB    1 
ATOM   3260  N  N     . ILE A 1 434 ? 128.517 156.196 86.129  1.00 70.38  ? 434  ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 434 ? 128.396 156.939 87.381  1.00 71.75  ? 434  ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 434 ? 127.847 156.042 88.480  1.00 71.67  ? 434  ILE A C     1 
ATOM   3263  O  O     . ILE A 1 434 ? 128.356 156.029 89.607  1.00 73.98  ? 434  ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 434 ? 127.518 158.190 87.174  1.00 71.36  ? 434  ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 434 ? 128.346 159.348 86.612  1.00 67.26  ? 434  ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 434 ? 126.843 158.607 88.469  1.00 72.33  ? 434  ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 434 ? 128.604 159.272 85.123  1.00 69.37  ? 434  ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 435 ? 126.819 155.267 88.165  1.00 64.37  ? 435  GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 435 ? 126.247 154.346 89.120  1.00 63.27  ? 435  GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 435 ? 125.175 153.502 88.475  1.00 62.02  ? 435  GLY A C     1 
ATOM   3271  O  O     . GLY A 1 435 ? 125.285 153.146 87.299  1.00 63.92  ? 435  GLY A O     1 
ATOM   3272  N  N     . GLN A 1 436 ? 124.127 153.188 89.229  1.00 50.28  ? 436  GLN A N     1 
ATOM   3273  C  CA    . GLN A 1 436 ? 123.025 152.395 88.712  1.00 46.16  ? 436  GLN A CA    1 
ATOM   3274  C  C     . GLN A 1 436 ? 121.787 152.683 89.547  1.00 48.36  ? 436  GLN A C     1 
ATOM   3275  O  O     . GLN A 1 436 ? 121.882 153.092 90.707  1.00 55.42  ? 436  GLN A O     1 
ATOM   3276  C  CB    . GLN A 1 436 ? 123.351 150.898 88.737  1.00 48.88  ? 436  GLN A CB    1 
ATOM   3277  C  CG    . GLN A 1 436 ? 123.972 150.343 87.465  1.00 50.02  ? 436  GLN A CG    1 
ATOM   3278  C  CD    . GLN A 1 436 ? 123.926 148.829 87.415  1.00 52.27  ? 436  GLN A CD    1 
ATOM   3279  O  OE1   . GLN A 1 436 ? 124.317 148.216 86.423  1.00 54.04  ? 436  GLN A OE1   1 
ATOM   3280  N  NE2   . GLN A 1 436 ? 123.443 148.217 88.488  1.00 50.31  ? 436  GLN A NE2   1 
ATOM   3281  N  N     . TYR A 1 437 ? 120.625 152.464 88.937  1.00 53.43  ? 437  TYR A N     1 
ATOM   3282  C  CA    . TYR A 1 437 ? 119.352 152.490 89.645  1.00 55.40  ? 437  TYR A CA    1 
ATOM   3283  C  C     . TYR A 1 437 ? 118.325 151.754 88.797  1.00 53.36  ? 437  TYR A C     1 
ATOM   3284  O  O     . TYR A 1 437 ? 118.579 151.406 87.643  1.00 58.88  ? 437  TYR A O     1 
ATOM   3285  C  CB    . TYR A 1 437 ? 118.890 153.921 89.960  1.00 60.67  ? 437  TYR A CB    1 
ATOM   3286  C  CG    . TYR A 1 437 ? 118.589 154.796 88.758  1.00 59.02  ? 437  TYR A CG    1 
ATOM   3287  C  CD1   . TYR A 1 437 ? 117.372 154.712 88.094  1.00 58.47  ? 437  TYR A CD1   1 
ATOM   3288  C  CD2   . TYR A 1 437 ? 119.508 155.730 88.312  1.00 57.78  ? 437  TYR A CD2   1 
ATOM   3289  C  CE1   . TYR A 1 437 ? 117.093 155.508 87.009  1.00 59.27  ? 437  TYR A CE1   1 
ATOM   3290  C  CE2   . TYR A 1 437 ? 119.233 156.535 87.229  1.00 59.05  ? 437  TYR A CE2   1 
ATOM   3291  C  CZ    . TYR A 1 437 ? 118.025 156.420 86.581  1.00 61.37  ? 437  TYR A CZ    1 
ATOM   3292  O  OH    . TYR A 1 437 ? 117.749 157.222 85.499  1.00 64.01  ? 437  TYR A OH    1 
ATOM   3293  N  N     . CYS A 1 438 ? 117.159 151.521 89.385  1.00 52.78  ? 438  CYS A N     1 
ATOM   3294  C  CA    . CYS A 1 438 ? 116.022 150.984 88.656  1.00 58.86  ? 438  CYS A CA    1 
ATOM   3295  C  C     . CYS A 1 438 ? 115.087 152.122 88.270  1.00 63.71  ? 438  CYS A C     1 
ATOM   3296  O  O     . CYS A 1 438 ? 114.956 153.110 88.997  1.00 63.65  ? 438  CYS A O     1 
ATOM   3297  C  CB    . CYS A 1 438 ? 115.272 149.944 89.486  1.00 57.84  ? 438  CYS A CB    1 
ATOM   3298  S  SG    . CYS A 1 438 ? 114.031 149.012 88.567  1.00 60.27  ? 438  CYS A SG    1 
ATOM   3299  N  N     . ASP A 1 439 ? 114.434 151.966 87.117  1.00 70.15  ? 439  ASP A N     1 
ATOM   3300  C  CA    . ASP A 1 439 ? 113.675 153.054 86.511  1.00 65.90  ? 439  ASP A CA    1 
ATOM   3301  C  C     . ASP A 1 439 ? 112.608 153.578 87.463  1.00 67.33  ? 439  ASP A C     1 
ATOM   3302  O  O     . ASP A 1 439 ? 111.796 152.813 87.990  1.00 69.01  ? 439  ASP A O     1 
ATOM   3303  C  CB    . ASP A 1 439 ? 113.031 152.574 85.210  1.00 68.25  ? 439  ASP A CB    1 
ATOM   3304  C  CG    . ASP A 1 439 ? 112.657 153.716 84.283  1.00 73.02  ? 439  ASP A CG    1 
ATOM   3305  O  OD1   . ASP A 1 439 ? 112.440 154.846 84.768  1.00 72.72  ? 439  ASP A OD1   1 
ATOM   3306  O  OD2   . ASP A 1 439 ? 112.579 153.481 83.059  1.00 71.49  ? 439  ASP A OD2   1 
ATOM   3307  N  N     . GLU A 1 440 ? 112.619 154.895 87.682  1.00 71.64  ? 440  GLU A N     1 
ATOM   3308  C  CA    . GLU A 1 440 ? 111.652 155.502 88.587  1.00 74.84  ? 440  GLU A CA    1 
ATOM   3309  C  C     . GLU A 1 440 ? 110.237 155.415 88.036  1.00 76.99  ? 440  GLU A C     1 
ATOM   3310  O  O     . GLU A 1 440 ? 109.284 155.290 88.810  1.00 78.50  ? 440  GLU A O     1 
ATOM   3311  C  CB    . GLU A 1 440 ? 112.017 156.960 88.867  1.00 74.84  ? 440  GLU A CB    1 
ATOM   3312  C  CG    . GLU A 1 440 ? 113.304 157.153 89.643  1.00 75.56  ? 440  GLU A CG    1 
ATOM   3313  C  CD    . GLU A 1 440 ? 114.524 157.199 88.748  1.00 76.19  ? 440  GLU A CD    1 
ATOM   3314  O  OE1   . GLU A 1 440 ? 114.363 157.069 87.516  1.00 74.73  ? 440  GLU A OE1   1 
ATOM   3315  O  OE2   . GLU A 1 440 ? 115.643 157.368 89.275  1.00 77.24  ? 440  GLU A OE2   1 
ATOM   3316  N  N     . GLU A 1 441 ? 110.077 155.492 86.713  1.00 78.58  ? 441  GLU A N     1 
ATOM   3317  C  CA    . GLU A 1 441 ? 108.753 155.320 86.125  1.00 78.87  ? 441  GLU A CA    1 
ATOM   3318  C  C     . GLU A 1 441 ? 108.230 153.909 86.359  1.00 78.38  ? 441  GLU A C     1 
ATOM   3319  O  O     . GLU A 1 441 ? 107.056 153.720 86.701  1.00 80.04  ? 441  GLU A O     1 
ATOM   3320  C  CB    . GLU A 1 441 ? 108.799 155.636 84.631  1.00 76.92  ? 441  GLU A CB    1 
ATOM   3321  C  CG    . GLU A 1 441 ? 109.413 156.987 84.297  1.00 77.78  ? 441  GLU A CG    1 
ATOM   3322  C  CD    . GLU A 1 441 ? 108.556 158.154 84.747  1.00 77.62  ? 441  GLU A CD    1 
ATOM   3323  O  OE1   . GLU A 1 441 ? 107.338 157.962 84.953  1.00 76.32  ? 441  GLU A OE1   1 
ATOM   3324  O  OE2   . GLU A 1 441 ? 109.101 159.268 84.897  1.00 77.33  ? 441  GLU A OE2   1 
ATOM   3325  N  N     . PHE A 1 442 ? 109.091 152.906 86.186  1.00 76.43  ? 442  PHE A N     1 
ATOM   3326  C  CA    . PHE A 1 442 ? 108.691 151.529 86.454  1.00 76.02  ? 442  PHE A CA    1 
ATOM   3327  C  C     . PHE A 1 442 ? 108.437 151.304 87.938  1.00 75.78  ? 442  PHE A C     1 
ATOM   3328  O  O     . PHE A 1 442 ? 107.505 150.583 88.308  1.00 80.25  ? 442  PHE A O     1 
ATOM   3329  C  CB    . PHE A 1 442 ? 109.754 150.563 85.940  1.00 77.20  ? 442  PHE A CB    1 
ATOM   3330  C  CG    . PHE A 1 442 ? 109.508 149.135 86.326  1.00 77.42  ? 442  PHE A CG    1 
ATOM   3331  C  CD1   . PHE A 1 442 ? 108.452 148.431 85.780  1.00 76.28  ? 442  PHE A CD1   1 
ATOM   3332  C  CD2   . PHE A 1 442 ? 110.337 148.496 87.231  1.00 76.46  ? 442  PHE A CD2   1 
ATOM   3333  C  CE1   . PHE A 1 442 ? 108.224 147.119 86.130  1.00 76.73  ? 442  PHE A CE1   1 
ATOM   3334  C  CE2   . PHE A 1 442 ? 110.114 147.184 87.586  1.00 76.07  ? 442  PHE A CE2   1 
ATOM   3335  C  CZ    . PHE A 1 442 ? 109.055 146.494 87.035  1.00 77.45  ? 442  PHE A CZ    1 
ATOM   3336  N  N     . LEU A 1 443 ? 109.262 151.898 88.803  1.00 69.53  ? 443  LEU A N     1 
ATOM   3337  C  CA    . LEU A 1 443 ? 109.043 151.764 90.239  1.00 70.98  ? 443  LEU A CA    1 
ATOM   3338  C  C     . LEU A 1 443 ? 107.742 152.425 90.672  1.00 71.94  ? 443  LEU A C     1 
ATOM   3339  O  O     . LEU A 1 443 ? 107.069 151.932 91.584  1.00 70.45  ? 443  LEU A O     1 
ATOM   3340  C  CB    . LEU A 1 443 ? 110.223 152.353 91.008  1.00 69.02  ? 443  LEU A CB    1 
ATOM   3341  C  CG    . LEU A 1 443 ? 111.480 151.487 91.025  1.00 68.86  ? 443  LEU A CG    1 
ATOM   3342  C  CD1   . LEU A 1 443 ? 112.676 152.287 91.498  1.00 66.16  ? 443  LEU A CD1   1 
ATOM   3343  C  CD2   . LEU A 1 443 ? 111.266 150.269 91.906  1.00 69.39  ? 443  LEU A CD2   1 
ATOM   3344  N  N     . ARG A 1 444 ? 107.374 153.533 90.032  1.00 82.19  ? 444  ARG A N     1 
ATOM   3345  C  CA    . ARG A 1 444 ? 106.132 154.214 90.370  1.00 81.85  ? 444  ARG A CA    1 
ATOM   3346  C  C     . ARG A 1 444 ? 104.921 153.461 89.835  1.00 81.26  ? 444  ARG A C     1 
ATOM   3347  O  O     . ARG A 1 444 ? 103.887 153.384 90.509  1.00 82.37  ? 444  ARG A O     1 
ATOM   3348  C  CB    . ARG A 1 444 ? 106.163 155.638 89.822  1.00 80.83  ? 444  ARG A CB    1 
ATOM   3349  C  CG    . ARG A 1 444 ? 105.065 156.542 90.338  1.00 82.52  ? 444  ARG A CG    1 
ATOM   3350  C  CD    . ARG A 1 444 ? 105.011 157.849 89.556  1.00 84.35  ? 444  ARG A CD    1 
ATOM   3351  N  NE    . ARG A 1 444 ? 106.297 158.538 89.521  1.00 84.17  ? 444  ARG A NE    1 
ATOM   3352  C  CZ    . ARG A 1 444 ? 107.110 158.560 88.473  1.00 83.63  ? 444  ARG A CZ    1 
ATOM   3353  N  NH1   . ARG A 1 444 ? 106.803 157.935 87.348  1.00 82.73  ? 444  ARG A NH1   1 
ATOM   3354  N  NH2   . ARG A 1 444 ? 108.260 159.222 88.558  1.00 83.69  ? 444  ARG A NH2   1 
ATOM   3355  N  N     . THR A 1 445 ? 105.024 152.899 88.628  1.00 81.43  ? 445  THR A N     1 
ATOM   3356  C  CA    . THR A 1 445 ? 103.860 152.274 88.009  1.00 82.06  ? 445  THR A CA    1 
ATOM   3357  C  C     . THR A 1 445 ? 103.517 150.926 88.632  1.00 80.51  ? 445  THR A C     1 
ATOM   3358  O  O     . THR A 1 445 ? 102.411 150.424 88.413  1.00 83.46  ? 445  THR A O     1 
ATOM   3359  C  CB    . THR A 1 445 ? 104.077 152.109 86.504  1.00 82.67  ? 445  THR A CB    1 
ATOM   3360  O  OG1   . THR A 1 445 ? 102.827 151.808 85.872  1.00 83.27  ? 445  THR A OG1   1 
ATOM   3361  C  CG2   . THR A 1 445 ? 105.052 150.983 86.220  1.00 81.08  ? 445  THR A CG2   1 
ATOM   3362  N  N     . ILE A 1 446 ? 104.430 150.331 89.401  1.00 74.39  ? 446  ILE A N     1 
ATOM   3363  C  CA    . ILE A 1 446 ? 104.158 149.077 90.091  1.00 76.10  ? 446  ILE A CA    1 
ATOM   3364  C  C     . ILE A 1 446 ? 103.744 149.292 91.535  1.00 76.92  ? 446  ILE A C     1 
ATOM   3365  O  O     . ILE A 1 446 ? 103.461 148.316 92.243  1.00 75.06  ? 446  ILE A O     1 
ATOM   3366  C  CB    . ILE A 1 446 ? 105.374 148.135 90.026  1.00 77.50  ? 446  ILE A CB    1 
ATOM   3367  C  CG1   . ILE A 1 446 ? 106.574 148.765 90.735  1.00 74.33  ? 446  ILE A CG1   1 
ATOM   3368  C  CG2   . ILE A 1 446 ? 105.707 147.797 88.583  1.00 77.52  ? 446  ILE A CG2   1 
ATOM   3369  C  CD1   . ILE A 1 446 ? 107.845 147.959 90.623  1.00 74.10  ? 446  ILE A CD1   1 
ATOM   3370  N  N     . GLY A 1 447 ? 103.697 150.539 91.995  1.00 75.26  ? 447  GLY A N     1 
ATOM   3371  C  CA    . GLY A 1 447 ? 103.322 150.828 93.364  1.00 74.40  ? 447  GLY A CA    1 
ATOM   3372  C  C     . GLY A 1 447 ? 104.304 150.334 94.399  1.00 76.40  ? 447  GLY A C     1 
ATOM   3373  O  O     . GLY A 1 447 ? 103.893 149.937 95.494  1.00 78.15  ? 447  GLY A O     1 
ATOM   3374  N  N     . ILE A 1 448 ? 105.595 150.348 94.086  1.00 68.43  ? 448  ILE A N     1 
ATOM   3375  C  CA    . ILE A 1 448 ? 106.644 149.979 95.028  1.00 67.30  ? 448  ILE A CA    1 
ATOM   3376  C  C     . ILE A 1 448 ? 107.442 151.235 95.332  1.00 64.47  ? 448  ILE A C     1 
ATOM   3377  O  O     . ILE A 1 448 ? 107.982 151.873 94.421  1.00 62.64  ? 448  ILE A O     1 
ATOM   3378  C  CB    . ILE A 1 448 ? 107.547 148.867 94.475  1.00 65.13  ? 448  ILE A CB    1 
ATOM   3379  C  CG1   . ILE A 1 448 ? 106.776 147.551 94.384  1.00 61.26  ? 448  ILE A CG1   1 
ATOM   3380  C  CG2   . ILE A 1 448 ? 108.778 148.698 95.350  1.00 60.44  ? 448  ILE A CG2   1 
ATOM   3381  C  CD1   . ILE A 1 448 ? 106.302 147.042 95.713  1.00 60.61  ? 448  ILE A CD1   1 
ATOM   3382  N  N     . GLU A 1 449 ? 107.510 151.593 96.609  1.00 61.45  ? 449  GLU A N     1 
ATOM   3383  C  CA    . GLU A 1 449 ? 108.155 152.835 96.996  1.00 62.38  ? 449  GLU A CA    1 
ATOM   3384  C  C     . GLU A 1 449 ? 109.669 152.722 96.878  1.00 60.25  ? 449  GLU A C     1 
ATOM   3385  O  O     . GLU A 1 449 ? 110.262 151.671 97.131  1.00 61.68  ? 449  GLU A O     1 
ATOM   3386  C  CB    . GLU A 1 449 ? 107.758 153.217 98.420  1.00 61.53  ? 449  GLU A CB    1 
ATOM   3387  C  CG    . GLU A 1 449 ? 106.265 153.430 98.589  1.00 62.20  ? 449  GLU A CG    1 
ATOM   3388  C  CD    . GLU A 1 449 ? 105.714 154.476 97.639  1.00 63.34  ? 449  GLU A CD    1 
ATOM   3389  O  OE1   . GLU A 1 449 ? 106.360 155.533 97.474  1.00 65.54  ? 449  GLU A OE1   1 
ATOM   3390  O  OE2   . GLU A 1 449 ? 104.638 154.240 97.052  1.00 59.00  ? 449  GLU A OE2   1 
ATOM   3391  N  N     . ALA A 1 450 ? 110.291 153.828 96.485  1.00 54.99  ? 450  ALA A N     1 
ATOM   3392  C  CA    . ALA A 1 450 ? 111.733 153.889 96.307  1.00 51.40  ? 450  ALA A CA    1 
ATOM   3393  C  C     . ALA A 1 450 ? 112.159 155.346 96.378  1.00 55.16  ? 450  ALA A C     1 
ATOM   3394  O  O     . ALA A 1 450 ? 111.339 156.259 96.266  1.00 60.89  ? 450  ALA A O     1 
ATOM   3395  C  CB    . ALA A 1 450 ? 112.159 153.256 94.981  1.00 54.68  ? 450  ALA A CB    1 
ATOM   3396  N  N     . LYS A 1 451 ? 113.459 155.553 96.568  1.00 55.97  ? 451  LYS A N     1 
ATOM   3397  C  CA    . LYS A 1 451 ? 114.027 156.894 96.622  1.00 57.68  ? 451  LYS A CA    1 
ATOM   3398  C  C     . LYS A 1 451 ? 115.316 156.895 95.821  1.00 55.60  ? 451  LYS A C     1 
ATOM   3399  O  O     . LYS A 1 451 ? 116.228 156.118 96.119  1.00 56.78  ? 451  LYS A O     1 
ATOM   3400  C  CB    . LYS A 1 451 ? 114.280 157.332 98.066  1.00 57.60  ? 451  LYS A CB    1 
ATOM   3401  C  CG    . LYS A 1 451 ? 114.600 158.804 98.217  1.00 57.27  ? 451  LYS A CG    1 
ATOM   3402  C  CD    . LYS A 1 451 ? 114.717 159.189 99.679  1.00 58.67  ? 451  LYS A CD    1 
ATOM   3403  C  CE    . LYS A 1 451 ? 113.424 158.908 100.421 1.00 56.82  ? 451  LYS A CE    1 
ATOM   3404  N  NZ    . LYS A 1 451 ? 112.272 159.615 99.802  1.00 57.42  ? 451  LYS A NZ    1 
ATOM   3405  N  N     . ARG A 1 452 ? 115.380 157.759 94.804  1.00 58.75  ? 452  ARG A N     1 
ATOM   3406  C  CA    . ARG A 1 452 ? 116.498 157.819 93.859  1.00 59.87  ? 452  ARG A CA    1 
ATOM   3407  C  C     . ARG A 1 452 ? 116.665 156.501 93.105  1.00 60.55  ? 452  ARG A C     1 
ATOM   3408  O  O     . ARG A 1 452 ? 117.765 156.150 92.674  1.00 61.28  ? 452  ARG A O     1 
ATOM   3409  C  CB    . ARG A 1 452 ? 117.803 158.215 94.560  1.00 61.02  ? 452  ARG A CB    1 
ATOM   3410  C  CG    . ARG A 1 452 ? 118.806 158.938 93.676  1.00 63.63  ? 452  ARG A CG    1 
ATOM   3411  C  CD    . ARG A 1 452 ? 120.070 159.278 94.446  1.00 60.48  ? 452  ARG A CD    1 
ATOM   3412  N  NE    . ARG A 1 452 ? 119.794 160.138 95.590  1.00 62.75  ? 452  ARG A NE    1 
ATOM   3413  C  CZ    . ARG A 1 452 ? 119.758 161.462 95.539  1.00 62.10  ? 452  ARG A CZ    1 
ATOM   3414  N  NH1   . ARG A 1 452 ? 119.976 162.117 94.411  1.00 58.82  ? 452  ARG A NH1   1 
ATOM   3415  N  NH2   . ARG A 1 452 ? 119.497 162.147 96.649  1.00 61.64  ? 452  ARG A NH2   1 
ATOM   3416  N  N     . GLY A 1 453 ? 115.571 155.761 92.937  1.00 60.39  ? 453  GLY A N     1 
ATOM   3417  C  CA    . GLY A 1 453 ? 115.600 154.481 92.268  1.00 59.66  ? 453  GLY A CA    1 
ATOM   3418  C  C     . GLY A 1 453 ? 115.913 153.300 93.159  1.00 58.33  ? 453  GLY A C     1 
ATOM   3419  O  O     . GLY A 1 453 ? 115.723 152.156 92.731  1.00 59.14  ? 453  GLY A O     1 
ATOM   3420  N  N     . ARG A 1 454 ? 116.382 153.537 94.381  1.00 45.37  ? 454  ARG A N     1 
ATOM   3421  C  CA    . ARG A 1 454 ? 116.687 152.468 95.319  1.00 45.25  ? 454  ARG A CA    1 
ATOM   3422  C  C     . ARG A 1 454 ? 115.460 152.175 96.170  1.00 50.67  ? 454  ARG A C     1 
ATOM   3423  O  O     . ARG A 1 454 ? 114.905 153.082 96.800  1.00 53.41  ? 454  ARG A O     1 
ATOM   3424  C  CB    . ARG A 1 454 ? 117.876 152.850 96.201  1.00 46.69  ? 454  ARG A CB    1 
ATOM   3425  C  CG    . ARG A 1 454 ? 119.189 152.959 95.447  1.00 49.13  ? 454  ARG A CG    1 
ATOM   3426  C  CD    . ARG A 1 454 ? 120.326 153.322 96.378  1.00 43.67  ? 454  ARG A CD    1 
ATOM   3427  N  NE    . ARG A 1 454 ? 120.329 152.485 97.571  1.00 44.68  ? 454  ARG A NE    1 
ATOM   3428  C  CZ    . ARG A 1 454 ? 121.169 152.631 98.585  1.00 52.08  ? 454  ARG A CZ    1 
ATOM   3429  N  NH1   . ARG A 1 454 ? 122.100 153.572 98.582  1.00 49.31  ? 454  ARG A NH1   1 
ATOM   3430  N  NH2   . ARG A 1 454 ? 121.073 151.814 99.630  1.00 52.29  ? 454  ARG A NH2   1 
ATOM   3431  N  N     . VAL A 1 455 ? 115.039 150.909 96.184  1.00 42.86  ? 455  VAL A N     1 
ATOM   3432  C  CA    . VAL A 1 455 ? 113.787 150.535 96.830  1.00 36.84  ? 455  VAL A CA    1 
ATOM   3433  C  C     . VAL A 1 455 ? 113.890 150.742 98.336  1.00 41.94  ? 455  VAL A C     1 
ATOM   3434  O  O     . VAL A 1 455 ? 114.893 150.383 98.969  1.00 43.15  ? 455  VAL A O     1 
ATOM   3435  C  CB    . VAL A 1 455 ? 113.420 149.084 96.471  1.00 33.77  ? 455  VAL A CB    1 
ATOM   3436  C  CG1   . VAL A 1 455 ? 112.600 148.437 97.566  1.00 37.53  ? 455  VAL A CG1   1 
ATOM   3437  C  CG2   . VAL A 1 455 ? 112.642 149.055 95.172  1.00 37.31  ? 455  VAL A CG2   1 
ATOM   3438  N  N     . LEU A 1 456 ? 112.853 151.349 98.913  1.00 50.79  ? 456  LEU A N     1 
ATOM   3439  C  CA    . LEU A 1 456 ? 112.790 151.612 100.345 1.00 50.51  ? 456  LEU A CA    1 
ATOM   3440  C  C     . LEU A 1 456 ? 112.170 150.416 101.055 1.00 52.93  ? 456  LEU A C     1 
ATOM   3441  O  O     . LEU A 1 456 ? 111.008 150.075 100.810 1.00 46.82  ? 456  LEU A O     1 
ATOM   3442  C  CB    . LEU A 1 456 ? 111.981 152.876 100.622 1.00 47.59  ? 456  LEU A CB    1 
ATOM   3443  C  CG    . LEU A 1 456 ? 112.515 154.159 99.991  1.00 51.49  ? 456  LEU A CG    1 
ATOM   3444  C  CD1   . LEU A 1 456 ? 111.556 155.311 100.233 1.00 51.64  ? 456  LEU A CD1   1 
ATOM   3445  C  CD2   . LEU A 1 456 ? 113.894 154.482 100.539 1.00 51.08  ? 456  LEU A CD2   1 
ATOM   3446  N  N     . VAL A 1 457 ? 112.947 149.780 101.934 1.00 52.15  ? 457  VAL A N     1 
ATOM   3447  C  CA    . VAL A 1 457 ? 112.493 148.631 102.706 1.00 48.31  ? 457  VAL A CA    1 
ATOM   3448  C  C     . VAL A 1 457 ? 112.958 148.773 104.147 1.00 50.61  ? 457  VAL A C     1 
ATOM   3449  O  O     . VAL A 1 457 ? 113.886 149.522 104.457 1.00 49.99  ? 457  VAL A O     1 
ATOM   3450  C  CB    . VAL A 1 457 ? 113.006 147.295 102.130 1.00 43.81  ? 457  VAL A CB    1 
ATOM   3451  C  CG1   . VAL A 1 457 ? 112.268 146.947 100.863 1.00 46.95  ? 457  VAL A CG1   1 
ATOM   3452  C  CG2   . VAL A 1 457 ? 114.503 147.373 101.880 1.00 44.71  ? 457  VAL A CG2   1 
ATOM   3453  N  N     . ASP A 1 458 ? 112.287 148.041 105.030 1.00 52.83  ? 458  ASP A N     1 
ATOM   3454  C  CA    . ASP A 1 458 ? 112.777 147.868 106.388 1.00 48.11  ? 458  ASP A CA    1 
ATOM   3455  C  C     . ASP A 1 458 ? 114.131 147.172 106.352 1.00 47.20  ? 458  ASP A C     1 
ATOM   3456  O  O     . ASP A 1 458 ? 114.364 146.283 105.533 1.00 49.55  ? 458  ASP A O     1 
ATOM   3457  C  CB    . ASP A 1 458 ? 111.774 147.051 107.201 1.00 44.55  ? 458  ASP A CB    1 
ATOM   3458  C  CG    . ASP A 1 458 ? 112.230 146.806 108.621 1.00 52.37  ? 458  ASP A CG    1 
ATOM   3459  O  OD1   . ASP A 1 458 ? 113.041 147.602 109.140 1.00 55.57  ? 458  ASP A OD1   1 
ATOM   3460  O  OD2   . ASP A 1 458 ? 111.779 145.807 109.218 1.00 53.92  ? 458  ASP A OD2   1 
ATOM   3461  N  N     . GLU A 1 459 ? 115.041 147.595 107.229 1.00 50.93  ? 459  GLU A N     1 
ATOM   3462  C  CA    . GLU A 1 459 ? 116.392 147.046 107.184 1.00 53.31  ? 459  GLU A CA    1 
ATOM   3463  C  C     . GLU A 1 459 ? 116.405 145.567 107.550 1.00 56.76  ? 459  GLU A C     1 
ATOM   3464  O  O     . GLU A 1 459 ? 117.103 144.771 106.910 1.00 56.49  ? 459  GLU A O     1 
ATOM   3465  C  CB    . GLU A 1 459 ? 117.316 147.838 108.106 1.00 57.37  ? 459  GLU A CB    1 
ATOM   3466  C  CG    . GLU A 1 459 ? 118.743 147.955 107.593 1.00 58.73  ? 459  GLU A CG    1 
ATOM   3467  C  CD    . GLU A 1 459 ? 119.460 146.621 107.530 1.00 61.77  ? 459  GLU A CD    1 
ATOM   3468  O  OE1   . GLU A 1 459 ? 119.317 145.821 108.478 1.00 59.80  ? 459  GLU A OE1   1 
ATOM   3469  O  OE2   . GLU A 1 459 ? 120.163 146.369 106.530 1.00 61.02  ? 459  GLU A OE2   1 
ATOM   3470  N  N     . VAL A 1 460 ? 115.639 145.176 108.566 1.00 53.20  ? 460  VAL A N     1 
ATOM   3471  C  CA    . VAL A 1 460 ? 115.655 143.786 109.013 1.00 46.39  ? 460  VAL A CA    1 
ATOM   3472  C  C     . VAL A 1 460 ? 114.886 142.904 108.039 1.00 39.59  ? 460  VAL A C     1 
ATOM   3473  O  O     . VAL A 1 460 ? 115.446 141.990 107.424 1.00 40.60  ? 460  VAL A O     1 
ATOM   3474  C  CB    . VAL A 1 460 ? 115.091 143.672 110.439 1.00 43.92  ? 460  VAL A CB    1 
ATOM   3475  C  CG1   . VAL A 1 460 ? 114.946 142.216 110.832 1.00 43.11  ? 460  VAL A CG1   1 
ATOM   3476  C  CG2   . VAL A 1 460 ? 115.989 144.399 111.420 1.00 43.43  ? 460  VAL A CG2   1 
ATOM   3477  N  N     . THR A 1 461 ? 113.591 143.175 107.874 1.00 39.15  ? 461  THR A N     1 
ATOM   3478  C  CA    . THR A 1 461 ? 112.729 142.301 107.091 1.00 38.60  ? 461  THR A CA    1 
ATOM   3479  C  C     . THR A 1 461 ? 112.922 142.453 105.588 1.00 43.59  ? 461  THR A C     1 
ATOM   3480  O  O     . THR A 1 461 ? 112.568 141.533 104.843 1.00 40.92  ? 461  THR A O     1 
ATOM   3481  C  CB    . THR A 1 461 ? 111.264 142.558 107.446 1.00 43.35  ? 461  THR A CB    1 
ATOM   3482  O  OG1   . THR A 1 461 ? 110.953 143.940 107.233 1.00 42.72  ? 461  THR A OG1   1 
ATOM   3483  C  CG2   . THR A 1 461 ? 111.005 142.212 108.900 1.00 43.40  ? 461  THR A CG2   1 
ATOM   3484  N  N     . LEU A 1 462 ? 113.474 143.581 105.132 1.00 44.72  ? 462  LEU A N     1 
ATOM   3485  C  CA    . LEU A 1 462 ? 113.643 143.884 103.708 1.00 35.58  ? 462  LEU A CA    1 
ATOM   3486  C  C     . LEU A 1 462 ? 112.319 143.833 102.953 1.00 35.45  ? 462  LEU A C     1 
ATOM   3487  O  O     . LEU A 1 462 ? 112.277 143.460 101.779 1.00 41.88  ? 462  LEU A O     1 
ATOM   3488  C  CB    . LEU A 1 462 ? 114.673 142.959 103.051 1.00 31.69  ? 462  LEU A CB    1 
ATOM   3489  C  CG    . LEU A 1 462 ? 116.119 143.099 103.525 1.00 30.63  ? 462  LEU A CG    1 
ATOM   3490  C  CD1   . LEU A 1 462 ? 117.043 142.251 102.674 1.00 31.96  ? 462  LEU A CD1   1 
ATOM   3491  C  CD2   . LEU A 1 462 ? 116.555 144.551 103.499 1.00 42.10  ? 462  LEU A CD2   1 
ATOM   3492  N  N     . GLN A 1 463 ? 111.233 144.220 103.614 1.00 35.91  ? 463  GLN A N     1 
ATOM   3493  C  CA    . GLN A 1 463 ? 109.897 144.142 103.043 1.00 36.99  ? 463  GLN A CA    1 
ATOM   3494  C  C     . GLN A 1 463 ? 109.438 145.521 102.591 1.00 42.26  ? 463  GLN A C     1 
ATOM   3495  O  O     . GLN A 1 463 ? 109.606 146.509 103.311 1.00 54.16  ? 463  GLN A O     1 
ATOM   3496  C  CB    . GLN A 1 463 ? 108.906 143.567 104.054 1.00 34.59  ? 463  GLN A CB    1 
ATOM   3497  C  CG    . GLN A 1 463 ? 107.564 143.209 103.460 1.00 40.17  ? 463  GLN A CG    1 
ATOM   3498  C  CD    . GLN A 1 463 ? 106.605 142.671 104.495 1.00 47.69  ? 463  GLN A CD    1 
ATOM   3499  O  OE1   . GLN A 1 463 ? 106.833 142.809 105.696 1.00 48.16  ? 463  GLN A OE1   1 
ATOM   3500  N  NE2   . GLN A 1 463 ? 105.526 142.051 104.037 1.00 46.08  ? 463  GLN A NE2   1 
ATOM   3501  N  N     . THR A 1 464 ? 108.857 145.582 101.395 1.00 46.72  ? 464  THR A N     1 
ATOM   3502  C  CA    . THR A 1 464 ? 108.473 146.853 100.804 1.00 49.78  ? 464  THR A CA    1 
ATOM   3503  C  C     . THR A 1 464 ? 107.148 147.336 101.385 1.00 49.59  ? 464  THR A C     1 
ATOM   3504  O  O     . THR A 1 464 ? 106.571 146.730 102.292 1.00 50.83  ? 464  THR A O     1 
ATOM   3505  C  CB    . THR A 1 464 ? 108.368 146.733 99.286  1.00 51.78  ? 464  THR A CB    1 
ATOM   3506  O  OG1   . THR A 1 464 ? 107.159 146.045 98.946  1.00 56.52  ? 464  THR A OG1   1 
ATOM   3507  C  CG2   . THR A 1 464 ? 109.549 145.965 98.723  1.00 49.62  ? 464  THR A CG2   1 
ATOM   3508  N  N     . ASN A 1 465 ? 106.657 148.451 100.845 1.00 53.05  ? 465  ASN A N     1 
ATOM   3509  C  CA    . ASN A 1 465 ? 105.372 148.997 101.254 1.00 56.88  ? 465  ASN A CA    1 
ATOM   3510  C  C     . ASN A 1 465 ? 104.197 148.176 100.747 1.00 54.90  ? 465  ASN A C     1 
ATOM   3511  O  O     . ASN A 1 465 ? 103.067 148.404 101.190 1.00 54.99  ? 465  ASN A O     1 
ATOM   3512  C  CB    . ASN A 1 465 ? 105.249 150.439 100.772 1.00 57.73  ? 465  ASN A CB    1 
ATOM   3513  C  CG    . ASN A 1 465 ? 106.309 151.337 101.369 1.00 57.52  ? 465  ASN A CG    1 
ATOM   3514  O  OD1   . ASN A 1 465 ? 107.482 151.253 101.007 1.00 58.42  ? 465  ASN A OD1   1 
ATOM   3515  N  ND2   . ASN A 1 465 ? 105.904 152.203 102.290 1.00 55.77  ? 465  ASN A ND2   1 
ATOM   3516  N  N     . LYS A 1 466 ? 104.432 147.240 99.836  1.00 47.88  ? 466  LYS A N     1 
ATOM   3517  C  CA    . LYS A 1 466 ? 103.410 146.315 99.373  1.00 50.32  ? 466  LYS A CA    1 
ATOM   3518  C  C     . LYS A 1 466 ? 103.609 144.980 100.076 1.00 51.53  ? 466  LYS A C     1 
ATOM   3519  O  O     . LYS A 1 466 ? 104.706 144.413 100.041 1.00 51.81  ? 466  LYS A O     1 
ATOM   3520  C  CB    . LYS A 1 466 ? 103.482 146.146 97.856  1.00 47.89  ? 466  LYS A CB    1 
ATOM   3521  C  CG    . LYS A 1 466 ? 102.232 145.567 97.229  1.00 48.03  ? 466  LYS A CG    1 
ATOM   3522  C  CD    . LYS A 1 466 ? 102.107 145.973 95.766  1.00 51.50  ? 466  LYS A CD    1 
ATOM   3523  C  CE    . LYS A 1 466 ? 101.342 147.280 95.594  1.00 55.44  ? 466  LYS A CE    1 
ATOM   3524  N  NZ    . LYS A 1 466 ? 102.080 148.473 96.093  1.00 52.01  ? 466  LYS A NZ    1 
ATOM   3525  N  N     . GLU A 1 467 ? 102.557 144.494 100.727 1.00 48.55  ? 467  GLU A N     1 
ATOM   3526  C  CA    . GLU A 1 467 ? 102.672 143.296 101.546 1.00 46.49  ? 467  GLU A CA    1 
ATOM   3527  C  C     . GLU A 1 467 ? 102.949 142.071 100.686 1.00 46.21  ? 467  GLU A C     1 
ATOM   3528  O  O     . GLU A 1 467 ? 102.339 141.878 99.631  1.00 45.18  ? 467  GLU A O     1 
ATOM   3529  C  CB    . GLU A 1 467 ? 101.398 143.091 102.362 1.00 48.91  ? 467  GLU A CB    1 
ATOM   3530  C  CG    . GLU A 1 467 ? 101.112 144.217 103.340 1.00 50.63  ? 467  GLU A CG    1 
ATOM   3531  C  CD    . GLU A 1 467 ? 99.847  143.984 104.141 1.00 52.81  ? 467  GLU A CD    1 
ATOM   3532  O  OE1   . GLU A 1 467 ? 99.187  142.946 103.925 1.00 51.41  ? 467  GLU A OE1   1 
ATOM   3533  O  OE2   . GLU A 1 467 ? 99.512  144.840 104.987 1.00 49.51  ? 467  GLU A OE2   1 
ATOM   3534  N  N     . GLY A 1 468 ? 103.870 141.234 101.153 1.00 45.99  ? 468  GLY A N     1 
ATOM   3535  C  CA    . GLY A 1 468 ? 104.317 140.083 100.404 1.00 43.66  ? 468  GLY A CA    1 
ATOM   3536  C  C     . GLY A 1 468 ? 105.485 140.339 99.480  1.00 44.40  ? 468  GLY A C     1 
ATOM   3537  O  O     . GLY A 1 468 ? 105.990 139.387 98.873  1.00 44.78  ? 468  GLY A O     1 
ATOM   3538  N  N     . VAL A 1 469 ? 105.939 141.582 99.360  1.00 41.10  ? 469  VAL A N     1 
ATOM   3539  C  CA    . VAL A 1 469 ? 106.998 141.956 98.431  1.00 32.50  ? 469  VAL A CA    1 
ATOM   3540  C  C     . VAL A 1 469 ? 108.255 142.262 99.230  1.00 32.79  ? 469  VAL A C     1 
ATOM   3541  O  O     . VAL A 1 469 ? 108.259 143.157 100.084 1.00 35.43  ? 469  VAL A O     1 
ATOM   3542  C  CB    . VAL A 1 469 ? 106.596 143.157 97.563  1.00 31.13  ? 469  VAL A CB    1 
ATOM   3543  C  CG1   . VAL A 1 469 ? 107.714 143.509 96.604  1.00 33.73  ? 469  VAL A CG1   1 
ATOM   3544  C  CG2   . VAL A 1 469 ? 105.316 142.865 96.805  1.00 36.81  ? 469  VAL A CG2   1 
ATOM   3545  N  N     . PHE A 1 470 ? 109.318 141.519 98.948  1.00 34.33  ? 470  PHE A N     1 
ATOM   3546  C  CA    . PHE A 1 470 ? 110.639 141.748 99.507  1.00 29.96  ? 470  PHE A CA    1 
ATOM   3547  C  C     . PHE A 1 470 ? 111.580 142.175 98.389  1.00 26.04  ? 470  PHE A C     1 
ATOM   3548  O  O     . PHE A 1 470 ? 111.289 141.996 97.204  1.00 35.95  ? 470  PHE A O     1 
ATOM   3549  C  CB    . PHE A 1 470 ? 111.172 140.490 100.202 1.00 27.46  ? 470  PHE A CB    1 
ATOM   3550  C  CG    . PHE A 1 470 ? 110.331 140.031 101.362 1.00 25.97  ? 470  PHE A CG    1 
ATOM   3551  C  CD1   . PHE A 1 470 ? 109.176 139.297 101.154 1.00 29.22  ? 470  PHE A CD1   1 
ATOM   3552  C  CD2   . PHE A 1 470 ? 110.702 140.323 102.659 1.00 25.73  ? 470  PHE A CD2   1 
ATOM   3553  C  CE1   . PHE A 1 470 ? 108.405 138.872 102.217 1.00 31.40  ? 470  PHE A CE1   1 
ATOM   3554  C  CE2   . PHE A 1 470 ? 109.934 139.901 103.724 1.00 33.58  ? 470  PHE A CE2   1 
ATOM   3555  C  CZ    . PHE A 1 470 ? 108.783 139.173 103.501 1.00 32.22  ? 470  PHE A CZ    1 
ATOM   3556  N  N     . ALA A 1 471 ? 112.716 142.751 98.770  1.00 21.11  ? 471  ALA A N     1 
ATOM   3557  C  CA    . ALA A 1 471 ? 113.647 143.253 97.774  1.00 29.60  ? 471  ALA A CA    1 
ATOM   3558  C  C     . ALA A 1 471 ? 115.063 143.222 98.327  1.00 24.97  ? 471  ALA A C     1 
ATOM   3559  O  O     . ALA A 1 471 ? 115.280 143.163 99.539  1.00 40.13  ? 471  ALA A O     1 
ATOM   3560  C  CB    . ALA A 1 471 ? 113.273 144.669 97.325  1.00 31.35  ? 471  ALA A CB    1 
ATOM   3561  N  N     . GLY A 1 472 ? 116.024 143.260 97.414  1.00 17.29  ? 472  GLY A N     1 
ATOM   3562  C  CA    . GLY A 1 472 ? 117.425 143.208 97.784  1.00 24.34  ? 472  GLY A CA    1 
ATOM   3563  C  C     . GLY A 1 472 ? 118.285 143.244 96.543  1.00 29.90  ? 472  GLY A C     1 
ATOM   3564  O  O     . GLY A 1 472 ? 117.789 143.316 95.415  1.00 33.27  ? 472  GLY A O     1 
ATOM   3565  N  N     . GLY A 1 473 ? 119.595 143.183 96.766  1.00 19.83  ? 473  GLY A N     1 
ATOM   3566  C  CA    . GLY A 1 473 ? 120.539 143.244 95.670  1.00 22.66  ? 473  GLY A CA    1 
ATOM   3567  C  C     . GLY A 1 473 ? 120.892 144.669 95.302  1.00 36.04  ? 473  GLY A C     1 
ATOM   3568  O  O     . GLY A 1 473 ? 120.883 145.550 96.165  1.00 39.73  ? 473  GLY A O     1 
ATOM   3569  N  N     . ASP A 1 474 ? 121.217 144.907 94.028  1.00 34.51  ? 474  ASP A N     1 
ATOM   3570  C  CA    . ASP A 1 474 ? 121.496 146.264 93.570  1.00 23.80  ? 474  ASP A CA    1 
ATOM   3571  C  C     . ASP A 1 474 ? 120.251 147.140 93.568  1.00 28.22  ? 474  ASP A C     1 
ATOM   3572  O  O     . ASP A 1 474 ? 120.372 148.368 93.535  1.00 38.01  ? 474  ASP A O     1 
ATOM   3573  C  CB    . ASP A 1 474 ? 122.110 146.235 92.169  1.00 33.89  ? 474  ASP A CB    1 
ATOM   3574  C  CG    . ASP A 1 474 ? 123.587 145.892 92.185  1.00 36.60  ? 474  ASP A CG    1 
ATOM   3575  O  OD1   . ASP A 1 474 ? 124.146 145.719 93.285  1.00 25.87  ? 474  ASP A OD1   1 
ATOM   3576  O  OD2   . ASP A 1 474 ? 124.192 145.804 91.096  1.00 35.15  ? 474  ASP A OD2   1 
ATOM   3577  N  N     . LEU A 1 475 ? 119.062 146.536 93.590  1.00 29.25  ? 475  LEU A N     1 
ATOM   3578  C  CA    . LEU A 1 475 ? 117.832 147.316 93.663  1.00 23.15  ? 475  LEU A CA    1 
ATOM   3579  C  C     . LEU A 1 475 ? 117.741 148.083 94.976  1.00 33.81  ? 475  LEU A C     1 
ATOM   3580  O  O     . LEU A 1 475 ? 117.315 149.243 94.999  1.00 38.89  ? 475  LEU A O     1 
ATOM   3581  C  CB    . LEU A 1 475 ? 116.626 146.395 93.491  1.00 22.77  ? 475  LEU A CB    1 
ATOM   3582  C  CG    . LEU A 1 475 ? 115.246 147.040 93.576  1.00 26.48  ? 475  LEU A CG    1 
ATOM   3583  C  CD1   . LEU A 1 475 ? 115.130 148.163 92.577  1.00 30.14  ? 475  LEU A CD1   1 
ATOM   3584  C  CD2   . LEU A 1 475 ? 114.163 146.013 93.340  1.00 27.64  ? 475  LEU A CD2   1 
ATOM   3585  N  N     . VAL A 1 476 ? 118.139 147.456 96.078  1.00 32.53  ? 476  VAL A N     1 
ATOM   3586  C  CA    . VAL A 1 476 ? 118.076 148.098 97.387  1.00 25.55  ? 476  VAL A CA    1 
ATOM   3587  C  C     . VAL A 1 476 ? 119.402 148.750 97.754  1.00 32.24  ? 476  VAL A C     1 
ATOM   3588  O  O     . VAL A 1 476 ? 119.443 149.916 98.151  1.00 37.90  ? 476  VAL A O     1 
ATOM   3589  C  CB    . VAL A 1 476 ? 117.640 147.072 98.454  1.00 26.02  ? 476  VAL A CB    1 
ATOM   3590  C  CG1   . VAL A 1 476 ? 117.766 147.665 99.845  1.00 30.09  ? 476  VAL A CG1   1 
ATOM   3591  C  CG2   . VAL A 1 476 ? 116.219 146.630 98.200  1.00 31.52  ? 476  VAL A CG2   1 
ATOM   3592  N  N     . LEU A 1 477 ? 120.504 148.018 97.621  1.00 25.79  ? 477  LEU A N     1 
ATOM   3593  C  CA    . LEU A 1 477 ? 121.806 148.480 98.080  1.00 24.67  ? 477  LEU A CA    1 
ATOM   3594  C  C     . LEU A 1 477 ? 122.549 149.317 97.049  1.00 29.62  ? 477  LEU A C     1 
ATOM   3595  O  O     . LEU A 1 477 ? 123.625 149.836 97.360  1.00 30.78  ? 477  LEU A O     1 
ATOM   3596  C  CB    . LEU A 1 477 ? 122.676 147.288 98.480  1.00 26.98  ? 477  LEU A CB    1 
ATOM   3597  C  CG    . LEU A 1 477 ? 122.057 146.255 99.417  1.00 28.51  ? 477  LEU A CG    1 
ATOM   3598  C  CD1   . LEU A 1 477 ? 123.103 145.228 99.801  1.00 26.06  ? 477  LEU A CD1   1 
ATOM   3599  C  CD2   . LEU A 1 477 ? 121.473 146.918 100.651 1.00 27.43  ? 477  LEU A CD2   1 
ATOM   3600  N  N     . GLY A 1 478 ? 122.018 149.457 95.839  1.00 28.76  ? 478  GLY A N     1 
ATOM   3601  C  CA    . GLY A 1 478 ? 122.656 150.260 94.824  1.00 29.54  ? 478  GLY A CA    1 
ATOM   3602  C  C     . GLY A 1 478 ? 123.895 149.600 94.256  1.00 28.81  ? 478  GLY A C     1 
ATOM   3603  O  O     . GLY A 1 478 ? 123.826 148.548 93.617  1.00 28.70  ? 478  GLY A O     1 
ATOM   3604  N  N     . PRO A 1 479 ? 125.056 150.213 94.466  1.00 32.45  ? 479  PRO A N     1 
ATOM   3605  C  CA    . PRO A 1 479 ? 126.321 149.609 93.995  1.00 28.79  ? 479  PRO A CA    1 
ATOM   3606  C  C     . PRO A 1 479 ? 126.861 148.550 94.955  1.00 27.16  ? 479  PRO A C     1 
ATOM   3607  O  O     . PRO A 1 479 ? 127.748 148.777 95.777  1.00 20.21  ? 479  PRO A O     1 
ATOM   3608  C  CB    . PRO A 1 479 ? 127.249 150.821 93.893  1.00 28.43  ? 479  PRO A CB    1 
ATOM   3609  C  CG    . PRO A 1 479 ? 126.756 151.746 94.958  1.00 31.87  ? 479  PRO A CG    1 
ATOM   3610  C  CD    . PRO A 1 479 ? 125.261 151.557 95.034  1.00 32.06  ? 479  PRO A CD    1 
ATOM   3611  N  N     . SER A 1 480 ? 126.312 147.345 94.850  1.00 29.26  ? 480  SER A N     1 
ATOM   3612  C  CA    . SER A 1 480 ? 126.680 146.233 95.712  1.00 19.73  ? 480  SER A CA    1 
ATOM   3613  C  C     . SER A 1 480 ? 127.512 145.219 94.935  1.00 21.12  ? 480  SER A C     1 
ATOM   3614  O  O     . SER A 1 480 ? 127.812 145.395 93.752  1.00 31.96  ? 480  SER A O     1 
ATOM   3615  C  CB    . SER A 1 480 ? 125.433 145.573 96.302  1.00 20.82  ? 480  SER A CB    1 
ATOM   3616  O  OG    . SER A 1 480 ? 124.694 144.902 95.298  1.00 5.70   ? 480  SER A OG    1 
ATOM   3617  N  N     . THR A 1 481 ? 127.885 144.146 95.620  1.00 15.10  ? 481  THR A N     1 
ATOM   3618  C  CA    . THR A 1 481 ? 128.681 143.069 95.054  1.00 18.40  ? 481  THR A CA    1 
ATOM   3619  C  C     . THR A 1 481 ? 127.823 141.816 94.914  1.00 13.85  ? 481  THR A C     1 
ATOM   3620  O  O     . THR A 1 481 ? 126.636 141.803 95.246  1.00 15.15  ? 481  THR A O     1 
ATOM   3621  C  CB    . THR A 1 481 ? 129.917 142.799 95.916  1.00 13.68  ? 481  THR A CB    1 
ATOM   3622  O  OG1   . THR A 1 481 ? 129.510 142.419 97.234  1.00 18.13  ? 481  THR A OG1   1 
ATOM   3623  C  CG2   . THR A 1 481 ? 130.792 144.036 96.001  1.00 18.39  ? 481  THR A CG2   1 
ATOM   3624  N  N     . VAL A 1 482 ? 128.437 140.754 94.392  1.00 21.44  ? 482  VAL A N     1 
ATOM   3625  C  CA    . VAL A 1 482 ? 127.729 139.487 94.258  1.00 16.26  ? 482  VAL A CA    1 
ATOM   3626  C  C     . VAL A 1 482 ? 127.432 138.895 95.629  1.00 18.33  ? 482  VAL A C     1 
ATOM   3627  O  O     . VAL A 1 482 ? 126.329 138.397 95.881  1.00 27.63  ? 482  VAL A O     1 
ATOM   3628  C  CB    . VAL A 1 482 ? 128.539 138.511 93.385  1.00 6.64   ? 482  VAL A CB    1 
ATOM   3629  C  CG1   . VAL A 1 482 ? 127.778 137.212 93.193  1.00 7.97   ? 482  VAL A CG1   1 
ATOM   3630  C  CG2   . VAL A 1 482 ? 128.866 139.142 92.047  1.00 22.01  ? 482  VAL A CG2   1 
ATOM   3631  N  N     . ILE A 1 483 ? 128.408 138.941 96.536  1.00 18.71  ? 483  ILE A N     1 
ATOM   3632  C  CA    . ILE A 1 483 ? 128.229 138.304 97.835  1.00 14.63  ? 483  ILE A CA    1 
ATOM   3633  C  C     . ILE A 1 483 ? 127.217 139.072 98.680  1.00 23.72  ? 483  ILE A C     1 
ATOM   3634  O  O     . ILE A 1 483 ? 126.418 138.470 99.404  1.00 28.37  ? 483  ILE A O     1 
ATOM   3635  C  CB    . ILE A 1 483 ? 129.584 138.140 98.549  1.00 15.48  ? 483  ILE A CB    1 
ATOM   3636  C  CG1   . ILE A 1 483 ? 129.394 137.411 99.878  1.00 16.24  ? 483  ILE A CG1   1 
ATOM   3637  C  CG2   . ILE A 1 483 ? 130.284 139.474 98.725  1.00 17.18  ? 483  ILE A CG2   1 
ATOM   3638  C  CD1   . ILE A 1 483 ? 128.709 136.071 99.723  1.00 17.51  ? 483  ILE A CD1   1 
ATOM   3639  N  N     . GLU A 1 484 ? 127.224 140.404 98.599  1.00 22.75  ? 484  GLU A N     1 
ATOM   3640  C  CA    . GLU A 1 484 ? 126.237 141.185 99.341  1.00 13.13  ? 484  GLU A CA    1 
ATOM   3641  C  C     . GLU A 1 484 ? 124.828 140.925 98.822  1.00 18.70  ? 484  GLU A C     1 
ATOM   3642  O  O     . GLU A 1 484 ? 123.876 140.837 99.607  1.00 25.82  ? 484  GLU A O     1 
ATOM   3643  C  CB    . GLU A 1 484 ? 126.580 142.671 99.265  1.00 12.33  ? 484  GLU A CB    1 
ATOM   3644  C  CG    . GLU A 1 484 ? 127.896 143.029 99.925  1.00 18.62  ? 484  GLU A CG    1 
ATOM   3645  C  CD    . GLU A 1 484 ? 128.261 144.486 99.746  1.00 32.35  ? 484  GLU A CD    1 
ATOM   3646  O  OE1   . GLU A 1 484 ? 127.429 145.248 99.215  1.00 30.42  ? 484  GLU A OE1   1 
ATOM   3647  O  OE2   . GLU A 1 484 ? 129.381 144.871 100.137 1.00 38.49  ? 484  GLU A OE2   1 
ATOM   3648  N  N     . SER A 1 485 ? 124.678 140.789 97.504  1.00 21.46  ? 485  SER A N     1 
ATOM   3649  C  CA    . SER A 1 485 ? 123.374 140.470 96.936  1.00 15.98  ? 485  SER A CA    1 
ATOM   3650  C  C     . SER A 1 485 ? 122.919 139.073 97.337  1.00 17.81  ? 485  SER A C     1 
ATOM   3651  O  O     . SER A 1 485 ? 121.736 138.859 97.620  1.00 27.12  ? 485  SER A O     1 
ATOM   3652  C  CB    . SER A 1 485 ? 123.419 140.613 95.418  1.00 22.16  ? 485  SER A CB    1 
ATOM   3653  O  OG    . SER A 1 485 ? 123.773 141.935 95.058  1.00 34.31  ? 485  SER A OG    1 
ATOM   3654  N  N     . ILE A 1 486 ? 123.844 138.111 97.374  1.00 22.30  ? 486  ILE A N     1 
ATOM   3655  C  CA    . ILE A 1 486 ? 123.499 136.764 97.823  1.00 24.67  ? 486  ILE A CA    1 
ATOM   3656  C  C     . ILE A 1 486 ? 123.100 136.776 99.295  1.00 23.08  ? 486  ILE A C     1 
ATOM   3657  O  O     . ILE A 1 486 ? 122.180 136.063 99.709  1.00 28.95  ? 486  ILE A O     1 
ATOM   3658  C  CB    . ILE A 1 486 ? 124.668 135.798 97.552  1.00 30.18  ? 486  ILE A CB    1 
ATOM   3659  C  CG1   . ILE A 1 486 ? 124.838 135.573 96.051  1.00 20.47  ? 486  ILE A CG1   1 
ATOM   3660  C  CG2   . ILE A 1 486 ? 124.455 134.466 98.247  1.00 25.13  ? 486  ILE A CG2   1 
ATOM   3661  C  CD1   . ILE A 1 486 ? 126.093 134.830 95.693  1.00 12.99  ? 486  ILE A CD1   1 
ATOM   3662  N  N     . ALA A 1 487 ? 123.781 137.589 100.107 1.00 17.43  ? 487  ALA A N     1 
ATOM   3663  C  CA    . ALA A 1 487 ? 123.424 137.707 101.518 1.00 22.92  ? 487  ALA A CA    1 
ATOM   3664  C  C     . ALA A 1 487 ? 122.034 138.306 101.692 1.00 26.23  ? 487  ALA A C     1 
ATOM   3665  O  O     . ALA A 1 487 ? 121.241 137.829 102.514 1.00 27.71  ? 487  ALA A O     1 
ATOM   3666  C  CB    . ALA A 1 487 ? 124.469 138.548 102.249 1.00 18.59  ? 487  ALA A CB    1 
ATOM   3667  N  N     . THR A 1 488 ? 121.717 139.350 100.920 1.00 24.49  ? 488  THR A N     1 
ATOM   3668  C  CA    . THR A 1 488 ? 120.378 139.929 100.976 1.00 20.35  ? 488  THR A CA    1 
ATOM   3669  C  C     . THR A 1 488 ? 119.327 138.937 100.493 1.00 17.86  ? 488  THR A C     1 
ATOM   3670  O  O     . THR A 1 488 ? 118.220 138.884 101.036 1.00 28.55  ? 488  THR A O     1 
ATOM   3671  C  CB    . THR A 1 488 ? 120.312 141.217 100.155 1.00 18.82  ? 488  THR A CB    1 
ATOM   3672  O  OG1   . THR A 1 488 ? 120.756 140.961 98.818  1.00 29.23  ? 488  THR A OG1   1 
ATOM   3673  C  CG2   . THR A 1 488 ? 121.181 142.287 100.777 1.00 24.17  ? 488  THR A CG2   1 
ATOM   3674  N  N     . GLY A 1 489 ? 119.658 138.135 99.479  1.00 18.40  ? 489  GLY A N     1 
ATOM   3675  C  CA    . GLY A 1 489 ? 118.727 137.118 99.016  1.00 17.73  ? 489  GLY A CA    1 
ATOM   3676  C  C     . GLY A 1 489 ? 118.486 136.021 100.036 1.00 22.40  ? 489  GLY A C     1 
ATOM   3677  O  O     . GLY A 1 489 ? 117.362 135.541 100.189 1.00 28.98  ? 489  GLY A O     1 
ATOM   3678  N  N     . ARG A 1 490 ? 119.537 135.601 100.742 1.00 25.16  ? 490  ARG A N     1 
ATOM   3679  C  CA    . ARG A 1 490 ? 119.367 134.606 101.796 1.00 15.87  ? 490  ARG A CA    1 
ATOM   3680  C  C     . ARG A 1 490 ? 118.542 135.161 102.949 1.00 29.16  ? 490  ARG A C     1 
ATOM   3681  O  O     . ARG A 1 490 ? 117.672 134.467 103.494 1.00 27.88  ? 490  ARG A O     1 
ATOM   3682  C  CB    . ARG A 1 490 ? 120.730 134.128 102.294 1.00 17.39  ? 490  ARG A CB    1 
ATOM   3683  C  CG    . ARG A 1 490 ? 120.633 133.104 103.406 1.00 26.62  ? 490  ARG A CG    1 
ATOM   3684  C  CD    . ARG A 1 490 ? 121.991 132.624 103.871 1.00 21.97  ? 490  ARG A CD    1 
ATOM   3685  N  NE    . ARG A 1 490 ? 121.859 131.640 104.937 1.00 19.79  ? 490  ARG A NE    1 
ATOM   3686  C  CZ    . ARG A 1 490 ? 121.889 131.930 106.230 1.00 25.13  ? 490  ARG A CZ    1 
ATOM   3687  N  NH1   . ARG A 1 490 ? 122.073 133.168 106.656 1.00 29.32  ? 490  ARG A NH1   1 
ATOM   3688  N  NH2   . ARG A 1 490 ? 121.733 130.953 107.117 1.00 26.82  ? 490  ARG A NH2   1 
ATOM   3689  N  N     . ARG A 1 491 ? 118.800 136.415 103.330 1.00 33.50  ? 491  ARG A N     1 
ATOM   3690  C  CA    . ARG A 1 491 ? 117.996 137.063 104.359 1.00 20.84  ? 491  ARG A CA    1 
ATOM   3691  C  C     . ARG A 1 491 ? 116.542 137.170 103.923 1.00 27.95  ? 491  ARG A C     1 
ATOM   3692  O  O     . ARG A 1 491 ? 115.625 136.970 104.727 1.00 33.49  ? 491  ARG A O     1 
ATOM   3693  C  CB    . ARG A 1 491 ? 118.573 138.444 104.667 1.00 19.03  ? 491  ARG A CB    1 
ATOM   3694  C  CG    . ARG A 1 491 ? 118.272 138.969 106.053 1.00 25.35  ? 491  ARG A CG    1 
ATOM   3695  C  CD    . ARG A 1 491 ? 118.849 140.361 106.228 1.00 25.86  ? 491  ARG A CD    1 
ATOM   3696  N  NE    . ARG A 1 491 ? 118.850 140.792 107.619 1.00 26.50  ? 491  ARG A NE    1 
ATOM   3697  C  CZ    . ARG A 1 491 ? 119.914 140.770 108.409 1.00 26.35  ? 491  ARG A CZ    1 
ATOM   3698  N  NH1   . ARG A 1 491 ? 121.088 140.343 107.975 1.00 27.61  ? 491  ARG A NH1   1 
ATOM   3699  N  NH2   . ARG A 1 491 ? 119.798 141.191 109.664 1.00 27.54  ? 491  ARG A NH2   1 
ATOM   3700  N  N     . ALA A 1 492 ? 116.314 137.464 102.642 1.00 26.33  ? 492  ALA A N     1 
ATOM   3701  C  CA    . ALA A 1 492 ? 114.958 137.539 102.119 1.00 25.37  ? 492  ALA A CA    1 
ATOM   3702  C  C     . ALA A 1 492 ? 114.289 136.174 102.082 1.00 21.95  ? 492  ALA A C     1 
ATOM   3703  O  O     . ALA A 1 492 ? 113.078 136.085 102.266 1.00 30.54  ? 492  ALA A O     1 
ATOM   3704  C  CB    . ALA A 1 492 ? 114.968 138.164 100.727 1.00 25.43  ? 492  ALA A CB    1 
ATOM   3705  N  N     . ALA A 1 493 ? 115.049 135.106 101.839 1.00 16.18  ? 493  ALA A N     1 
ATOM   3706  C  CA    . ALA A 1 493 ? 114.473 133.767 101.919 1.00 18.81  ? 493  ALA A CA    1 
ATOM   3707  C  C     . ALA A 1 493 ? 114.073 133.428 103.350 1.00 26.19  ? 493  ALA A C     1 
ATOM   3708  O  O     . ALA A 1 493 ? 113.007 132.842 103.583 1.00 40.57  ? 493  ALA A O     1 
ATOM   3709  C  CB    . ALA A 1 493 ? 115.458 132.735 101.374 1.00 27.89  ? 493  ALA A CB    1 
ATOM   3710  N  N     . ILE A 1 494 ? 114.911 133.807 104.319 1.00 25.11  ? 494  ILE A N     1 
ATOM   3711  C  CA    . ILE A 1 494 ? 114.564 133.628 105.729 1.00 28.89  ? 494  ILE A CA    1 
ATOM   3712  C  C     . ILE A 1 494 ? 113.280 134.383 106.059 1.00 32.25  ? 494  ILE A C     1 
ATOM   3713  O  O     . ILE A 1 494 ? 112.359 133.844 106.687 1.00 29.67  ? 494  ILE A O     1 
ATOM   3714  C  CB    . ILE A 1 494 ? 115.729 134.085 106.626 1.00 26.19  ? 494  ILE A CB    1 
ATOM   3715  C  CG1   . ILE A 1 494 ? 116.981 133.251 106.357 1.00 24.57  ? 494  ILE A CG1   1 
ATOM   3716  C  CG2   . ILE A 1 494 ? 115.341 134.002 108.090 1.00 26.54  ? 494  ILE A CG2   1 
ATOM   3717  C  CD1   . ILE A 1 494 ? 118.227 133.793 107.016 1.00 22.05  ? 494  ILE A CD1   1 
ATOM   3718  N  N     . MET A 1 495 ? 113.192 135.638 105.615 1.00 32.36  ? 495  MET A N     1 
ATOM   3719  C  CA    . MET A 1 495 ? 112.022 136.455 105.922 1.00 24.51  ? 495  MET A CA    1 
ATOM   3720  C  C     . MET A 1 495 ? 110.784 136.001 105.156 1.00 30.17  ? 495  MET A C     1 
ATOM   3721  O  O     . MET A 1 495 ? 109.668 136.156 105.653 1.00 37.56  ? 495  MET A O     1 
ATOM   3722  C  CB    . MET A 1 495 ? 112.318 137.924 105.631 1.00 27.89  ? 495  MET A CB    1 
ATOM   3723  C  CG    . MET A 1 495 ? 113.436 138.501 106.474 1.00 37.74  ? 495  MET A CG    1 
ATOM   3724  S  SD    . MET A 1 495 ? 113.173 138.275 108.239 1.00 57.41  ? 495  MET A SD    1 
ATOM   3725  C  CE    . MET A 1 495 ? 114.675 138.990 108.891 1.00 32.82  ? 495  MET A CE    1 
ATOM   3726  N  N     . ILE A 1 496 ? 110.952 135.441 103.957 1.00 31.27  ? 496  ILE A N     1 
ATOM   3727  C  CA    . ILE A 1 496 ? 109.814 134.919 103.210 1.00 32.13  ? 496  ILE A CA    1 
ATOM   3728  C  C     . ILE A 1 496 ? 109.276 133.664 103.877 1.00 36.71  ? 496  ILE A C     1 
ATOM   3729  O  O     . ILE A 1 496 ? 108.059 133.463 103.964 1.00 47.91  ? 496  ILE A O     1 
ATOM   3730  C  CB    . ILE A 1 496 ? 110.203 134.668 101.740 1.00 29.13  ? 496  ILE A CB    1 
ATOM   3731  C  CG1   . ILE A 1 496 ? 110.079 135.960 100.933 1.00 28.19  ? 496  ILE A CG1   1 
ATOM   3732  C  CG2   . ILE A 1 496 ? 109.345 133.577 101.119 1.00 33.13  ? 496  ILE A CG2   1 
ATOM   3733  C  CD1   . ILE A 1 496 ? 110.241 135.783 99.448  1.00 34.07  ? 496  ILE A CD1   1 
ATOM   3734  N  N     . ASP A 1 497 ? 110.169 132.808 104.375 1.00 32.27  ? 497  ASP A N     1 
ATOM   3735  C  CA    . ASP A 1 497 ? 109.714 131.661 105.149 1.00 36.08  ? 497  ASP A CA    1 
ATOM   3736  C  C     . ASP A 1 497 ? 109.000 132.109 106.420 1.00 43.33  ? 497  ASP A C     1 
ATOM   3737  O  O     . ASP A 1 497 ? 107.967 131.542 106.787 1.00 48.01  ? 497  ASP A O     1 
ATOM   3738  C  CB    . ASP A 1 497 ? 110.889 130.744 105.476 1.00 43.27  ? 497  ASP A CB    1 
ATOM   3739  C  CG    . ASP A 1 497 ? 110.442 129.383 105.961 1.00 50.35  ? 497  ASP A CG    1 
ATOM   3740  O  OD1   . ASP A 1 497 ? 109.625 128.747 105.266 1.00 48.09  ? 497  ASP A OD1   1 
ATOM   3741  O  OD2   . ASP A 1 497 ? 110.909 128.947 107.033 1.00 49.97  ? 497  ASP A OD2   1 
ATOM   3742  N  N     . LEU A 1 498 ? 109.526 133.136 107.093 1.00 40.79  ? 498  LEU A N     1 
ATOM   3743  C  CA    . LEU A 1 498 ? 108.874 133.641 108.301 1.00 40.12  ? 498  LEU A CA    1 
ATOM   3744  C  C     . LEU A 1 498 ? 107.506 134.249 107.998 1.00 41.80  ? 498  LEU A C     1 
ATOM   3745  O  O     . LEU A 1 498 ? 106.553 134.057 108.761 1.00 44.98  ? 498  LEU A O     1 
ATOM   3746  C  CB    . LEU A 1 498 ? 109.772 134.663 108.994 1.00 43.19  ? 498  LEU A CB    1 
ATOM   3747  C  CG    . LEU A 1 498 ? 111.034 134.118 109.663 1.00 37.75  ? 498  LEU A CG    1 
ATOM   3748  C  CD1   . LEU A 1 498 ? 111.917 135.256 110.125 1.00 40.25  ? 498  LEU A CD1   1 
ATOM   3749  C  CD2   . LEU A 1 498 ? 110.680 133.215 110.829 1.00 37.32  ? 498  LEU A CD2   1 
ATOM   3750  N  N     . TYR A 1 499 ? 107.395 134.994 106.897 1.00 37.71  ? 499  TYR A N     1 
ATOM   3751  C  CA    . TYR A 1 499 ? 106.124 135.600 106.513 1.00 45.77  ? 499  TYR A CA    1 
ATOM   3752  C  C     . TYR A 1 499 ? 105.125 134.558 106.032 1.00 46.59  ? 499  TYR A C     1 
ATOM   3753  O  O     . TYR A 1 499 ? 103.912 134.768 106.139 1.00 50.39  ? 499  TYR A O     1 
ATOM   3754  C  CB    . TYR A 1 499 ? 106.368 136.657 105.432 1.00 46.14  ? 499  TYR A CB    1 
ATOM   3755  C  CG    . TYR A 1 499 ? 105.120 137.253 104.810 1.00 47.30  ? 499  TYR A CG    1 
ATOM   3756  C  CD1   . TYR A 1 499 ? 104.455 138.306 105.416 1.00 45.74  ? 499  TYR A CD1   1 
ATOM   3757  C  CD2   . TYR A 1 499 ? 104.626 136.776 103.602 1.00 45.62  ? 499  TYR A CD2   1 
ATOM   3758  C  CE1   . TYR A 1 499 ? 103.323 138.856 104.847 1.00 45.89  ? 499  TYR A CE1   1 
ATOM   3759  C  CE2   . TYR A 1 499 ? 103.497 137.319 103.027 1.00 46.81  ? 499  TYR A CE2   1 
ATOM   3760  C  CZ    . TYR A 1 499 ? 102.850 138.358 103.653 1.00 48.40  ? 499  TYR A CZ    1 
ATOM   3761  O  OH    . TYR A 1 499 ? 101.723 138.905 103.084 1.00 48.84  ? 499  TYR A OH    1 
ATOM   3762  N  N     . LEU A 1 500 ? 105.610 133.434 105.502 1.00 37.28  ? 500  LEU A N     1 
ATOM   3763  C  CA    . LEU A 1 500 ? 104.710 132.397 105.012 1.00 39.88  ? 500  LEU A CA    1 
ATOM   3764  C  C     . LEU A 1 500 ? 104.027 131.650 106.148 1.00 43.07  ? 500  LEU A C     1 
ATOM   3765  O  O     . LEU A 1 500 ? 102.897 131.180 105.982 1.00 46.64  ? 500  LEU A O     1 
ATOM   3766  C  CB    . LEU A 1 500 ? 105.473 131.421 104.122 1.00 44.46  ? 500  LEU A CB    1 
ATOM   3767  C  CG    . LEU A 1 500 ? 105.012 131.359 102.670 1.00 47.49  ? 500  LEU A CG    1 
ATOM   3768  C  CD1   . LEU A 1 500 ? 104.751 132.760 102.142 1.00 47.85  ? 500  LEU A CD1   1 
ATOM   3769  C  CD2   . LEU A 1 500 ? 106.063 130.658 101.834 1.00 46.23  ? 500  LEU A CD2   1 
ATOM   3770  N  N     . LYS A 1 501 ? 104.687 131.518 107.295 1.00 45.15  ? 501  LYS A N     1 
ATOM   3771  C  CA    . LYS A 1 501 ? 104.086 130.876 108.455 1.00 48.39  ? 501  LYS A CA    1 
ATOM   3772  C  C     . LYS A 1 501 ? 103.549 131.881 109.465 1.00 49.91  ? 501  LYS A C     1 
ATOM   3773  O  O     . LYS A 1 501 ? 103.237 131.502 110.597 1.00 46.57  ? 501  LYS A O     1 
ATOM   3774  C  CB    . LYS A 1 501 ? 105.086 129.926 109.117 1.00 47.19  ? 501  LYS A CB    1 
ATOM   3775  C  CG    . LYS A 1 501 ? 106.466 130.501 109.325 1.00 48.20  ? 501  LYS A CG    1 
ATOM   3776  C  CD    . LYS A 1 501 ? 107.512 129.400 109.297 1.00 46.35  ? 501  LYS A CD    1 
ATOM   3777  C  CE    . LYS A 1 501 ? 108.910 129.960 109.459 1.00 44.07  ? 501  LYS A CE    1 
ATOM   3778  N  NZ    . LYS A 1 501 ? 109.938 128.896 109.339 1.00 44.98  ? 501  LYS A NZ    1 
ATOM   3779  N  N     . GLY A 1 502 ? 103.434 133.149 109.078 1.00 57.06  ? 502  GLY A N     1 
ATOM   3780  C  CA    . GLY A 1 502 ? 102.798 134.147 109.912 1.00 58.03  ? 502  GLY A CA    1 
ATOM   3781  C  C     . GLY A 1 502 ? 103.605 134.631 111.092 1.00 61.71  ? 502  GLY A C     1 
ATOM   3782  O  O     . GLY A 1 502 ? 103.021 135.129 112.058 1.00 60.63  ? 502  GLY A O     1 
ATOM   3783  N  N     . LYS A 1 503 ? 104.931 134.514 111.048 1.00 56.61  ? 503  LYS A N     1 
ATOM   3784  C  CA    . LYS A 1 503 ? 105.772 134.858 112.187 1.00 54.06  ? 503  LYS A CA    1 
ATOM   3785  C  C     . LYS A 1 503 ? 106.650 136.078 111.932 1.00 53.67  ? 503  LYS A C     1 
ATOM   3786  O  O     . LYS A 1 503 ? 107.640 136.273 112.639 1.00 59.01  ? 503  LYS A O     1 
ATOM   3787  C  CB    . LYS A 1 503 ? 106.644 133.665 112.579 1.00 51.29  ? 503  LYS A CB    1 
ATOM   3788  C  CG    . LYS A 1 503 ? 105.870 132.437 113.006 1.00 51.09  ? 503  LYS A CG    1 
ATOM   3789  C  CD    . LYS A 1 503 ? 106.809 131.288 113.316 1.00 54.03  ? 503  LYS A CD    1 
ATOM   3790  C  CE    . LYS A 1 503 ? 106.042 130.033 113.669 1.00 54.63  ? 503  LYS A CE    1 
ATOM   3791  N  NZ    . LYS A 1 503 ? 106.953 128.882 113.888 1.00 54.29  ? 503  LYS A NZ    1 
ATOM   3792  N  N     . LEU A 1 504 ? 106.306 136.913 110.951 1.00 54.97  ? 504  LEU A N     1 
ATOM   3793  C  CA    . LEU A 1 504 ? 107.219 137.981 110.551 1.00 54.69  ? 504  LEU A CA    1 
ATOM   3794  C  C     . LEU A 1 504 ? 107.258 139.115 111.571 1.00 58.85  ? 504  LEU A C     1 
ATOM   3795  O  O     . LEU A 1 504 ? 108.322 139.692 111.816 1.00 60.49  ? 504  LEU A O     1 
ATOM   3796  C  CB    . LEU A 1 504 ? 106.835 138.513 109.172 1.00 57.24  ? 504  LEU A CB    1 
ATOM   3797  C  CG    . LEU A 1 504 ? 107.794 139.535 108.559 1.00 58.19  ? 504  LEU A CG    1 
ATOM   3798  C  CD1   . LEU A 1 504 ? 109.214 139.001 108.534 1.00 52.79  ? 504  LEU A CD1   1 
ATOM   3799  C  CD2   . LEU A 1 504 ? 107.343 139.910 107.160 1.00 57.35  ? 504  LEU A CD2   1 
ATOM   3800  N  N     . GLU A 1 505 ? 106.117 139.458 112.171 1.00 62.69  ? 505  GLU A N     1 
ATOM   3801  C  CA    . GLU A 1 505 ? 106.087 140.584 113.103 1.00 59.63  ? 505  GLU A CA    1 
ATOM   3802  C  C     . GLU A 1 505 ? 106.812 140.251 114.403 1.00 62.28  ? 505  GLU A C     1 
ATOM   3803  O  O     . GLU A 1 505 ? 107.629 141.044 114.897 1.00 66.50  ? 505  GLU A O     1 
ATOM   3804  C  CB    . GLU A 1 505 ? 104.642 140.994 113.378 1.00 60.79  ? 505  GLU A CB    1 
ATOM   3805  C  CG    . GLU A 1 505 ? 103.883 141.420 112.138 1.00 63.00  ? 505  GLU A CG    1 
ATOM   3806  C  CD    . GLU A 1 505 ? 102.513 141.977 112.461 1.00 66.46  ? 505  GLU A CD    1 
ATOM   3807  O  OE1   . GLU A 1 505 ? 102.169 142.048 113.659 1.00 67.59  ? 505  GLU A OE1   1 
ATOM   3808  O  OE2   . GLU A 1 505 ? 101.782 142.346 111.518 1.00 64.93  ? 505  GLU A OE2   1 
ATOM   3809  N  N     . LYS A 1 506 ? 106.523 139.079 114.975 1.00 61.68  ? 506  LYS A N     1 
ATOM   3810  C  CA    . LYS A 1 506 ? 107.226 138.661 116.182 1.00 62.29  ? 506  LYS A CA    1 
ATOM   3811  C  C     . LYS A 1 506 ? 108.710 138.472 115.909 1.00 63.24  ? 506  LYS A C     1 
ATOM   3812  O  O     . LYS A 1 506 ? 109.546 138.786 116.761 1.00 62.89  ? 506  LYS A O     1 
ATOM   3813  C  CB    . LYS A 1 506 ? 106.609 137.380 116.748 1.00 61.89  ? 506  LYS A CB    1 
ATOM   3814  C  CG    . LYS A 1 506 ? 106.575 136.207 115.789 1.00 64.01  ? 506  LYS A CG    1 
ATOM   3815  C  CD    . LYS A 1 506 ? 106.263 134.913 116.517 1.00 64.35  ? 506  LYS A CD    1 
ATOM   3816  C  CE    . LYS A 1 506 ? 104.893 134.955 117.161 1.00 65.63  ? 506  LYS A CE    1 
ATOM   3817  N  NZ    . LYS A 1 506 ? 103.815 135.089 116.146 1.00 66.24  ? 506  LYS A NZ    1 
ATOM   3818  N  N     . ALA A 1 507 ? 109.057 137.968 114.722 1.00 59.55  ? 507  ALA A N     1 
ATOM   3819  C  CA    . ALA A 1 507 ? 110.464 137.826 114.366 1.00 53.75  ? 507  ALA A CA    1 
ATOM   3820  C  C     . ALA A 1 507 ? 111.143 139.181 114.261 1.00 51.29  ? 507  ALA A C     1 
ATOM   3821  O  O     . ALA A 1 507 ? 112.289 139.337 114.689 1.00 58.48  ? 507  ALA A O     1 
ATOM   3822  C  CB    . ALA A 1 507 ? 110.612 137.059 113.055 1.00 54.49  ? 507  ALA A CB    1 
ATOM   3823  N  N     . ARG A 1 508 ? 110.460 140.169 113.680 1.00 45.97  ? 508  ARG A N     1 
ATOM   3824  C  CA    . ARG A 1 508 ? 111.035 141.506 113.605 1.00 54.18  ? 508  ARG A CA    1 
ATOM   3825  C  C     . ARG A 1 508 ? 111.280 142.074 114.995 1.00 57.42  ? 508  ARG A C     1 
ATOM   3826  O  O     . ARG A 1 508 ? 112.354 142.625 115.269 1.00 55.57  ? 508  ARG A O     1 
ATOM   3827  C  CB    . ARG A 1 508 ? 110.124 142.430 112.797 1.00 56.06  ? 508  ARG A CB    1 
ATOM   3828  C  CG    . ARG A 1 508 ? 110.360 143.902 113.077 1.00 55.11  ? 508  ARG A CG    1 
ATOM   3829  C  CD    . ARG A 1 508 ? 109.978 144.786 111.909 1.00 52.15  ? 508  ARG A CD    1 
ATOM   3830  N  NE    . ARG A 1 508 ? 110.207 146.193 112.217 1.00 57.76  ? 508  ARG A NE    1 
ATOM   3831  C  CZ    . ARG A 1 508 ? 111.384 146.799 112.132 1.00 57.22  ? 508  ARG A CZ    1 
ATOM   3832  N  NH1   . ARG A 1 508 ? 112.470 146.151 111.746 1.00 56.73  ? 508  ARG A NH1   1 
ATOM   3833  N  NH2   . ARG A 1 508 ? 111.474 148.088 112.445 1.00 54.27  ? 508  ARG A NH2   1 
ATOM   3834  N  N     . GLU A 1 509 ? 110.307 141.920 115.895 1.00 64.05  ? 509  GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 509 ? 110.481 142.421 117.256 1.00 61.45  ? 509  GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 509 ? 111.604 141.687 117.986 1.00 62.87  ? 509  GLU A C     1 
ATOM   3837  O  O     . GLU A 1 509 ? 112.383 142.305 118.719 1.00 62.09  ? 509  GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 509 ? 109.169 142.310 118.028 1.00 62.03  ? 509  GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 509 ? 108.074 143.206 117.485 1.00 62.82  ? 509  GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 509 ? 106.761 143.031 118.216 1.00 65.72  ? 509  GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 509 ? 106.719 142.246 119.185 1.00 64.07  ? 509  GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 509 ? 105.770 143.679 117.819 1.00 67.69  ? 509  GLU A OE2   1 
ATOM   3843  N  N     . VAL A 1 510 ? 111.701 140.369 117.796 1.00 54.67  ? 510  VAL A N     1 
ATOM   3844  C  CA    . VAL A 1 510 ? 112.741 139.580 118.452 1.00 51.85  ? 510  VAL A CA    1 
ATOM   3845  C  C     . VAL A 1 510 ? 114.121 139.954 117.924 1.00 51.44  ? 510  VAL A C     1 
ATOM   3846  O  O     . VAL A 1 510 ? 115.079 140.094 118.692 1.00 50.98  ? 510  VAL A O     1 
ATOM   3847  C  CB    . VAL A 1 510 ? 112.448 138.079 118.273 1.00 46.97  ? 510  VAL A CB    1 
ATOM   3848  C  CG1   . VAL A 1 510 ? 113.707 137.256 118.461 1.00 48.64  ? 510  VAL A CG1   1 
ATOM   3849  C  CG2   . VAL A 1 510 ? 111.374 137.634 119.245 1.00 50.26  ? 510  VAL A CG2   1 
ATOM   3850  N  N     . LEU A 1 511 ? 114.248 140.117 116.608 1.00 54.94  ? 511  LEU A N     1 
ATOM   3851  C  CA    . LEU A 1 511 ? 115.522 140.520 116.029 1.00 52.61  ? 511  LEU A CA    1 
ATOM   3852  C  C     . LEU A 1 511 ? 115.890 141.940 116.426 1.00 53.92  ? 511  LEU A C     1 
ATOM   3853  O  O     . LEU A 1 511 ? 117.076 142.282 116.458 1.00 56.22  ? 511  LEU A O     1 
ATOM   3854  C  CB    . LEU A 1 511 ? 115.472 140.380 114.510 1.00 51.32  ? 511  LEU A CB    1 
ATOM   3855  C  CG    . LEU A 1 511 ? 115.398 138.941 114.003 1.00 50.65  ? 511  LEU A CG    1 
ATOM   3856  C  CD1   . LEU A 1 511 ? 115.072 138.918 112.526 1.00 54.39  ? 511  LEU A CD1   1 
ATOM   3857  C  CD2   . LEU A 1 511 ? 116.700 138.214 114.270 1.00 49.92  ? 511  LEU A CD2   1 
ATOM   3858  N  N     . LEU A 1 512 ? 114.897 142.784 116.716 1.00 54.20  ? 512  LEU A N     1 
ATOM   3859  C  CA    . LEU A 1 512 ? 115.204 144.095 117.274 1.00 54.82  ? 512  LEU A CA    1 
ATOM   3860  C  C     . LEU A 1 512 ? 115.716 143.973 118.705 1.00 56.87  ? 512  LEU A C     1 
ATOM   3861  O  O     . LEU A 1 512 ? 116.745 144.561 119.057 1.00 58.22  ? 512  LEU A O     1 
ATOM   3862  C  CB    . LEU A 1 512 ? 113.976 145.000 117.207 1.00 57.62  ? 512  LEU A CB    1 
ATOM   3863  C  CG    . LEU A 1 512 ? 113.657 145.562 115.822 1.00 59.05  ? 512  LEU A CG    1 
ATOM   3864  C  CD1   . LEU A 1 512 ? 112.520 146.564 115.905 1.00 55.05  ? 512  LEU A CD1   1 
ATOM   3865  C  CD2   . LEU A 1 512 ? 114.889 146.195 115.206 1.00 56.48  ? 512  LEU A CD2   1 
ATOM   3866  N  N     . ASP A 1 513 ? 115.013 143.208 119.546 1.00 54.52  ? 513  ASP A N     1 
ATOM   3867  C  CA    . ASP A 1 513 ? 115.498 142.916 120.890 1.00 51.98  ? 513  ASP A CA    1 
ATOM   3868  C  C     . ASP A 1 513 ? 114.886 141.623 121.417 1.00 50.91  ? 513  ASP A C     1 
ATOM   3869  O  O     . ASP A 1 513 ? 113.685 141.576 121.712 1.00 48.41  ? 513  ASP A O     1 
ATOM   3870  C  CB    . ASP A 1 513 ? 115.188 144.072 121.839 1.00 54.89  ? 513  ASP A CB    1 
ATOM   3871  C  CG    . ASP A 1 513 ? 116.215 144.205 122.940 1.00 60.91  ? 513  ASP A CG    1 
ATOM   3872  O  OD1   . ASP A 1 513 ? 117.183 143.417 122.941 1.00 59.67  ? 513  ASP A OD1   1 
ATOM   3873  O  OD2   . ASP A 1 513 ? 116.059 145.097 123.800 1.00 59.65  ? 513  ASP A OD2   1 
ATOM   3874  N  N     . PRO A 1 514 ? 115.681 140.561 121.571 1.00 43.91  ? 514  PRO A N     1 
ATOM   3875  C  CA    . PRO A 1 514 ? 115.139 139.278 122.029 1.00 40.15  ? 514  PRO A CA    1 
ATOM   3876  C  C     . PRO A 1 514 ? 115.022 139.140 123.536 1.00 43.85  ? 514  PRO A C     1 
ATOM   3877  O  O     . PRO A 1 514 ? 114.337 138.218 123.999 1.00 43.24  ? 514  PRO A O     1 
ATOM   3878  C  CB    . PRO A 1 514 ? 116.161 138.275 121.479 1.00 39.20  ? 514  PRO A CB    1 
ATOM   3879  C  CG    . PRO A 1 514 ? 117.439 139.021 121.527 1.00 42.03  ? 514  PRO A CG    1 
ATOM   3880  C  CD    . PRO A 1 514 ? 117.106 140.459 121.218 1.00 45.89  ? 514  PRO A CD    1 
ATOM   3881  N  N     . SER A 1 515 ? 115.659 140.023 124.306 1.00 45.83  ? 515  SER A N     1 
ATOM   3882  C  CA    . SER A 1 515 ? 115.595 139.952 125.760 1.00 38.85  ? 515  SER A CA    1 
ATOM   3883  C  C     . SER A 1 515 ? 114.228 140.338 126.311 1.00 44.43  ? 515  SER A C     1 
ATOM   3884  O  O     . SER A 1 515 ? 113.996 140.169 127.512 1.00 41.70  ? 515  SER A O     1 
ATOM   3885  C  CB    . SER A 1 515 ? 116.681 140.835 126.373 1.00 34.82  ? 515  SER A CB    1 
ATOM   3886  O  OG    . SER A 1 515 ? 116.679 142.125 125.793 1.00 40.64  ? 515  SER A OG    1 
ATOM   3887  N  N     . LYS A 1 516 ? 113.327 140.853 125.474 1.00 52.78  ? 516  LYS A N     1 
ATOM   3888  C  CA    . LYS A 1 516 ? 111.954 141.115 125.881 1.00 50.11  ? 516  LYS A CA    1 
ATOM   3889  C  C     . LYS A 1 516 ? 110.993 139.982 125.544 1.00 52.76  ? 516  LYS A C     1 
ATOM   3890  O  O     . LYS A 1 516 ? 109.905 139.928 126.124 1.00 56.82  ? 516  LYS A O     1 
ATOM   3891  C  CB    . LYS A 1 516 ? 111.434 142.405 125.232 1.00 50.52  ? 516  LYS A CB    1 
ATOM   3892  C  CG    . LYS A 1 516 ? 111.902 143.689 125.893 1.00 53.85  ? 516  LYS A CG    1 
ATOM   3893  C  CD    . LYS A 1 516 ? 113.276 144.109 125.406 1.00 55.02  ? 516  LYS A CD    1 
ATOM   3894  C  CE    . LYS A 1 516 ? 113.686 145.436 126.013 1.00 54.32  ? 516  LYS A CE    1 
ATOM   3895  N  NZ    . LYS A 1 516 ? 113.736 145.372 127.499 1.00 53.91  ? 516  LYS A NZ    1 
ATOM   3896  N  N     . HIS A 1 517 ? 111.360 139.084 124.633 1.00 49.94  ? 517  HIS A N     1 
ATOM   3897  C  CA    . HIS A 1 517 ? 110.481 138.011 124.174 1.00 52.17  ? 517  HIS A CA    1 
ATOM   3898  C  C     . HIS A 1 517 ? 111.175 136.658 124.287 1.00 56.37  ? 517  HIS A C     1 
ATOM   3899  O  O     . HIS A 1 517 ? 111.136 135.838 123.368 1.00 61.75  ? 517  HIS A O     1 
ATOM   3900  C  CB    . HIS A 1 517 ? 110.038 138.238 122.731 1.00 56.30  ? 517  HIS A CB    1 
ATOM   3901  C  CG    . HIS A 1 517 ? 109.647 139.650 122.425 1.00 56.01  ? 517  HIS A CG    1 
ATOM   3902  N  ND1   . HIS A 1 517 ? 110.524 140.564 121.885 1.00 57.25  ? 517  HIS A ND1   1 
ATOM   3903  C  CD2   . HIS A 1 517 ? 108.468 140.300 122.569 1.00 56.53  ? 517  HIS A CD2   1 
ATOM   3904  C  CE1   . HIS A 1 517 ? 109.906 141.718 121.716 1.00 54.42  ? 517  HIS A CE1   1 
ATOM   3905  N  NE2   . HIS A 1 517 ? 108.657 141.585 122.124 1.00 57.50  ? 517  HIS A NE2   1 
ATOM   3906  N  N     . ILE A 1 518 ? 111.817 136.403 125.429 1.00 50.19  ? 518  ILE A N     1 
ATOM   3907  C  CA    . ILE A 1 518 ? 112.642 135.204 125.566 1.00 51.32  ? 518  ILE A CA    1 
ATOM   3908  C  C     . ILE A 1 518 ? 111.780 133.948 125.559 1.00 49.95  ? 518  ILE A C     1 
ATOM   3909  O  O     . ILE A 1 518 ? 112.168 132.913 124.999 1.00 50.29  ? 518  ILE A O     1 
ATOM   3910  C  CB    . ILE A 1 518 ? 113.506 135.296 126.836 1.00 46.38  ? 518  ILE A CB    1 
ATOM   3911  C  CG1   . ILE A 1 518 ? 114.300 136.599 126.842 1.00 46.44  ? 518  ILE A CG1   1 
ATOM   3912  C  CG2   . ILE A 1 518 ? 114.454 134.115 126.925 1.00 44.51  ? 518  ILE A CG2   1 
ATOM   3913  C  CD1   . ILE A 1 518 ? 115.200 136.753 128.038 1.00 45.57  ? 518  ILE A CD1   1 
ATOM   3914  N  N     . GLU A 1 519 ? 110.600 134.014 126.179 1.00 62.61  ? 519  GLU A N     1 
ATOM   3915  C  CA    . GLU A 1 519 ? 109.704 132.863 126.179 1.00 66.85  ? 519  GLU A CA    1 
ATOM   3916  C  C     . GLU A 1 519 ? 109.245 132.520 124.768 1.00 67.30  ? 519  GLU A C     1 
ATOM   3917  O  O     . GLU A 1 519 ? 109.156 131.342 124.408 1.00 64.54  ? 519  GLU A O     1 
ATOM   3918  C  CB    . GLU A 1 519 ? 108.506 133.130 127.090 1.00 63.40  ? 519  GLU A CB    1 
ATOM   3919  C  CG    . GLU A 1 519 ? 108.290 134.593 127.459 1.00 64.06  ? 519  GLU A CG    1 
ATOM   3920  C  CD    . GLU A 1 519 ? 107.640 135.402 126.351 1.00 68.21  ? 519  GLU A CD    1 
ATOM   3921  O  OE1   . GLU A 1 519 ? 108.252 135.553 125.273 1.00 69.81  ? 519  GLU A OE1   1 
ATOM   3922  O  OE2   . GLU A 1 519 ? 106.510 135.890 126.561 1.00 65.20  ? 519  GLU A OE2   1 
ATOM   3923  N  N     . GLU A 1 520 ? 108.948 133.536 123.955 1.00 69.18  ? 520  GLU A N     1 
ATOM   3924  C  CA    . GLU A 1 520 ? 108.554 133.282 122.572 1.00 66.33  ? 520  GLU A CA    1 
ATOM   3925  C  C     . GLU A 1 520 ? 109.712 132.713 121.763 1.00 67.38  ? 520  GLU A C     1 
ATOM   3926  O  O     . GLU A 1 520 ? 109.504 131.866 120.888 1.00 70.17  ? 520  GLU A O     1 
ATOM   3927  C  CB    . GLU A 1 520 ? 108.027 134.562 121.928 1.00 62.95  ? 520  GLU A CB    1 
ATOM   3928  C  CG    . GLU A 1 520 ? 106.682 135.008 122.465 1.00 67.36  ? 520  GLU A CG    1 
ATOM   3929  C  CD    . GLU A 1 520 ? 106.200 136.296 121.830 1.00 71.48  ? 520  GLU A CD    1 
ATOM   3930  O  OE1   . GLU A 1 520 ? 106.958 136.885 121.031 1.00 71.77  ? 520  GLU A OE1   1 
ATOM   3931  O  OE2   . GLU A 1 520 ? 105.064 136.718 122.128 1.00 70.09  ? 520  GLU A OE2   1 
ATOM   3932  N  N     . VAL A 1 521 ? 110.935 133.174 122.035 1.00 52.56  ? 521  VAL A N     1 
ATOM   3933  C  CA    . VAL A 1 521 ? 112.108 132.630 121.354 1.00 50.33  ? 521  VAL A CA    1 
ATOM   3934  C  C     . VAL A 1 521 ? 112.276 131.153 121.681 1.00 57.22  ? 521  VAL A C     1 
ATOM   3935  O  O     . VAL A 1 521 ? 112.537 130.331 120.795 1.00 57.80  ? 521  VAL A O     1 
ATOM   3936  C  CB    . VAL A 1 521 ? 113.364 133.441 121.726 1.00 46.23  ? 521  VAL A CB    1 
ATOM   3937  C  CG1   . VAL A 1 521 ? 114.616 132.750 121.225 1.00 49.81  ? 521  VAL A CG1   1 
ATOM   3938  C  CG2   . VAL A 1 521 ? 113.277 134.836 121.154 1.00 52.10  ? 521  VAL A CG2   1 
ATOM   3939  N  N     . ILE A 1 522 ? 112.127 130.792 122.957 1.00 65.29  ? 522  ILE A N     1 
ATOM   3940  C  CA    . ILE A 1 522 ? 112.268 129.394 123.354 1.00 64.01  ? 522  ILE A CA    1 
ATOM   3941  C  C     . ILE A 1 522 ? 111.139 128.550 122.773 1.00 64.97  ? 522  ILE A C     1 
ATOM   3942  O  O     . ILE A 1 522 ? 111.363 127.428 122.304 1.00 64.84  ? 522  ILE A O     1 
ATOM   3943  C  CB    . ILE A 1 522 ? 112.328 129.285 124.889 1.00 65.40  ? 522  ILE A CB    1 
ATOM   3944  C  CG1   . ILE A 1 522 ? 113.593 129.955 125.421 1.00 63.22  ? 522  ILE A CG1   1 
ATOM   3945  C  CG2   . ILE A 1 522 ? 112.279 127.831 125.331 1.00 65.36  ? 522  ILE A CG2   1 
ATOM   3946  C  CD1   . ILE A 1 522 ? 114.862 129.278 124.973 1.00 60.88  ? 522  ILE A CD1   1 
ATOM   3947  N  N     . TYR A 1 523 ? 109.913 129.079 122.788 1.00 72.34  ? 523  TYR A N     1 
ATOM   3948  C  CA    . TYR A 1 523 ? 108.745 128.294 122.404 1.00 73.49  ? 523  TYR A CA    1 
ATOM   3949  C  C     . TYR A 1 523 ? 108.784 127.899 120.931 1.00 74.64  ? 523  TYR A C     1 
ATOM   3950  O  O     . TYR A 1 523 ? 108.478 126.752 120.584 1.00 74.47  ? 523  TYR A O     1 
ATOM   3951  C  CB    . TYR A 1 523 ? 107.473 129.081 122.716 1.00 72.41  ? 523  TYR A CB    1 
ATOM   3952  C  CG    . TYR A 1 523 ? 106.207 128.263 122.653 1.00 74.16  ? 523  TYR A CG    1 
ATOM   3953  C  CD1   . TYR A 1 523 ? 105.756 127.564 123.763 1.00 74.72  ? 523  TYR A CD1   1 
ATOM   3954  C  CD2   . TYR A 1 523 ? 105.458 128.194 121.486 1.00 75.08  ? 523  TYR A CD2   1 
ATOM   3955  C  CE1   . TYR A 1 523 ? 104.598 126.816 123.714 1.00 76.38  ? 523  TYR A CE1   1 
ATOM   3956  C  CE2   . TYR A 1 523 ? 104.297 127.447 121.426 1.00 76.68  ? 523  TYR A CE2   1 
ATOM   3957  C  CZ    . TYR A 1 523 ? 103.872 126.760 122.543 1.00 78.17  ? 523  TYR A CZ    1 
ATOM   3958  O  OH    . TYR A 1 523 ? 102.716 126.015 122.490 1.00 78.13  ? 523  TYR A OH    1 
ATOM   3959  N  N     . ASP A 1 524 ? 109.157 128.823 120.054 1.00 70.68  ? 524  ASP A N     1 
ATOM   3960  C  CA    . ASP A 1 524 ? 109.166 128.577 118.619 1.00 68.32  ? 524  ASP A CA    1 
ATOM   3961  C  C     . ASP A 1 524 ? 110.578 128.244 118.162 1.00 68.40  ? 524  ASP A C     1 
ATOM   3962  O  O     . ASP A 1 524 ? 111.512 129.015 118.404 1.00 66.81  ? 524  ASP A O     1 
ATOM   3963  C  CB    . ASP A 1 524 ? 108.636 129.787 117.849 1.00 67.89  ? 524  ASP A CB    1 
ATOM   3964  C  CG    . ASP A 1 524 ? 107.139 129.960 117.992 1.00 72.16  ? 524  ASP A CG    1 
ATOM   3965  O  OD1   . ASP A 1 524 ? 106.447 128.955 118.257 1.00 72.34  ? 524  ASP A OD1   1 
ATOM   3966  O  OD2   . ASP A 1 524 ? 106.652 131.098 117.835 1.00 73.41  ? 524  ASP A OD2   1 
ATOM   3967  N  N     . GLU A 1 525 ? 110.728 127.095 117.503 1.00 64.09  ? 525  GLU A N     1 
ATOM   3968  C  CA    . GLU A 1 525 ? 112.035 126.718 116.980 1.00 62.65  ? 525  GLU A CA    1 
ATOM   3969  C  C     . GLU A 1 525 ? 112.466 127.633 115.842 1.00 60.87  ? 525  GLU A C     1 
ATOM   3970  O  O     . GLU A 1 525 ? 113.665 127.868 115.659 1.00 63.61  ? 525  GLU A O     1 
ATOM   3971  C  CB    . GLU A 1 525 ? 112.021 125.261 116.522 1.00 61.27  ? 525  GLU A CB    1 
ATOM   3972  C  CG    . GLU A 1 525 ? 110.958 124.937 115.490 1.00 61.40  ? 525  GLU A CG    1 
ATOM   3973  C  CD    . GLU A 1 525 ? 110.981 123.482 115.076 1.00 65.32  ? 525  GLU A CD    1 
ATOM   3974  O  OE1   . GLU A 1 525 ? 111.789 122.715 115.639 1.00 63.31  ? 525  GLU A OE1   1 
ATOM   3975  O  OE2   . GLU A 1 525 ? 110.192 123.104 114.185 1.00 65.24  ? 525  GLU A OE2   1 
ATOM   3976  N  N     . ASP A 1 526 ? 111.507 128.159 115.077 1.00 56.83  ? 526  ASP A N     1 
ATOM   3977  C  CA    . ASP A 1 526 ? 111.844 129.058 113.979 1.00 54.35  ? 526  ASP A CA    1 
ATOM   3978  C  C     . ASP A 1 526 ? 112.472 130.347 114.490 1.00 51.30  ? 526  ASP A C     1 
ATOM   3979  O  O     . ASP A 1 526 ? 113.457 130.830 113.923 1.00 48.65  ? 526  ASP A O     1 
ATOM   3980  C  CB    . ASP A 1 526 ? 110.599 129.362 113.150 1.00 57.56  ? 526  ASP A CB    1 
ATOM   3981  C  CG    . ASP A 1 526 ? 109.992 128.119 112.538 1.00 60.79  ? 526  ASP A CG    1 
ATOM   3982  O  OD1   . ASP A 1 526 ? 110.744 127.154 112.283 1.00 57.26  ? 526  ASP A OD1   1 
ATOM   3983  O  OD2   . ASP A 1 526 ? 108.764 128.104 112.310 1.00 63.30  ? 526  ASP A OD2   1 
ATOM   3984  N  N     . LEU A 1 527 ? 111.917 130.920 115.561 1.00 51.59  ? 527  LEU A N     1 
ATOM   3985  C  CA    . LEU A 1 527 ? 112.488 132.139 116.126 1.00 47.34  ? 527  LEU A CA    1 
ATOM   3986  C  C     . LEU A 1 527 ? 113.871 131.884 116.708 1.00 48.78  ? 527  LEU A C     1 
ATOM   3987  O  O     . LEU A 1 527 ? 114.769 132.721 116.572 1.00 49.31  ? 527  LEU A O     1 
ATOM   3988  C  CB    . LEU A 1 527 ? 111.558 132.715 117.191 1.00 47.57  ? 527  LEU A CB    1 
ATOM   3989  C  CG    . LEU A 1 527 ? 110.590 133.811 116.747 1.00 49.22  ? 527  LEU A CG    1 
ATOM   3990  C  CD1   . LEU A 1 527 ? 109.620 133.302 115.696 1.00 52.27  ? 527  LEU A CD1   1 
ATOM   3991  C  CD2   . LEU A 1 527 ? 109.844 134.365 117.946 1.00 51.10  ? 527  LEU A CD2   1 
ATOM   3992  N  N     . TYR A 1 528 ? 114.059 130.734 117.358 1.00 45.29  ? 528  TYR A N     1 
ATOM   3993  C  CA    . TYR A 1 528 ? 115.376 130.361 117.863 1.00 43.63  ? 528  TYR A CA    1 
ATOM   3994  C  C     . TYR A 1 528 ? 116.390 130.273 116.728 1.00 48.73  ? 528  TYR A C     1 
ATOM   3995  O  O     . TYR A 1 528 ? 117.497 130.823 116.817 1.00 42.93  ? 528  TYR A O     1 
ATOM   3996  C  CB    . TYR A 1 528 ? 115.269 129.029 118.608 1.00 43.35  ? 528  TYR A CB    1 
ATOM   3997  C  CG    . TYR A 1 528 ? 116.501 128.617 119.379 1.00 47.49  ? 528  TYR A CG    1 
ATOM   3998  C  CD1   . TYR A 1 528 ? 117.522 127.906 118.767 1.00 49.06  ? 528  TYR A CD1   1 
ATOM   3999  C  CD2   . TYR A 1 528 ? 116.631 128.918 120.726 1.00 45.71  ? 528  TYR A CD2   1 
ATOM   4000  C  CE1   . TYR A 1 528 ? 118.645 127.522 119.470 1.00 46.37  ? 528  TYR A CE1   1 
ATOM   4001  C  CE2   . TYR A 1 528 ? 117.747 128.536 121.437 1.00 43.59  ? 528  TYR A CE2   1 
ATOM   4002  C  CZ    . TYR A 1 528 ? 118.751 127.838 120.804 1.00 48.08  ? 528  TYR A CZ    1 
ATOM   4003  O  OH    . TYR A 1 528 ? 119.869 127.457 121.507 1.00 48.24  ? 528  TYR A OH    1 
ATOM   4004  N  N     . ARG A 1 529 ? 116.014 129.600 115.637 1.00 52.55  ? 529  ARG A N     1 
ATOM   4005  C  CA    . ARG A 1 529 ? 116.917 129.458 114.499 1.00 43.92  ? 529  ARG A CA    1 
ATOM   4006  C  C     . ARG A 1 529 ? 117.230 130.802 113.860 1.00 44.22  ? 529  ARG A C     1 
ATOM   4007  O  O     . ARG A 1 529 ? 118.380 131.068 113.498 1.00 51.88  ? 529  ARG A O     1 
ATOM   4008  C  CB    . ARG A 1 529 ? 116.316 128.521 113.458 1.00 45.81  ? 529  ARG A CB    1 
ATOM   4009  C  CG    . ARG A 1 529 ? 116.365 127.054 113.807 1.00 50.77  ? 529  ARG A CG    1 
ATOM   4010  C  CD    . ARG A 1 529 ? 116.259 126.195 112.554 1.00 50.64  ? 529  ARG A CD    1 
ATOM   4011  N  NE    . ARG A 1 529 ? 115.094 126.526 111.742 1.00 54.54  ? 529  ARG A NE    1 
ATOM   4012  C  CZ    . ARG A 1 529 ? 115.129 127.273 110.646 1.00 56.04  ? 529  ARG A CZ    1 
ATOM   4013  N  NH1   . ARG A 1 529 ? 116.260 127.795 110.203 1.00 55.32  ? 529  ARG A NH1   1 
ATOM   4014  N  NH2   . ARG A 1 529 ? 114.000 127.506 109.983 1.00 49.85  ? 529  ARG A NH2   1 
ATOM   4015  N  N     . VAL A 1 530 ? 116.216 131.652 113.690 1.00 35.88  ? 530  VAL A N     1 
ATOM   4016  C  CA    . VAL A 1 530 ? 116.434 132.957 113.076 1.00 35.06  ? 530  VAL A CA    1 
ATOM   4017  C  C     . VAL A 1 530 ? 117.331 133.818 113.956 1.00 34.80  ? 530  VAL A C     1 
ATOM   4018  O  O     . VAL A 1 530 ? 118.229 134.509 113.461 1.00 38.89  ? 530  VAL A O     1 
ATOM   4019  C  CB    . VAL A 1 530 ? 115.085 133.638 112.784 1.00 39.71  ? 530  VAL A CB    1 
ATOM   4020  C  CG1   . VAL A 1 530 ? 115.283 135.092 112.403 1.00 37.03  ? 530  VAL A CG1   1 
ATOM   4021  C  CG2   . VAL A 1 530 ? 114.365 132.907 111.671 1.00 39.65  ? 530  VAL A CG2   1 
ATOM   4022  N  N     . LEU A 1 531 ? 117.118 133.774 115.273 1.00 30.83  ? 531  LEU A N     1 
ATOM   4023  C  CA    . LEU A 1 531 ? 117.957 134.534 116.191 1.00 29.63  ? 531  LEU A CA    1 
ATOM   4024  C  C     . LEU A 1 531 ? 119.403 134.060 116.145 1.00 33.17  ? 531  LEU A C     1 
ATOM   4025  O  O     . LEU A 1 531 ? 120.331 134.875 116.170 1.00 33.28  ? 531  LEU A O     1 
ATOM   4026  C  CB    . LEU A 1 531 ? 117.402 134.428 117.609 1.00 33.28  ? 531  LEU A CB    1 
ATOM   4027  C  CG    . LEU A 1 531 ? 118.199 135.120 118.713 1.00 29.73  ? 531  LEU A CG    1 
ATOM   4028  C  CD1   . LEU A 1 531 ? 118.320 136.605 118.434 1.00 28.44  ? 531  LEU A CD1   1 
ATOM   4029  C  CD2   . LEU A 1 531 ? 117.547 134.876 120.059 1.00 32.84  ? 531  LEU A CD2   1 
ATOM   4030  N  N     . PHE A 1 532 ? 119.621 132.747 116.077 1.00 36.38  ? 532  PHE A N     1 
ATOM   4031  C  CA    . PHE A 1 532 ? 120.991 132.251 116.080 1.00 31.68  ? 532  PHE A CA    1 
ATOM   4032  C  C     . PHE A 1 532 ? 121.650 132.292 114.706 1.00 35.44  ? 532  PHE A C     1 
ATOM   4033  O  O     . PHE A 1 532 ? 122.876 132.173 114.623 1.00 41.18  ? 532  PHE A O     1 
ATOM   4034  C  CB    . PHE A 1 532 ? 121.030 130.834 116.649 1.00 32.65  ? 532  PHE A CB    1 
ATOM   4035  C  CG    . PHE A 1 532 ? 121.122 130.799 118.142 1.00 35.82  ? 532  PHE A CG    1 
ATOM   4036  C  CD1   . PHE A 1 532 ? 119.982 130.827 118.920 1.00 30.45  ? 532  PHE A CD1   1 
ATOM   4037  C  CD2   . PHE A 1 532 ? 122.355 130.763 118.769 1.00 37.42  ? 532  PHE A CD2   1 
ATOM   4038  C  CE1   . PHE A 1 532 ? 120.068 130.810 120.294 1.00 32.06  ? 532  PHE A CE1   1 
ATOM   4039  C  CE2   . PHE A 1 532 ? 122.445 130.741 120.142 1.00 31.89  ? 532  PHE A CE2   1 
ATOM   4040  C  CZ    . PHE A 1 532 ? 121.300 130.763 120.905 1.00 30.31  ? 532  PHE A CZ    1 
ATOM   4041  N  N     . ASP A 1 533 ? 120.876 132.465 113.636 1.00 34.52  ? 533  ASP A N     1 
ATOM   4042  C  CA    . ASP A 1 533 ? 121.446 132.617 112.304 1.00 29.01  ? 533  ASP A CA    1 
ATOM   4043  C  C     . ASP A 1 533 ? 121.748 134.070 111.969 1.00 28.38  ? 533  ASP A C     1 
ATOM   4044  O  O     . ASP A 1 533 ? 122.794 134.362 111.381 1.00 37.09  ? 533  ASP A O     1 
ATOM   4045  C  CB    . ASP A 1 533 ? 120.497 132.044 111.247 1.00 31.08  ? 533  ASP A CB    1 
ATOM   4046  C  CG    . ASP A 1 533 ? 120.728 130.571 110.988 1.00 35.39  ? 533  ASP A CG    1 
ATOM   4047  O  OD1   . ASP A 1 533 ? 121.550 129.961 111.703 1.00 37.35  ? 533  ASP A OD1   1 
ATOM   4048  O  OD2   . ASP A 1 533 ? 120.089 130.024 110.065 1.00 34.45  ? 533  ASP A OD2   1 
ATOM   4049  N  N     . LEU A 1 534 ? 120.855 134.987 112.332 1.00 21.16  ? 534  LEU A N     1 
ATOM   4050  C  CA    . LEU A 1 534 ? 120.982 136.385 111.948 1.00 24.90  ? 534  LEU A CA    1 
ATOM   4051  C  C     . LEU A 1 534 ? 121.625 137.248 113.022 1.00 27.59  ? 534  LEU A C     1 
ATOM   4052  O  O     . LEU A 1 534 ? 122.419 138.135 112.696 1.00 32.70  ? 534  LEU A O     1 
ATOM   4053  C  CB    . LEU A 1 534 ? 119.611 136.964 111.592 1.00 28.57  ? 534  LEU A CB    1 
ATOM   4054  C  CG    . LEU A 1 534 ? 118.926 136.384 110.357 1.00 27.17  ? 534  LEU A CG    1 
ATOM   4055  C  CD1   . LEU A 1 534 ? 117.605 137.081 110.120 1.00 26.60  ? 534  LEU A CD1   1 
ATOM   4056  C  CD2   . LEU A 1 534 ? 119.822 136.508 109.141 1.00 25.33  ? 534  LEU A CD2   1 
ATOM   4057  N  N     . ARG A 1 535 ? 121.318 137.007 114.294 1.00 31.65  ? 535  ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 535 ? 121.803 137.845 115.391 1.00 33.19  ? 535  ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 535 ? 122.448 137.000 116.486 1.00 36.68  ? 535  ARG A C     1 
ATOM   4060  O  O     . ARG A 1 535 ? 121.965 136.962 117.621 1.00 40.32  ? 535  ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 535 ? 120.652 138.673 115.959 1.00 29.20  ? 535  ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 535 ? 120.998 140.117 116.245 1.00 31.22  ? 535  ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 535 ? 119.864 140.803 116.979 1.00 35.61  ? 535  ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 535 ? 119.830 140.427 118.385 1.00 40.77  ? 535  ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 535 ? 120.304 141.178 119.369 1.00 40.95  ? 535  ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 535 ? 120.810 142.377 119.141 1.00 30.31  ? 535  ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 535 ? 120.273 140.711 120.613 1.00 41.18  ? 535  ARG A NH2   1 
ATOM   4068  N  N     . PRO A 1 536 ? 123.554 136.319 116.190 1.00 27.42  ? 536  PRO A N     1 
ATOM   4069  C  CA    . PRO A 1 536 ? 124.199 135.501 117.216 1.00 28.18  ? 536  PRO A CA    1 
ATOM   4070  C  C     . PRO A 1 536 ? 125.228 136.292 118.005 1.00 23.96  ? 536  PRO A C     1 
ATOM   4071  O  O     . PRO A 1 536 ? 125.857 137.227 117.508 1.00 28.71  ? 536  PRO A O     1 
ATOM   4072  C  CB    . PRO A 1 536 ? 124.868 134.397 116.388 1.00 23.78  ? 536  PRO A CB    1 
ATOM   4073  C  CG    . PRO A 1 536 ? 125.275 135.104 115.144 1.00 29.74  ? 536  PRO A CG    1 
ATOM   4074  C  CD    . PRO A 1 536 ? 124.272 136.218 114.906 1.00 26.45  ? 536  PRO A CD    1 
ATOM   4075  N  N     . TYR A 1 537 ? 125.390 135.911 119.268 1.00 18.46  ? 537  TYR A N     1 
ATOM   4076  C  CA    . TYR A 1 537 ? 126.398 136.552 120.099 1.00 16.08  ? 537  TYR A CA    1 
ATOM   4077  C  C     . TYR A 1 537 ? 127.765 136.001 119.732 1.00 18.38  ? 537  TYR A C     1 
ATOM   4078  O  O     . TYR A 1 537 ? 128.025 134.806 119.897 1.00 32.17  ? 537  TYR A O     1 
ATOM   4079  C  CB    . TYR A 1 537 ? 126.131 136.341 121.587 1.00 27.35  ? 537  TYR A CB    1 
ATOM   4080  C  CG    . TYR A 1 537 ? 127.214 136.969 122.430 1.00 22.75  ? 537  TYR A CG    1 
ATOM   4081  C  CD1   . TYR A 1 537 ? 127.261 138.343 122.613 1.00 16.51  ? 537  TYR A CD1   1 
ATOM   4082  C  CD2   . TYR A 1 537 ? 128.212 136.197 123.004 1.00 15.10  ? 537  TYR A CD2   1 
ATOM   4083  C  CE1   . TYR A 1 537 ? 128.255 138.928 123.361 1.00 13.09  ? 537  TYR A CE1   1 
ATOM   4084  C  CE2   . TYR A 1 537 ? 129.213 136.775 123.751 1.00 12.85  ? 537  TYR A CE2   1 
ATOM   4085  C  CZ    . TYR A 1 537 ? 129.230 138.140 123.926 1.00 17.02  ? 537  TYR A CZ    1 
ATOM   4086  O  OH    . TYR A 1 537 ? 130.224 138.723 124.673 1.00 25.94  ? 537  TYR A OH    1 
ATOM   4087  N  N     . ASN A 1 538 ? 128.638 136.864 119.232 1.00 13.52  ? 538  ASN A N     1 
ATOM   4088  C  CA    . ASN A 1 538 ? 130.010 136.490 118.933 1.00 9.96   ? 538  ASN A CA    1 
ATOM   4089  C  C     . ASN A 1 538 ? 130.925 137.258 119.874 1.00 14.49  ? 538  ASN A C     1 
ATOM   4090  O  O     . ASN A 1 538 ? 130.945 138.493 119.856 1.00 27.19  ? 538  ASN A O     1 
ATOM   4091  C  CB    . ASN A 1 538 ? 130.352 136.767 117.468 1.00 16.96  ? 538  ASN A CB    1 
ATOM   4092  C  CG    . ASN A 1 538 ? 129.518 135.934 116.506 1.00 20.49  ? 538  ASN A CG    1 
ATOM   4093  O  OD1   . ASN A 1 538 ? 129.251 134.759 116.751 1.00 7.63   ? 538  ASN A OD1   1 
ATOM   4094  N  ND2   . ASN A 1 538 ? 129.101 136.546 115.407 1.00 25.87  ? 538  ASN A ND2   1 
ATOM   4095  N  N     . HIS A 1 539 ? 131.651 136.527 120.712 1.00 9.63   ? 539  HIS A N     1 
ATOM   4096  C  CA    . HIS A 1 539 ? 132.644 137.129 121.586 1.00 5.96   ? 539  HIS A CA    1 
ATOM   4097  C  C     . HIS A 1 539 ? 133.876 137.472 120.764 1.00 14.99  ? 539  HIS A C     1 
ATOM   4098  O  O     . HIS A 1 539 ? 134.324 136.667 119.942 1.00 20.12  ? 539  HIS A O     1 
ATOM   4099  C  CB    . HIS A 1 539 ? 133.002 136.171 122.720 1.00 8.82   ? 539  HIS A CB    1 
ATOM   4100  C  CG    . HIS A 1 539 ? 133.521 136.848 123.947 1.00 11.24  ? 539  HIS A CG    1 
ATOM   4101  N  ND1   . HIS A 1 539 ? 132.723 137.617 124.766 1.00 14.49  ? 539  HIS A ND1   1 
ATOM   4102  C  CD2   . HIS A 1 539 ? 134.756 136.865 124.501 1.00 17.83  ? 539  HIS A CD2   1 
ATOM   4103  C  CE1   . HIS A 1 539 ? 133.444 138.081 125.770 1.00 15.56  ? 539  HIS A CE1   1 
ATOM   4104  N  NE2   . HIS A 1 539 ? 134.681 137.640 125.633 1.00 18.00  ? 539  HIS A NE2   1 
ATOM   4105  N  N     . TRP A 1 540 ? 134.418 138.665 120.971 1.00 13.99  ? 540  TRP A N     1 
ATOM   4106  C  CA    . TRP A 1 540 ? 135.518 139.155 120.158 1.00 10.93  ? 540  TRP A CA    1 
ATOM   4107  C  C     . TRP A 1 540 ? 136.735 139.451 121.016 1.00 17.90  ? 540  TRP A C     1 
ATOM   4108  O  O     . TRP A 1 540 ? 136.618 139.927 122.149 1.00 28.09  ? 540  TRP A O     1 
ATOM   4109  C  CB    . TRP A 1 540 ? 135.110 140.400 119.364 1.00 15.97  ? 540  TRP A CB    1 
ATOM   4110  C  CG    . TRP A 1 540 ? 134.181 140.065 118.251 1.00 18.44  ? 540  TRP A CG    1 
ATOM   4111  C  CD1   . TRP A 1 540 ? 132.884 140.456 118.117 1.00 16.35  ? 540  TRP A CD1   1 
ATOM   4112  C  CD2   . TRP A 1 540 ? 134.468 139.231 117.126 1.00 21.29  ? 540  TRP A CD2   1 
ATOM   4113  N  NE1   . TRP A 1 540 ? 132.348 139.929 116.969 1.00 15.72  ? 540  TRP A NE1   1 
ATOM   4114  C  CE2   . TRP A 1 540 ? 133.301 139.170 116.345 1.00 23.00  ? 540  TRP A CE2   1 
ATOM   4115  C  CE3   . TRP A 1 540 ? 135.601 138.533 116.700 1.00 14.69  ? 540  TRP A CE3   1 
ATOM   4116  C  CZ2   . TRP A 1 540 ? 133.235 138.442 115.166 1.00 19.35  ? 540  TRP A CZ2   1 
ATOM   4117  C  CZ3   . TRP A 1 540 ? 135.532 137.812 115.531 1.00 14.85  ? 540  TRP A CZ3   1 
ATOM   4118  C  CH2   . TRP A 1 540 ? 134.360 137.771 114.777 1.00 17.38  ? 540  TRP A CH2   1 
ATOM   4119  N  N     . LYS A 1 541 ? 137.900 139.153 120.459 1.00 14.16  ? 541  LYS A N     1 
ATOM   4120  C  CA    . LYS A 1 541 ? 139.181 139.396 121.099 1.00 25.70  ? 541  LYS A CA    1 
ATOM   4121  C  C     . LYS A 1 541 ? 139.789 140.657 120.503 1.00 28.86  ? 541  LYS A C     1 
ATOM   4122  O  O     . LYS A 1 541 ? 139.929 140.762 119.280 1.00 37.87  ? 541  LYS A O     1 
ATOM   4123  C  CB    . LYS A 1 541 ? 140.111 138.202 120.888 1.00 24.18  ? 541  LYS A CB    1 
ATOM   4124  C  CG    . LYS A 1 541 ? 141.012 137.883 122.054 1.00 15.63  ? 541  LYS A CG    1 
ATOM   4125  C  CD    . LYS A 1 541 ? 141.973 136.750 121.722 1.00 23.81  ? 541  LYS A CD    1 
ATOM   4126  C  CE    . LYS A 1 541 ? 141.244 135.481 121.343 1.00 26.67  ? 541  LYS A CE    1 
ATOM   4127  N  NZ    . LYS A 1 541 ? 142.175 134.346 121.121 1.00 26.87  ? 541  LYS A NZ    1 
ATOM   4128  N  N     . LYS A 1 542 ? 140.131 141.617 121.357 1.00 32.12  ? 542  LYS A N     1 
ATOM   4129  C  CA    . LYS A 1 542 ? 140.801 142.832 120.895 1.00 37.82  ? 542  LYS A CA    1 
ATOM   4130  C  C     . LYS A 1 542 ? 142.280 142.514 120.739 1.00 40.42  ? 542  LYS A C     1 
ATOM   4131  O  O     . LYS A 1 542 ? 143.074 142.651 121.670 1.00 44.31  ? 542  LYS A O     1 
ATOM   4132  C  CB    . LYS A 1 542 ? 140.571 143.988 121.858 1.00 38.36  ? 542  LYS A CB    1 
ATOM   4133  C  CG    . LYS A 1 542 ? 139.180 144.585 121.784 1.00 37.91  ? 542  LYS A CG    1 
ATOM   4134  C  CD    . LYS A 1 542 ? 139.104 145.936 122.481 1.00 45.98  ? 542  LYS A CD    1 
ATOM   4135  C  CE    . LYS A 1 542 ? 139.230 145.812 123.991 1.00 42.20  ? 542  LYS A CE    1 
ATOM   4136  N  NZ    . LYS A 1 542 ? 140.639 145.884 124.470 1.00 36.09  ? 542  LYS A NZ    1 
ATOM   4137  N  N     . VAL A 1 543 ? 142.653 142.086 119.540 1.00 30.46  ? 543  VAL A N     1 
ATOM   4138  C  CA    . VAL A 1 543 ? 143.996 141.601 119.273 1.00 28.72  ? 543  VAL A CA    1 
ATOM   4139  C  C     . VAL A 1 543 ? 144.740 142.600 118.404 1.00 32.39  ? 543  VAL A C     1 
ATOM   4140  O  O     . VAL A 1 543 ? 144.153 143.402 117.672 1.00 35.36  ? 543  VAL A O     1 
ATOM   4141  C  CB    . VAL A 1 543 ? 143.986 140.218 118.601 1.00 35.37  ? 543  VAL A CB    1 
ATOM   4142  C  CG1   . VAL A 1 543 ? 143.357 139.198 119.508 1.00 37.27  ? 543  VAL A CG1   1 
ATOM   4143  C  CG2   . VAL A 1 543 ? 143.245 140.296 117.294 1.00 35.54  ? 543  VAL A CG2   1 
ATOM   4144  N  N     . THR A 1 544 ? 146.064 142.529 118.483 1.00 43.30  ? 544  THR A N     1 
ATOM   4145  C  CA    . THR A 1 544 ? 146.954 143.332 117.663 1.00 43.32  ? 544  THR A CA    1 
ATOM   4146  C  C     . THR A 1 544 ? 148.122 142.443 117.248 1.00 44.87  ? 544  THR A C     1 
ATOM   4147  O  O     . THR A 1 544 ? 148.072 141.218 117.388 1.00 42.85  ? 544  THR A O     1 
ATOM   4148  C  CB    . THR A 1 544 ? 147.391 144.596 118.416 1.00 43.58  ? 544  THR A CB    1 
ATOM   4149  O  OG1   . THR A 1 544 ? 148.577 145.131 117.817 1.00 45.01  ? 544  THR A OG1   1 
ATOM   4150  C  CG2   . THR A 1 544 ? 147.652 144.286 119.877 1.00 42.99  ? 544  THR A CG2   1 
ATOM   4151  N  N     . GLU A 1 545 ? 149.180 143.067 116.725 1.00 50.15  ? 545  GLU A N     1 
ATOM   4152  C  CA    . GLU A 1 545 ? 150.310 142.308 116.197 1.00 44.52  ? 545  GLU A CA    1 
ATOM   4153  C  C     . GLU A 1 545 ? 151.036 141.531 117.287 1.00 45.91  ? 545  GLU A C     1 
ATOM   4154  O  O     . GLU A 1 545 ? 151.674 140.513 117.001 1.00 46.36  ? 545  GLU A O     1 
ATOM   4155  C  CB    . GLU A 1 545 ? 151.287 143.247 115.493 1.00 46.20  ? 545  GLU A CB    1 
ATOM   4156  C  CG    . GLU A 1 545 ? 150.632 144.244 114.557 1.00 49.82  ? 545  GLU A CG    1 
ATOM   4157  C  CD    . GLU A 1 545 ? 150.155 143.610 113.267 1.00 51.76  ? 545  GLU A CD    1 
ATOM   4158  O  OE1   . GLU A 1 545 ? 150.674 142.533 112.906 1.00 51.46  ? 545  GLU A OE1   1 
ATOM   4159  O  OE2   . GLU A 1 545 ? 149.262 144.188 112.613 1.00 48.22  ? 545  GLU A OE2   1 
ATOM   4160  N  N     . LYS A 1 546 ? 150.952 141.991 118.537 1.00 47.00  ? 546  LYS A N     1 
ATOM   4161  C  CA    . LYS A 1 546 ? 151.734 141.394 119.612 1.00 49.48  ? 546  LYS A CA    1 
ATOM   4162  C  C     . LYS A 1 546 ? 151.186 140.049 120.064 1.00 52.02  ? 546  LYS A C     1 
ATOM   4163  O  O     . LYS A 1 546 ? 151.891 139.307 120.755 1.00 54.61  ? 546  LYS A O     1 
ATOM   4164  C  CB    . LYS A 1 546 ? 151.804 142.344 120.809 1.00 50.74  ? 546  LYS A CB    1 
ATOM   4165  C  CG    . LYS A 1 546 ? 152.875 143.418 120.705 1.00 52.75  ? 546  LYS A CG    1 
ATOM   4166  C  CD    . LYS A 1 546 ? 152.465 144.542 119.772 1.00 52.02  ? 546  LYS A CD    1 
ATOM   4167  C  CE    . LYS A 1 546 ? 151.180 145.195 120.237 1.00 51.98  ? 546  LYS A CE    1 
ATOM   4168  N  NZ    . LYS A 1 546 ? 150.722 146.252 119.296 1.00 52.75  ? 546  LYS A NZ    1 
ATOM   4169  N  N     . ASP A 1 547 ? 149.953 139.717 119.700 1.00 47.50  ? 547  ASP A N     1 
ATOM   4170  C  CA    . ASP A 1 547 ? 149.329 138.488 120.163 1.00 45.69  ? 547  ASP A CA    1 
ATOM   4171  C  C     . ASP A 1 547 ? 149.639 137.286 119.282 1.00 47.60  ? 547  ASP A C     1 
ATOM   4172  O  O     . ASP A 1 547 ? 149.285 136.162 119.653 1.00 49.16  ? 547  ASP A O     1 
ATOM   4173  C  CB    . ASP A 1 547 ? 147.814 138.686 120.261 1.00 42.52  ? 547  ASP A CB    1 
ATOM   4174  C  CG    . ASP A 1 547 ? 147.437 139.778 121.244 1.00 48.68  ? 547  ASP A CG    1 
ATOM   4175  O  OD1   . ASP A 1 547 ? 147.986 139.787 122.363 1.00 48.49  ? 547  ASP A OD1   1 
ATOM   4176  O  OD2   . ASP A 1 547 ? 146.603 140.635 120.897 1.00 50.05  ? 547  ASP A OD2   1 
ATOM   4177  N  N     . TYR A 1 548 ? 150.295 137.484 118.144 1.00 41.10  ? 548  TYR A N     1 
ATOM   4178  C  CA    . TYR A 1 548 ? 150.622 136.399 117.228 1.00 33.18  ? 548  TYR A CA    1 
ATOM   4179  C  C     . TYR A 1 548 ? 152.105 136.408 116.886 1.00 44.93  ? 548  TYR A C     1 
ATOM   4180  O  O     . TYR A 1 548 ? 152.503 136.142 115.750 1.00 46.70  ? 548  TYR A O     1 
ATOM   4181  C  CB    . TYR A 1 548 ? 149.767 136.476 115.966 1.00 31.49  ? 548  TYR A CB    1 
ATOM   4182  C  CG    . TYR A 1 548 ? 148.286 136.345 116.236 1.00 31.94  ? 548  TYR A CG    1 
ATOM   4183  C  CD1   . TYR A 1 548 ? 147.728 135.117 116.555 1.00 33.39  ? 548  TYR A CD1   1 
ATOM   4184  C  CD2   . TYR A 1 548 ? 147.448 137.450 116.179 1.00 35.69  ? 548  TYR A CD2   1 
ATOM   4185  C  CE1   . TYR A 1 548 ? 146.379 134.990 116.807 1.00 37.11  ? 548  TYR A CE1   1 
ATOM   4186  C  CE2   . TYR A 1 548 ? 146.097 137.333 116.432 1.00 32.72  ? 548  TYR A CE2   1 
ATOM   4187  C  CZ    . TYR A 1 548 ? 145.569 136.100 116.746 1.00 32.87  ? 548  TYR A CZ    1 
ATOM   4188  O  OH    . TYR A 1 548 ? 144.225 135.972 116.997 1.00 28.13  ? 548  TYR A OH    1 
ATOM   4189  N  N     . GLU A 1 549 ? 152.947 136.707 117.875 1.00 59.10  ? 549  GLU A N     1 
ATOM   4190  C  CA    . GLU A 1 549 ? 154.391 136.683 117.690 1.00 54.05  ? 549  GLU A CA    1 
ATOM   4191  C  C     . GLU A 1 549 ? 154.977 135.282 117.786 1.00 52.74  ? 549  GLU A C     1 
ATOM   4192  O  O     . GLU A 1 549 ? 156.152 135.097 117.457 1.00 56.75  ? 549  GLU A O     1 
ATOM   4193  C  CB    . GLU A 1 549 ? 155.075 137.577 118.728 1.00 54.56  ? 549  GLU A CB    1 
ATOM   4194  C  CG    . GLU A 1 549 ? 154.490 138.971 118.862 1.00 57.05  ? 549  GLU A CG    1 
ATOM   4195  C  CD    . GLU A 1 549 ? 155.061 139.956 117.866 1.00 57.74  ? 549  GLU A CD    1 
ATOM   4196  O  OE1   . GLU A 1 549 ? 155.739 139.524 116.913 1.00 55.38  ? 549  GLU A OE1   1 
ATOM   4197  O  OE2   . GLU A 1 549 ? 154.836 141.171 118.042 1.00 58.98  ? 549  GLU A OE2   1 
ATOM   4198  N  N     . HIS A 1 550 ? 154.197 134.302 118.236 1.00 58.01  ? 550  HIS A N     1 
ATOM   4199  C  CA    . HIS A 1 550 ? 154.698 132.958 118.471 1.00 59.70  ? 550  HIS A CA    1 
ATOM   4200  C  C     . HIS A 1 550 ? 154.469 132.010 117.304 1.00 60.20  ? 550  HIS A C     1 
ATOM   4201  O  O     . HIS A 1 550 ? 155.091 130.944 117.265 1.00 59.85  ? 550  HIS A O     1 
ATOM   4202  C  CB    . HIS A 1 550 ? 154.052 132.370 119.730 1.00 58.24  ? 550  HIS A CB    1 
ATOM   4203  C  CG    . HIS A 1 550 ? 152.563 132.252 119.645 1.00 61.52  ? 550  HIS A CG    1 
ATOM   4204  N  ND1   . HIS A 1 550 ? 151.713 133.269 120.022 1.00 60.38  ? 550  HIS A ND1   1 
ATOM   4205  C  CD2   . HIS A 1 550 ? 151.771 131.234 119.232 1.00 59.99  ? 550  HIS A CD2   1 
ATOM   4206  C  CE1   . HIS A 1 550 ? 150.462 132.883 119.841 1.00 61.41  ? 550  HIS A CE1   1 
ATOM   4207  N  NE2   . HIS A 1 550 ? 150.470 131.653 119.363 1.00 61.29  ? 550  HIS A NE2   1 
ATOM   4208  N  N     . VAL A 1 551 ? 153.604 132.359 116.364 1.00 57.34  ? 551  VAL A N     1 
ATOM   4209  C  CA    . VAL A 1 551 ? 153.303 131.466 115.253 1.00 56.76  ? 551  VAL A CA    1 
ATOM   4210  C  C     . VAL A 1 551 ? 154.440 131.511 114.242 1.00 53.41  ? 551  VAL A C     1 
ATOM   4211  O  O     . VAL A 1 551 ? 155.185 132.492 114.148 1.00 55.50  ? 551  VAL A O     1 
ATOM   4212  C  CB    . VAL A 1 551 ? 151.953 131.830 114.606 1.00 51.55  ? 551  VAL A CB    1 
ATOM   4213  C  CG1   . VAL A 1 551 ? 150.809 131.470 115.532 1.00 51.13  ? 551  VAL A CG1   1 
ATOM   4214  C  CG2   . VAL A 1 551 ? 151.910 133.298 114.283 1.00 47.97  ? 551  VAL A CG2   1 
ATOM   4215  N  N     . GLU A 1 552 ? 154.580 130.430 113.483 1.00 46.67  ? 552  GLU A N     1 
ATOM   4216  C  CA    . GLU A 1 552 ? 155.626 130.338 112.477 1.00 46.99  ? 552  GLU A CA    1 
ATOM   4217  C  C     . GLU A 1 552 ? 155.158 130.994 111.185 1.00 53.00  ? 552  GLU A C     1 
ATOM   4218  O  O     . GLU A 1 552 ? 154.066 130.701 110.690 1.00 54.22  ? 552  GLU A O     1 
ATOM   4219  C  CB    . GLU A 1 552 ? 155.999 128.878 112.232 1.00 46.19  ? 552  GLU A CB    1 
ATOM   4220  C  CG    . GLU A 1 552 ? 157.107 128.683 111.219 1.00 51.55  ? 552  GLU A CG    1 
ATOM   4221  C  CD    . GLU A 1 552 ? 157.401 127.220 110.958 1.00 58.95  ? 552  GLU A CD    1 
ATOM   4222  O  OE1   . GLU A 1 552 ? 156.697 126.360 111.529 1.00 58.71  ? 552  GLU A OE1   1 
ATOM   4223  O  OE2   . GLU A 1 552 ? 158.335 126.928 110.182 1.00 57.12  ? 552  GLU A OE2   1 
ATOM   4224  N  N     . ARG A 1 553 ? 155.981 131.890 110.649 1.00 45.39  ? 553  ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 553 ? 155.639 132.579 109.413 1.00 39.34  ? 553  ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 553 ? 155.640 131.598 108.248 1.00 40.69  ? 553  ARG A C     1 
ATOM   4227  O  O     . ARG A 1 553 ? 156.599 130.845 108.056 1.00 46.52  ? 553  ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 553 ? 156.626 133.715 109.147 1.00 37.53  ? 553  ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 553 ? 156.191 135.083 109.655 1.00 37.62  ? 553  ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 553 ? 155.995 135.105 111.159 1.00 39.78  ? 553  ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 553 ? 155.663 136.441 111.637 1.00 39.05  ? 553  ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 553 ? 155.167 136.705 112.838 1.00 41.87  ? 553  ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 553 ? 154.921 135.742 113.710 1.00 39.34  ? 553  ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 553 ? 154.907 137.966 113.169 1.00 41.49  ? 553  ARG A NH2   1 
ATOM   4235  N  N     . LYS A 1 554 ? 154.561 131.606 107.469 1.00 36.68  ? 554  LYS A N     1 
ATOM   4236  C  CA    . LYS A 1 554 ? 154.438 130.750 106.301 1.00 37.11  ? 554  LYS A CA    1 
ATOM   4237  C  C     . LYS A 1 554 ? 154.047 131.609 105.105 1.00 37.83  ? 554  LYS A C     1 
ATOM   4238  O  O     . LYS A 1 554 ? 153.085 132.391 105.195 1.00 40.57  ? 554  LYS A O     1 
ATOM   4239  C  CB    . LYS A 1 554 ? 153.403 129.644 106.530 1.00 33.51  ? 554  LYS A CB    1 
ATOM   4240  C  CG    . LYS A 1 554 ? 153.707 128.738 107.705 1.00 41.43  ? 554  LYS A CG    1 
ATOM   4241  C  CD    . LYS A 1 554 ? 152.645 127.666 107.858 1.00 37.89  ? 554  LYS A CD    1 
ATOM   4242  C  CE    . LYS A 1 554 ? 152.884 126.831 109.100 1.00 36.20  ? 554  LYS A CE    1 
ATOM   4243  N  NZ    . LYS A 1 554 ? 151.815 125.818 109.296 1.00 38.45  ? 554  LYS A NZ    1 
ATOM   4244  N  N     . PRO A 1 555 ? 154.756 131.507 103.983 1.00 31.32  ? 555  PRO A N     1 
ATOM   4245  C  CA    . PRO A 1 555 ? 154.444 132.362 102.834 1.00 28.03  ? 555  PRO A CA    1 
ATOM   4246  C  C     . PRO A 1 555 ? 153.106 132.016 102.201 1.00 27.79  ? 555  PRO A C     1 
ATOM   4247  O  O     . PRO A 1 555 ? 152.673 130.861 102.186 1.00 31.66  ? 555  PRO A O     1 
ATOM   4248  C  CB    . PRO A 1 555 ? 155.601 132.089 101.867 1.00 27.94  ? 555  PRO A CB    1 
ATOM   4249  C  CG    . PRO A 1 555 ? 156.068 130.722 102.227 1.00 30.01  ? 555  PRO A CG    1 
ATOM   4250  C  CD    . PRO A 1 555 ? 155.887 130.604 103.711 1.00 28.70  ? 555  PRO A CD    1 
ATOM   4251  N  N     . ARG A 1 556 ? 152.449 133.043 101.668 1.00 22.50  ? 556  ARG A N     1 
ATOM   4252  C  CA    . ARG A 1 556 ? 151.202 132.845 100.947 1.00 22.84  ? 556  ARG A CA    1 
ATOM   4253  C  C     . ARG A 1 556 ? 151.492 132.434 99.511  1.00 29.11  ? 556  ARG A C     1 
ATOM   4254  O  O     . ARG A 1 556 ? 152.352 133.014 98.844  1.00 35.29  ? 556  ARG A O     1 
ATOM   4255  C  CB    . ARG A 1 556 ? 150.351 134.115 100.968 1.00 27.00  ? 556  ARG A CB    1 
ATOM   4256  C  CG    . ARG A 1 556 ? 149.051 133.975 100.197 1.00 25.06  ? 556  ARG A CG    1 
ATOM   4257  C  CD    . ARG A 1 556 ? 148.165 135.191 100.337 1.00 27.39  ? 556  ARG A CD    1 
ATOM   4258  N  NE    . ARG A 1 556 ? 146.898 135.007 99.642  1.00 23.30  ? 556  ARG A NE    1 
ATOM   4259  C  CZ    . ARG A 1 556 ? 145.870 135.839 99.727  1.00 26.47  ? 556  ARG A CZ    1 
ATOM   4260  N  NH1   . ARG A 1 556 ? 145.922 136.926 100.477 1.00 30.04  ? 556  ARG A NH1   1 
ATOM   4261  N  NH2   . ARG A 1 556 ? 144.762 135.573 99.044  1.00 18.37  ? 556  ARG A NH2   1 
ATOM   4262  N  N     . VAL A 1 557 ? 150.768 131.419 99.040  1.00 33.93  ? 557  VAL A N     1 
ATOM   4263  C  CA    . VAL A 1 557 ? 151.029 130.867 97.718  1.00 31.63  ? 557  VAL A CA    1 
ATOM   4264  C  C     . VAL A 1 557 ? 150.583 131.857 96.650  1.00 34.38  ? 557  VAL A C     1 
ATOM   4265  O  O     . VAL A 1 557 ? 149.564 132.547 96.795  1.00 41.84  ? 557  VAL A O     1 
ATOM   4266  C  CB    . VAL A 1 557 ? 150.336 129.501 97.566  1.00 31.64  ? 557  VAL A CB    1 
ATOM   4267  C  CG1   . VAL A 1 557 ? 148.830 129.645 97.652  1.00 35.46  ? 557  VAL A CG1   1 
ATOM   4268  C  CG2   . VAL A 1 557 ? 150.747 128.831 96.269  1.00 33.00  ? 557  VAL A CG2   1 
ATOM   4269  N  N     . LYS A 1 558 ? 151.367 131.959 95.583  1.00 33.45  ? 558  LYS A N     1 
ATOM   4270  C  CA    . LYS A 1 558 ? 151.081 132.861 94.479  1.00 33.71  ? 558  LYS A CA    1 
ATOM   4271  C  C     . LYS A 1 558 ? 150.672 132.058 93.254  1.00 38.21  ? 558  LYS A C     1 
ATOM   4272  O  O     . LYS A 1 558 ? 151.343 131.087 92.888  1.00 36.53  ? 558  LYS A O     1 
ATOM   4273  C  CB    . LYS A 1 558 ? 152.293 133.737 94.159  1.00 38.60  ? 558  LYS A CB    1 
ATOM   4274  C  CG    . LYS A 1 558 ? 152.715 134.639 95.301  1.00 37.29  ? 558  LYS A CG    1 
ATOM   4275  C  CD    . LYS A 1 558 ? 151.569 135.521 95.755  1.00 37.49  ? 558  LYS A CD    1 
ATOM   4276  C  CE    . LYS A 1 558 ? 151.973 136.380 96.938  1.00 40.82  ? 558  LYS A CE    1 
ATOM   4277  N  NZ    . LYS A 1 558 ? 150.841 137.211 97.427  1.00 38.81  ? 558  LYS A NZ    1 
ATOM   4278  N  N     . VAL A 1 559 ? 149.570 132.459 92.632  1.00 47.14  ? 559  VAL A N     1 
ATOM   4279  C  CA    . VAL A 1 559 ? 149.099 131.864 91.389  1.00 44.77  ? 559  VAL A CA    1 
ATOM   4280  C  C     . VAL A 1 559 ? 149.542 132.759 90.242  1.00 45.31  ? 559  VAL A C     1 
ATOM   4281  O  O     . VAL A 1 559 ? 149.383 133.984 90.302  1.00 45.43  ? 559  VAL A O     1 
ATOM   4282  C  CB    . VAL A 1 559 ? 147.572 131.683 91.400  1.00 39.91  ? 559  VAL A CB    1 
ATOM   4283  C  CG1   . VAL A 1 559 ? 147.117 130.967 90.146  1.00 42.99  ? 559  VAL A CG1   1 
ATOM   4284  C  CG2   . VAL A 1 559 ? 147.143 130.914 92.635  1.00 40.85  ? 559  VAL A CG2   1 
ATOM   4285  N  N     . LYS A 1 560 ? 150.110 132.154 89.204  1.00 53.03  ? 560  LYS A N     1 
ATOM   4286  C  CA    . LYS A 1 560 ? 150.687 132.911 88.102  1.00 54.19  ? 560  LYS A CA    1 
ATOM   4287  C  C     . LYS A 1 560 ? 149.588 133.369 87.153  1.00 53.85  ? 560  LYS A C     1 
ATOM   4288  O  O     . LYS A 1 560 ? 148.848 132.546 86.608  1.00 53.50  ? 560  LYS A O     1 
ATOM   4289  C  CB    . LYS A 1 560 ? 151.715 132.061 87.361  1.00 55.24  ? 560  LYS A CB    1 
ATOM   4290  C  CG    . LYS A 1 560 ? 153.152 132.465 87.616  1.00 53.66  ? 560  LYS A CG    1 
ATOM   4291  C  CD    . LYS A 1 560 ? 153.474 133.776 86.931  1.00 52.26  ? 560  LYS A CD    1 
ATOM   4292  C  CE    . LYS A 1 560 ? 153.229 133.678 85.437  1.00 52.99  ? 560  LYS A CE    1 
ATOM   4293  N  NZ    . LYS A 1 560 ? 153.992 132.556 84.830  1.00 54.35  ? 560  LYS A NZ    1 
ATOM   4294  N  N     . LEU A 1 561 ? 149.490 134.677 86.950  1.00 58.84  ? 561  LEU A N     1 
ATOM   4295  C  CA    . LEU A 1 561 ? 148.531 135.217 86.004  1.00 56.93  ? 561  LEU A CA    1 
ATOM   4296  C  C     . LEU A 1 561 ? 149.050 135.065 84.579  1.00 55.68  ? 561  LEU A C     1 
ATOM   4297  O  O     . LEU A 1 561 ? 150.228 134.790 84.343  1.00 57.53  ? 561  LEU A O     1 
ATOM   4298  C  CB    . LEU A 1 561 ? 148.257 136.692 86.297  1.00 57.25  ? 561  LEU A CB    1 
ATOM   4299  C  CG    . LEU A 1 561 ? 147.881 137.079 87.726  1.00 59.94  ? 561  LEU A CG    1 
ATOM   4300  C  CD1   . LEU A 1 561 ? 147.646 138.573 87.818  1.00 58.10  ? 561  LEU A CD1   1 
ATOM   4301  C  CD2   . LEU A 1 561 ? 146.655 136.315 88.183  1.00 59.27  ? 561  LEU A CD2   1 
ATOM   4302  N  N     . LEU A 1 562 ? 148.146 135.241 83.621  1.00 58.31  ? 562  LEU A N     1 
ATOM   4303  C  CA    . LEU A 1 562 ? 148.565 135.368 82.234  1.00 61.23  ? 562  LEU A CA    1 
ATOM   4304  C  C     . LEU A 1 562 ? 149.379 136.645 82.065  1.00 63.62  ? 562  LEU A C     1 
ATOM   4305  O  O     . LEU A 1 562 ? 149.177 137.631 82.779  1.00 64.14  ? 562  LEU A O     1 
ATOM   4306  C  CB    . LEU A 1 562 ? 147.351 135.379 81.304  1.00 60.42  ? 562  LEU A CB    1 
ATOM   4307  C  CG    . LEU A 1 562 ? 146.890 134.039 80.724  1.00 56.88  ? 562  LEU A CG    1 
ATOM   4308  C  CD1   . LEU A 1 562 ? 146.552 133.038 81.813  1.00 58.20  ? 562  LEU A CD1   1 
ATOM   4309  C  CD2   . LEU A 1 562 ? 145.702 134.244 79.803  1.00 58.37  ? 562  LEU A CD2   1 
ATOM   4310  N  N     . ASP A 1 563 ? 150.321 136.612 81.129  1.00 71.29  ? 563  ASP A N     1 
ATOM   4311  C  CA    . ASP A 1 563 ? 151.234 137.734 80.953  1.00 70.65  ? 563  ASP A CA    1 
ATOM   4312  C  C     . ASP A 1 563 ? 150.455 138.989 80.572  1.00 70.07  ? 563  ASP A C     1 
ATOM   4313  O  O     . ASP A 1 563 ? 149.567 138.927 79.719  1.00 70.16  ? 563  ASP A O     1 
ATOM   4314  C  CB    . ASP A 1 563 ? 152.273 137.420 79.878  1.00 72.90  ? 563  ASP A CB    1 
ATOM   4315  C  CG    . ASP A 1 563 ? 153.172 136.269 80.259  1.00 76.32  ? 563  ASP A CG    1 
ATOM   4316  O  OD1   . ASP A 1 563 ? 153.453 136.107 81.464  1.00 74.80  ? 563  ASP A OD1   1 
ATOM   4317  O  OD2   . ASP A 1 563 ? 153.599 135.523 79.353  1.00 76.70  ? 563  ASP A OD2   1 
ATOM   4318  N  N     . PRO A 1 564 ? 150.755 140.137 81.189  1.00 69.69  ? 564  PRO A N     1 
ATOM   4319  C  CA    . PRO A 1 564 ? 149.976 141.354 80.895  1.00 72.56  ? 564  PRO A CA    1 
ATOM   4320  C  C     . PRO A 1 564 ? 149.969 141.743 79.428  1.00 73.26  ? 564  PRO A C     1 
ATOM   4321  O  O     . PRO A 1 564 ? 148.923 142.151 78.901  1.00 76.62  ? 564  PRO A O     1 
ATOM   4322  C  CB    . PRO A 1 564 ? 150.669 142.419 81.756  1.00 70.49  ? 564  PRO A CB    1 
ATOM   4323  C  CG    . PRO A 1 564 ? 151.328 141.654 82.849  1.00 68.54  ? 564  PRO A CG    1 
ATOM   4324  C  CD    . PRO A 1 564 ? 151.755 140.356 82.246  1.00 71.00  ? 564  PRO A CD    1 
ATOM   4325  N  N     . GLU A 1 565 ? 151.109 141.611 78.747  1.00 72.34  ? 565  GLU A N     1 
ATOM   4326  C  CA    . GLU A 1 565 ? 151.179 141.994 77.341  1.00 72.32  ? 565  GLU A CA    1 
ATOM   4327  C  C     . GLU A 1 565 ? 150.297 141.104 76.478  1.00 72.60  ? 565  GLU A C     1 
ATOM   4328  O  O     . GLU A 1 565 ? 149.632 141.588 75.556  1.00 71.18  ? 565  GLU A O     1 
ATOM   4329  C  CB    . GLU A 1 565 ? 152.627 141.954 76.859  1.00 73.18  ? 565  GLU A CB    1 
ATOM   4330  C  CG    . GLU A 1 565 ? 153.505 143.030 77.475  1.00 73.39  ? 565  GLU A CG    1 
ATOM   4331  C  CD    . GLU A 1 565 ? 153.037 144.434 77.135  1.00 75.01  ? 565  GLU A CD    1 
ATOM   4332  O  OE1   . GLU A 1 565 ? 152.502 144.635 76.024  1.00 74.89  ? 565  GLU A OE1   1 
ATOM   4333  O  OE2   . GLU A 1 565 ? 153.202 145.337 77.981  1.00 73.85  ? 565  GLU A OE2   1 
ATOM   4334  N  N     . ILE A 1 566 ? 150.280 139.799 76.755  1.00 71.96  ? 566  ILE A N     1 
ATOM   4335  C  CA    . ILE A 1 566 ? 149.350 138.920 76.058  1.00 72.75  ? 566  ILE A CA    1 
ATOM   4336  C  C     . ILE A 1 566 ? 147.951 139.013 76.655  1.00 73.68  ? 566  ILE A C     1 
ATOM   4337  O  O     . ILE A 1 566 ? 146.975 138.640 75.996  1.00 71.90  ? 566  ILE A O     1 
ATOM   4338  C  CB    . ILE A 1 566 ? 149.864 137.469 76.064  1.00 73.24  ? 566  ILE A CB    1 
ATOM   4339  C  CG1   . ILE A 1 566 ? 149.212 136.658 74.945  1.00 72.74  ? 566  ILE A CG1   1 
ATOM   4340  C  CG2   . ILE A 1 566 ? 149.596 136.797 77.395  1.00 70.80  ? 566  ILE A CG2   1 
ATOM   4341  C  CD1   . ILE A 1 566 ? 149.562 135.189 74.976  1.00 73.19  ? 566  ILE A CD1   1 
ATOM   4342  N  N     . ARG A 1 567 ? 147.826 139.524 77.882  1.00 67.66  ? 567  ARG A N     1 
ATOM   4343  C  CA    . ARG A 1 567 ? 146.519 139.655 78.515  1.00 63.14  ? 567  ARG A CA    1 
ATOM   4344  C  C     . ARG A 1 567 ? 145.699 140.778 77.898  1.00 64.96  ? 567  ARG A C     1 
ATOM   4345  O  O     . ARG A 1 567 ? 144.472 140.668 77.802  1.00 69.30  ? 567  ARG A O     1 
ATOM   4346  C  CB    . ARG A 1 567 ? 146.693 139.900 80.010  1.00 61.02  ? 567  ARG A CB    1 
ATOM   4347  C  CG    . ARG A 1 567 ? 145.453 139.767 80.843  1.00 60.93  ? 567  ARG A CG    1 
ATOM   4348  C  CD    . ARG A 1 567 ? 145.681 140.433 82.181  1.00 65.48  ? 567  ARG A CD    1 
ATOM   4349  N  NE    . ARG A 1 567 ? 146.895 139.958 82.831  1.00 67.28  ? 567  ARG A NE    1 
ATOM   4350  C  CZ    . ARG A 1 567 ? 147.535 140.616 83.788  1.00 65.95  ? 567  ARG A CZ    1 
ATOM   4351  N  NH1   . ARG A 1 567 ? 147.116 141.793 84.217  1.00 68.98  ? 567  ARG A NH1   1 
ATOM   4352  N  NH2   . ARG A 1 567 ? 148.627 140.080 84.324  1.00 60.16  ? 567  ARG A NH2   1 
ATOM   4353  N  N     . LYS A 1 568 ? 146.348 141.862 77.479  1.00 66.03  ? 568  LYS A N     1 
ATOM   4354  C  CA    . LYS A 1 568 ? 145.630 143.035 76.996  1.00 62.76  ? 568  LYS A CA    1 
ATOM   4355  C  C     . LYS A 1 568 ? 145.158 142.907 75.546  1.00 64.04  ? 568  LYS A C     1 
ATOM   4356  O  O     . LYS A 1 568 ? 144.830 143.926 74.928  1.00 60.98  ? 568  LYS A O     1 
ATOM   4357  C  CB    . LYS A 1 568 ? 146.499 144.285 77.155  1.00 63.16  ? 568  LYS A CB    1 
ATOM   4358  C  CG    . LYS A 1 568 ? 147.807 144.236 76.397  1.00 66.99  ? 568  LYS A CG    1 
ATOM   4359  C  CD    . LYS A 1 568 ? 148.638 145.476 76.671  1.00 67.55  ? 568  LYS A CD    1 
ATOM   4360  C  CE    . LYS A 1 568 ? 147.900 146.733 76.261  1.00 65.34  ? 568  LYS A CE    1 
ATOM   4361  N  NZ    . LYS A 1 568 ? 148.676 147.956 76.596  1.00 65.77  ? 568  LYS A NZ    1 
ATOM   4362  N  N     . SER A 1 569 ? 145.114 141.696 74.984  1.00 70.11  ? 569  SER A N     1 
ATOM   4363  C  CA    . SER A 1 569 ? 144.674 141.534 73.603  1.00 69.49  ? 569  SER A CA    1 
ATOM   4364  C  C     . SER A 1 569 ? 143.798 140.302 73.396  1.00 67.50  ? 569  SER A C     1 
ATOM   4365  O  O     . SER A 1 569 ? 143.625 139.867 72.252  1.00 67.62  ? 569  SER A O     1 
ATOM   4366  C  CB    . SER A 1 569 ? 145.875 141.458 72.658  1.00 69.00  ? 569  SER A CB    1 
ATOM   4367  O  OG    . SER A 1 569 ? 145.459 141.156 71.338  1.00 66.82  ? 569  SER A OG    1 
ATOM   4368  N  N     . ASN A 1 570 ? 143.247 139.724 74.460  1.00 60.20  ? 570  ASN A N     1 
ATOM   4369  C  CA    . ASN A 1 570 ? 142.404 138.546 74.332  1.00 61.12  ? 570  ASN A CA    1 
ATOM   4370  C  C     . ASN A 1 570 ? 141.421 138.496 75.489  1.00 61.30  ? 570  ASN A C     1 
ATOM   4371  O  O     . ASN A 1 570 ? 141.702 138.989 76.584  1.00 61.59  ? 570  ASN A O     1 
ATOM   4372  C  CB    . ASN A 1 570 ? 143.232 137.257 74.293  1.00 59.66  ? 570  ASN A CB    1 
ATOM   4373  C  CG    . ASN A 1 570 ? 144.323 137.234 75.342  1.00 61.05  ? 570  ASN A CG    1 
ATOM   4374  O  OD1   . ASN A 1 570 ? 144.051 137.212 76.540  1.00 60.26  ? 570  ASN A OD1   1 
ATOM   4375  N  ND2   . ASN A 1 570 ? 145.569 137.228 74.893  1.00 61.14  ? 570  ASN A ND2   1 
ATOM   4376  N  N     . PHE A 1 571 ? 140.264 137.895 75.235  1.00 53.23  ? 571  PHE A N     1 
ATOM   4377  C  CA    . PHE A 1 571 ? 139.255 137.683 76.271  1.00 51.74  ? 571  PHE A CA    1 
ATOM   4378  C  C     . PHE A 1 571 ? 139.404 136.311 76.922  1.00 54.87  ? 571  PHE A C     1 
ATOM   4379  O  O     . PHE A 1 571 ? 138.453 135.536 77.004  1.00 54.94  ? 571  PHE A O     1 
ATOM   4380  C  CB    . PHE A 1 571 ? 137.860 137.862 75.685  1.00 52.00  ? 571  PHE A CB    1 
ATOM   4381  C  CG    . PHE A 1 571 ? 137.535 139.280 75.314  1.00 52.21  ? 571  PHE A CG    1 
ATOM   4382  C  CD1   . PHE A 1 571 ? 137.011 140.151 76.251  1.00 52.56  ? 571  PHE A CD1   1 
ATOM   4383  C  CD2   . PHE A 1 571 ? 137.751 139.740 74.030  1.00 50.53  ? 571  PHE A CD2   1 
ATOM   4384  C  CE1   . PHE A 1 571 ? 136.712 141.454 75.913  1.00 51.59  ? 571  PHE A CE1   1 
ATOM   4385  C  CE2   . PHE A 1 571 ? 137.452 141.044 73.688  1.00 52.14  ? 571  PHE A CE2   1 
ATOM   4386  C  CZ    . PHE A 1 571 ? 136.932 141.900 74.631  1.00 53.13  ? 571  PHE A CZ    1 
ATOM   4387  N  N     . LYS A 1 572 ? 140.606 136.002 77.396  1.00 50.67  ? 572  LYS A N     1 
ATOM   4388  C  CA    . LYS A 1 572 ? 140.886 134.735 78.051  1.00 46.25  ? 572  LYS A CA    1 
ATOM   4389  C  C     . LYS A 1 572 ? 141.200 134.960 79.524  1.00 48.64  ? 572  LYS A C     1 
ATOM   4390  O  O     . LYS A 1 572 ? 141.588 136.055 79.940  1.00 51.63  ? 572  LYS A O     1 
ATOM   4391  C  CB    . LYS A 1 572 ? 142.037 133.996 77.361  1.00 48.69  ? 572  LYS A CB    1 
ATOM   4392  C  CG    . LYS A 1 572 ? 141.602 133.236 76.120  1.00 50.16  ? 572  LYS A CG    1 
ATOM   4393  C  CD    . LYS A 1 572 ? 142.732 132.420 75.528  1.00 49.60  ? 572  LYS A CD    1 
ATOM   4394  C  CE    . LYS A 1 572 ? 143.860 133.312 75.048  1.00 52.90  ? 572  LYS A CE    1 
ATOM   4395  N  NZ    . LYS A 1 572 ? 144.970 132.522 74.448  1.00 51.62  ? 572  LYS A NZ    1 
ATOM   4396  N  N     . GLU A 1 573 ? 141.029 133.896 80.306  1.00 48.27  ? 573  GLU A N     1 
ATOM   4397  C  CA    . GLU A 1 573 ? 140.986 134.007 81.760  1.00 47.55  ? 573  GLU A CA    1 
ATOM   4398  C  C     . GLU A 1 573 ? 142.342 134.422 82.314  1.00 45.67  ? 573  GLU A C     1 
ATOM   4399  O  O     . GLU A 1 573 ? 143.356 133.765 82.062  1.00 49.06  ? 573  GLU A O     1 
ATOM   4400  C  CB    . GLU A 1 573 ? 140.539 132.682 82.368  1.00 45.68  ? 573  GLU A CB    1 
ATOM   4401  C  CG    . GLU A 1 573 ? 140.009 132.804 83.779  1.00 50.21  ? 573  GLU A CG    1 
ATOM   4402  C  CD    . GLU A 1 573 ? 139.450 131.501 84.298  1.00 51.84  ? 573  GLU A CD    1 
ATOM   4403  O  OE1   . GLU A 1 573 ? 139.644 130.466 83.628  1.00 48.40  ? 573  GLU A OE1   1 
ATOM   4404  O  OE2   . GLU A 1 573 ? 138.813 131.510 85.372  1.00 48.29  ? 573  GLU A OE2   1 
ATOM   4405  N  N     . VAL A 1 574 ? 142.350 135.512 83.080  1.00 36.85  ? 574  VAL A N     1 
ATOM   4406  C  CA    . VAL A 1 574 ? 143.598 136.076 83.584  1.00 36.09  ? 574  VAL A CA    1 
ATOM   4407  C  C     . VAL A 1 574 ? 144.203 135.180 84.658  1.00 39.71  ? 574  VAL A C     1 
ATOM   4408  O  O     . VAL A 1 574 ? 145.409 134.906 84.653  1.00 44.69  ? 574  VAL A O     1 
ATOM   4409  C  CB    . VAL A 1 574 ? 143.354 137.500 84.111  1.00 37.79  ? 574  VAL A CB    1 
ATOM   4410  C  CG1   . VAL A 1 574 ? 144.630 138.083 84.688  1.00 38.72  ? 574  VAL A CG1   1 
ATOM   4411  C  CG2   . VAL A 1 574 ? 142.798 138.376 83.006  1.00 40.67  ? 574  VAL A CG2   1 
ATOM   4412  N  N     . GLU A 1 575 ? 143.381 134.713 85.591  1.00 46.75  ? 575  GLU A N     1 
ATOM   4413  C  CA    . GLU A 1 575 ? 143.861 133.992 86.758  1.00 44.71  ? 575  GLU A CA    1 
ATOM   4414  C  C     . GLU A 1 575 ? 143.411 132.541 86.716  1.00 44.82  ? 575  GLU A C     1 
ATOM   4415  O  O     . GLU A 1 575 ? 142.209 132.275 86.586  1.00 50.55  ? 575  GLU A O     1 
ATOM   4416  C  CB    . GLU A 1 575 ? 143.347 134.660 88.036  1.00 42.76  ? 575  GLU A CB    1 
ATOM   4417  C  CG    . GLU A 1 575 ? 143.726 133.943 89.310  1.00 44.62  ? 575  GLU A CG    1 
ATOM   4418  C  CD    . GLU A 1 575 ? 143.129 134.598 90.533  1.00 49.21  ? 575  GLU A CD    1 
ATOM   4419  O  OE1   . GLU A 1 575 ? 142.571 135.704 90.400  1.00 43.98  ? 575  GLU A OE1   1 
ATOM   4420  O  OE2   . GLU A 1 575 ? 143.214 134.006 91.628  1.00 51.14  ? 575  GLU A OE2   1 
ATOM   4421  N  N     . PRO A 1 576 ? 144.330 131.587 86.808  1.00 33.59  ? 576  PRO A N     1 
ATOM   4422  C  CA    . PRO A 1 576 ? 143.957 130.173 86.802  1.00 28.33  ? 576  PRO A CA    1 
ATOM   4423  C  C     . PRO A 1 576 ? 143.769 129.615 88.210  1.00 36.00  ? 576  PRO A C     1 
ATOM   4424  O  O     . PRO A 1 576 ? 144.072 130.259 89.215  1.00 34.49  ? 576  PRO A O     1 
ATOM   4425  C  CB    . PRO A 1 576 ? 145.157 129.517 86.110  1.00 31.72  ? 576  PRO A CB    1 
ATOM   4426  C  CG    . PRO A 1 576 ? 146.308 130.365 86.525  1.00 35.53  ? 576  PRO A CG    1 
ATOM   4427  C  CD    . PRO A 1 576 ? 145.785 131.772 86.697  1.00 37.80  ? 576  PRO A CD    1 
ATOM   4428  N  N     . THR A 1 577 ? 143.256 128.389 88.257  1.00 43.49  ? 577  THR A N     1 
ATOM   4429  C  CA    . THR A 1 577 ? 143.069 127.685 89.517  1.00 41.98  ? 577  THR A CA    1 
ATOM   4430  C  C     . THR A 1 577 ? 144.404 127.149 90.020  1.00 37.04  ? 577  THR A C     1 
ATOM   4431  O  O     . THR A 1 577 ? 145.212 126.630 89.246  1.00 31.05  ? 577  THR A O     1 
ATOM   4432  C  CB    . THR A 1 577 ? 142.065 126.543 89.343  1.00 41.33  ? 577  THR A CB    1 
ATOM   4433  O  OG1   . THR A 1 577 ? 140.847 127.057 88.791  1.00 46.02  ? 577  THR A OG1   1 
ATOM   4434  C  CG2   . THR A 1 577 ? 141.758 125.887 90.670  1.00 31.90  ? 577  THR A CG2   1 
ATOM   4435  N  N     . MET A 1 578 ? 144.632 127.282 91.325  1.00 44.37  ? 578  MET A N     1 
ATOM   4436  C  CA    . MET A 1 578 ? 145.912 126.930 91.917  1.00 41.45  ? 578  MET A CA    1 
ATOM   4437  C  C     . MET A 1 578 ? 146.162 125.426 91.833  1.00 45.21  ? 578  MET A C     1 
ATOM   4438  O  O     . MET A 1 578 ? 145.240 124.618 91.696  1.00 47.37  ? 578  MET A O     1 
ATOM   4439  C  CB    . MET A 1 578 ? 145.973 127.387 93.373  1.00 39.63  ? 578  MET A CB    1 
ATOM   4440  C  CG    . MET A 1 578 ? 144.854 126.844 94.236  1.00 41.86  ? 578  MET A CG    1 
ATOM   4441  S  SD    . MET A 1 578 ? 145.247 126.900 95.991  1.00 52.01  ? 578  MET A SD    1 
ATOM   4442  C  CE    . MET A 1 578 ? 145.707 128.613 96.177  1.00 34.50  ? 578  MET A CE    1 
ATOM   4443  N  N     . ASP A 1 579 ? 147.439 125.060 91.908  1.00 47.48  ? 579  ASP A N     1 
ATOM   4444  C  CA    . ASP A 1 579 ? 147.838 123.667 91.785  1.00 45.75  ? 579  ASP A CA    1 
ATOM   4445  C  C     . ASP A 1 579 ? 147.378 122.856 92.991  1.00 47.23  ? 579  ASP A C     1 
ATOM   4446  O  O     . ASP A 1 579 ? 147.259 123.369 94.105  1.00 47.18  ? 579  ASP A O     1 
ATOM   4447  C  CB    . ASP A 1 579 ? 149.354 123.562 91.640  1.00 48.76  ? 579  ASP A CB    1 
ATOM   4448  C  CG    . ASP A 1 579 ? 149.907 124.520 90.608  1.00 52.16  ? 579  ASP A CG    1 
ATOM   4449  O  OD1   . ASP A 1 579 ? 149.130 125.348 90.089  1.00 45.25  ? 579  ASP A OD1   1 
ATOM   4450  O  OD2   . ASP A 1 579 ? 151.118 124.444 90.313  1.00 55.26  ? 579  ASP A OD2   1 
ATOM   4451  N  N     . GLU A 1 580 ? 147.125 121.566 92.755  1.00 49.66  ? 580  GLU A N     1 
ATOM   4452  C  CA    . GLU A 1 580 ? 146.689 120.677 93.826  1.00 41.73  ? 580  GLU A CA    1 
ATOM   4453  C  C     . GLU A 1 580 ? 147.770 120.458 94.876  1.00 47.69  ? 580  GLU A C     1 
ATOM   4454  O  O     . GLU A 1 580 ? 147.449 120.118 96.020  1.00 50.44  ? 580  GLU A O     1 
ATOM   4455  C  CB    . GLU A 1 580 ? 146.251 119.334 93.239  1.00 45.67  ? 580  GLU A CB    1 
ATOM   4456  C  CG    . GLU A 1 580 ? 145.523 118.427 94.214  1.00 51.65  ? 580  GLU A CG    1 
ATOM   4457  C  CD    . GLU A 1 580 ? 145.072 117.129 93.575  1.00 58.38  ? 580  GLU A CD    1 
ATOM   4458  O  OE1   . GLU A 1 580 ? 145.363 116.922 92.378  1.00 57.47  ? 580  GLU A OE1   1 
ATOM   4459  O  OE2   . GLU A 1 580 ? 144.427 116.315 94.269  1.00 54.50  ? 580  GLU A OE2   1 
ATOM   4460  N  N     . GLU A 1 581 ? 149.040 120.655 94.519  1.00 54.25  ? 581  GLU A N     1 
ATOM   4461  C  CA    . GLU A 1 581 ? 150.122 120.438 95.472  1.00 54.16  ? 581  GLU A CA    1 
ATOM   4462  C  C     . GLU A 1 581 ? 150.189 121.536 96.527  1.00 53.97  ? 581  GLU A C     1 
ATOM   4463  O  O     . GLU A 1 581 ? 150.531 121.260 97.681  1.00 53.88  ? 581  GLU A O     1 
ATOM   4464  C  CB    . GLU A 1 581 ? 151.452 120.333 94.729  1.00 49.61  ? 581  GLU A CB    1 
ATOM   4465  C  CG    . GLU A 1 581 ? 151.453 119.296 93.622  1.00 55.01  ? 581  GLU A CG    1 
ATOM   4466  C  CD    . GLU A 1 581 ? 151.253 117.885 94.141  1.00 59.71  ? 581  GLU A CD    1 
ATOM   4467  O  OE1   . GLU A 1 581 ? 151.676 117.600 95.280  1.00 57.19  ? 581  GLU A OE1   1 
ATOM   4468  O  OE2   . GLU A 1 581 ? 150.669 117.061 93.408  1.00 54.83  ? 581  GLU A OE2   1 
ATOM   4469  N  N     . THR A 1 582 ? 149.874 122.775 96.159  1.00 43.56  ? 582  THR A N     1 
ATOM   4470  C  CA    . THR A 1 582 ? 149.957 123.899 97.083  1.00 44.33  ? 582  THR A CA    1 
ATOM   4471  C  C     . THR A 1 582 ? 148.677 124.114 97.881  1.00 47.36  ? 582  THR A C     1 
ATOM   4472  O  O     . THR A 1 582 ? 148.658 124.964 98.779  1.00 47.39  ? 582  THR A O     1 
ATOM   4473  C  CB    . THR A 1 582 ? 150.311 125.180 96.323  1.00 46.73  ? 582  THR A CB    1 
ATOM   4474  O  OG1   . THR A 1 582 ? 149.308 125.451 95.338  1.00 44.08  ? 582  THR A OG1   1 
ATOM   4475  C  CG2   . THR A 1 582 ? 151.655 125.028 95.639  1.00 45.61  ? 582  THR A CG2   1 
ATOM   4476  N  N     . VAL A 1 583 ? 147.624 123.348 97.589  1.00 35.96  ? 583  VAL A N     1 
ATOM   4477  C  CA    . VAL A 1 583 ? 146.348 123.516 98.279  1.00 30.04  ? 583  VAL A CA    1 
ATOM   4478  C  C     . VAL A 1 583 ? 146.485 123.179 99.759  1.00 38.00  ? 583  VAL A C     1 
ATOM   4479  O  O     . VAL A 1 583 ? 146.044 123.938 100.629 1.00 40.50  ? 583  VAL A O     1 
ATOM   4480  C  CB    . VAL A 1 583 ? 145.264 122.660 97.600  1.00 30.81  ? 583  VAL A CB    1 
ATOM   4481  C  CG1   . VAL A 1 583 ? 144.040 122.556 98.473  1.00 28.27  ? 583  VAL A CG1   1 
ATOM   4482  C  CG2   . VAL A 1 583 ? 144.898 123.258 96.265  1.00 37.00  ? 583  VAL A CG2   1 
ATOM   4483  N  N     . LEU A 1 584 ? 147.098 122.032 100.067 1.00 36.68  ? 584  LEU A N     1 
ATOM   4484  C  CA    . LEU A 1 584 ? 147.264 121.635 101.462 1.00 28.87  ? 584  LEU A CA    1 
ATOM   4485  C  C     . LEU A 1 584 ? 148.190 122.589 102.205 1.00 25.80  ? 584  LEU A C     1 
ATOM   4486  O  O     . LEU A 1 584 ? 147.929 122.942 103.362 1.00 32.49  ? 584  LEU A O     1 
ATOM   4487  C  CB    . LEU A 1 584 ? 147.791 120.202 101.547 1.00 39.53  ? 584  LEU A CB    1 
ATOM   4488  C  CG    . LEU A 1 584 ? 146.760 119.070 101.575 1.00 39.21  ? 584  LEU A CG    1 
ATOM   4489  C  CD1   . LEU A 1 584 ? 146.149 118.839 100.204 1.00 35.53  ? 584  LEU A CD1   1 
ATOM   4490  C  CD2   . LEU A 1 584 ? 147.384 117.794 102.106 1.00 30.36  ? 584  LEU A CD2   1 
ATOM   4491  N  N     . THR A 1 585 ? 149.272 123.020 101.553 1.00 27.96  ? 585  THR A N     1 
ATOM   4492  C  CA    . THR A 1 585 ? 150.200 123.953 102.182 1.00 31.98  ? 585  THR A CA    1 
ATOM   4493  C  C     . THR A 1 585 ? 149.516 125.272 102.516 1.00 32.91  ? 585  THR A C     1 
ATOM   4494  O  O     . THR A 1 585 ? 149.723 125.828 103.601 1.00 26.85  ? 585  THR A O     1 
ATOM   4495  C  CB    . THR A 1 585 ? 151.406 124.189 101.271 1.00 39.55  ? 585  THR A CB    1 
ATOM   4496  O  OG1   . THR A 1 585 ? 152.145 122.970 101.132 1.00 39.62  ? 585  THR A OG1   1 
ATOM   4497  C  CG2   . THR A 1 585 ? 152.316 125.267 101.844 1.00 33.94  ? 585  THR A CG2   1 
ATOM   4498  N  N     . GLU A 1 586 ? 148.688 125.785 101.604 1.00 33.47  ? 586  GLU A N     1 
ATOM   4499  C  CA    . GLU A 1 586 ? 148.001 127.042 101.881 1.00 26.53  ? 586  GLU A CA    1 
ATOM   4500  C  C     . GLU A 1 586 ? 146.909 126.863 102.929 1.00 29.29  ? 586  GLU A C     1 
ATOM   4501  O  O     . GLU A 1 586 ? 146.693 127.750 103.761 1.00 33.61  ? 586  GLU A O     1 
ATOM   4502  C  CB    . GLU A 1 586 ? 147.427 127.628 100.594 1.00 25.42  ? 586  GLU A CB    1 
ATOM   4503  C  CG    . GLU A 1 586 ? 146.808 129.005 100.772 1.00 31.96  ? 586  GLU A CG    1 
ATOM   4504  C  CD    . GLU A 1 586 ? 147.799 130.043 101.264 1.00 28.07  ? 586  GLU A CD    1 
ATOM   4505  O  OE1   . GLU A 1 586 ? 148.993 129.941 100.923 1.00 35.69  ? 586  GLU A OE1   1 
ATOM   4506  O  OE2   . GLU A 1 586 ? 147.384 130.964 101.996 1.00 27.67  ? 586  GLU A OE2   1 
ATOM   4507  N  N     . ALA A 1 587 ? 146.213 125.728 102.915 1.00 28.59  ? 587  ALA A N     1 
ATOM   4508  C  CA    . ALA A 1 587 ? 145.154 125.506 103.890 1.00 22.48  ? 587  ALA A CA    1 
ATOM   4509  C  C     . ALA A 1 587 ? 145.678 125.138 105.272 1.00 25.26  ? 587  ALA A C     1 
ATOM   4510  O  O     . ALA A 1 587 ? 144.897 125.134 106.228 1.00 22.83  ? 587  ALA A O     1 
ATOM   4511  C  CB    . ALA A 1 587 ? 144.201 124.416 103.399 1.00 22.21  ? 587  ALA A CB    1 
ATOM   4512  N  N     . GLN A 1 588 ? 146.965 124.827 105.405 1.00 23.74  ? 588  GLN A N     1 
ATOM   4513  C  CA    . GLN A 1 588 ? 147.543 124.518 106.705 1.00 18.59  ? 588  GLN A CA    1 
ATOM   4514  C  C     . GLN A 1 588 ? 148.193 125.725 107.373 1.00 23.47  ? 588  GLN A C     1 
ATOM   4515  O  O     . GLN A 1 588 ? 148.808 125.576 108.432 1.00 31.78  ? 588  GLN A O     1 
ATOM   4516  C  CB    . GLN A 1 588 ? 148.552 123.377 106.574 1.00 22.95  ? 588  GLN A CB    1 
ATOM   4517  C  CG    . GLN A 1 588 ? 147.891 122.017 106.456 1.00 23.52  ? 588  GLN A CG    1 
ATOM   4518  C  CD    . GLN A 1 588 ? 148.852 120.930 106.051 1.00 32.24  ? 588  GLN A CD    1 
ATOM   4519  O  OE1   . GLN A 1 588 ? 150.068 121.102 106.121 1.00 34.97  ? 588  GLN A OE1   1 
ATOM   4520  N  NE2   . GLN A 1 588 ? 148.313 119.801 105.616 1.00 32.06  ? 588  GLN A NE2   1 
ATOM   4521  N  N     . ARG A 1 589 ? 148.073 126.910 106.783 1.00 22.21  ? 589  ARG A N     1 
ATOM   4522  C  CA    . ARG A 1 589 ? 148.512 128.141 107.424 1.00 14.94  ? 589  ARG A CA    1 
ATOM   4523  C  C     . ARG A 1 589 ? 147.449 128.737 108.336 1.00 29.32  ? 589  ARG A C     1 
ATOM   4524  O  O     . ARG A 1 589 ? 147.700 129.773 108.959 1.00 31.89  ? 589  ARG A O     1 
ATOM   4525  C  CB    . ARG A 1 589 ? 148.917 129.175 106.371 1.00 16.62  ? 589  ARG A CB    1 
ATOM   4526  C  CG    . ARG A 1 589 ? 150.048 128.745 105.470 1.00 27.79  ? 589  ARG A CG    1 
ATOM   4527  C  CD    . ARG A 1 589 ? 150.370 129.810 104.436 1.00 26.75  ? 589  ARG A CD    1 
ATOM   4528  N  NE    . ARG A 1 589 ? 150.410 131.148 105.013 1.00 22.73  ? 589  ARG A NE    1 
ATOM   4529  C  CZ    . ARG A 1 589 ? 149.609 132.141 104.655 1.00 24.50  ? 589  ARG A CZ    1 
ATOM   4530  N  NH1   . ARG A 1 589 ? 148.707 131.992 103.700 1.00 26.14  ? 589  ARG A NH1   1 
ATOM   4531  N  NH2   . ARG A 1 589 ? 149.723 133.317 105.264 1.00 19.11  ? 589  ARG A NH2   1 
ATOM   4532  N  N     . CYS A 1 590 ? 146.274 128.119 108.419 1.00 26.94  ? 590  CYS A N     1 
ATOM   4533  C  CA    . CYS A 1 590 ? 145.202 128.642 109.253 1.00 12.13  ? 590  CYS A CA    1 
ATOM   4534  C  C     . CYS A 1 590 ? 145.557 128.496 110.727 1.00 17.73  ? 590  CYS A C     1 
ATOM   4535  O  O     . CYS A 1 590 ? 146.104 127.477 111.155 1.00 17.50  ? 590  CYS A O     1 
ATOM   4536  C  CB    . CYS A 1 590 ? 143.890 127.919 108.949 1.00 14.09  ? 590  CYS A CB    1 
ATOM   4537  S  SG    . CYS A 1 590 ? 142.403 128.785 109.512 1.00 11.79  ? 590  CYS A SG    1 
ATOM   4538  N  N     . MET A 1 591 ? 145.246 129.528 111.503 1.00 25.75  ? 591  MET A N     1 
ATOM   4539  C  CA    . MET A 1 591 ? 145.573 129.557 112.919 1.00 22.88  ? 591  MET A CA    1 
ATOM   4540  C  C     . MET A 1 591 ? 144.425 129.104 113.812 1.00 24.22  ? 591  MET A C     1 
ATOM   4541  O  O     . MET A 1 591 ? 144.609 129.027 115.030 1.00 30.04  ? 591  MET A O     1 
ATOM   4542  C  CB    . MET A 1 591 ? 146.023 130.962 113.320 1.00 21.05  ? 591  MET A CB    1 
ATOM   4543  C  CG    . MET A 1 591 ? 147.235 131.445 112.551 1.00 19.86  ? 591  MET A CG    1 
ATOM   4544  S  SD    . MET A 1 591 ? 147.964 132.924 113.264 1.00 30.32  ? 591  MET A SD    1 
ATOM   4545  C  CE    . MET A 1 591 ? 146.538 133.995 113.307 1.00 22.15  ? 591  MET A CE    1 
ATOM   4546  N  N     . SER A 1 592 ? 143.262 128.798 113.238 1.00 10.55  ? 592  SER A N     1 
ATOM   4547  C  CA    . SER A 1 592 ? 142.096 128.300 113.972 1.00 6.00   ? 592  SER A CA    1 
ATOM   4548  C  C     . SER A 1 592 ? 141.713 129.246 115.113 1.00 15.49  ? 592  SER A C     1 
ATOM   4549  O  O     . SER A 1 592 ? 141.781 128.912 116.295 1.00 25.48  ? 592  SER A O     1 
ATOM   4550  C  CB    . SER A 1 592 ? 142.338 126.878 114.485 1.00 16.44  ? 592  SER A CB    1 
ATOM   4551  O  OG    . SER A 1 592 ? 142.416 125.954 113.414 1.00 18.96  ? 592  SER A OG    1 
ATOM   4552  N  N     . CYS A 1 593 ? 141.309 130.456 114.726 1.00 20.24  ? 593  CYS A N     1 
ATOM   4553  C  CA    . CYS A 1 593 ? 141.002 131.486 115.710 1.00 18.02  ? 593  CYS A CA    1 
ATOM   4554  C  C     . CYS A 1 593 ? 139.672 131.234 116.407 1.00 17.35  ? 593  CYS A C     1 
ATOM   4555  O  O     . CYS A 1 593 ? 139.503 131.617 117.570 1.00 28.43  ? 593  CYS A O     1 
ATOM   4556  C  CB    . CYS A 1 593 ? 140.998 132.855 115.035 1.00 15.13  ? 593  CYS A CB    1 
ATOM   4557  S  SG    . CYS A 1 593 ? 142.363 133.097 113.882 1.00 15.88  ? 593  CYS A SG    1 
ATOM   4558  N  N     . GLY A 1 594 ? 138.721 130.605 115.723 1.00 11.31  ? 594  GLY A N     1 
ATOM   4559  C  CA    . GLY A 1 594 ? 137.427 130.355 116.324 1.00 12.43  ? 594  GLY A CA    1 
ATOM   4560  C  C     . GLY A 1 594 ? 137.504 129.366 117.470 1.00 20.63  ? 594  GLY A C     1 
ATOM   4561  O  O     . GLY A 1 594 ? 138.366 128.489 117.517 1.00 36.94  ? 594  GLY A O     1 
ATOM   4562  N  N     . CYS A 1 595 ? 136.582 129.522 118.415 1.00 21.29  ? 595  CYS A N     1 
ATOM   4563  C  CA    . CYS A 1 595 ? 136.535 128.649 119.578 1.00 16.91  ? 595  CYS A CA    1 
ATOM   4564  C  C     . CYS A 1 595 ? 136.169 127.233 119.156 1.00 20.79  ? 595  CYS A C     1 
ATOM   4565  O  O     . CYS A 1 595 ? 135.274 127.025 118.335 1.00 28.32  ? 595  CYS A O     1 
ATOM   4566  C  CB    . CYS A 1 595 ? 135.520 129.179 120.591 1.00 17.25  ? 595  CYS A CB    1 
ATOM   4567  S  SG    . CYS A 1 595 ? 135.792 128.704 122.307 1.00 4.83   ? 595  CYS A SG    1 
ATOM   4568  N  N     . MET A 1 596 ? 136.875 126.253 119.721 1.00 21.53  ? 596  MET A N     1 
ATOM   4569  C  CA    . MET A 1 596 ? 136.621 124.860 119.375 1.00 19.83  ? 596  MET A CA    1 
ATOM   4570  C  C     . MET A 1 596 ? 135.273 124.374 119.884 1.00 21.14  ? 596  MET A C     1 
ATOM   4571  O  O     . MET A 1 596 ? 134.754 123.376 119.373 1.00 31.10  ? 596  MET A O     1 
ATOM   4572  C  CB    . MET A 1 596 ? 137.734 123.974 119.926 1.00 21.89  ? 596  MET A CB    1 
ATOM   4573  C  CG    . MET A 1 596 ? 139.089 124.226 119.299 1.00 31.34  ? 596  MET A CG    1 
ATOM   4574  S  SD    . MET A 1 596 ? 139.104 123.864 117.536 1.00 40.95  ? 596  MET A SD    1 
ATOM   4575  C  CE    . MET A 1 596 ? 138.471 122.193 117.552 1.00 30.20  ? 596  MET A CE    1 
ATOM   4576  N  N     . GLU A 1 597 ? 134.697 125.054 120.871 1.00 22.33  ? 597  GLU A N     1 
ATOM   4577  C  CA    . GLU A 1 597 ? 133.397 124.706 121.421 1.00 21.73  ? 597  GLU A CA    1 
ATOM   4578  C  C     . GLU A 1 597 ? 132.339 125.745 121.072 1.00 23.32  ? 597  GLU A C     1 
ATOM   4579  O  O     . GLU A 1 597 ? 131.421 125.987 121.854 1.00 38.76  ? 597  GLU A O     1 
ATOM   4580  C  CB    . GLU A 1 597 ? 133.491 124.531 122.935 1.00 21.28  ? 597  GLU A CB    1 
ATOM   4581  C  CG    . GLU A 1 597 ? 134.353 123.363 123.364 1.00 37.01  ? 597  GLU A CG    1 
ATOM   4582  C  CD    . GLU A 1 597 ? 133.739 122.024 123.017 1.00 36.04  ? 597  GLU A CD    1 
ATOM   4583  O  OE1   . GLU A 1 597 ? 132.497 121.944 122.903 1.00 40.47  ? 597  GLU A OE1   1 
ATOM   4584  O  OE2   . GLU A 1 597 ? 134.499 121.046 122.856 1.00 20.66  ? 597  GLU A OE2   1 
ATOM   4585  N  N     . VAL A 1 598 ? 132.457 126.364 119.896 1.00 19.94  ? 598  VAL A N     1 
ATOM   4586  C  CA    . VAL A 1 598 ? 131.516 127.409 119.508 1.00 19.61  ? 598  VAL A CA    1 
ATOM   4587  C  C     . VAL A 1 598 ? 130.112 126.840 119.328 1.00 24.39  ? 598  VAL A C     1 
ATOM   4588  O  O     . VAL A 1 598 ? 129.119 127.516 119.623 1.00 29.44  ? 598  VAL A O     1 
ATOM   4589  C  CB    . VAL A 1 598 ? 132.026 128.135 118.245 1.00 14.53  ? 598  VAL A CB    1 
ATOM   4590  C  CG1   . VAL A 1 598 ? 132.302 127.156 117.130 1.00 25.07  ? 598  VAL A CG1   1 
ATOM   4591  C  CG2   . VAL A 1 598 ? 131.046 129.198 117.790 1.00 27.15  ? 598  VAL A CG2   1 
ATOM   4592  N  N     . PHE A 1 599 ? 129.996 125.596 118.877 1.00 21.30  ? 599  PHE A N     1 
ATOM   4593  C  CA    . PHE A 1 599 ? 128.688 124.991 118.674 1.00 21.64  ? 599  PHE A CA    1 
ATOM   4594  C  C     . PHE A 1 599 ? 128.110 124.369 119.938 1.00 26.68  ? 599  PHE A C     1 
ATOM   4595  O  O     . PHE A 1 599 ? 126.946 123.957 119.928 1.00 31.18  ? 599  PHE A O     1 
ATOM   4596  C  CB    . PHE A 1 599 ? 128.766 123.939 117.564 1.00 23.74  ? 599  PHE A CB    1 
ATOM   4597  C  CG    . PHE A 1 599 ? 129.250 124.487 116.256 1.00 28.37  ? 599  PHE A CG    1 
ATOM   4598  C  CD1   . PHE A 1 599 ? 128.376 125.122 115.393 1.00 24.82  ? 599  PHE A CD1   1 
ATOM   4599  C  CD2   . PHE A 1 599 ? 130.580 124.382 115.894 1.00 29.86  ? 599  PHE A CD2   1 
ATOM   4600  C  CE1   . PHE A 1 599 ? 128.821 125.638 114.196 1.00 25.76  ? 599  PHE A CE1   1 
ATOM   4601  C  CE2   . PHE A 1 599 ? 131.029 124.896 114.696 1.00 13.66  ? 599  PHE A CE2   1 
ATOM   4602  C  CZ    . PHE A 1 599 ? 130.148 125.523 113.847 1.00 26.79  ? 599  PHE A CZ    1 
ATOM   4603  N  N     . ARG A 1 600 ? 128.879 124.305 121.025 1.00 27.29  ? 600  ARG A N     1 
ATOM   4604  C  CA    . ARG A 1 600 ? 128.401 123.729 122.271 1.00 16.79  ? 600  ARG A CA    1 
ATOM   4605  C  C     . ARG A 1 600 ? 128.524 124.649 123.476 1.00 18.24  ? 600  ARG A C     1 
ATOM   4606  O  O     . ARG A 1 600 ? 128.007 124.299 124.543 1.00 27.90  ? 600  ARG A O     1 
ATOM   4607  C  CB    . ARG A 1 600 ? 129.144 122.421 122.578 1.00 19.31  ? 600  ARG A CB    1 
ATOM   4608  C  CG    . ARG A 1 600 ? 128.843 121.293 121.616 1.00 23.31  ? 600  ARG A CG    1 
ATOM   4609  C  CD    . ARG A 1 600 ? 129.268 119.967 122.202 1.00 30.40  ? 600  ARG A CD    1 
ATOM   4610  N  NE    . ARG A 1 600 ? 130.655 119.993 122.649 1.00 34.23  ? 600  ARG A NE    1 
ATOM   4611  C  CZ    . ARG A 1 600 ? 131.252 118.999 123.291 1.00 35.36  ? 600  ARG A CZ    1 
ATOM   4612  N  NH1   . ARG A 1 600 ? 130.611 117.879 123.582 1.00 29.21  ? 600  ARG A NH1   1 
ATOM   4613  N  NH2   . ARG A 1 600 ? 132.525 119.132 123.653 1.00 34.96  ? 600  ARG A NH2   1 
ATOM   4614  N  N     . CYS A 1 601 ? 129.187 125.797 123.350 1.00 18.64  ? 601  CYS A N     1 
ATOM   4615  C  CA    . CYS A 1 601 ? 129.366 126.686 124.491 1.00 16.01  ? 601  CYS A CA    1 
ATOM   4616  C  C     . CYS A 1 601 ? 128.027 127.260 124.932 1.00 21.44  ? 601  CYS A C     1 
ATOM   4617  O  O     . CYS A 1 601 ? 127.281 127.818 124.123 1.00 28.56  ? 601  CYS A O     1 
ATOM   4618  C  CB    . CYS A 1 601 ? 130.331 127.817 124.145 1.00 12.18  ? 601  CYS A CB    1 
ATOM   4619  S  SG    . CYS A 1 601 ? 130.564 129.028 125.459 1.00 29.78  ? 601  CYS A SG    1 
ATOM   4620  N  N     . LYS A 1 602 ? 127.723 127.119 126.221 1.00 22.46  ? 602  LYS A N     1 
ATOM   4621  C  CA    . LYS A 1 602 ? 126.450 127.585 126.749 1.00 12.16  ? 602  LYS A CA    1 
ATOM   4622  C  C     . LYS A 1 602 ? 126.470 129.062 127.109 1.00 19.56  ? 602  LYS A C     1 
ATOM   4623  O  O     . LYS A 1 602 ? 125.405 129.689 127.152 1.00 34.70  ? 602  LYS A O     1 
ATOM   4624  C  CB    . LYS A 1 602 ? 126.051 126.750 127.965 1.00 21.06  ? 602  LYS A CB    1 
ATOM   4625  C  CG    . LYS A 1 602 ? 125.749 125.307 127.621 1.00 27.10  ? 602  LYS A CG    1 
ATOM   4626  C  CD    . LYS A 1 602 ? 125.210 124.550 128.812 1.00 31.11  ? 602  LYS A CD    1 
ATOM   4627  C  CE    . LYS A 1 602 ? 124.895 123.116 128.439 1.00 35.14  ? 602  LYS A CE    1 
ATOM   4628  N  NZ    . LYS A 1 602 ? 124.353 122.352 129.594 1.00 28.27  ? 602  LYS A NZ    1 
ATOM   4629  N  N     . LEU A 1 603 ? 127.653 129.627 127.360 1.00 14.05  ? 603  LEU A N     1 
ATOM   4630  C  CA    . LEU A 1 603 ? 127.761 131.070 127.534 1.00 11.88  ? 603  LEU A CA    1 
ATOM   4631  C  C     . LEU A 1 603 ? 127.290 131.799 126.285 1.00 20.32  ? 603  LEU A C     1 
ATOM   4632  O  O     . LEU A 1 603 ? 126.558 132.790 126.374 1.00 23.54  ? 603  LEU A O     1 
ATOM   4633  C  CB    . LEU A 1 603 ? 129.205 131.454 127.856 1.00 15.08  ? 603  LEU A CB    1 
ATOM   4634  C  CG    . LEU A 1 603 ? 129.491 132.532 128.905 1.00 12.11  ? 603  LEU A CG    1 
ATOM   4635  C  CD1   . LEU A 1 603 ? 130.918 133.015 128.771 1.00 18.85  ? 603  LEU A CD1   1 
ATOM   4636  C  CD2   . LEU A 1 603 ? 128.524 133.699 128.826 1.00 23.14  ? 603  LEU A CD2   1 
ATOM   4637  N  N     . ARG A 1 604 ? 127.698 131.314 125.112 1.00 19.52  ? 604  ARG A N     1 
ATOM   4638  C  CA    . ARG A 1 604 ? 127.290 131.935 123.858 1.00 10.48  ? 604  ARG A CA    1 
ATOM   4639  C  C     . ARG A 1 604 ? 125.783 131.843 123.662 1.00 12.76  ? 604  ARG A C     1 
ATOM   4640  O  O     . ARG A 1 604 ? 125.140 132.815 123.249 1.00 27.21  ? 604  ARG A O     1 
ATOM   4641  C  CB    . ARG A 1 604 ? 128.026 131.271 122.698 1.00 10.86  ? 604  ARG A CB    1 
ATOM   4642  C  CG    . ARG A 1 604 ? 128.091 132.103 121.450 1.00 17.02  ? 604  ARG A CG    1 
ATOM   4643  C  CD    . ARG A 1 604 ? 128.337 131.247 120.227 1.00 20.00  ? 604  ARG A CD    1 
ATOM   4644  N  NE    . ARG A 1 604 ? 128.524 132.060 119.033 1.00 14.96  ? 604  ARG A NE    1 
ATOM   4645  C  CZ    . ARG A 1 604 ? 128.352 131.623 117.795 1.00 16.64  ? 604  ARG A CZ    1 
ATOM   4646  N  NH1   . ARG A 1 604 ? 127.955 130.386 117.548 1.00 21.22  ? 604  ARG A NH1   1 
ATOM   4647  N  NH2   . ARG A 1 604 ? 128.578 132.449 116.779 1.00 14.76  ? 604  ARG A NH2   1 
ATOM   4648  N  N     . GLU A 1 605 ? 125.202 130.682 123.966 1.00 14.62  ? 605  GLU A N     1 
ATOM   4649  C  CA    . GLU A 1 605 ? 123.762 130.500 123.826 1.00 20.01  ? 605  GLU A CA    1 
ATOM   4650  C  C     . GLU A 1 605 ? 122.997 131.440 124.750 1.00 19.59  ? 605  GLU A C     1 
ATOM   4651  O  O     . GLU A 1 605 ? 122.027 132.089 124.337 1.00 26.79  ? 605  GLU A O     1 
ATOM   4652  C  CB    . GLU A 1 605 ? 123.407 129.043 124.116 1.00 18.56  ? 605  GLU A CB    1 
ATOM   4653  C  CG    . GLU A 1 605 ? 121.938 128.713 124.024 1.00 26.06  ? 605  GLU A CG    1 
ATOM   4654  C  CD    . GLU A 1 605 ? 121.674 127.247 124.267 1.00 36.20  ? 605  GLU A CD    1 
ATOM   4655  O  OE1   . GLU A 1 605 ? 122.644 126.509 124.530 1.00 28.45  ? 605  GLU A OE1   1 
ATOM   4656  O  OE2   . GLU A 1 605 ? 120.499 126.830 124.196 1.00 45.24  ? 605  GLU A OE2   1 
ATOM   4657  N  N     . TYR A 1 606 ? 123.440 131.540 126.005 1.00 23.07  ? 606  TYR A N     1 
ATOM   4658  C  CA    . TYR A 1 606 ? 122.749 132.388 126.969 1.00 14.92  ? 606  TYR A CA    1 
ATOM   4659  C  C     . TYR A 1 606 ? 122.913 133.864 126.627 1.00 16.39  ? 606  TYR A C     1 
ATOM   4660  O  O     . TYR A 1 606 ? 121.987 134.658 126.828 1.00 36.97  ? 606  TYR A O     1 
ATOM   4661  C  CB    . TYR A 1 606 ? 123.259 132.097 128.380 1.00 24.10  ? 606  TYR A CB    1 
ATOM   4662  C  CG    . TYR A 1 606 ? 122.984 130.689 128.861 1.00 23.38  ? 606  TYR A CG    1 
ATOM   4663  C  CD1   . TYR A 1 606 ? 121.992 129.914 128.275 1.00 19.12  ? 606  TYR A CD1   1 
ATOM   4664  C  CD2   . TYR A 1 606 ? 123.713 130.138 129.903 1.00 9.88   ? 606  TYR A CD2   1 
ATOM   4665  C  CE1   . TYR A 1 606 ? 121.741 128.631 128.708 1.00 20.72  ? 606  TYR A CE1   1 
ATOM   4666  C  CE2   . TYR A 1 606 ? 123.467 128.855 130.344 1.00 10.37  ? 606  TYR A CE2   1 
ATOM   4667  C  CZ    . TYR A 1 606 ? 122.482 128.107 129.742 1.00 20.86  ? 606  TYR A CZ    1 
ATOM   4668  O  OH    . TYR A 1 606 ? 122.234 126.829 130.178 1.00 27.83  ? 606  TYR A OH    1 
ATOM   4669  N  N     . ALA A 1 607 ? 124.077 134.251 126.101 1.00 15.09  ? 607  ALA A N     1 
ATOM   4670  C  CA    . ALA A 1 607 ? 124.282 135.644 125.725 1.00 13.47  ? 607  ALA A CA    1 
ATOM   4671  C  C     . ALA A 1 607 ? 123.528 135.998 124.450 1.00 13.97  ? 607  ALA A C     1 
ATOM   4672  O  O     . ALA A 1 607 ? 123.195 137.167 124.232 1.00 24.63  ? 607  ALA A O     1 
ATOM   4673  C  CB    . ALA A 1 607 ? 125.774 135.928 125.565 1.00 9.66   ? 607  ALA A CB    1 
ATOM   4674  N  N     . THR A 1 608 ? 123.264 135.011 123.591 1.00 19.62  ? 608  THR A N     1 
ATOM   4675  C  CA    . THR A 1 608 ? 122.387 135.250 122.451 1.00 17.90  ? 608  THR A CA    1 
ATOM   4676  C  C     . THR A 1 608 ? 120.939 135.406 122.898 1.00 26.98  ? 608  THR A C     1 
ATOM   4677  O  O     . THR A 1 608 ? 120.226 136.294 122.415 1.00 31.35  ? 608  THR A O     1 
ATOM   4678  C  CB    . THR A 1 608 ? 122.518 134.110 121.441 1.00 21.14  ? 608  THR A CB    1 
ATOM   4679  O  OG1   . THR A 1 608 ? 123.870 134.033 120.976 1.00 25.80  ? 608  THR A OG1   1 
ATOM   4680  C  CG2   . THR A 1 608 ? 121.600 134.336 120.255 1.00 19.18  ? 608  THR A CG2   1 
ATOM   4681  N  N     . LEU A 1 609 ? 120.490 134.560 123.828 1.00 30.02  ? 609  LEU A N     1 
ATOM   4682  C  CA    . LEU A 1 609 ? 119.095 134.613 124.257 1.00 22.44  ? 609  LEU A CA    1 
ATOM   4683  C  C     . LEU A 1 609 ? 118.794 135.845 125.102 1.00 22.63  ? 609  LEU A C     1 
ATOM   4684  O  O     . LEU A 1 609 ? 117.688 136.389 125.025 1.00 34.61  ? 609  LEU A O     1 
ATOM   4685  C  CB    . LEU A 1 609 ? 118.733 133.344 125.028 1.00 19.53  ? 609  LEU A CB    1 
ATOM   4686  C  CG    . LEU A 1 609 ? 118.693 132.056 124.207 1.00 23.62  ? 609  LEU A CG    1 
ATOM   4687  C  CD1   . LEU A 1 609 ? 118.190 130.897 125.043 1.00 31.74  ? 609  LEU A CD1   1 
ATOM   4688  C  CD2   . LEU A 1 609 ? 117.832 132.237 122.976 1.00 30.82  ? 609  LEU A CD2   1 
ATOM   4689  N  N     . TYR A 1 610 ? 119.745 136.295 125.916 1.00 19.65  ? 610  TYR A N     1 
ATOM   4690  C  CA    . TYR A 1 610 ? 119.503 137.384 126.852 1.00 28.89  ? 610  TYR A CA    1 
ATOM   4691  C  C     . TYR A 1 610 ? 120.056 138.718 126.374 1.00 29.18  ? 610  TYR A C     1 
ATOM   4692  O  O     . TYR A 1 610 ? 120.053 139.681 127.147 1.00 33.57  ? 610  TYR A O     1 
ATOM   4693  C  CB    . TYR A 1 610 ? 120.075 137.033 128.228 1.00 25.03  ? 610  TYR A CB    1 
ATOM   4694  C  CG    . TYR A 1 610 ? 119.219 136.039 128.973 1.00 25.89  ? 610  TYR A CG    1 
ATOM   4695  C  CD1   . TYR A 1 610 ? 119.284 134.684 128.683 1.00 25.59  ? 610  TYR A CD1   1 
ATOM   4696  C  CD2   . TYR A 1 610 ? 118.325 136.457 129.946 1.00 30.48  ? 610  TYR A CD2   1 
ATOM   4697  C  CE1   . TYR A 1 610 ? 118.494 133.775 129.345 1.00 25.73  ? 610  TYR A CE1   1 
ATOM   4698  C  CE2   . TYR A 1 610 ? 117.531 135.552 130.616 1.00 31.60  ? 610  TYR A CE2   1 
ATOM   4699  C  CZ    . TYR A 1 610 ? 117.619 134.212 130.311 1.00 29.79  ? 610  TYR A CZ    1 
ATOM   4700  O  OH    . TYR A 1 610 ? 116.832 133.305 130.977 1.00 33.92  ? 610  TYR A OH    1 
ATOM   4701  N  N     . ASP A 1 611 ? 120.515 138.798 125.124 1.00 26.37  ? 611  ASP A N     1 
ATOM   4702  C  CA    . ASP A 1 611 ? 120.978 140.051 124.524 1.00 26.25  ? 611  ASP A CA    1 
ATOM   4703  C  C     . ASP A 1 611 ? 122.086 140.684 125.366 1.00 28.97  ? 611  ASP A C     1 
ATOM   4704  O  O     . ASP A 1 611 ? 122.048 141.865 125.712 1.00 36.03  ? 611  ASP A O     1 
ATOM   4705  C  CB    . ASP A 1 611 ? 119.806 141.016 124.317 1.00 30.85  ? 611  ASP A CB    1 
ATOM   4706  C  CG    . ASP A 1 611 ? 120.182 142.230 123.497 1.00 41.15  ? 611  ASP A CG    1 
ATOM   4707  O  OD1   . ASP A 1 611 ? 120.688 142.058 122.372 1.00 41.74  ? 611  ASP A OD1   1 
ATOM   4708  O  OD2   . ASP A 1 611 ? 119.967 143.361 123.982 1.00 39.33  ? 611  ASP A OD2   1 
ATOM   4709  N  N     . ALA A 1 612 ? 123.072 139.870 125.720 1.00 22.18  ? 612  ALA A N     1 
ATOM   4710  C  CA    . ALA A 1 612 ? 124.178 140.345 126.534 1.00 21.14  ? 612  ALA A CA    1 
ATOM   4711  C  C     . ALA A 1 612 ? 125.205 141.061 125.669 1.00 25.48  ? 612  ALA A C     1 
ATOM   4712  O  O     . ALA A 1 612 ? 125.517 140.627 124.557 1.00 31.45  ? 612  ALA A O     1 
ATOM   4713  C  CB    . ALA A 1 612 ? 124.828 139.182 127.281 1.00 20.49  ? 612  ALA A CB    1 
ATOM   4714  N  N     . LYS A 1 613 ? 125.718 142.172 126.182 1.00 30.28  ? 613  LYS A N     1 
ATOM   4715  C  CA    . LYS A 1 613 ? 126.725 142.964 125.495 1.00 25.79  ? 613  LYS A CA    1 
ATOM   4716  C  C     . LYS A 1 613 ? 128.082 142.743 126.147 1.00 25.80  ? 613  LYS A C     1 
ATOM   4717  O  O     . LYS A 1 613 ? 128.195 142.711 127.375 1.00 34.47  ? 613  LYS A O     1 
ATOM   4718  C  CB    . LYS A 1 613 ? 126.373 144.453 125.526 1.00 26.01  ? 613  LYS A CB    1 
ATOM   4719  C  CG    . LYS A 1 613 ? 124.978 144.787 125.036 1.00 27.94  ? 613  LYS A CG    1 
ATOM   4720  C  CD    . LYS A 1 613 ? 124.794 144.416 123.582 1.00 31.45  ? 613  LYS A CD    1 
ATOM   4721  C  CE    . LYS A 1 613 ? 123.377 144.696 123.126 1.00 29.83  ? 613  LYS A CE    1 
ATOM   4722  N  NZ    . LYS A 1 613 ? 123.119 144.146 121.771 1.00 23.88  ? 613  LYS A NZ    1 
ATOM   4723  N  N     . GLN A 1 614 ? 129.110 142.580 125.317 1.00 16.52  ? 614  GLN A N     1 
ATOM   4724  C  CA    . GLN A 1 614 ? 130.458 142.418 125.846 1.00 11.99  ? 614  GLN A CA    1 
ATOM   4725  C  C     . GLN A 1 614 ? 130.971 143.709 126.474 1.00 26.39  ? 614  GLN A C     1 
ATOM   4726  O  O     . GLN A 1 614 ? 131.770 143.663 127.415 1.00 36.41  ? 614  GLN A O     1 
ATOM   4727  C  CB    . GLN A 1 614 ? 131.396 141.947 124.734 1.00 20.37  ? 614  GLN A CB    1 
ATOM   4728  C  CG    . GLN A 1 614 ? 132.821 141.680 125.173 1.00 20.77  ? 614  GLN A CG    1 
ATOM   4729  C  CD    . GLN A 1 614 ? 133.724 141.319 124.015 1.00 23.43  ? 614  GLN A CD    1 
ATOM   4730  O  OE1   . GLN A 1 614 ? 133.260 140.856 122.976 1.00 15.57  ? 614  GLN A OE1   1 
ATOM   4731  N  NE2   . GLN A 1 614 ? 135.020 141.534 124.186 1.00 23.12  ? 614  GLN A NE2   1 
ATOM   4732  N  N     . ASP A 1 615 ? 130.515 144.859 125.987 1.00 19.56  ? 615  ASP A N     1 
ATOM   4733  C  CA    . ASP A 1 615 ? 131.027 146.149 126.429 1.00 19.62  ? 615  ASP A CA    1 
ATOM   4734  C  C     . ASP A 1 615 ? 130.261 146.734 127.607 1.00 28.35  ? 615  ASP A C     1 
ATOM   4735  O  O     . ASP A 1 615 ? 130.546 147.868 128.002 1.00 34.34  ? 615  ASP A O     1 
ATOM   4736  C  CB    . ASP A 1 615 ? 131.005 147.150 125.271 1.00 23.52  ? 615  ASP A CB    1 
ATOM   4737  C  CG    . ASP A 1 615 ? 129.599 147.527 124.857 1.00 32.92  ? 615  ASP A CG    1 
ATOM   4738  O  OD1   . ASP A 1 615 ? 128.720 146.643 124.856 1.00 37.75  ? 615  ASP A OD1   1 
ATOM   4739  O  OD2   . ASP A 1 615 ? 129.369 148.710 124.535 1.00 26.75  ? 615  ASP A OD2   1 
ATOM   4740  N  N     . ALA A 1 616 ? 129.296 146.003 128.168 1.00 29.81  ? 616  ALA A N     1 
ATOM   4741  C  CA    . ALA A 1 616 ? 128.469 146.556 129.236 1.00 30.78  ? 616  ALA A CA    1 
ATOM   4742  C  C     . ALA A 1 616 ? 129.292 146.840 130.487 1.00 24.78  ? 616  ALA A C     1 
ATOM   4743  O  O     . ALA A 1 616 ? 129.233 147.942 131.044 1.00 29.30  ? 616  ALA A O     1 
ATOM   4744  C  CB    . ALA A 1 616 ? 127.319 145.602 129.550 1.00 24.69  ? 616  ALA A CB    1 
ATOM   4745  N  N     . PHE A 1 617 ? 130.063 145.859 130.945 1.00 20.96  ? 617  PHE A N     1 
ATOM   4746  C  CA    . PHE A 1 617 ? 131.013 146.044 132.034 1.00 23.81  ? 617  PHE A CA    1 
ATOM   4747  C  C     . PHE A 1 617 ? 132.399 145.736 131.494 1.00 29.55  ? 617  PHE A C     1 
ATOM   4748  O  O     . PHE A 1 617 ? 132.636 144.642 130.974 1.00 38.36  ? 617  PHE A O     1 
ATOM   4749  C  CB    . PHE A 1 617 ? 130.678 145.147 133.227 1.00 19.17  ? 617  PHE A CB    1 
ATOM   4750  C  CG    . PHE A 1 617 ? 129.307 145.374 133.786 1.00 21.07  ? 617  PHE A CG    1 
ATOM   4751  C  CD1   . PHE A 1 617 ? 129.061 146.430 134.645 1.00 25.61  ? 617  PHE A CD1   1 
ATOM   4752  C  CD2   . PHE A 1 617 ? 128.262 144.532 133.453 1.00 24.97  ? 617  PHE A CD2   1 
ATOM   4753  C  CE1   . PHE A 1 617 ? 127.800 146.641 135.157 1.00 24.76  ? 617  PHE A CE1   1 
ATOM   4754  C  CE2   . PHE A 1 617 ? 126.998 144.741 133.964 1.00 27.05  ? 617  PHE A CE2   1 
ATOM   4755  C  CZ    . PHE A 1 617 ? 126.768 145.796 134.816 1.00 24.67  ? 617  PHE A CZ    1 
ATOM   4756  N  N     . VAL A 1 618 ? 133.301 146.704 131.594 1.00 26.60  ? 618  VAL A N     1 
ATOM   4757  C  CA    . VAL A 1 618 ? 134.636 146.596 131.023 1.00 25.74  ? 618  VAL A CA    1 
ATOM   4758  C  C     . VAL A 1 618 ? 135.647 146.883 132.120 1.00 26.58  ? 618  VAL A C     1 
ATOM   4759  O  O     . VAL A 1 618 ? 135.435 147.768 132.956 1.00 31.35  ? 618  VAL A O     1 
ATOM   4760  C  CB    . VAL A 1 618 ? 134.827 147.560 129.831 1.00 21.56  ? 618  VAL A CB    1 
ATOM   4761  C  CG1   . VAL A 1 618 ? 136.174 147.339 129.168 1.00 24.15  ? 618  VAL A CG1   1 
ATOM   4762  C  CG2   . VAL A 1 618 ? 133.713 147.387 128.820 1.00 14.51  ? 618  VAL A CG2   1 
ATOM   4763  N  N     . GLY A 1 619 ? 136.740 146.130 132.126 1.00 14.58  ? 619  GLY A N     1 
ATOM   4764  C  CA    . GLY A 1 619 ? 137.770 146.344 133.127 1.00 18.20  ? 619  GLY A CA    1 
ATOM   4765  C  C     . GLY A 1 619 ? 138.835 145.278 133.049 1.00 20.43  ? 619  GLY A C     1 
ATOM   4766  O  O     . GLY A 1 619 ? 139.048 144.667 131.997 1.00 29.40  ? 619  GLY A O     1 
ATOM   4767  N  N     . GLU A 1 620 ? 139.504 145.067 134.177 1.00 17.30  ? 620  GLU A N     1 
ATOM   4768  C  CA    . GLU A 1 620 ? 140.561 144.070 134.242 1.00 22.98  ? 620  GLU A CA    1 
ATOM   4769  C  C     . GLU A 1 620 ? 139.995 142.673 134.039 1.00 26.05  ? 620  GLU A C     1 
ATOM   4770  O  O     . GLU A 1 620 ? 138.938 142.325 134.572 1.00 22.19  ? 620  GLU A O     1 
ATOM   4771  C  CB    . GLU A 1 620 ? 141.279 144.148 135.588 1.00 19.57  ? 620  GLU A CB    1 
ATOM   4772  C  CG    . GLU A 1 620 ? 141.867 145.509 135.896 1.00 23.02  ? 620  GLU A CG    1 
ATOM   4773  C  CD    . GLU A 1 620 ? 142.492 145.572 137.275 1.00 29.85  ? 620  GLU A CD    1 
ATOM   4774  O  OE1   . GLU A 1 620 ? 142.413 144.567 138.011 1.00 14.70  ? 620  GLU A OE1   1 
ATOM   4775  O  OE2   . GLU A 1 620 ? 143.063 146.627 137.623 1.00 35.31  ? 620  GLU A OE2   1 
ATOM   4776  N  N     . GLN A 1 621 ? 140.698 141.876 133.246 1.00 22.70  ? 621  GLN A N     1 
ATOM   4777  C  CA    . GLN A 1 621 ? 140.425 140.454 133.136 1.00 24.01  ? 621  GLN A CA    1 
ATOM   4778  C  C     . GLN A 1 621 ? 141.741 139.699 133.235 1.00 29.87  ? 621  GLN A C     1 
ATOM   4779  O  O     . GLN A 1 621 ? 142.794 140.196 132.830 1.00 29.77  ? 621  GLN A O     1 
ATOM   4780  C  CB    . GLN A 1 621 ? 139.687 140.106 131.834 1.00 14.82  ? 621  GLN A CB    1 
ATOM   4781  C  CG    . GLN A 1 621 ? 140.239 140.754 130.584 1.00 21.43  ? 621  GLN A CG    1 
ATOM   4782  C  CD    . GLN A 1 621 ? 139.393 140.455 129.362 1.00 28.74  ? 621  GLN A CD    1 
ATOM   4783  O  OE1   . GLN A 1 621 ? 138.286 139.933 129.473 1.00 19.09  ? 621  GLN A OE1   1 
ATOM   4784  N  NE2   . GLN A 1 621 ? 139.912 140.784 128.189 1.00 32.50  ? 621  GLN A NE2   1 
ATOM   4785  N  N     . ASN A 1 622 ? 141.674 138.503 133.807 1.00 26.61  ? 622  ASN A N     1 
ATOM   4786  C  CA    . ASN A 1 622 ? 142.879 137.720 134.024 1.00 17.37  ? 622  ASN A CA    1 
ATOM   4787  C  C     . ASN A 1 622 ? 143.356 137.104 132.716 1.00 27.20  ? 622  ASN A C     1 
ATOM   4788  O  O     . ASN A 1 622 ? 142.563 136.574 131.934 1.00 22.43  ? 622  ASN A O     1 
ATOM   4789  C  CB    . ASN A 1 622 ? 142.622 136.627 135.056 1.00 9.75   ? 622  ASN A CB    1 
ATOM   4790  C  CG    . ASN A 1 622 ? 141.931 137.148 136.294 1.00 28.23  ? 622  ASN A CG    1 
ATOM   4791  O  OD1   . ASN A 1 622 ? 142.559 137.751 137.161 1.00 27.27  ? 622  ASN A OD1   1 
ATOM   4792  N  ND2   . ASN A 1 622 ? 140.631 136.908 136.388 1.00 32.70  ? 622  ASN A ND2   1 
ATOM   4793  N  N     . LYS A 1 623 ? 144.661 137.181 132.480 1.00 25.64  ? 623  LYS A N     1 
ATOM   4794  C  CA    . LYS A 1 623 ? 145.274 136.602 131.294 1.00 14.72  ? 623  LYS A CA    1 
ATOM   4795  C  C     . LYS A 1 623 ? 145.997 135.322 131.685 1.00 21.48  ? 623  LYS A C     1 
ATOM   4796  O  O     . LYS A 1 623 ? 146.942 135.354 132.480 1.00 20.37  ? 623  LYS A O     1 
ATOM   4797  C  CB    . LYS A 1 623 ? 146.239 137.587 130.635 1.00 20.42  ? 623  LYS A CB    1 
ATOM   4798  C  CG    . LYS A 1 623 ? 145.568 138.828 130.076 1.00 29.29  ? 623  LYS A CG    1 
ATOM   4799  C  CD    . LYS A 1 623 ? 144.522 138.473 129.033 1.00 28.04  ? 623  LYS A CD    1 
ATOM   4800  C  CE    . LYS A 1 623 ? 145.144 137.777 127.835 1.00 29.63  ? 623  LYS A CE    1 
ATOM   4801  N  NZ    . LYS A 1 623 ? 146.175 138.625 127.177 1.00 25.69  ? 623  LYS A NZ    1 
ATOM   4802  N  N     . PHE A 1 624 ? 145.553 134.204 131.127 1.00 25.86  ? 624  PHE A N     1 
ATOM   4803  C  CA    . PHE A 1 624 ? 146.134 132.900 131.396 1.00 26.53  ? 624  PHE A CA    1 
ATOM   4804  C  C     . PHE A 1 624 ? 146.762 132.350 130.126 1.00 27.05  ? 624  PHE A C     1 
ATOM   4805  O  O     . PHE A 1 624 ? 146.202 132.486 129.035 1.00 27.46  ? 624  PHE A O     1 
ATOM   4806  C  CB    . PHE A 1 624 ? 145.082 131.916 131.912 1.00 21.12  ? 624  PHE A CB    1 
ATOM   4807  C  CG    . PHE A 1 624 ? 144.389 132.362 133.166 1.00 21.33  ? 624  PHE A CG    1 
ATOM   4808  C  CD1   . PHE A 1 624 ? 145.027 132.283 134.390 1.00 20.23  ? 624  PHE A CD1   1 
ATOM   4809  C  CD2   . PHE A 1 624 ? 143.090 132.836 133.123 1.00 21.28  ? 624  PHE A CD2   1 
ATOM   4810  C  CE1   . PHE A 1 624 ? 144.388 132.682 135.543 1.00 24.71  ? 624  PHE A CE1   1 
ATOM   4811  C  CE2   . PHE A 1 624 ? 142.445 133.232 134.274 1.00 22.66  ? 624  PHE A CE2   1 
ATOM   4812  C  CZ    . PHE A 1 624 ? 143.096 133.157 135.485 1.00 25.39  ? 624  PHE A CZ    1 
ATOM   4813  N  N     . GLU A 1 625 ? 147.931 131.740 130.269 1.00 20.72  ? 625  GLU A N     1 
ATOM   4814  C  CA    . GLU A 1 625 ? 148.519 131.003 129.165 1.00 25.19  ? 625  GLU A CA    1 
ATOM   4815  C  C     . GLU A 1 625 ? 147.812 129.663 129.011 1.00 34.78  ? 625  GLU A C     1 
ATOM   4816  O  O     . GLU A 1 625 ? 147.263 129.110 129.968 1.00 35.13  ? 625  GLU A O     1 
ATOM   4817  C  CB    . GLU A 1 625 ? 150.019 130.796 129.380 1.00 24.69  ? 625  GLU A CB    1 
ATOM   4818  C  CG    . GLU A 1 625 ? 150.381 129.936 130.582 1.00 31.07  ? 625  GLU A CG    1 
ATOM   4819  C  CD    . GLU A 1 625 ? 150.323 130.697 131.893 1.00 36.74  ? 625  GLU A CD    1 
ATOM   4820  O  OE1   . GLU A 1 625 ? 150.087 131.923 131.864 1.00 30.87  ? 625  GLU A OE1   1 
ATOM   4821  O  OE2   . GLU A 1 625 ? 150.515 130.067 132.955 1.00 33.45  ? 625  GLU A OE2   1 
ATOM   4822  N  N     . ILE A 1 626 ? 147.822 129.151 127.800 1.00 33.22  ? 626  ILE A N     1 
ATOM   4823  C  CA    . ILE A 1 626 ? 147.085 127.941 127.464 1.00 31.89  ? 626  ILE A CA    1 
ATOM   4824  C  C     . ILE A 1 626 ? 147.950 126.727 127.772 1.00 34.08  ? 626  ILE A C     1 
ATOM   4825  O  O     . ILE A 1 626 ? 149.154 126.712 127.494 1.00 33.75  ? 626  ILE A O     1 
ATOM   4826  C  CB    . ILE A 1 626 ? 146.642 127.965 125.989 1.00 29.69  ? 626  ILE A CB    1 
ATOM   4827  C  CG1   . ILE A 1 626 ? 145.906 129.267 125.673 1.00 32.90  ? 626  ILE A CG1   1 
ATOM   4828  C  CG2   . ILE A 1 626 ? 145.728 126.807 125.689 1.00 31.84  ? 626  ILE A CG2   1 
ATOM   4829  C  CD1   . ILE A 1 626 ? 146.738 130.279 124.911 1.00 32.11  ? 626  ILE A CD1   1 
ATOM   4830  N  N     . ASP A 1 627 ? 147.333 125.705 128.364 1.00 41.78  ? 627  ASP A N     1 
ATOM   4831  C  CA    . ASP A 1 627 ? 148.032 124.489 128.775 1.00 39.31  ? 627  ASP A CA    1 
ATOM   4832  C  C     . ASP A 1 627 ? 147.814 123.417 127.711 1.00 45.19  ? 627  ASP A C     1 
ATOM   4833  O  O     . ASP A 1 627 ? 146.942 122.556 127.820 1.00 49.03  ? 627  ASP A O     1 
ATOM   4834  C  CB    . ASP A 1 627 ? 147.540 124.037 130.145 1.00 35.86  ? 627  ASP A CB    1 
ATOM   4835  C  CG    . ASP A 1 627 ? 148.255 122.801 130.645 1.00 45.95  ? 627  ASP A CG    1 
ATOM   4836  O  OD1   . ASP A 1 627 ? 149.341 122.477 130.120 1.00 50.94  ? 627  ASP A OD1   1 
ATOM   4837  O  OD2   . ASP A 1 627 ? 147.727 122.148 131.567 1.00 47.60  ? 627  ASP A OD2   1 
ATOM   4838  N  N     . GLU A 1 628 ? 148.635 123.475 126.665 1.00 45.69  ? 628  GLU A N     1 
ATOM   4839  C  CA    . GLU A 1 628 ? 148.595 122.498 125.588 1.00 42.43  ? 628  GLU A CA    1 
ATOM   4840  C  C     . GLU A 1 628 ? 149.635 121.401 125.759 1.00 46.58  ? 628  GLU A C     1 
ATOM   4841  O  O     . GLU A 1 628 ? 149.812 120.582 124.854 1.00 51.71  ? 628  GLU A O     1 
ATOM   4842  C  CB    . GLU A 1 628 ? 148.783 123.191 124.238 1.00 41.71  ? 628  GLU A CB    1 
ATOM   4843  C  CG    . GLU A 1 628 ? 147.662 124.141 123.880 1.00 49.27  ? 628  GLU A CG    1 
ATOM   4844  C  CD    . GLU A 1 628 ? 147.874 124.809 122.544 1.00 53.94  ? 628  GLU A CD    1 
ATOM   4845  O  OE1   . GLU A 1 628 ? 148.934 124.582 121.927 1.00 51.01  ? 628  GLU A OE1   1 
ATOM   4846  O  OE2   . GLU A 1 628 ? 146.979 125.562 122.108 1.00 50.64  ? 628  GLU A OE2   1 
ATOM   4847  N  N     . THR A 1 629 ? 150.323 121.369 126.900 1.00 47.81  ? 629  THR A N     1 
ATOM   4848  C  CA    . THR A 1 629 ? 151.406 120.417 127.104 1.00 49.23  ? 629  THR A CA    1 
ATOM   4849  C  C     . THR A 1 629 ? 150.921 118.977 127.157 1.00 48.93  ? 629  THR A C     1 
ATOM   4850  O  O     . THR A 1 629 ? 151.711 118.063 126.898 1.00 47.64  ? 629  THR A O     1 
ATOM   4851  C  CB    . THR A 1 629 ? 152.159 120.754 128.389 1.00 51.85  ? 629  THR A CB    1 
ATOM   4852  O  OG1   . THR A 1 629 ? 151.294 120.555 129.512 1.00 51.67  ? 629  THR A OG1   1 
ATOM   4853  C  CG2   . THR A 1 629 ? 152.615 122.199 128.364 1.00 48.32  ? 629  THR A CG2   1 
ATOM   4854  N  N     . HIS A 1 630 ? 149.655 118.751 127.488 1.00 42.43  ? 630  HIS A N     1 
ATOM   4855  C  CA    . HIS A 1 630 ? 149.135 117.397 127.527 1.00 42.67  ? 630  HIS A CA    1 
ATOM   4856  C  C     . HIS A 1 630 ? 149.082 116.815 126.115 1.00 43.89  ? 630  HIS A C     1 
ATOM   4857  O  O     . HIS A 1 630 ? 148.908 117.550 125.139 1.00 46.11  ? 630  HIS A O     1 
ATOM   4858  C  CB    . HIS A 1 630 ? 147.747 117.375 128.162 1.00 37.29  ? 630  HIS A CB    1 
ATOM   4859  C  CG    . HIS A 1 630 ? 147.291 116.011 128.574 1.00 39.09  ? 630  HIS A CG    1 
ATOM   4860  N  ND1   . HIS A 1 630 ? 146.578 115.180 127.738 1.00 37.91  ? 630  HIS A ND1   1 
ATOM   4861  C  CD2   . HIS A 1 630 ? 147.452 115.329 129.733 1.00 46.27  ? 630  HIS A CD2   1 
ATOM   4862  C  CE1   . HIS A 1 630 ? 146.319 114.046 128.363 1.00 43.01  ? 630  HIS A CE1   1 
ATOM   4863  N  NE2   . HIS A 1 630 ? 146.839 114.111 129.575 1.00 44.29  ? 630  HIS A NE2   1 
ATOM   4864  N  N     . PRO A 1 631 ? 149.272 115.501 125.976 1.00 42.83  ? 631  PRO A N     1 
ATOM   4865  C  CA    . PRO A 1 631 ? 149.176 114.887 124.642 1.00 36.92  ? 631  PRO A CA    1 
ATOM   4866  C  C     . PRO A 1 631 ? 147.821 115.048 123.972 1.00 39.82  ? 631  PRO A C     1 
ATOM   4867  O  O     . PRO A 1 631 ? 147.767 115.140 122.740 1.00 42.54  ? 631  PRO A O     1 
ATOM   4868  C  CB    . PRO A 1 631 ? 149.492 113.413 124.920 1.00 37.16  ? 631  PRO A CB    1 
ATOM   4869  C  CG    . PRO A 1 631 ? 150.356 113.441 126.122 1.00 40.78  ? 631  PRO A CG    1 
ATOM   4870  C  CD    . PRO A 1 631 ? 149.853 114.576 126.965 1.00 40.24  ? 631  PRO A CD    1 
ATOM   4871  N  N     . ASN A 1 632 ? 146.719 115.077 124.729 1.00 33.34  ? 632  ASN A N     1 
ATOM   4872  C  CA    . ASN A 1 632 ? 145.407 115.047 124.094 1.00 30.77  ? 632  ASN A CA    1 
ATOM   4873  C  C     . ASN A 1 632 ? 144.365 115.973 124.714 1.00 38.80  ? 632  ASN A C     1 
ATOM   4874  O  O     . ASN A 1 632 ? 143.202 115.923 124.294 1.00 42.28  ? 632  ASN A O     1 
ATOM   4875  C  CB    . ASN A 1 632 ? 144.861 113.619 124.096 1.00 33.35  ? 632  ASN A CB    1 
ATOM   4876  C  CG    . ASN A 1 632 ? 145.712 112.670 123.288 1.00 44.90  ? 632  ASN A CG    1 
ATOM   4877  O  OD1   . ASN A 1 632 ? 146.662 112.081 123.801 1.00 46.90  ? 632  ASN A OD1   1 
ATOM   4878  N  ND2   . ASN A 1 632 ? 145.377 112.515 122.015 1.00 44.64  ? 632  ASN A ND2   1 
ATOM   4879  N  N     . VAL A 1 633 ? 144.718 116.806 125.691 1.00 32.32  ? 633  VAL A N     1 
ATOM   4880  C  CA    . VAL A 1 633 ? 143.754 117.693 126.339 1.00 27.37  ? 633  VAL A CA    1 
ATOM   4881  C  C     . VAL A 1 633 ? 144.359 119.086 126.474 1.00 28.77  ? 633  VAL A C     1 
ATOM   4882  O  O     . VAL A 1 633 ? 145.520 119.237 126.866 1.00 38.82  ? 633  VAL A O     1 
ATOM   4883  C  CB    . VAL A 1 633 ? 143.310 117.144 127.715 1.00 37.60  ? 633  VAL A CB    1 
ATOM   4884  C  CG1   . VAL A 1 633 ? 142.519 118.182 128.484 1.00 33.30  ? 633  VAL A CG1   1 
ATOM   4885  C  CG2   . VAL A 1 633 ? 142.470 115.891 127.545 1.00 35.53  ? 633  VAL A CG2   1 
ATOM   4886  N  N     . VAL A 1 634 ? 143.567 120.103 126.148 1.00 28.67  ? 634  VAL A N     1 
ATOM   4887  C  CA    . VAL A 1 634 ? 143.957 121.503 126.267 1.00 28.30  ? 634  VAL A CA    1 
ATOM   4888  C  C     . VAL A 1 634 ? 143.159 122.133 127.400 1.00 31.03  ? 634  VAL A C     1 
ATOM   4889  O  O     . VAL A 1 634 ? 141.959 121.873 127.542 1.00 36.99  ? 634  VAL A O     1 
ATOM   4890  C  CB    . VAL A 1 634 ? 143.722 122.256 124.943 1.00 30.80  ? 634  VAL A CB    1 
ATOM   4891  C  CG1   . VAL A 1 634 ? 144.076 123.713 125.081 1.00 28.85  ? 634  VAL A CG1   1 
ATOM   4892  C  CG2   . VAL A 1 634 ? 144.527 121.629 123.834 1.00 40.92  ? 634  VAL A CG2   1 
ATOM   4893  N  N     . LEU A 1 635 ? 143.826 122.949 128.215 1.00 28.57  ? 635  LEU A N     1 
ATOM   4894  C  CA    . LEU A 1 635 ? 143.188 123.668 129.315 1.00 24.49  ? 635  LEU A CA    1 
ATOM   4895  C  C     . LEU A 1 635 ? 143.419 125.162 129.119 1.00 28.20  ? 635  LEU A C     1 
ATOM   4896  O  O     . LEU A 1 635 ? 144.543 125.648 129.279 1.00 34.63  ? 635  LEU A O     1 
ATOM   4897  C  CB    . LEU A 1 635 ? 143.728 123.191 130.663 1.00 24.20  ? 635  LEU A CB    1 
ATOM   4898  C  CG    . LEU A 1 635 ? 143.252 123.888 131.940 1.00 32.36  ? 635  LEU A CG    1 
ATOM   4899  C  CD1   . LEU A 1 635 ? 141.741 123.884 132.053 1.00 30.03  ? 635  LEU A CD1   1 
ATOM   4900  C  CD2   . LEU A 1 635 ? 143.871 123.229 133.159 1.00 25.14  ? 635  LEU A CD2   1 
ATOM   4901  N  N     . ASP A 1 636 ? 142.356 125.885 128.776 1.00 29.87  ? 636  ASP A N     1 
ATOM   4902  C  CA    . ASP A 1 636 ? 142.407 127.322 128.514 1.00 27.91  ? 636  ASP A CA    1 
ATOM   4903  C  C     . ASP A 1 636 ? 141.608 128.029 129.605 1.00 32.26  ? 636  ASP A C     1 
ATOM   4904  O  O     . ASP A 1 636 ? 140.378 128.089 129.547 1.00 35.37  ? 636  ASP A O     1 
ATOM   4905  C  CB    . ASP A 1 636 ? 141.859 127.635 127.124 1.00 22.44  ? 636  ASP A CB    1 
ATOM   4906  C  CG    . ASP A 1 636 ? 142.148 129.056 126.683 1.00 31.17  ? 636  ASP A CG    1 
ATOM   4907  O  OD1   . ASP A 1 636 ? 142.814 129.795 127.434 1.00 36.19  ? 636  ASP A OD1   1 
ATOM   4908  O  OD2   . ASP A 1 636 ? 141.711 129.434 125.577 1.00 36.07  ? 636  ASP A OD2   1 
ATOM   4909  N  N     . ASN A 1 637 ? 142.313 128.570 130.600 1.00 28.84  ? 637  ASN A N     1 
ATOM   4910  C  CA    . ASN A 1 637 ? 141.648 129.234 131.714 1.00 17.29  ? 637  ASN A CA    1 
ATOM   4911  C  C     . ASN A 1 637 ? 141.056 130.587 131.338 1.00 24.51  ? 637  ASN A C     1 
ATOM   4912  O  O     . ASN A 1 637 ? 140.267 131.131 132.117 1.00 35.70  ? 637  ASN A O     1 
ATOM   4913  C  CB    . ASN A 1 637 ? 142.622 129.410 132.880 1.00 22.08  ? 637  ASN A CB    1 
ATOM   4914  C  CG    . ASN A 1 637 ? 142.921 128.114 133.594 1.00 23.38  ? 637  ASN A CG    1 
ATOM   4915  O  OD1   . ASN A 1 637 ? 144.072 127.684 133.667 1.00 25.36  ? 637  ASN A OD1   1 
ATOM   4916  N  ND2   . ASN A 1 637 ? 141.888 127.486 134.136 1.00 21.03  ? 637  ASN A ND2   1 
ATOM   4917  N  N     . ASN A 1 638 ? 141.416 131.143 130.179 1.00 22.94  ? 638  ASN A N     1 
ATOM   4918  C  CA    . ASN A 1 638 ? 140.832 132.406 129.740 1.00 24.10  ? 638  ASN A CA    1 
ATOM   4919  C  C     . ASN A 1 638 ? 139.351 132.281 129.417 1.00 25.61  ? 638  ASN A C     1 
ATOM   4920  O  O     . ASN A 1 638 ? 138.644 133.293 129.405 1.00 24.95  ? 638  ASN A O     1 
ATOM   4921  C  CB    . ASN A 1 638 ? 141.570 132.931 128.511 1.00 21.68  ? 638  ASN A CB    1 
ATOM   4922  C  CG    . ASN A 1 638 ? 143.061 132.997 128.713 1.00 28.83  ? 638  ASN A CG    1 
ATOM   4923  O  OD1   . ASN A 1 638 ? 143.590 134.002 129.181 1.00 36.22  ? 638  ASN A OD1   1 
ATOM   4924  N  ND2   . ASN A 1 638 ? 143.752 131.924 128.357 1.00 29.06  ? 638  ASN A ND2   1 
ATOM   4925  N  N     . LYS A 1 639 ? 138.872 131.069 129.140 1.00 21.17  ? 639  LYS A N     1 
ATOM   4926  C  CA    . LYS A 1 639 ? 137.468 130.819 128.847 1.00 15.06  ? 639  LYS A CA    1 
ATOM   4927  C  C     . LYS A 1 639 ? 136.753 130.150 130.014 1.00 24.08  ? 639  LYS A C     1 
ATOM   4928  O  O     . LYS A 1 639 ? 135.653 129.618 129.843 1.00 34.82  ? 639  LYS A O     1 
ATOM   4929  C  CB    . LYS A 1 639 ? 137.341 129.972 127.582 1.00 22.12  ? 639  LYS A CB    1 
ATOM   4930  C  CG    . LYS A 1 639 ? 137.971 130.608 126.363 1.00 18.44  ? 639  LYS A CG    1 
ATOM   4931  C  CD    . LYS A 1 639 ? 137.972 129.675 125.175 1.00 20.26  ? 639  LYS A CD    1 
ATOM   4932  C  CE    . LYS A 1 639 ? 138.599 130.342 123.969 1.00 23.16  ? 639  LYS A CE    1 
ATOM   4933  N  NZ    . LYS A 1 639 ? 138.749 129.398 122.836 1.00 16.96  ? 639  LYS A NZ    1 
ATOM   4934  N  N     . CYS A 1 640 ? 137.361 130.165 131.195 1.00 21.01  ? 640  CYS A N     1 
ATOM   4935  C  CA    . CYS A 1 640 ? 136.789 129.521 132.367 1.00 9.67   ? 640  CYS A CA    1 
ATOM   4936  C  C     . CYS A 1 640 ? 135.780 130.444 133.038 1.00 15.54  ? 640  CYS A C     1 
ATOM   4937  O  O     . CYS A 1 640 ? 136.078 131.611 133.308 1.00 26.48  ? 640  CYS A O     1 
ATOM   4938  C  CB    . CYS A 1 640 ? 137.902 129.144 133.344 1.00 10.99  ? 640  CYS A CB    1 
ATOM   4939  S  SG    . CYS A 1 640 ? 137.369 128.312 134.849 1.00 7.66   ? 640  CYS A SG    1 
ATOM   4940  N  N     . VAL A 1 641 ? 134.580 129.921 133.303 1.00 10.45  ? 641  VAL A N     1 
ATOM   4941  C  CA    . VAL A 1 641 ? 133.557 130.667 134.025 1.00 14.11  ? 641  VAL A CA    1 
ATOM   4942  C  C     . VAL A 1 641 ? 133.500 130.294 135.498 1.00 16.66  ? 641  VAL A C     1 
ATOM   4943  O  O     . VAL A 1 641 ? 132.660 130.833 136.231 1.00 23.75  ? 641  VAL A O     1 
ATOM   4944  C  CB    . VAL A 1 641 ? 132.168 130.485 133.379 1.00 8.13   ? 641  VAL A CB    1 
ATOM   4945  C  CG1   . VAL A 1 641 ? 132.183 130.963 131.941 1.00 9.39   ? 641  VAL A CG1   1 
ATOM   4946  C  CG2   . VAL A 1 641 ? 131.721 129.040 133.460 1.00 14.27  ? 641  VAL A CG2   1 
ATOM   4947  N  N     . LEU A 1 642 ? 134.370 129.389 135.950 1.00 21.17  ? 642  LEU A N     1 
ATOM   4948  C  CA    . LEU A 1 642 ? 134.465 128.962 137.348 1.00 14.17  ? 642  LEU A CA    1 
ATOM   4949  C  C     . LEU A 1 642 ? 133.137 128.394 137.856 1.00 15.77  ? 642  LEU A C     1 
ATOM   4950  O  O     . LEU A 1 642 ? 132.513 128.919 138.778 1.00 25.33  ? 642  LEU A O     1 
ATOM   4951  C  CB    . LEU A 1 642 ? 134.958 130.103 138.242 1.00 4.68   ? 642  LEU A CB    1 
ATOM   4952  C  CG    . LEU A 1 642 ? 136.434 130.479 138.118 1.00 6.30   ? 642  LEU A CG    1 
ATOM   4953  C  CD1   . LEU A 1 642 ? 136.762 131.631 139.044 1.00 20.97  ? 642  LEU A CD1   1 
ATOM   4954  C  CD2   . LEU A 1 642 ? 137.317 129.289 138.423 1.00 13.99  ? 642  LEU A CD2   1 
ATOM   4955  N  N     . CYS A 1 643 ? 132.713 127.300 137.227 1.00 16.58  ? 643  CYS A N     1 
ATOM   4956  C  CA    . CYS A 1 643 ? 131.573 126.542 137.719 1.00 13.50  ? 643  CYS A CA    1 
ATOM   4957  C  C     . CYS A 1 643 ? 131.982 125.402 138.639 1.00 19.08  ? 643  CYS A C     1 
ATOM   4958  O  O     . CYS A 1 643 ? 131.135 124.878 139.370 1.00 20.30  ? 643  CYS A O     1 
ATOM   4959  C  CB    . CYS A 1 643 ? 130.753 125.989 136.550 1.00 10.58  ? 643  CYS A CB    1 
ATOM   4960  S  SG    . CYS A 1 643 ? 131.663 124.919 135.426 1.00 5.65   ? 643  CYS A SG    1 
ATOM   4961  N  N     . GLY A 1 644 ? 133.252 125.005 138.615 1.00 5.44   ? 644  GLY A N     1 
ATOM   4962  C  CA    . GLY A 1 644 ? 133.763 124.006 139.527 1.00 5.79   ? 644  GLY A CA    1 
ATOM   4963  C  C     . GLY A 1 644 ? 133.404 122.575 139.208 1.00 13.04  ? 644  GLY A C     1 
ATOM   4964  O  O     . GLY A 1 644 ? 133.729 121.686 140.001 1.00 15.75  ? 644  GLY A O     1 
ATOM   4965  N  N     . GLN A 1 645 ? 132.751 122.318 138.073 1.00 19.05  ? 645  GLN A N     1 
ATOM   4966  C  CA    . GLN A 1 645 ? 132.308 120.960 137.768 1.00 13.54  ? 645  GLN A CA    1 
ATOM   4967  C  C     . GLN A 1 645 ? 133.485 120.025 137.521 1.00 13.56  ? 645  GLN A C     1 
ATOM   4968  O  O     . GLN A 1 645 ? 133.430 118.845 137.884 1.00 24.83  ? 645  GLN A O     1 
ATOM   4969  C  CB    . GLN A 1 645 ? 131.367 120.971 136.567 1.00 10.36  ? 645  GLN A CB    1 
ATOM   4970  C  CG    . GLN A 1 645 ? 130.024 121.608 136.844 1.00 21.88  ? 645  GLN A CG    1 
ATOM   4971  C  CD    . GLN A 1 645 ? 128.996 121.267 135.792 1.00 19.16  ? 645  GLN A CD    1 
ATOM   4972  O  OE1   . GLN A 1 645 ? 129.271 120.515 134.861 1.00 28.04  ? 645  GLN A OE1   1 
ATOM   4973  N  NE2   . GLN A 1 645 ? 127.799 121.818 135.935 1.00 21.75  ? 645  GLN A NE2   1 
ATOM   4974  N  N     . CYS A 1 646 ? 134.555 120.526 136.901 1.00 16.25  ? 646  CYS A N     1 
ATOM   4975  C  CA    . CYS A 1 646 ? 135.745 119.705 136.702 1.00 15.66  ? 646  CYS A CA    1 
ATOM   4976  C  C     . CYS A 1 646 ? 136.415 119.366 138.029 1.00 20.92  ? 646  CYS A C     1 
ATOM   4977  O  O     . CYS A 1 646 ? 136.831 118.222 138.246 1.00 24.19  ? 646  CYS A O     1 
ATOM   4978  C  CB    . CYS A 1 646 ? 136.723 120.419 135.774 1.00 17.46  ? 646  CYS A CB    1 
ATOM   4979  S  SG    . CYS A 1 646 ? 137.214 122.053 136.339 1.00 3.64   ? 646  CYS A SG    1 
ATOM   4980  N  N     . VAL A 1 647 ? 136.529 120.350 138.924 1.00 29.83  ? 647  VAL A N     1 
ATOM   4981  C  CA    . VAL A 1 647 ? 137.102 120.105 140.245 1.00 17.24  ? 647  VAL A CA    1 
ATOM   4982  C  C     . VAL A 1 647 ? 136.242 119.118 141.018 1.00 19.06  ? 647  VAL A C     1 
ATOM   4983  O  O     . VAL A 1 647 ? 136.753 118.183 141.647 1.00 31.07  ? 647  VAL A O     1 
ATOM   4984  C  CB    . VAL A 1 647 ? 137.263 121.431 141.010 1.00 8.45   ? 647  VAL A CB    1 
ATOM   4985  C  CG1   . VAL A 1 647 ? 137.787 121.181 142.411 1.00 24.65  ? 647  VAL A CG1   1 
ATOM   4986  C  CG2   . VAL A 1 647 ? 138.184 122.359 140.261 1.00 14.57  ? 647  VAL A CG2   1 
ATOM   4987  N  N     . ASN A 1 648 ? 134.921 119.305 140.974 1.00 11.67  ? 648  ASN A N     1 
ATOM   4988  C  CA    . ASN A 1 648 ? 134.018 118.406 141.681 1.00 12.77  ? 648  ASN A CA    1 
ATOM   4989  C  C     . ASN A 1 648 ? 134.118 116.987 141.140 1.00 20.54  ? 648  ASN A C     1 
ATOM   4990  O  O     . ASN A 1 648 ? 134.148 116.025 141.913 1.00 31.82  ? 648  ASN A O     1 
ATOM   4991  C  CB    . ASN A 1 648 ? 132.584 118.925 141.588 1.00 22.02  ? 648  ASN A CB    1 
ATOM   4992  C  CG    . ASN A 1 648 ? 132.377 120.213 142.365 1.00 31.55  ? 648  ASN A CG    1 
ATOM   4993  O  OD1   . ASN A 1 648 ? 133.326 120.813 142.869 1.00 33.72  ? 648  ASN A OD1   1 
ATOM   4994  N  ND2   . ASN A 1 648 ? 131.128 120.647 142.459 1.00 29.90  ? 648  ASN A ND2   1 
ATOM   4995  N  N     . PHE A 1 649 ? 134.210 116.836 139.817 1.00 19.94  ? 649  PHE A N     1 
ATOM   4996  C  CA    . PHE A 1 649 ? 134.406 115.514 139.232 1.00 5.98   ? 649  PHE A CA    1 
ATOM   4997  C  C     . PHE A 1 649 ? 135.710 114.891 139.714 1.00 12.97  ? 649  PHE A C     1 
ATOM   4998  O  O     . PHE A 1 649 ? 135.709 113.830 140.347 1.00 27.42  ? 649  PHE A O     1 
ATOM   4999  C  CB    . PHE A 1 649 ? 134.384 115.602 137.705 1.00 16.38  ? 649  PHE A CB    1 
ATOM   5000  C  CG    . PHE A 1 649 ? 134.725 114.307 137.022 1.00 21.66  ? 649  PHE A CG    1 
ATOM   5001  C  CD1   . PHE A 1 649 ? 133.762 113.331 136.840 1.00 19.85  ? 649  PHE A CD1   1 
ATOM   5002  C  CD2   . PHE A 1 649 ? 136.008 114.064 136.564 1.00 21.48  ? 649  PHE A CD2   1 
ATOM   5003  C  CE1   . PHE A 1 649 ? 134.072 112.140 136.220 1.00 15.24  ? 649  PHE A CE1   1 
ATOM   5004  C  CE2   . PHE A 1 649 ? 136.322 112.874 135.943 1.00 23.61  ? 649  PHE A CE2   1 
ATOM   5005  C  CZ    . PHE A 1 649 ? 135.353 111.911 135.773 1.00 23.98  ? 649  PHE A CZ    1 
ATOM   5006  N  N     . THR A 1 650 ? 136.835 115.561 139.452 1.00 16.13  ? 650  THR A N     1 
ATOM   5007  C  CA    . THR A 1 650 ? 138.139 114.966 139.719 1.00 11.78  ? 650  THR A CA    1 
ATOM   5008  C  C     . THR A 1 650 ? 138.399 114.756 141.206 1.00 13.40  ? 650  THR A C     1 
ATOM   5009  O  O     . THR A 1 650 ? 139.260 113.944 141.558 1.00 22.18  ? 650  THR A O     1 
ATOM   5010  C  CB    . THR A 1 650 ? 139.250 115.824 139.103 1.00 15.78  ? 650  THR A CB    1 
ATOM   5011  O  OG1   . THR A 1 650 ? 140.491 115.111 139.150 1.00 28.47  ? 650  THR A OG1   1 
ATOM   5012  C  CG2   . THR A 1 650 ? 139.409 117.128 139.852 1.00 22.20  ? 650  THR A CG2   1 
ATOM   5013  N  N     . HIS A 1 651 ? 137.673 115.443 142.089 1.00 27.95  ? 651  HIS A N     1 
ATOM   5014  C  CA    . HIS A 1 651 ? 137.876 115.265 143.516 1.00 27.21  ? 651  HIS A CA    1 
ATOM   5015  C  C     . HIS A 1 651 ? 136.766 114.492 144.209 1.00 30.53  ? 651  HIS A C     1 
ATOM   5016  O  O     . HIS A 1 651 ? 136.917 114.164 145.390 1.00 37.73  ? 651  HIS A O     1 
ATOM   5017  C  CB    . HIS A 1 651 ? 138.048 116.628 144.200 1.00 21.17  ? 651  HIS A CB    1 
ATOM   5018  C  CG    . HIS A 1 651 ? 139.391 117.247 143.975 1.00 24.43  ? 651  HIS A CG    1 
ATOM   5019  N  ND1   . HIS A 1 651 ? 140.513 116.862 144.674 1.00 30.42  ? 651  HIS A ND1   1 
ATOM   5020  C  CD2   . HIS A 1 651 ? 139.792 118.223 143.128 1.00 26.90  ? 651  HIS A CD2   1 
ATOM   5021  C  CE1   . HIS A 1 651 ? 141.548 117.576 144.269 1.00 28.15  ? 651  HIS A CE1   1 
ATOM   5022  N  NE2   . HIS A 1 651 ? 141.138 118.407 143.330 1.00 25.14  ? 651  HIS A NE2   1 
ATOM   5023  N  N     . GLU A 1 652 ? 135.672 114.180 143.525 1.00 26.40  ? 652  GLU A N     1 
ATOM   5024  C  CA    . GLU A 1 652 ? 134.594 113.429 144.148 1.00 26.18  ? 652  GLU A CA    1 
ATOM   5025  C  C     . GLU A 1 652 ? 134.338 112.082 143.496 1.00 36.09  ? 652  GLU A C     1 
ATOM   5026  O  O     . GLU A 1 652 ? 134.096 111.103 144.203 1.00 44.27  ? 652  GLU A O     1 
ATOM   5027  C  CB    . GLU A 1 652 ? 133.304 114.263 144.128 1.00 26.46  ? 652  GLU A CB    1 
ATOM   5028  C  CG    . GLU A 1 652 ? 132.152 113.648 144.899 1.00 36.88  ? 652  GLU A CG    1 
ATOM   5029  C  CD    . GLU A 1 652 ? 132.383 113.646 146.397 1.00 39.70  ? 652  GLU A CD    1 
ATOM   5030  O  OE1   . GLU A 1 652 ? 133.169 114.487 146.882 1.00 36.37  ? 652  GLU A OE1   1 
ATOM   5031  O  OE2   . GLU A 1 652 ? 131.778 112.802 147.091 1.00 38.96  ? 652  GLU A OE2   1 
ATOM   5032  N  N     . ILE A 1 653 ? 134.382 111.996 142.172 1.00 27.59  ? 653  ILE A N     1 
ATOM   5033  C  CA    . ILE A 1 653 ? 134.062 110.765 141.465 1.00 22.07  ? 653  ILE A CA    1 
ATOM   5034  C  C     . ILE A 1 653 ? 135.317 110.054 140.982 1.00 26.37  ? 653  ILE A C     1 
ATOM   5035  O  O     . ILE A 1 653 ? 135.510 108.870 141.255 1.00 37.53  ? 653  ILE A O     1 
ATOM   5036  C  CB    . ILE A 1 653 ? 133.095 111.062 140.299 1.00 17.38  ? 653  ILE A CB    1 
ATOM   5037  C  CG1   . ILE A 1 653 ? 131.799 111.658 140.849 1.00 21.60  ? 653  ILE A CG1   1 
ATOM   5038  C  CG2   . ILE A 1 653 ? 132.829 109.804 139.492 1.00 28.36  ? 653  ILE A CG2   1 
ATOM   5039  C  CD1   . ILE A 1 653 ? 130.684 111.717 139.853 1.00 28.10  ? 653  ILE A CD1   1 
ATOM   5040  N  N     . ALA A 1 654 ? 136.185 110.763 140.260 1.00 27.42  ? 654  ALA A N     1 
ATOM   5041  C  CA    . ALA A 1 654 ? 137.446 110.164 139.838 1.00 25.75  ? 654  ALA A CA    1 
ATOM   5042  C  C     . ALA A 1 654 ? 138.360 109.912 141.028 1.00 34.69  ? 654  ALA A C     1 
ATOM   5043  O  O     . ALA A 1 654 ? 139.073 108.903 141.066 1.00 41.75  ? 654  ALA A O     1 
ATOM   5044  C  CB    . ALA A 1 654 ? 138.138 111.056 138.809 1.00 23.70  ? 654  ALA A CB    1 
ATOM   5045  N  N     . ARG A 1 655 ? 138.338 110.814 142.011 1.00 38.53  ? 655  ARG A N     1 
ATOM   5046  C  CA    . ARG A 1 655 ? 139.236 110.765 143.165 1.00 40.42  ? 655  ARG A CA    1 
ATOM   5047  C  C     . ARG A 1 655 ? 140.694 110.703 142.723 1.00 39.25  ? 655  ARG A C     1 
ATOM   5048  O  O     . ARG A 1 655 ? 141.511 109.974 143.288 1.00 39.77  ? 655  ARG A O     1 
ATOM   5049  C  CB    . ARG A 1 655 ? 138.890 109.600 144.094 1.00 33.77  ? 655  ARG A CB    1 
ATOM   5050  C  CG    . ARG A 1 655 ? 137.559 109.750 144.805 1.00 35.26  ? 655  ARG A CG    1 
ATOM   5051  C  CD    . ARG A 1 655 ? 137.662 109.310 146.255 1.00 39.71  ? 655  ARG A CD    1 
ATOM   5052  N  NE    . ARG A 1 655 ? 138.113 107.929 146.380 1.00 41.27  ? 655  ARG A NE    1 
ATOM   5053  C  CZ    . ARG A 1 655 ? 138.345 107.318 147.535 1.00 42.44  ? 655  ARG A CZ    1 
ATOM   5054  N  NH1   . ARG A 1 655 ? 138.181 107.940 148.691 1.00 39.84  ? 655  ARG A NH1   1 
ATOM   5055  N  NH2   . ARG A 1 655 ? 138.751 106.052 147.529 1.00 39.81  ? 655  ARG A NH2   1 
ATOM   5056  N  N     . GLU A 1 656 ? 141.022 111.480 141.689 1.00 28.01  ? 656  GLU A N     1 
ATOM   5057  C  CA    . GLU A 1 656 ? 142.385 111.578 141.194 1.00 33.16  ? 656  GLU A CA    1 
ATOM   5058  C  C     . GLU A 1 656 ? 143.062 112.895 141.534 1.00 32.51  ? 656  GLU A C     1 
ATOM   5059  O  O     . GLU A 1 656 ? 144.294 112.937 141.588 1.00 40.74  ? 656  GLU A O     1 
ATOM   5060  C  CB    . GLU A 1 656 ? 142.416 111.388 139.672 1.00 33.18  ? 656  GLU A CB    1 
ATOM   5061  C  CG    . GLU A 1 656 ? 141.972 110.016 139.220 1.00 37.59  ? 656  GLU A CG    1 
ATOM   5062  C  CD    . GLU A 1 656 ? 142.084 109.835 137.725 1.00 39.98  ? 656  GLU A CD    1 
ATOM   5063  O  OE1   . GLU A 1 656 ? 142.050 110.849 137.000 1.00 37.95  ? 656  GLU A OE1   1 
ATOM   5064  O  OE2   . GLU A 1 656 ? 142.210 108.678 137.275 1.00 37.26  ? 656  GLU A OE2   1 
ATOM   5065  N  N     . GLY A 1 657 ? 142.299 113.957 141.763 1.00 27.21  ? 657  GLY A N     1 
ATOM   5066  C  CA    . GLY A 1 657 ? 142.878 115.248 142.082 1.00 27.69  ? 657  GLY A CA    1 
ATOM   5067  C  C     . GLY A 1 657 ? 143.690 115.856 140.961 1.00 32.05  ? 657  GLY A C     1 
ATOM   5068  O  O     . GLY A 1 657 ? 144.765 116.413 141.215 1.00 36.54  ? 657  GLY A O     1 
ATOM   5069  N  N     . ILE A 1 658 ? 143.206 115.755 139.722 1.00 33.02  ? 658  ILE A N     1 
ATOM   5070  C  CA    . ILE A 1 658 ? 143.941 116.300 138.584 1.00 31.49  ? 658  ILE A CA    1 
ATOM   5071  C  C     . ILE A 1 658 ? 144.069 117.812 138.712 1.00 37.52  ? 658  ILE A C     1 
ATOM   5072  O  O     . ILE A 1 658 ? 145.168 118.368 138.626 1.00 37.60  ? 658  ILE A O     1 
ATOM   5073  C  CB    . ILE A 1 658 ? 143.254 115.905 137.264 1.00 21.63  ? 658  ILE A CB    1 
ATOM   5074  C  CG1   . ILE A 1 658 ? 143.240 114.386 137.096 1.00 27.03  ? 658  ILE A CG1   1 
ATOM   5075  C  CG2   . ILE A 1 658 ? 143.948 116.554 136.087 1.00 25.99  ? 658  ILE A CG2   1 
ATOM   5076  C  CD1   . ILE A 1 658 ? 144.611 113.775 137.021 1.00 39.60  ? 658  ILE A CD1   1 
ATOM   5077  N  N     . VAL A 1 659 ? 142.950 118.495 138.946 1.00 29.76  ? 659  VAL A N     1 
ATOM   5078  C  CA    . VAL A 1 659 ? 142.915 119.947 139.040 1.00 27.01  ? 659  VAL A CA    1 
ATOM   5079  C  C     . VAL A 1 659 ? 142.135 120.340 140.284 1.00 26.11  ? 659  VAL A C     1 
ATOM   5080  O  O     . VAL A 1 659 ? 141.386 119.546 140.855 1.00 29.83  ? 659  VAL A O     1 
ATOM   5081  C  CB    . VAL A 1 659 ? 142.289 120.606 137.791 1.00 28.12  ? 659  VAL A CB    1 
ATOM   5082  C  CG1   . VAL A 1 659 ? 143.171 120.402 136.574 1.00 25.36  ? 659  VAL A CG1   1 
ATOM   5083  C  CG2   . VAL A 1 659 ? 140.898 120.054 137.543 1.00 23.45  ? 659  VAL A CG2   1 
ATOM   5084  N  N     . ASP A 1 660 ? 142.320 121.587 140.701 1.00 20.40  ? 660  ASP A N     1 
ATOM   5085  C  CA    . ASP A 1 660 ? 141.569 122.126 141.824 1.00 21.73  ? 660  ASP A CA    1 
ATOM   5086  C  C     . ASP A 1 660 ? 141.588 123.644 141.733 1.00 25.78  ? 660  ASP A C     1 
ATOM   5087  O  O     . ASP A 1 660 ? 142.318 124.229 140.929 1.00 31.57  ? 660  ASP A O     1 
ATOM   5088  C  CB    . ASP A 1 660 ? 142.137 121.646 143.162 1.00 28.26  ? 660  ASP A CB    1 
ATOM   5089  C  CG    . ASP A 1 660 ? 141.112 121.681 144.275 1.00 32.85  ? 660  ASP A CG    1 
ATOM   5090  O  OD1   . ASP A 1 660 ? 140.226 122.558 144.245 1.00 35.66  ? 660  ASP A OD1   1 
ATOM   5091  O  OD2   . ASP A 1 660 ? 141.189 120.827 145.181 1.00 33.72  ? 660  ASP A OD2   1 
ATOM   5092  N  N     . TYR A 1 661 ? 140.752 124.272 142.556 1.00 24.21  ? 661  TYR A N     1 
ATOM   5093  C  CA    . TYR A 1 661 ? 140.772 125.721 142.688 1.00 14.29  ? 661  TYR A CA    1 
ATOM   5094  C  C     . TYR A 1 661 ? 142.133 126.183 143.185 1.00 15.04  ? 661  TYR A C     1 
ATOM   5095  O  O     . TYR A 1 661 ? 142.727 125.569 144.073 1.00 29.60  ? 661  TYR A O     1 
ATOM   5096  C  CB    . TYR A 1 661 ? 139.699 126.184 143.671 1.00 16.09  ? 661  TYR A CB    1 
ATOM   5097  C  CG    . TYR A 1 661 ? 138.276 126.159 143.172 1.00 4.11   ? 661  TYR A CG    1 
ATOM   5098  C  CD1   . TYR A 1 661 ? 137.486 125.029 143.322 1.00 11.13  ? 661  TYR A CD1   1 
ATOM   5099  C  CD2   . TYR A 1 661 ? 137.707 127.282 142.591 1.00 13.21  ? 661  TYR A CD2   1 
ATOM   5100  C  CE1   . TYR A 1 661 ? 136.179 125.012 142.888 1.00 14.75  ? 661  TYR A CE1   1 
ATOM   5101  C  CE2   . TYR A 1 661 ? 136.402 127.273 142.154 1.00 17.66  ? 661  TYR A CE2   1 
ATOM   5102  C  CZ    . TYR A 1 661 ? 135.643 126.137 142.306 1.00 18.78  ? 661  TYR A CZ    1 
ATOM   5103  O  OH    . TYR A 1 661 ? 134.341 126.128 141.871 1.00 29.38  ? 661  TYR A OH    1 
ATOM   5104  N  N     . LEU A 1 662 ? 142.626 127.273 142.610 1.00 30.00  ? 662  LEU A N     1 
ATOM   5105  C  CA    . LEU A 1 662 ? 143.868 127.886 143.057 1.00 30.00  ? 662  LEU A CA    1 
ATOM   5106  C  C     . LEU A 1 662 ? 143.620 129.366 143.296 1.00 30.00  ? 662  LEU A C     1 
ATOM   5107  O  O     . LEU A 1 662 ? 143.062 130.050 142.432 1.00 30.00  ? 662  LEU A O     1 
ATOM   5108  C  CB    . LEU A 1 662 ? 144.991 127.673 142.038 1.00 30.00  ? 662  LEU A CB    1 
ATOM   5109  C  CG    . LEU A 1 662 ? 145.437 126.220 141.851 1.00 30.00  ? 662  LEU A CG    1 
ATOM   5110  C  CD1   . LEU A 1 662 ? 146.535 126.118 140.813 1.00 30.00  ? 662  LEU A CD1   1 
ATOM   5111  C  CD2   . LEU A 1 662 ? 145.901 125.623 143.165 1.00 30.00  ? 662  LEU A CD2   1 
ATOM   5112  N  N     . PHE A 1 663 ? 144.011 129.841 144.482 1.00 30.00  ? 663  PHE A N     1 
ATOM   5113  C  CA    . PHE A 1 663 ? 143.818 131.215 144.943 1.00 30.00  ? 663  PHE A CA    1 
ATOM   5114  C  C     . PHE A 1 663 ? 142.337 131.569 145.048 1.00 30.00  ? 663  PHE A C     1 
ATOM   5115  O  O     . PHE A 1 663 ? 141.474 130.751 144.717 1.00 30.00  ? 663  PHE A O     1 
ATOM   5116  C  CB    . PHE A 1 663 ? 144.567 132.192 144.035 1.00 30.00  ? 663  PHE A CB    1 
ATOM   5117  C  CG    . PHE A 1 663 ? 146.047 131.937 143.974 1.00 30.00  ? 663  PHE A CG    1 
ATOM   5118  C  CD1   . PHE A 1 663 ? 146.891 132.445 144.947 1.00 30.00  ? 663  PHE A CD1   1 
ATOM   5119  C  CD2   . PHE A 1 663 ? 146.594 131.181 142.954 1.00 30.00  ? 663  PHE A CD2   1 
ATOM   5120  C  CE1   . PHE A 1 663 ? 148.250 132.207 144.899 1.00 30.00  ? 663  PHE A CE1   1 
ATOM   5121  C  CE2   . PHE A 1 663 ? 147.955 130.943 142.901 1.00 30.00  ? 663  PHE A CE2   1 
ATOM   5122  C  CZ    . PHE A 1 663 ? 148.783 131.457 143.875 1.00 30.00  ? 663  PHE A CZ    1 
ATOM   5123  N  N     . ARG A 1 664 ? 142.022 132.766 145.537 1.00 30.00  ? 664  ARG A N     1 
ATOM   5124  C  CA    . ARG A 1 664 ? 140.634 133.127 145.785 1.00 30.00  ? 664  ARG A CA    1 
ATOM   5125  C  C     . ARG A 1 664 ? 140.355 134.532 145.273 1.00 30.00  ? 664  ARG A C     1 
ATOM   5126  O  O     . ARG A 1 664 ? 141.262 135.351 145.110 1.00 30.00  ? 664  ARG A O     1 
ATOM   5127  C  CB    . ARG A 1 664 ? 140.275 133.032 147.276 1.00 30.00  ? 664  ARG A CB    1 
ATOM   5128  C  CG    . ARG A 1 664 ? 140.760 134.195 148.115 1.00 30.00  ? 664  ARG A CG    1 
ATOM   5129  C  CD    . ARG A 1 664 ? 140.202 134.131 149.524 1.00 30.00  ? 664  ARG A CD    1 
ATOM   5130  N  NE    . ARG A 1 664 ? 140.522 135.332 150.285 1.00 30.00  ? 664  ARG A NE    1 
ATOM   5131  C  CZ    . ARG A 1 664 ? 141.627 135.497 150.998 1.00 30.00  ? 664  ARG A CZ    1 
ATOM   5132  N  NH1   . ARG A 1 664 ? 142.539 134.545 151.090 1.00 30.00  ? 664  ARG A NH1   1 
ATOM   5133  N  NH2   . ARG A 1 664 ? 141.824 136.648 151.632 1.00 30.00  ? 664  ARG A NH2   1 
ATOM   5134  N  N     . GLY A 1 665 ? 139.077 134.793 145.012 1.00 19.86  ? 665  GLY A N     1 
ATOM   5135  C  CA    . GLY A 1 665 ? 138.630 136.107 144.598 1.00 19.55  ? 665  GLY A CA    1 
ATOM   5136  C  C     . GLY A 1 665 ? 138.504 136.251 143.098 1.00 12.99  ? 665  GLY A C     1 
ATOM   5137  O  O     . GLY A 1 665 ? 138.003 135.354 142.417 1.00 14.02  ? 665  GLY A O     1 
ATOM   5138  N  N     . PHE A 1 666 ? 138.951 137.388 142.572 1.00 23.42  ? 666  PHE A N     1 
ATOM   5139  C  CA    . PHE A 1 666 ? 138.990 137.584 141.132 1.00 23.17  ? 666  PHE A CA    1 
ATOM   5140  C  C     . PHE A 1 666 ? 140.133 136.820 140.479 1.00 27.85  ? 666  PHE A C     1 
ATOM   5141  O  O     . PHE A 1 666 ? 140.114 136.621 139.261 1.00 27.67  ? 666  PHE A O     1 
ATOM   5142  C  CB    . PHE A 1 666 ? 139.104 139.076 140.815 1.00 18.43  ? 666  PHE A CB    1 
ATOM   5143  C  CG    . PHE A 1 666 ? 138.816 139.418 139.386 1.00 20.04  ? 666  PHE A CG    1 
ATOM   5144  C  CD1   . PHE A 1 666 ? 137.532 139.314 138.882 1.00 23.68  ? 666  PHE A CD1   1 
ATOM   5145  C  CD2   . PHE A 1 666 ? 139.824 139.859 138.549 1.00 19.97  ? 666  PHE A CD2   1 
ATOM   5146  C  CE1   . PHE A 1 666 ? 137.263 139.633 137.571 1.00 17.45  ? 666  PHE A CE1   1 
ATOM   5147  C  CE2   . PHE A 1 666 ? 139.558 140.178 137.237 1.00 24.55  ? 666  PHE A CE2   1 
ATOM   5148  C  CZ    . PHE A 1 666 ? 138.276 140.064 136.748 1.00 27.15  ? 666  PHE A CZ    1 
ATOM   5149  N  N     . LYS A 1 667 ? 141.110 136.374 141.263 1.00 26.01  ? 667  LYS A N     1 
ATOM   5150  C  CA    . LYS A 1 667 ? 142.296 135.703 140.755 1.00 15.67  ? 667  LYS A CA    1 
ATOM   5151  C  C     . LYS A 1 667 ? 142.160 134.185 140.744 1.00 15.71  ? 667  LYS A C     1 
ATOM   5152  O  O     . LYS A 1 667 ? 143.154 133.487 140.522 1.00 27.84  ? 667  LYS A O     1 
ATOM   5153  C  CB    . LYS A 1 667 ? 143.515 136.106 141.587 1.00 19.89  ? 667  LYS A CB    1 
ATOM   5154  C  CG    . LYS A 1 667 ? 143.583 137.587 141.913 1.00 23.09  ? 667  LYS A CG    1 
ATOM   5155  C  CD    . LYS A 1 667 ? 143.829 138.429 140.675 1.00 23.86  ? 667  LYS A CD    1 
ATOM   5156  C  CE    . LYS A 1 667 ? 145.208 138.178 140.102 1.00 25.67  ? 667  LYS A CE    1 
ATOM   5157  N  NZ    . LYS A 1 667 ? 145.487 139.047 138.931 1.00 33.24  ? 667  LYS A NZ    1 
ATOM   5158  N  N     . THR A 1 668 ? 140.962 133.662 140.979 1.00 12.58  ? 668  THR A N     1 
ATOM   5159  C  CA    . THR A 1 668 ? 140.771 132.221 141.058 1.00 6.19   ? 668  THR A CA    1 
ATOM   5160  C  C     . THR A 1 668 ? 140.853 131.583 139.677 1.00 21.89  ? 668  THR A C     1 
ATOM   5161  O  O     . THR A 1 668 ? 140.347 132.126 138.692 1.00 34.46  ? 668  THR A O     1 
ATOM   5162  C  CB    . THR A 1 668 ? 139.418 131.905 141.695 1.00 3.83   ? 668  THR A CB    1 
ATOM   5163  O  OG1   . THR A 1 668 ? 139.211 132.758 142.825 1.00 25.58  ? 668  THR A OG1   1 
ATOM   5164  C  CG2   . THR A 1 668 ? 139.366 130.461 142.155 1.00 12.36  ? 668  THR A CG2   1 
ATOM   5165  N  N     . TYR A 1 669 ? 141.493 130.419 139.607 1.00 12.60  ? 669  TYR A N     1 
ATOM   5166  C  CA    . TYR A 1 669 ? 141.482 129.623 138.390 1.00 5.57   ? 669  TYR A CA    1 
ATOM   5167  C  C     . TYR A 1 669 ? 141.517 128.149 138.762 1.00 13.05  ? 669  TYR A C     1 
ATOM   5168  O  O     . TYR A 1 669 ? 141.646 127.783 139.932 1.00 22.53  ? 669  TYR A O     1 
ATOM   5169  C  CB    . TYR A 1 669 ? 142.638 129.996 137.453 1.00 14.34  ? 669  TYR A CB    1 
ATOM   5170  C  CG    . TYR A 1 669 ? 144.029 129.737 137.984 1.00 13.90  ? 669  TYR A CG    1 
ATOM   5171  C  CD1   . TYR A 1 669 ? 144.667 130.664 138.794 1.00 17.84  ? 669  TYR A CD1   1 
ATOM   5172  C  CD2   . TYR A 1 669 ? 144.719 128.583 137.641 1.00 18.07  ? 669  TYR A CD2   1 
ATOM   5173  C  CE1   . TYR A 1 669 ? 145.941 130.440 139.265 1.00 18.81  ? 669  TYR A CE1   1 
ATOM   5174  C  CE2   . TYR A 1 669 ? 145.994 128.352 138.107 1.00 15.10  ? 669  TYR A CE2   1 
ATOM   5175  C  CZ    . TYR A 1 669 ? 146.600 129.283 138.919 1.00 12.53  ? 669  TYR A CZ    1 
ATOM   5176  O  OH    . TYR A 1 669 ? 147.870 129.058 139.388 1.00 19.61  ? 669  TYR A OH    1 
ATOM   5177  N  N     . ILE A 1 670 ? 141.373 127.302 137.749 1.00 19.55  ? 670  ILE A N     1 
ATOM   5178  C  CA    . ILE A 1 670 ? 141.338 125.855 137.919 1.00 15.61  ? 670  ILE A CA    1 
ATOM   5179  C  C     . ILE A 1 670 ? 142.583 125.284 137.258 1.00 24.84  ? 670  ILE A C     1 
ATOM   5180  O  O     . ILE A 1 670 ? 142.679 125.241 136.026 1.00 32.55  ? 670  ILE A O     1 
ATOM   5181  C  CB    . ILE A 1 670 ? 140.068 125.240 137.321 1.00 21.57  ? 670  ILE A CB    1 
ATOM   5182  C  CG1   . ILE A 1 670 ? 138.817 125.863 137.945 1.00 25.30  ? 670  ILE A CG1   1 
ATOM   5183  C  CG2   . ILE A 1 670 ? 140.085 123.740 137.497 1.00 23.97  ? 670  ILE A CG2   1 
ATOM   5184  C  CD1   . ILE A 1 670 ? 138.797 125.839 139.445 1.00 22.10  ? 670  ILE A CD1   1 
ATOM   5185  N  N     . GLY A 1 671 ? 143.533 124.834 138.071 1.00 17.53  ? 671  GLY A N     1 
ATOM   5186  C  CA    . GLY A 1 671 ? 144.782 124.317 137.567 1.00 22.52  ? 671  GLY A CA    1 
ATOM   5187  C  C     . GLY A 1 671 ? 145.215 123.068 138.303 1.00 32.91  ? 671  GLY A C     1 
ATOM   5188  O  O     . GLY A 1 671 ? 144.667 122.721 139.352 1.00 31.67  ? 671  GLY A O     1 
ATOM   5189  N  N     . PRO A 1 672 ? 146.201 122.353 137.753 1.00 38.90  ? 672  PRO A N     1 
ATOM   5190  C  CA    . PRO A 1 672 ? 146.638 121.101 138.383 1.00 31.41  ? 672  PRO A CA    1 
ATOM   5191  C  C     . PRO A 1 672 ? 147.243 121.301 139.761 1.00 32.56  ? 672  PRO A C     1 
ATOM   5192  O  O     . PRO A 1 672 ? 146.726 120.795 140.760 1.00 34.92  ? 672  PRO A O     1 
ATOM   5193  C  CB    . PRO A 1 672 ? 147.681 120.557 137.397 1.00 33.57  ? 672  PRO A CB    1 
ATOM   5194  C  CG    . PRO A 1 672 ? 147.389 121.244 136.108 1.00 33.17  ? 672  PRO A CG    1 
ATOM   5195  C  CD    . PRO A 1 672 ? 146.898 122.601 136.481 1.00 34.35  ? 672  PRO A CD    1 
ATOM   5196  N  N     . GLN A 1 673 ? 148.316 122.079 139.817 1.00 34.76  ? 673  GLN A N     1 
ATOM   5197  C  CA    . GLN A 1 673 ? 149.045 122.395 141.037 1.00 33.39  ? 673  GLN A CA    1 
ATOM   5198  C  C     . GLN A 1 673 ? 150.143 123.363 140.627 1.00 35.43  ? 673  GLN A C     1 
ATOM   5199  O  O     . GLN A 1 673 ? 150.418 123.546 139.438 1.00 48.85  ? 673  GLN A O     1 
ATOM   5200  C  CB    . GLN A 1 673 ? 149.634 121.160 141.724 1.00 37.72  ? 673  GLN A CB    1 
ATOM   5201  C  CG    . GLN A 1 673 ? 150.763 120.502 140.965 1.00 33.58  ? 673  GLN A CG    1 
ATOM   5202  C  CD    . GLN A 1 673 ? 151.186 119.185 141.577 1.00 39.89  ? 673  GLN A CD    1 
ATOM   5203  O  OE1   . GLN A 1 673 ? 152.339 119.009 141.964 1.00 39.36  ? 673  GLN A OE1   1 
ATOM   5204  N  NE2   . GLN A 1 673 ? 150.254 118.247 141.658 1.00 43.42  ? 673  GLN A NE2   1 
ATOM   5205  N  N     . LEU A 1 674 ? 150.765 123.985 141.619 1.00 38.65  ? 674  LEU A N     1 
ATOM   5206  C  CA    . LEU A 1 674 ? 151.837 124.923 141.328 1.00 40.92  ? 674  LEU A CA    1 
ATOM   5207  C  C     . LEU A 1 674 ? 153.096 124.165 140.928 1.00 51.40  ? 674  LEU A C     1 
ATOM   5208  O  O     . LEU A 1 674 ? 153.536 123.252 141.632 1.00 50.69  ? 674  LEU A O     1 
ATOM   5209  C  CB    . LEU A 1 674 ? 152.106 125.820 142.535 1.00 41.37  ? 674  LEU A CB    1 
ATOM   5210  C  CG    . LEU A 1 674 ? 151.191 127.034 142.716 1.00 46.85  ? 674  LEU A CG    1 
ATOM   5211  C  CD1   . LEU A 1 674 ? 149.823 126.638 143.243 1.00 45.29  ? 674  LEU A CD1   1 
ATOM   5212  C  CD2   . LEU A 1 674 ? 151.840 128.060 143.629 1.00 47.85  ? 674  LEU A CD2   1 
ATOM   5213  N  N     . GLY A 1 675 ? 153.674 124.545 139.793 1.00 58.12  ? 675  GLY A N     1 
ATOM   5214  C  CA    . GLY A 1 675 ? 154.884 123.924 139.307 1.00 59.17  ? 675  GLY A CA    1 
ATOM   5215  C  C     . GLY A 1 675 ? 154.688 122.717 138.418 1.00 60.80  ? 675  GLY A C     1 
ATOM   5216  O  O     . GLY A 1 675 ? 155.682 122.146 137.954 1.00 64.77  ? 675  GLY A O     1 
ATOM   5217  N  N     . GLU A 1 676 ? 153.449 122.303 138.168 1.00 54.10  ? 676  GLU A N     1 
ATOM   5218  C  CA    . GLU A 1 676 ? 153.180 121.182 137.281 1.00 56.70  ? 676  GLU A CA    1 
ATOM   5219  C  C     . GLU A 1 676 ? 152.039 121.539 136.344 1.00 58.49  ? 676  GLU A C     1 
ATOM   5220  O  O     . GLU A 1 676 ? 151.199 122.385 136.658 1.00 58.43  ? 676  GLU A O     1 
ATOM   5221  C  CB    . GLU A 1 676 ? 152.831 119.904 138.053 1.00 58.24  ? 676  GLU A CB    1 
ATOM   5222  C  CG    . GLU A 1 676 ? 153.999 119.288 138.795 1.00 58.66  ? 676  GLU A CG    1 
ATOM   5223  C  CD    . GLU A 1 676 ? 153.659 117.939 139.395 1.00 63.75  ? 676  GLU A CD    1 
ATOM   5224  O  OE1   . GLU A 1 676 ? 152.506 117.489 139.229 1.00 63.12  ? 676  GLU A OE1   1 
ATOM   5225  O  OE2   . GLU A 1 676 ? 154.543 117.329 140.032 1.00 61.02  ? 676  GLU A OE2   1 
ATOM   5226  N  N     . ARG A 1 677 ? 152.021 120.888 135.190 1.00 61.05  ? 677  ARG A N     1 
ATOM   5227  C  CA    . ARG A 1 677 ? 150.970 121.060 134.202 1.00 60.86  ? 677  ARG A CA    1 
ATOM   5228  C  C     . ARG A 1 677 ? 150.238 119.735 134.012 1.00 57.47  ? 677  ARG A C     1 
ATOM   5229  O  O     . ARG A 1 677 ? 150.516 118.744 134.688 1.00 59.72  ? 677  ARG A O     1 
ATOM   5230  C  CB    . ARG A 1 677 ? 151.546 121.591 132.888 1.00 57.07  ? 677  ARG A CB    1 
ATOM   5231  C  CG    . ARG A 1 677 ? 152.458 122.785 133.091 1.00 55.39  ? 677  ARG A CG    1 
ATOM   5232  C  CD    . ARG A 1 677 ? 152.835 123.450 131.787 1.00 55.54  ? 677  ARG A CD    1 
ATOM   5233  N  NE    . ARG A 1 677 ? 151.771 124.307 131.283 1.00 59.74  ? 677  ARG A NE    1 
ATOM   5234  C  CZ    . ARG A 1 677 ? 151.911 125.155 130.274 1.00 62.07  ? 677  ARG A CZ    1 
ATOM   5235  N  NH1   . ARG A 1 677 ? 153.061 125.284 129.635 1.00 57.10  ? 677  ARG A NH1   1 
ATOM   5236  N  NH2   . ARG A 1 677 ? 150.872 125.897 129.901 1.00 59.42  ? 677  ARG A NH2   1 
ATOM   5237  N  N     . LEU A 1 678 ? 149.286 119.730 133.078 1.00 50.67  ? 678  LEU A N     1 
ATOM   5238  C  CA    . LEU A 1 678 ? 148.376 118.598 132.946 1.00 55.53  ? 678  LEU A CA    1 
ATOM   5239  C  C     . LEU A 1 678 ? 149.052 117.352 132.388 1.00 54.49  ? 678  LEU A C     1 
ATOM   5240  O  O     . LEU A 1 678 ? 148.509 116.253 132.535 1.00 47.62  ? 678  LEU A O     1 
ATOM   5241  C  CB    . LEU A 1 678 ? 147.191 118.982 132.061 1.00 53.62  ? 678  LEU A CB    1 
ATOM   5242  C  CG    . LEU A 1 678 ? 145.839 118.398 132.464 1.00 50.35  ? 678  LEU A CG    1 
ATOM   5243  C  CD1   . LEU A 1 678 ? 145.370 119.030 133.758 1.00 49.84  ? 678  LEU A CD1   1 
ATOM   5244  C  CD2   . LEU A 1 678 ? 144.818 118.603 131.367 1.00 47.44  ? 678  LEU A CD2   1 
ATOM   5245  N  N     . GLU A 1 679 ? 150.211 117.495 131.742 1.00 63.67  ? 679  GLU A N     1 
ATOM   5246  C  CA    . GLU A 1 679 ? 150.898 116.327 131.201 1.00 63.12  ? 679  GLU A CA    1 
ATOM   5247  C  C     . GLU A 1 679 ? 151.501 115.465 132.301 1.00 64.77  ? 679  GLU A C     1 
ATOM   5248  O  O     . GLU A 1 679 ? 151.571 114.240 132.159 1.00 65.47  ? 679  GLU A O     1 
ATOM   5249  C  CB    . GLU A 1 679 ? 151.980 116.760 130.213 1.00 63.09  ? 679  GLU A CB    1 
ATOM   5250  C  CG    . GLU A 1 679 ? 152.985 117.741 130.782 1.00 64.97  ? 679  GLU A CG    1 
ATOM   5251  C  CD    . GLU A 1 679 ? 154.077 118.093 129.794 1.00 65.53  ? 679  GLU A CD    1 
ATOM   5252  O  OE1   . GLU A 1 679 ? 154.113 117.487 128.703 1.00 66.54  ? 679  GLU A OE1   1 
ATOM   5253  O  OE2   . GLU A 1 679 ? 154.901 118.979 130.107 1.00 65.26  ? 679  GLU A OE2   1 
ATOM   5254  N  N     . ASP A 1 680 ? 151.936 116.079 133.400 1.00 64.20  ? 680  ASP A N     1 
ATOM   5255  C  CA    . ASP A 1 680 ? 152.569 115.342 134.484 1.00 62.92  ? 680  ASP A CA    1 
ATOM   5256  C  C     . ASP A 1 680 ? 151.577 114.548 135.318 1.00 63.60  ? 680  ASP A C     1 
ATOM   5257  O  O     . ASP A 1 680 ? 152.003 113.708 136.116 1.00 66.01  ? 680  ASP A O     1 
ATOM   5258  C  CB    . ASP A 1 680 ? 153.335 116.307 135.385 1.00 63.80  ? 680  ASP A CB    1 
ATOM   5259  C  CG    . ASP A 1 680 ? 154.151 117.305 134.601 1.00 67.02  ? 680  ASP A CG    1 
ATOM   5260  O  OD1   . ASP A 1 680 ? 154.744 116.913 133.577 1.00 69.43  ? 680  ASP A OD1   1 
ATOM   5261  O  OD2   . ASP A 1 680 ? 154.194 118.485 135.004 1.00 65.27  ? 680  ASP A OD2   1 
ATOM   5262  N  N     . GLN A 1 681 ? 150.281 114.791 135.162 1.00 59.43  ? 681  GLN A N     1 
ATOM   5263  C  CA    . GLN A 1 681 ? 149.287 114.137 135.997 1.00 57.91  ? 681  GLN A CA    1 
ATOM   5264  C  C     . GLN A 1 681 ? 149.040 112.714 135.519 1.00 62.32  ? 681  GLN A C     1 
ATOM   5265  O  O     . GLN A 1 681 ? 148.944 112.452 134.317 1.00 64.13  ? 681  GLN A O     1 
ATOM   5266  C  CB    . GLN A 1 681 ? 147.987 114.937 135.995 1.00 56.55  ? 681  GLN A CB    1 
ATOM   5267  C  CG    . GLN A 1 681 ? 148.189 116.427 136.224 1.00 59.34  ? 681  GLN A CG    1 
ATOM   5268  C  CD    . GLN A 1 681 ? 148.934 116.735 137.509 1.00 61.10  ? 681  GLN A CD    1 
ATOM   5269  O  OE1   . GLN A 1 681 ? 149.867 117.536 137.522 1.00 59.35  ? 681  GLN A OE1   1 
ATOM   5270  N  NE2   . GLN A 1 681 ? 148.516 116.108 138.601 1.00 62.38  ? 681  GLN A NE2   1 
ATOM   5271  N  N     . LYS A 1 682 ? 148.935 111.791 136.474 1.00 65.44  ? 682  LYS A N     1 
ATOM   5272  C  CA    . LYS A 1 682 ? 148.839 110.365 136.193 1.00 64.60  ? 682  LYS A CA    1 
ATOM   5273  C  C     . LYS A 1 682 ? 147.403 109.858 136.240 1.00 65.16  ? 682  LYS A C     1 
ATOM   5274  O  O     . LYS A 1 682 ? 147.161 108.718 136.648 1.00 65.51  ? 682  LYS A O     1 
ATOM   5275  C  CB    . LYS A 1 682 ? 149.706 109.584 137.177 1.00 58.95  ? 682  LYS A CB    1 
ATOM   5276  C  CG    . LYS A 1 682 ? 151.090 110.167 137.365 1.00 60.08  ? 682  LYS A CG    1 
ATOM   5277  C  CD    . LYS A 1 682 ? 151.663 109.782 138.714 1.00 63.34  ? 682  LYS A CD    1 
ATOM   5278  C  CE    . LYS A 1 682 ? 150.734 110.210 139.839 1.00 61.43  ? 682  LYS A CE    1 
ATOM   5279  N  NZ    . LYS A 1 682 ? 150.405 111.660 139.764 1.00 59.35  ? 682  LYS A NZ    1 
ATOM   5280  N  N     . GLY A 1 683 ? 146.445 110.680 135.834 1.00 48.67  ? 683  GLY A N     1 
ATOM   5281  C  CA    . GLY A 1 683 ? 145.060 110.275 135.860 1.00 40.74  ? 683  GLY A CA    1 
ATOM   5282  C  C     . GLY A 1 683 ? 144.614 109.585 134.586 1.00 48.06  ? 683  GLY A C     1 
ATOM   5283  O  O     . GLY A 1 683 ? 145.174 109.778 133.510 1.00 49.79  ? 683  GLY A O     1 
ATOM   5284  N  N     . VAL A 1 684 ? 143.575 108.765 134.726 1.00 43.45  ? 684  VAL A N     1 
ATOM   5285  C  CA    . VAL A 1 684 ? 142.967 108.060 133.606 1.00 39.74  ? 684  VAL A CA    1 
ATOM   5286  C  C     . VAL A 1 684 ? 141.619 108.651 133.224 1.00 35.50  ? 684  VAL A C     1 
ATOM   5287  O  O     . VAL A 1 684 ? 141.012 108.211 132.237 1.00 42.32  ? 684  VAL A O     1 
ATOM   5288  C  CB    . VAL A 1 684 ? 142.845 106.552 133.907 1.00 39.42  ? 684  VAL A CB    1 
ATOM   5289  C  CG1   . VAL A 1 684 ? 141.629 106.270 134.761 1.00 40.38  ? 684  VAL A CG1   1 
ATOM   5290  C  CG2   . VAL A 1 684 ? 142.839 105.727 132.626 1.00 40.96  ? 684  VAL A CG2   1 
ATOM   5291  N  N     . PHE A 1 685 ? 141.142 109.655 133.957 1.00 36.66  ? 685  PHE A N     1 
ATOM   5292  C  CA    . PHE A 1 685 ? 139.922 110.365 133.595 1.00 39.18  ? 685  PHE A CA    1 
ATOM   5293  C  C     . PHE A 1 685 ? 140.208 111.843 133.370 1.00 38.79  ? 685  PHE A C     1 
ATOM   5294  O  O     . PHE A 1 685 ? 139.504 112.708 133.900 1.00 38.59  ? 685  PHE A O     1 
ATOM   5295  C  CB    . PHE A 1 685 ? 138.848 110.184 134.666 1.00 31.87  ? 685  PHE A CB    1 
ATOM   5296  C  CG    . PHE A 1 685 ? 138.283 108.799 134.720 1.00 29.72  ? 685  PHE A CG    1 
ATOM   5297  C  CD1   . PHE A 1 685 ? 137.362 108.378 133.780 1.00 30.18  ? 685  PHE A CD1   1 
ATOM   5298  C  CD2   . PHE A 1 685 ? 138.674 107.918 135.709 1.00 38.36  ? 685  PHE A CD2   1 
ATOM   5299  C  CE1   . PHE A 1 685 ? 136.843 107.102 133.826 1.00 33.59  ? 685  PHE A CE1   1 
ATOM   5300  C  CE2   . PHE A 1 685 ? 138.161 106.642 135.758 1.00 35.17  ? 685  PHE A CE2   1 
ATOM   5301  C  CZ    . PHE A 1 685 ? 137.246 106.233 134.815 1.00 33.76  ? 685  PHE A CZ    1 
ATOM   5302  N  N     . ILE A 1 686 ? 141.263 112.141 132.613 1.00 33.36  ? 686  ILE A N     1 
ATOM   5303  C  CA    . ILE A 1 686 ? 141.532 113.523 132.235 1.00 28.80  ? 686  ILE A CA    1 
ATOM   5304  C  C     . ILE A 1 686 ? 140.696 113.921 131.022 1.00 30.73  ? 686  ILE A C     1 
ATOM   5305  O  O     . ILE A 1 686 ? 140.335 115.093 130.866 1.00 41.11  ? 686  ILE A O     1 
ATOM   5306  C  CB    . ILE A 1 686 ? 143.037 113.715 131.984 1.00 35.82  ? 686  ILE A CB    1 
ATOM   5307  C  CG1   . ILE A 1 686 ? 143.839 113.221 133.189 1.00 34.89  ? 686  ILE A CG1   1 
ATOM   5308  C  CG2   . ILE A 1 686 ? 143.360 115.172 131.713 1.00 35.33  ? 686  ILE A CG2   1 
ATOM   5309  C  CD1   . ILE A 1 686 ? 145.325 113.420 133.062 1.00 34.78  ? 686  ILE A CD1   1 
ATOM   5310  N  N     . GLY A 1 687 ? 140.351 112.964 130.163 1.00 28.17  ? 687  GLY A N     1 
ATOM   5311  C  CA    . GLY A 1 687 ? 139.546 113.261 128.995 1.00 31.56  ? 687  GLY A CA    1 
ATOM   5312  C  C     . GLY A 1 687 ? 138.072 113.461 129.261 1.00 30.02  ? 687  GLY A C     1 
ATOM   5313  O  O     . GLY A 1 687 ? 137.350 113.902 128.363 1.00 29.38  ? 687  GLY A O     1 
ATOM   5314  N  N     . GLU A 1 688 ? 137.606 113.144 130.470 1.00 32.24  ? 688  GLU A N     1 
ATOM   5315  C  CA    . GLU A 1 688 ? 136.210 113.387 130.812 1.00 27.20  ? 688  GLU A CA    1 
ATOM   5316  C  C     . GLU A 1 688 ? 135.948 114.866 131.054 1.00 31.20  ? 688  GLU A C     1 
ATOM   5317  O  O     . GLU A 1 688 ? 134.823 115.341 130.851 1.00 37.23  ? 688  GLU A O     1 
ATOM   5318  C  CB    . GLU A 1 688 ? 135.828 112.564 132.042 1.00 21.51  ? 688  GLU A CB    1 
ATOM   5319  C  CG    . GLU A 1 688 ? 134.365 112.644 132.416 1.00 27.85  ? 688  GLU A CG    1 
ATOM   5320  C  CD    . GLU A 1 688 ? 133.458 112.099 131.338 1.00 29.23  ? 688  GLU A CD    1 
ATOM   5321  O  OE1   . GLU A 1 688 ? 133.871 111.161 130.628 1.00 30.90  ? 688  GLU A OE1   1 
ATOM   5322  O  OE2   . GLU A 1 688 ? 132.328 112.609 131.202 1.00 35.44  ? 688  GLU A OE2   1 
ATOM   5323  N  N     . LEU A 1 689 ? 136.976 115.609 131.467 1.00 26.68  ? 689  LEU A N     1 
ATOM   5324  C  CA    . LEU A 1 689 ? 136.821 117.030 131.744 1.00 12.57  ? 689  LEU A CA    1 
ATOM   5325  C  C     . LEU A 1 689 ? 136.462 117.831 130.499 1.00 22.97  ? 689  LEU A C     1 
ATOM   5326  O  O     . LEU A 1 689 ? 135.928 118.937 130.623 1.00 39.25  ? 689  LEU A O     1 
ATOM   5327  C  CB    . LEU A 1 689 ? 138.104 117.573 132.371 1.00 25.72  ? 689  LEU A CB    1 
ATOM   5328  C  CG    . LEU A 1 689 ? 138.617 116.818 133.598 1.00 27.01  ? 689  LEU A CG    1 
ATOM   5329  C  CD1   . LEU A 1 689 ? 139.880 117.468 134.136 1.00 26.31  ? 689  LEU A CD1   1 
ATOM   5330  C  CD2   . LEU A 1 689 ? 137.548 116.748 134.670 1.00 21.11  ? 689  LEU A CD2   1 
ATOM   5331  N  N     . THR A 1 690 ? 136.742 117.301 129.306 1.00 24.34  ? 690  THR A N     1 
ATOM   5332  C  CA    . THR A 1 690 ? 136.327 117.976 128.081 1.00 17.49  ? 690  THR A CA    1 
ATOM   5333  C  C     . THR A 1 690 ? 134.816 117.913 127.891 1.00 21.48  ? 690  THR A C     1 
ATOM   5334  O  O     . THR A 1 690 ? 134.220 118.848 127.348 1.00 39.60  ? 690  THR A O     1 
ATOM   5335  C  CB    . THR A 1 690 ? 137.044 117.370 126.874 1.00 26.05  ? 690  THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 690 ? 136.620 116.015 126.690 1.00 24.33  ? 690  THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 690 ? 138.547 117.394 127.089 1.00 24.76  ? 690  THR A CG2   1 
ATOM   5338  N  N     . ASP A 1 691 ? 134.184 116.823 128.323 1.00 16.68  ? 691  ASP A N     1 
ATOM   5339  C  CA    . ASP A 1 691 ? 132.730 116.756 128.340 1.00 21.01  ? 691  ASP A CA    1 
ATOM   5340  C  C     . ASP A 1 691 ? 132.132 117.439 129.560 1.00 23.54  ? 691  ASP A C     1 
ATOM   5341  O  O     . ASP A 1 691 ? 130.969 117.852 129.516 1.00 28.96  ? 691  ASP A O     1 
ATOM   5342  C  CB    . ASP A 1 691 ? 132.272 115.299 128.293 1.00 29.45  ? 691  ASP A CB    1 
ATOM   5343  C  CG    . ASP A 1 691 ? 132.421 114.689 126.918 1.00 40.04  ? 691  ASP A CG    1 
ATOM   5344  O  OD1   . ASP A 1 691 ? 132.077 115.364 125.927 1.00 35.94  ? 691  ASP A OD1   1 
ATOM   5345  O  OD2   . ASP A 1 691 ? 132.881 113.534 126.827 1.00 34.16  ? 691  ASP A OD2   1 
ATOM   5346  N  N     . ILE A 1 692 ? 132.896 117.547 130.648 1.00 27.50  ? 692  ILE A N     1 
ATOM   5347  C  CA    . ILE A 1 692 ? 132.394 118.196 131.855 1.00 21.66  ? 692  ILE A CA    1 
ATOM   5348  C  C     . ILE A 1 692 ? 132.274 119.703 131.652 1.00 18.63  ? 692  ILE A C     1 
ATOM   5349  O  O     . ILE A 1 692 ? 131.278 120.317 132.052 1.00 26.50  ? 692  ILE A O     1 
ATOM   5350  C  CB    . ILE A 1 692 ? 133.298 117.849 133.052 1.00 16.93  ? 692  ILE A CB    1 
ATOM   5351  C  CG1   . ILE A 1 692 ? 133.142 116.375 133.426 1.00 19.71  ? 692  ILE A CG1   1 
ATOM   5352  C  CG2   . ILE A 1 692 ? 132.987 118.730 134.239 1.00 21.22  ? 692  ILE A CG2   1 
ATOM   5353  C  CD1   . ILE A 1 692 ? 131.731 115.985 133.782 1.00 24.40  ? 692  ILE A CD1   1 
ATOM   5354  N  N     . CYS A 1 693 ? 133.271 120.317 131.024 1.00 13.54  ? 693  CYS A N     1 
ATOM   5355  C  CA    . CYS A 1 693 ? 133.308 121.772 130.914 1.00 16.48  ? 693  CYS A CA    1 
ATOM   5356  C  C     . CYS A 1 693 ? 132.195 122.269 129.997 1.00 22.19  ? 693  CYS A C     1 
ATOM   5357  O  O     . CYS A 1 693 ? 132.003 121.717 128.908 1.00 38.53  ? 693  CYS A O     1 
ATOM   5358  C  CB    . CYS A 1 693 ? 134.666 122.232 130.393 1.00 14.04  ? 693  CYS A CB    1 
ATOM   5359  S  SG    . CYS A 1 693 ? 134.963 124.003 130.555 1.00 18.89  ? 693  CYS A SG    1 
ATOM   5360  N  N     . PRO A 1 694 ? 131.434 123.289 130.402 1.00 14.71  ? 694  PRO A N     1 
ATOM   5361  C  CA    . PRO A 1 694 ? 130.351 123.795 129.554 1.00 23.20  ? 694  PRO A CA    1 
ATOM   5362  C  C     . PRO A 1 694 ? 130.730 124.932 128.619 1.00 18.16  ? 694  PRO A C     1 
ATOM   5363  O  O     . PRO A 1 694 ? 129.964 125.213 127.688 1.00 16.26  ? 694  PRO A O     1 
ATOM   5364  C  CB    . PRO A 1 694 ? 129.329 124.275 130.592 1.00 16.46  ? 694  PRO A CB    1 
ATOM   5365  C  CG    . PRO A 1 694 ? 130.182 124.783 131.704 1.00 20.34  ? 694  PRO A CG    1 
ATOM   5366  C  CD    . PRO A 1 694 ? 131.411 123.902 131.742 1.00 15.99  ? 694  PRO A CD    1 
ATOM   5367  N  N     . VAL A 1 695 ? 131.871 125.587 128.823 1.00 22.33  ? 695  VAL A N     1 
ATOM   5368  C  CA    . VAL A 1 695 ? 132.186 126.810 128.092 1.00 17.16  ? 695  VAL A CA    1 
ATOM   5369  C  C     . VAL A 1 695 ? 133.541 126.724 127.404 1.00 18.90  ? 695  VAL A C     1 
ATOM   5370  O  O     . VAL A 1 695 ? 134.231 127.736 127.256 1.00 34.93  ? 695  VAL A O     1 
ATOM   5371  C  CB    . VAL A 1 695 ? 132.138 128.035 129.022 1.00 12.27  ? 695  VAL A CB    1 
ATOM   5372  C  CG1   . VAL A 1 695 ? 130.710 128.331 129.432 1.00 15.16  ? 695  VAL A CG1   1 
ATOM   5373  C  CG2   . VAL A 1 695 ? 133.005 127.800 130.235 1.00 22.88  ? 695  VAL A CG2   1 
ATOM   5374  N  N     . GLY A 1 696 ? 133.948 125.524 127.006 1.00 9.39   ? 696  GLY A N     1 
ATOM   5375  C  CA    . GLY A 1 696 ? 135.135 125.388 126.176 1.00 24.59  ? 696  GLY A CA    1 
ATOM   5376  C  C     . GLY A 1 696 ? 136.433 125.839 126.809 1.00 26.95  ? 696  GLY A C     1 
ATOM   5377  O  O     . GLY A 1 696 ? 137.300 126.374 126.111 1.00 21.67  ? 696  GLY A O     1 
ATOM   5378  N  N     . ALA A 1 697 ? 136.593 125.639 128.114 1.00 27.19  ? 697  ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 697 ? 137.877 125.893 128.754 1.00 15.95  ? 697  ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 697 ? 138.779 124.667 128.712 1.00 19.55  ? 697  ALA A C     1 
ATOM   5381  O  O     . ALA A 1 697 ? 139.993 124.795 128.528 1.00 25.53  ? 697  ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 697 ? 137.668 126.346 130.199 1.00 19.85  ? 697  ALA A CB    1 
ATOM   5383  N  N     . ILE A 1 698 ? 138.203 123.479 128.874 1.00 29.19  ? 698  ILE A N     1 
ATOM   5384  C  CA    . ILE A 1 698 ? 138.913 122.216 128.716 1.00 20.85  ? 698  ILE A CA    1 
ATOM   5385  C  C     . ILE A 1 698 ? 138.442 121.597 127.409 1.00 23.72  ? 698  ILE A C     1 
ATOM   5386  O  O     . ILE A 1 698 ? 137.266 121.240 127.272 1.00 30.96  ? 698  ILE A O     1 
ATOM   5387  C  CB    . ILE A 1 698 ? 138.660 121.268 129.897 1.00 20.85  ? 698  ILE A CB    1 
ATOM   5388  C  CG1   . ILE A 1 698 ? 138.716 122.032 131.217 1.00 29.01  ? 698  ILE A CG1   1 
ATOM   5389  C  CG2   . ILE A 1 698 ? 139.678 120.145 129.904 1.00 26.80  ? 698  ILE A CG2   1 
ATOM   5390  C  CD1   . ILE A 1 698 ? 138.367 121.194 132.415 1.00 15.36  ? 698  ILE A CD1   1 
ATOM   5391  N  N     . THR A 1 699 ? 139.353 121.470 126.450 1.00 23.65  ? 699  THR A N     1 
ATOM   5392  C  CA    . THR A 1 699 ? 139.027 120.955 125.130 1.00 23.05  ? 699  THR A CA    1 
ATOM   5393  C  C     . THR A 1 699 ? 139.963 119.808 124.778 1.00 24.86  ? 699  THR A C     1 
ATOM   5394  O  O     . THR A 1 699 ? 140.987 119.585 125.426 1.00 37.94  ? 699  THR A O     1 
ATOM   5395  C  CB    . THR A 1 699 ? 139.107 122.051 124.059 1.00 34.83  ? 699  THR A CB    1 
ATOM   5396  O  OG1   . THR A 1 699 ? 140.336 122.771 124.200 1.00 39.30  ? 699  THR A OG1   1 
ATOM   5397  C  CG2   . THR A 1 699 ? 137.945 123.011 124.193 1.00 24.11  ? 699  THR A CG2   1 
ATOM   5398  N  N     . GLU A 1 700 ? 139.597 119.081 123.728 1.00 28.41  ? 700  GLU A N     1 
ATOM   5399  C  CA    . GLU A 1 700 ? 140.324 117.902 123.285 1.00 26.19  ? 700  GLU A CA    1 
ATOM   5400  C  C     . GLU A 1 700 ? 141.080 118.201 121.998 1.00 22.93  ? 700  GLU A C     1 
ATOM   5401  O  O     . GLU A 1 700 ? 140.552 118.851 121.091 1.00 26.97  ? 700  GLU A O     1 
ATOM   5402  C  CB    . GLU A 1 700 ? 139.372 116.724 123.064 1.00 23.72  ? 700  GLU A CB    1 
ATOM   5403  C  CG    . GLU A 1 700 ? 140.070 115.437 122.670 1.00 30.34  ? 700  GLU A CG    1 
ATOM   5404  C  CD    . GLU A 1 700 ? 139.103 114.324 122.337 1.00 36.11  ? 700  GLU A CD    1 
ATOM   5405  O  OE1   . GLU A 1 700 ? 137.908 114.454 122.669 1.00 34.16  ? 700  GLU A OE1   1 
ATOM   5406  O  OE2   . GLU A 1 700 ? 139.538 113.318 121.739 1.00 31.34  ? 700  GLU A OE2   1 
ATOM   5407  N  N     . LYS A 1 701 ? 142.321 117.727 121.927 1.00 29.07  ? 701  LYS A N     1 
ATOM   5408  C  CA    . LYS A 1 701 ? 143.119 117.829 120.711 1.00 30.12  ? 701  LYS A CA    1 
ATOM   5409  C  C     . LYS A 1 701 ? 142.641 116.773 119.725 1.00 39.72  ? 701  LYS A C     1 
ATOM   5410  O  O     . LYS A 1 701 ? 142.863 115.577 119.932 1.00 40.42  ? 701  LYS A O     1 
ATOM   5411  C  CB    . LYS A 1 701 ? 144.601 117.641 121.014 1.00 33.55  ? 701  LYS A CB    1 
ATOM   5412  C  CG    . LYS A 1 701 ? 145.246 118.770 121.777 1.00 33.44  ? 701  LYS A CG    1 
ATOM   5413  C  CD    . LYS A 1 701 ? 146.693 118.437 122.078 1.00 35.10  ? 701  LYS A CD    1 
ATOM   5414  C  CE    . LYS A 1 701 ? 147.366 119.532 122.869 1.00 37.99  ? 701  LYS A CE    1 
ATOM   5415  N  NZ    . LYS A 1 701 ? 148.746 119.145 123.249 1.00 42.45  ? 701  LYS A NZ    1 
ATOM   5416  N  N     . LEU A 1 702 ? 141.981 117.210 118.658 1.00 24.58  ? 702  LEU A N     1 
ATOM   5417  C  CA    . LEU A 1 702 ? 141.582 116.287 117.613 1.00 18.23  ? 702  LEU A CA    1 
ATOM   5418  C  C     . LEU A 1 702 ? 142.805 115.853 116.806 1.00 26.09  ? 702  LEU A C     1 
ATOM   5419  O  O     . LEU A 1 702 ? 143.740 116.633 116.615 1.00 25.99  ? 702  LEU A O     1 
ATOM   5420  C  CB    . LEU A 1 702 ? 140.541 116.927 116.697 1.00 28.12  ? 702  LEU A CB    1 
ATOM   5421  C  CG    . LEU A 1 702 ? 139.145 117.175 117.278 1.00 28.19  ? 702  LEU A CG    1 
ATOM   5422  C  CD1   . LEU A 1 702 ? 138.744 116.057 118.225 1.00 22.25  ? 702  LEU A CD1   1 
ATOM   5423  C  CD2   . LEU A 1 702 ? 139.053 118.529 117.964 1.00 29.88  ? 702  LEU A CD2   1 
ATOM   5424  N  N     . PRO A 1 703 ? 142.822 114.608 116.320 1.00 34.73  ? 703  PRO A N     1 
ATOM   5425  C  CA    . PRO A 1 703 ? 144.025 114.095 115.643 1.00 29.73  ? 703  PRO A CA    1 
ATOM   5426  C  C     . PRO A 1 703 ? 144.265 114.673 114.256 1.00 34.18  ? 703  PRO A C     1 
ATOM   5427  O  O     . PRO A 1 703 ? 145.330 114.413 113.683 1.00 34.09  ? 703  PRO A O     1 
ATOM   5428  C  CB    . PRO A 1 703 ? 143.763 112.587 115.570 1.00 25.55  ? 703  PRO A CB    1 
ATOM   5429  C  CG    . PRO A 1 703 ? 142.279 112.474 115.557 1.00 27.81  ? 703  PRO A CG    1 
ATOM   5430  C  CD    . PRO A 1 703 ? 141.774 113.578 116.437 1.00 30.67  ? 703  PRO A CD    1 
ATOM   5431  N  N     . PHE A 1 704 ? 143.328 115.432 113.698 1.00 31.73  ? 704  PHE A N     1 
ATOM   5432  C  CA    . PHE A 1 704 ? 143.474 115.928 112.339 1.00 29.42  ? 704  PHE A CA    1 
ATOM   5433  C  C     . PHE A 1 704 ? 144.490 117.065 112.286 1.00 33.82  ? 704  PHE A C     1 
ATOM   5434  O  O     . PHE A 1 704 ? 144.885 117.636 113.305 1.00 36.35  ? 704  PHE A O     1 
ATOM   5435  C  CB    . PHE A 1 704 ? 142.129 116.399 111.795 1.00 29.00  ? 704  PHE A CB    1 
ATOM   5436  C  CG    . PHE A 1 704 ? 140.989 115.513 112.171 1.00 28.22  ? 704  PHE A CG    1 
ATOM   5437  C  CD1   . PHE A 1 704 ? 140.765 114.331 111.493 1.00 28.94  ? 704  PHE A CD1   1 
ATOM   5438  C  CD2   . PHE A 1 704 ? 140.145 115.855 113.211 1.00 25.28  ? 704  PHE A CD2   1 
ATOM   5439  C  CE1   . PHE A 1 704 ? 139.722 113.510 111.839 1.00 35.84  ? 704  PHE A CE1   1 
ATOM   5440  C  CE2   . PHE A 1 704 ? 139.101 115.035 113.561 1.00 28.41  ? 704  PHE A CE2   1 
ATOM   5441  C  CZ    . PHE A 1 704 ? 138.891 113.862 112.875 1.00 35.13  ? 704  PHE A CZ    1 
ATOM   5442  N  N     . VAL A 1 705 ? 144.922 117.385 111.064 1.00 33.56  ? 705  VAL A N     1 
ATOM   5443  C  CA    . VAL A 1 705 ? 145.873 118.476 110.873 1.00 27.91  ? 705  VAL A CA    1 
ATOM   5444  C  C     . VAL A 1 705 ? 145.241 119.804 111.268 1.00 23.66  ? 705  VAL A C     1 
ATOM   5445  O  O     . VAL A 1 705 ? 145.828 120.595 112.015 1.00 23.95  ? 705  VAL A O     1 
ATOM   5446  C  CB    . VAL A 1 705 ? 146.381 118.499 109.421 1.00 26.95  ? 705  VAL A CB    1 
ATOM   5447  C  CG1   . VAL A 1 705 ? 147.584 117.584 109.272 1.00 22.14  ? 705  VAL A CG1   1 
ATOM   5448  C  CG2   . VAL A 1 705 ? 145.280 118.070 108.467 1.00 26.73  ? 705  VAL A CG2   1 
ATOM   5449  N  N     . LYS A 1 706 ? 144.034 120.060 110.782 1.00 24.78  ? 706  LYS A N     1 
ATOM   5450  C  CA    . LYS A 1 706 ? 143.280 121.260 111.139 1.00 29.74  ? 706  LYS A CA    1 
ATOM   5451  C  C     . LYS A 1 706 ? 141.969 120.834 111.777 1.00 21.71  ? 706  LYS A C     1 
ATOM   5452  O  O     . LYS A 1 706 ? 141.117 120.233 111.095 1.00 30.50  ? 706  LYS A O     1 
ATOM   5453  C  CB    . LYS A 1 706 ? 143.026 122.136 109.914 1.00 26.02  ? 706  LYS A CB    1 
ATOM   5454  C  CG    . LYS A 1 706 ? 143.752 123.469 109.932 1.00 22.96  ? 706  LYS A CG    1 
ATOM   5455  C  CD    . LYS A 1 706 ? 145.228 123.312 109.630 1.00 10.72  ? 706  LYS A CD    1 
ATOM   5456  C  CE    . LYS A 1 706 ? 146.076 123.715 110.819 1.00 14.74  ? 706  LYS A CE    1 
ATOM   5457  N  NZ    . LYS A 1 706 ? 145.757 125.088 111.273 1.00 30.00  ? 706  LYS A NZ    1 
ATOM   5458  N  N     . PRO A 1 707 ? 141.759 121.102 113.063 1.00 12.68  ? 707  PRO A N     1 
ATOM   5459  C  CA    . PRO A 1 707 ? 140.547 120.637 113.748 1.00 16.89  ? 707  PRO A CA    1 
ATOM   5460  C  C     . PRO A 1 707 ? 139.347 121.564 113.641 1.00 26.39  ? 707  PRO A C     1 
ATOM   5461  O  O     . PRO A 1 707 ? 138.394 121.364 114.399 1.00 24.14  ? 707  PRO A O     1 
ATOM   5462  C  CB    . PRO A 1 707 ? 141.020 120.560 115.203 1.00 24.11  ? 707  PRO A CB    1 
ATOM   5463  C  CG    . PRO A 1 707 ? 141.962 121.709 115.312 1.00 22.53  ? 707  PRO A CG    1 
ATOM   5464  C  CD    . PRO A 1 707 ? 142.676 121.793 113.985 1.00 26.25  ? 707  PRO A CD    1 
ATOM   5465  N  N     . GLY A 1 708 ? 139.386 122.550 112.734 1.00 30.00  ? 708  GLY A N     1 
ATOM   5466  C  CA    . GLY A 1 708 ? 138.408 123.615 112.641 1.00 30.00  ? 708  GLY A CA    1 
ATOM   5467  C  C     . GLY A 1 708 ? 136.993 123.149 112.884 1.00 30.00  ? 708  GLY A C     1 
ATOM   5468  O  O     . GLY A 1 708 ? 136.515 122.205 112.251 1.00 30.00  ? 708  GLY A O     1 
ATOM   5469  N  N     . PRO A 1 709 ? 136.312 123.781 113.840 1.00 22.16  ? 709  PRO A N     1 
ATOM   5470  C  CA    . PRO A 1 709 ? 135.073 123.203 114.371 1.00 23.09  ? 709  PRO A CA    1 
ATOM   5471  C  C     . PRO A 1 709 ? 134.027 122.988 113.290 1.00 21.69  ? 709  PRO A C     1 
ATOM   5472  O  O     . PRO A 1 709 ? 133.811 123.837 112.424 1.00 24.62  ? 709  PRO A O     1 
ATOM   5473  C  CB    . PRO A 1 709 ? 134.611 124.241 115.400 1.00 11.69  ? 709  PRO A CB    1 
ATOM   5474  C  CG    . PRO A 1 709 ? 135.838 124.983 115.764 1.00 21.11  ? 709  PRO A CG    1 
ATOM   5475  C  CD    . PRO A 1 709 ? 136.675 125.028 114.528 1.00 21.60  ? 709  PRO A CD    1 
ATOM   5476  N  N     . TRP A 1 710 ? 133.386 121.828 113.351 1.00 17.49  ? 710  TRP A N     1 
ATOM   5477  C  CA    . TRP A 1 710 ? 132.322 121.459 112.438 1.00 22.59  ? 710  TRP A CA    1 
ATOM   5478  C  C     . TRP A 1 710 ? 131.083 121.103 113.247 1.00 18.87  ? 710  TRP A C     1 
ATOM   5479  O  O     . TRP A 1 710 ? 131.180 120.629 114.381 1.00 17.56  ? 710  TRP A O     1 
ATOM   5480  C  CB    . TRP A 1 710 ? 132.736 120.280 111.544 1.00 23.77  ? 710  TRP A CB    1 
ATOM   5481  C  CG    . TRP A 1 710 ? 134.058 120.462 110.846 1.00 26.38  ? 710  TRP A CG    1 
ATOM   5482  C  CD1   . TRP A 1 710 ? 134.389 121.444 109.960 1.00 26.95  ? 710  TRP A CD1   1 
ATOM   5483  C  CD2   . TRP A 1 710 ? 135.215 119.623 110.962 1.00 31.68  ? 710  TRP A CD2   1 
ATOM   5484  N  NE1   . TRP A 1 710 ? 135.682 121.278 109.528 1.00 17.26  ? 710  TRP A NE1   1 
ATOM   5485  C  CE2   . TRP A 1 710 ? 136.209 120.165 110.125 1.00 24.05  ? 710  TRP A CE2   1 
ATOM   5486  C  CE3   . TRP A 1 710 ? 135.507 118.471 111.696 1.00 30.76  ? 710  TRP A CE3   1 
ATOM   5487  C  CZ2   . TRP A 1 710 ? 137.473 119.597 110.008 1.00 23.99  ? 710  TRP A CZ2   1 
ATOM   5488  C  CZ3   . TRP A 1 710 ? 136.760 117.909 111.575 1.00 26.09  ? 710  TRP A CZ3   1 
ATOM   5489  C  CH2   . TRP A 1 710 ? 137.727 118.471 110.737 1.00 21.29  ? 710  TRP A CH2   1 
ATOM   5490  N  N     . LYS A 1 711 ? 129.912 121.353 112.662 1.00 23.11  ? 711  LYS A N     1 
ATOM   5491  C  CA    . LYS A 1 711 ? 128.642 121.062 113.326 1.00 26.85  ? 711  LYS A CA    1 
ATOM   5492  C  C     . LYS A 1 711 ? 128.420 119.553 113.282 1.00 33.04  ? 711  LYS A C     1 
ATOM   5493  O  O     . LYS A 1 711 ? 127.726 119.009 112.419 1.00 35.31  ? 711  LYS A O     1 
ATOM   5494  C  CB    . LYS A 1 711 ? 127.501 121.825 112.666 1.00 20.70  ? 711  LYS A CB    1 
ATOM   5495  C  CG    . LYS A 1 711 ? 126.176 121.714 113.398 1.00 28.65  ? 711  LYS A CG    1 
ATOM   5496  C  CD    . LYS A 1 711 ? 125.071 122.426 112.646 1.00 29.27  ? 711  LYS A CD    1 
ATOM   5497  C  CE    . LYS A 1 711 ? 125.380 123.902 112.482 1.00 31.36  ? 711  LYS A CE    1 
ATOM   5498  N  NZ    . LYS A 1 711 ? 125.508 124.589 113.796 1.00 32.38  ? 711  LYS A NZ    1 
ATOM   5499  N  N     . THR A 1 712 ? 129.033 118.866 114.241 1.00 22.98  ? 712  THR A N     1 
ATOM   5500  C  CA    . THR A 1 712 ? 129.024 117.414 114.264 1.00 19.40  ? 712  THR A CA    1 
ATOM   5501  C  C     . THR A 1 712 ? 127.717 116.879 114.842 1.00 19.57  ? 712  THR A C     1 
ATOM   5502  O  O     . THR A 1 712 ? 126.987 117.571 115.555 1.00 12.40  ? 712  THR A O     1 
ATOM   5503  C  CB    . THR A 1 712 ? 130.202 116.882 115.079 1.00 20.74  ? 712  THR A CB    1 
ATOM   5504  O  OG1   . THR A 1 712 ? 130.134 117.399 116.412 1.00 28.04  ? 712  THR A OG1   1 
ATOM   5505  C  CG2   . THR A 1 712 ? 131.515 117.302 114.449 1.00 16.96  ? 712  THR A CG2   1 
ATOM   5506  N  N     . GLN A 1 713 ? 127.431 115.622 114.515 1.00 24.10  ? 713  GLN A N     1 
ATOM   5507  C  CA    . GLN A 1 713 ? 126.273 114.907 115.031 1.00 24.21  ? 713  GLN A CA    1 
ATOM   5508  C  C     . GLN A 1 713 ? 126.747 113.713 115.846 1.00 27.65  ? 713  GLN A C     1 
ATOM   5509  O  O     . GLN A 1 713 ? 127.523 112.890 115.333 1.00 36.21  ? 713  GLN A O     1 
ATOM   5510  C  CB    . GLN A 1 713 ? 125.359 114.446 113.894 1.00 25.09  ? 713  GLN A CB    1 
ATOM   5511  C  CG    . GLN A 1 713 ? 124.623 115.569 113.194 1.00 29.50  ? 713  GLN A CG    1 
ATOM   5512  C  CD    . GLN A 1 713 ? 123.623 116.258 114.098 1.00 37.26  ? 713  GLN A CD    1 
ATOM   5513  O  OE1   . GLN A 1 713 ? 123.083 115.652 115.022 1.00 30.08  ? 713  GLN A OE1   1 
ATOM   5514  N  NE2   . GLN A 1 713 ? 123.373 117.535 113.837 1.00 33.61  ? 713  GLN A NE2   1 
ATOM   5515  N  N     . PRO A 1 714 ? 126.337 113.579 117.101 1.00 24.72  ? 714  PRO A N     1 
ATOM   5516  C  CA    . PRO A 1 714 ? 126.715 112.398 117.877 1.00 28.99  ? 714  PRO A CA    1 
ATOM   5517  C  C     . PRO A 1 714 ? 125.871 111.184 117.524 1.00 29.68  ? 714  PRO A C     1 
ATOM   5518  O  O     . PRO A 1 714 ? 124.681 111.284 117.217 1.00 32.28  ? 714  PRO A O     1 
ATOM   5519  C  CB    . PRO A 1 714 ? 126.469 112.841 119.324 1.00 30.93  ? 714  PRO A CB    1 
ATOM   5520  C  CG    . PRO A 1 714 ? 125.402 113.864 119.216 1.00 29.73  ? 714  PRO A CG    1 
ATOM   5521  C  CD    . PRO A 1 714 ? 125.647 114.586 117.925 1.00 27.26  ? 714  PRO A CD    1 
ATOM   5522  N  N     . VAL A 1 715 ? 126.513 110.020 117.577 1.00 29.97  ? 715  VAL A N     1 
ATOM   5523  C  CA    . VAL A 1 715 ? 125.872 108.740 117.308 1.00 33.28  ? 715  VAL A CA    1 
ATOM   5524  C  C     . VAL A 1 715 ? 126.060 107.846 118.528 1.00 37.65  ? 715  VAL A C     1 
ATOM   5525  O  O     . VAL A 1 715 ? 127.115 107.872 119.171 1.00 35.65  ? 715  VAL A O     1 
ATOM   5526  C  CB    . VAL A 1 715 ? 126.434 108.082 116.027 1.00 31.10  ? 715  VAL A CB    1 
ATOM   5527  C  CG1   . VAL A 1 715 ? 127.943 107.975 116.087 1.00 31.01  ? 715  VAL A CG1   1 
ATOM   5528  C  CG2   . VAL A 1 715 ? 125.808 106.717 115.788 1.00 36.69  ? 715  VAL A CG2   1 
ATOM   5529  N  N     . LYS A 1 716 ? 125.024 107.079 118.862 1.00 44.16  ? 716  LYS A N     1 
ATOM   5530  C  CA    . LYS A 1 716 ? 125.009 106.256 120.065 1.00 44.73  ? 716  LYS A CA    1 
ATOM   5531  C  C     . LYS A 1 716 ? 125.647 104.901 119.783 1.00 42.69  ? 716  LYS A C     1 
ATOM   5532  O  O     . LYS A 1 716 ? 125.117 104.112 118.995 1.00 44.76  ? 716  LYS A O     1 
ATOM   5533  C  CB    . LYS A 1 716 ? 123.578 106.075 120.566 1.00 43.79  ? 716  LYS A CB    1 
ATOM   5534  C  CG    . LYS A 1 716 ? 122.851 107.376 120.843 1.00 46.95  ? 716  LYS A CG    1 
ATOM   5535  C  CD    . LYS A 1 716 ? 121.394 107.126 121.184 1.00 45.82  ? 716  LYS A CD    1 
ATOM   5536  C  CE    . LYS A 1 716 ? 120.675 106.439 120.037 1.00 44.45  ? 716  LYS A CE    1 
ATOM   5537  N  NZ    . LYS A 1 716 ? 119.244 106.182 120.354 1.00 38.87  ? 716  LYS A NZ    1 
ATOM   5538  N  N     . THR A 1 717 ? 126.770 104.628 120.439 1.00 49.00  ? 717  THR A N     1 
ATOM   5539  C  CA    . THR A 1 717 ? 127.484 103.367 120.283 1.00 50.07  ? 717  THR A CA    1 
ATOM   5540  C  C     . THR A 1 717 ? 128.146 103.024 121.615 1.00 53.72  ? 717  THR A C     1 
ATOM   5541  O  O     . THR A 1 717 ? 127.930 103.699 122.626 1.00 60.71  ? 717  THR A O     1 
ATOM   5542  C  CB    . THR A 1 717 ? 128.498 103.460 119.137 1.00 48.69  ? 717  THR A CB    1 
ATOM   5543  O  OG1   . THR A 1 717 ? 129.264 102.252 119.072 1.00 53.08  ? 717  THR A OG1   1 
ATOM   5544  C  CG2   . THR A 1 717 ? 129.432 104.628 119.357 1.00 47.71  ? 717  THR A CG2   1 
ATOM   5545  N  N     . VAL A 1 718 ? 128.960 101.966 121.617 1.00 45.32  ? 718  VAL A N     1 
ATOM   5546  C  CA    . VAL A 1 718 ? 129.663 101.525 122.814 1.00 37.47  ? 718  VAL A CA    1 
ATOM   5547  C  C     . VAL A 1 718 ? 131.151 101.420 122.505 1.00 41.27  ? 718  VAL A C     1 
ATOM   5548  O  O     . VAL A 1 718 ? 131.572 101.382 121.347 1.00 52.17  ? 718  VAL A O     1 
ATOM   5549  C  CB    . VAL A 1 718 ? 129.139 100.173 123.352 1.00 41.49  ? 718  VAL A CB    1 
ATOM   5550  C  CG1   . VAL A 1 718 ? 127.627 100.189 123.472 1.00 48.37  ? 718  VAL A CG1   1 
ATOM   5551  C  CG2   . VAL A 1 718 ? 129.604 99.029  122.469 1.00 42.26  ? 718  VAL A CG2   1 
ATOM   5552  N  N     . CYS A 1 719 ? 131.947 101.380 123.567 1.00 53.95  ? 719  CYS A N     1 
ATOM   5553  C  CA    . CYS A 1 719 ? 133.388 101.220 123.455 1.00 55.77  ? 719  CYS A CA    1 
ATOM   5554  C  C     . CYS A 1 719 ? 133.767 99.742  123.423 1.00 60.19  ? 719  CYS A C     1 
ATOM   5555  O  O     . CYS A 1 719 ? 133.014 98.870  123.862 1.00 63.54  ? 719  CYS A O     1 
ATOM   5556  C  CB    . CYS A 1 719 ? 134.099 101.916 124.615 1.00 56.64  ? 719  CYS A CB    1 
ATOM   5557  S  SG    . CYS A 1 719 ? 135.848 101.495 124.771 1.00 72.35  ? 719  CYS A SG    1 
ATOM   5558  N  N     . ASN A 1 720 ? 134.959 99.470  122.893 1.00 60.60  ? 720  ASN A N     1 
ATOM   5559  C  CA    . ASN A 1 720 ? 135.481 98.111  122.803 1.00 57.44  ? 720  ASN A CA    1 
ATOM   5560  C  C     . ASN A 1 720 ? 136.831 97.969  123.494 1.00 63.04  ? 720  ASN A C     1 
ATOM   5561  O  O     . ASN A 1 720 ? 137.570 97.020  123.213 1.00 67.84  ? 720  ASN A O     1 
ATOM   5562  C  CB    . ASN A 1 720 ? 135.586 97.671  121.342 1.00 62.28  ? 720  ASN A CB    1 
ATOM   5563  C  CG    . ASN A 1 720 ? 136.583 98.494  120.557 1.00 63.45  ? 720  ASN A CG    1 
ATOM   5564  O  OD1   . ASN A 1 720 ? 136.737 99.692  120.790 1.00 63.14  ? 720  ASN A OD1   1 
ATOM   5565  N  ND2   . ASN A 1 720 ? 137.270 97.852  119.620 1.00 60.24  ? 720  ASN A ND2   1 
ATOM   5566  N  N     . GLY A 1 721 ? 137.174 98.900  124.386 1.00 68.90  ? 721  GLY A N     1 
ATOM   5567  C  CA    . GLY A 1 721 ? 138.451 98.814  125.075 1.00 67.84  ? 721  GLY A CA    1 
ATOM   5568  C  C     . GLY A 1 721 ? 138.538 97.620  126.005 1.00 70.98  ? 721  GLY A C     1 
ATOM   5569  O  O     . GLY A 1 721 ? 139.570 96.947  126.070 1.00 72.96  ? 721  GLY A O     1 
ATOM   5570  N  N     . CYS A 1 722 ? 137.463 97.339  126.734 1.00 71.90  ? 722  CYS A N     1 
ATOM   5571  C  CA    . CYS A 1 722 ? 137.411 96.188  127.624 1.00 75.29  ? 722  CYS A CA    1 
ATOM   5572  C  C     . CYS A 1 722 ? 135.981 95.659  127.637 1.00 74.40  ? 722  CYS A C     1 
ATOM   5573  O  O     . CYS A 1 722 ? 135.149 96.049  126.813 1.00 75.45  ? 722  CYS A O     1 
ATOM   5574  C  CB    . CYS A 1 722 ? 137.918 96.558  129.024 1.00 77.45  ? 722  CYS A CB    1 
ATOM   5575  S  SG    . CYS A 1 722 ? 137.016 97.893  129.830 1.00 74.54  ? 722  CYS A SG    1 
ATOM   5576  N  N     . SER A 1 723 ? 135.694 94.762  128.580 1.00 73.91  ? 723  SER A N     1 
ATOM   5577  C  CA    . SER A 1 723 ? 134.392 94.112  128.630 1.00 71.83  ? 723  SER A CA    1 
ATOM   5578  C  C     . SER A 1 723 ? 133.308 94.987  129.242 1.00 70.78  ? 723  SER A C     1 
ATOM   5579  O  O     . SER A 1 723 ? 132.137 94.597  129.213 1.00 71.91  ? 723  SER A O     1 
ATOM   5580  C  CB    . SER A 1 723 ? 134.490 92.798  129.408 1.00 72.39  ? 723  SER A CB    1 
ATOM   5581  O  OG    . SER A 1 723 ? 133.280 92.069  129.328 1.00 72.22  ? 723  SER A OG    1 
ATOM   5582  N  N     . PHE A 1 724 ? 133.667 96.146  129.799 1.00 69.77  ? 724  PHE A N     1 
ATOM   5583  C  CA    . PHE A 1 724 ? 132.654 97.056  130.323 1.00 71.29  ? 724  PHE A CA    1 
ATOM   5584  C  C     . PHE A 1 724 ? 131.749 97.574  129.214 1.00 71.34  ? 724  PHE A C     1 
ATOM   5585  O  O     . PHE A 1 724 ? 130.540 97.733  129.416 1.00 68.23  ? 724  PHE A O     1 
ATOM   5586  C  CB    . PHE A 1 724 ? 133.317 98.220  131.057 1.00 69.27  ? 724  PHE A CB    1 
ATOM   5587  C  CG    . PHE A 1 724 ? 133.729 97.898  132.463 1.00 70.26  ? 724  PHE A CG    1 
ATOM   5588  C  CD1   . PHE A 1 724 ? 132.779 97.704  133.446 1.00 68.78  ? 724  PHE A CD1   1 
ATOM   5589  C  CD2   . PHE A 1 724 ? 135.067 97.811  132.805 1.00 71.40  ? 724  PHE A CD2   1 
ATOM   5590  C  CE1   . PHE A 1 724 ? 133.153 97.417  134.739 1.00 70.04  ? 724  PHE A CE1   1 
ATOM   5591  C  CE2   . PHE A 1 724 ? 135.445 97.525  134.098 1.00 68.83  ? 724  PHE A CE2   1 
ATOM   5592  C  CZ    . PHE A 1 724 ? 134.488 97.327  135.065 1.00 69.77  ? 724  PHE A CZ    1 
ATOM   5593  N  N     . ALA A 1 725 ? 132.323 97.856  128.043 1.00 69.42  ? 725  ALA A N     1 
ATOM   5594  C  CA    . ALA A 1 725 ? 131.594 98.345  126.873 1.00 64.04  ? 725  ALA A CA    1 
ATOM   5595  C  C     . ALA A 1 725 ? 130.789 99.599  127.213 1.00 62.98  ? 725  ALA A C     1 
ATOM   5596  O  O     . ALA A 1 725 ? 129.562 99.639  127.104 1.00 67.23  ? 725  ALA A O     1 
ATOM   5597  C  CB    . ALA A 1 725 ? 130.696 97.251  126.289 1.00 66.05  ? 725  ALA A CB    1 
ATOM   5598  N  N     . CYS A 1 726 ? 131.512 100.630 127.640 1.00 49.54  ? 726  CYS A N     1 
ATOM   5599  C  CA    . CYS A 1 726 ? 130.876 101.868 128.066 1.00 48.71  ? 726  CYS A CA    1 
ATOM   5600  C  C     . CYS A 1 726 ? 130.183 102.556 126.898 1.00 54.64  ? 726  CYS A C     1 
ATOM   5601  O  O     . CYS A 1 726 ? 130.734 102.660 125.798 1.00 55.96  ? 726  CYS A O     1 
ATOM   5602  C  CB    . CYS A 1 726 ? 131.910 102.807 128.686 1.00 48.78  ? 726  CYS A CB    1 
ATOM   5603  S  SG    . CYS A 1 726 ? 132.575 102.240 130.263 1.00 60.93  ? 726  CYS A SG    1 
ATOM   5604  N  N     . GLU A 1 727 ? 128.962 103.021 127.142 1.00 52.37  ? 727  GLU A N     1 
ATOM   5605  C  CA    . GLU A 1 727 ? 128.232 103.772 126.133 1.00 45.98  ? 727  GLU A CA    1 
ATOM   5606  C  C     . GLU A 1 727 ? 128.887 105.128 125.908 1.00 44.92  ? 727  GLU A C     1 
ATOM   5607  O  O     . GLU A 1 727 ? 129.324 105.790 126.853 1.00 44.65  ? 727  GLU A O     1 
ATOM   5608  C  CB    . GLU A 1 727 ? 126.776 103.957 126.553 1.00 43.86  ? 727  GLU A CB    1 
ATOM   5609  C  CG    . GLU A 1 727 ? 126.016 102.666 126.775 1.00 45.07  ? 727  GLU A CG    1 
ATOM   5610  C  CD    . GLU A 1 727 ? 124.566 102.906 127.137 1.00 50.63  ? 727  GLU A CD    1 
ATOM   5611  O  OE1   . GLU A 1 727 ? 124.104 104.057 127.008 1.00 56.36  ? 727  GLU A OE1   1 
ATOM   5612  O  OE2   . GLU A 1 727 ? 123.886 101.948 127.553 1.00 47.57  ? 727  GLU A OE2   1 
ATOM   5613  N  N     . MET A 1 728 ? 128.953 105.542 124.646 1.00 34.29  ? 728  MET A N     1 
ATOM   5614  C  CA    . MET A 1 728 ? 129.585 106.804 124.302 1.00 32.55  ? 728  MET A CA    1 
ATOM   5615  C  C     . MET A 1 728 ? 128.972 107.340 123.018 1.00 39.22  ? 728  MET A C     1 
ATOM   5616  O  O     . MET A 1 728 ? 128.322 106.614 122.264 1.00 36.73  ? 728  MET A O     1 
ATOM   5617  C  CB    . MET A 1 728 ? 131.099 106.649 124.135 1.00 36.66  ? 728  MET A CB    1 
ATOM   5618  C  CG    . MET A 1 728 ? 131.490 105.807 122.939 1.00 38.87  ? 728  MET A CG    1 
ATOM   5619  S  SD    . MET A 1 728 ? 133.260 105.816 122.622 1.00 41.86  ? 728  MET A SD    1 
ATOM   5620  C  CE    . MET A 1 728 ? 133.321 104.852 121.117 1.00 37.75  ? 728  MET A CE    1 
ATOM   5621  N  N     . ASN A 1 729 ? 129.186 108.630 122.787 1.00 43.38  ? 729  ASN A N     1 
ATOM   5622  C  CA    . ASN A 1 729 ? 128.795 109.294 121.554 1.00 32.21  ? 729  ASN A CA    1 
ATOM   5623  C  C     . ASN A 1 729 ? 130.035 109.545 120.710 1.00 34.60  ? 729  ASN A C     1 
ATOM   5624  O  O     . ASN A 1 729 ? 131.001 110.148 121.185 1.00 37.60  ? 729  ASN A O     1 
ATOM   5625  C  CB    . ASN A 1 729 ? 128.083 110.619 121.837 1.00 34.18  ? 729  ASN A CB    1 
ATOM   5626  C  CG    . ASN A 1 729 ? 126.578 110.488 121.835 1.00 36.75  ? 729  ASN A CG    1 
ATOM   5627  O  OD1   . ASN A 1 729 ? 126.024 109.544 121.274 1.00 32.78  ? 729  ASN A OD1   1 
ATOM   5628  N  ND2   . ASN A 1 729 ? 125.903 111.446 122.456 1.00 35.58  ? 729  ASN A ND2   1 
ATOM   5629  N  N     . ILE A 1 730 ? 130.009 109.076 119.472 1.00 36.05  ? 730  ILE A N     1 
ATOM   5630  C  CA    . ILE A 1 730 ? 131.044 109.403 118.502 1.00 38.41  ? 730  ILE A CA    1 
ATOM   5631  C  C     . ILE A 1 730 ? 130.576 110.611 117.707 1.00 37.85  ? 730  ILE A C     1 
ATOM   5632  O  O     . ILE A 1 730 ? 129.484 110.600 117.129 1.00 44.90  ? 730  ILE A O     1 
ATOM   5633  C  CB    . ILE A 1 730 ? 131.341 108.210 117.580 1.00 28.12  ? 730  ILE A CB    1 
ATOM   5634  C  CG1   . ILE A 1 730 ? 131.958 107.061 118.374 1.00 27.37  ? 730  ILE A CG1   1 
ATOM   5635  C  CG2   . ILE A 1 730 ? 132.271 108.624 116.454 1.00 31.82  ? 730  ILE A CG2   1 
ATOM   5636  C  CD1   . ILE A 1 730 ? 132.356 105.884 117.522 1.00 34.28  ? 730  ILE A CD1   1 
ATOM   5637  N  N     . GLU A 1 731 ? 131.389 111.660 117.690 1.00 20.52  ? 731  GLU A N     1 
ATOM   5638  C  CA    . GLU A 1 731 ? 131.038 112.887 116.991 1.00 22.33  ? 731  GLU A CA    1 
ATOM   5639  C  C     . GLU A 1 731 ? 131.501 112.779 115.544 1.00 27.84  ? 731  GLU A C     1 
ATOM   5640  O  O     . GLU A 1 731 ? 132.694 112.608 115.278 1.00 30.18  ? 731  GLU A O     1 
ATOM   5641  C  CB    . GLU A 1 731 ? 131.651 114.098 117.691 1.00 26.36  ? 731  GLU A CB    1 
ATOM   5642  C  CG    . GLU A 1 731 ? 131.164 114.262 119.121 1.00 30.51  ? 731  GLU A CG    1 
ATOM   5643  C  CD    . GLU A 1 731 ? 131.480 115.624 119.701 1.00 38.68  ? 731  GLU A CD    1 
ATOM   5644  O  OE1   . GLU A 1 731 ? 132.128 116.432 119.004 1.00 37.14  ? 731  GLU A OE1   1 
ATOM   5645  O  OE2   . GLU A 1 731 ? 131.076 115.889 120.852 1.00 42.60  ? 731  GLU A OE2   1 
ATOM   5646  N  N     . VAL A 1 732 ? 130.552 112.862 114.616 1.00 22.19  ? 732  VAL A N     1 
ATOM   5647  C  CA    . VAL A 1 732 ? 130.792 112.613 113.201 1.00 23.46  ? 732  VAL A CA    1 
ATOM   5648  C  C     . VAL A 1 732 ? 130.415 113.857 112.412 1.00 28.19  ? 732  VAL A C     1 
ATOM   5649  O  O     . VAL A 1 732 ? 129.412 114.512 112.713 1.00 36.83  ? 732  VAL A O     1 
ATOM   5650  C  CB    . VAL A 1 732 ? 129.988 111.395 112.699 1.00 21.04  ? 732  VAL A CB    1 
ATOM   5651  C  CG1   . VAL A 1 732 ? 130.518 110.917 111.361 1.00 22.78  ? 732  VAL A CG1   1 
ATOM   5652  C  CG2   . VAL A 1 732 ? 130.017 110.280 113.723 1.00 26.43  ? 732  VAL A CG2   1 
ATOM   5653  N  N     . TYR A 1 733 ? 131.218 114.179 111.400 1.00 22.21  ? 733  TYR A N     1 
ATOM   5654  C  CA    . TYR A 1 733 ? 130.916 115.261 110.463 1.00 27.95  ? 733  TYR A CA    1 
ATOM   5655  C  C     . TYR A 1 733 ? 131.056 114.712 109.046 1.00 25.86  ? 733  TYR A C     1 
ATOM   5656  O  O     . TYR A 1 733 ? 132.119 114.838 108.432 1.00 31.07  ? 733  TYR A O     1 
ATOM   5657  C  CB    . TYR A 1 733 ? 131.820 116.464 110.690 1.00 27.84  ? 733  TYR A CB    1 
ATOM   5658  C  CG    . TYR A 1 733 ? 131.524 117.604 109.750 1.00 28.60  ? 733  TYR A CG    1 
ATOM   5659  C  CD1   . TYR A 1 733 ? 130.330 118.305 109.836 1.00 30.49  ? 733  TYR A CD1   1 
ATOM   5660  C  CD2   . TYR A 1 733 ? 132.432 117.977 108.773 1.00 27.51  ? 733  TYR A CD2   1 
ATOM   5661  C  CE1   . TYR A 1 733 ? 130.051 119.345 108.977 1.00 30.23  ? 733  TYR A CE1   1 
ATOM   5662  C  CE2   . TYR A 1 733 ? 132.159 119.016 107.908 1.00 27.98  ? 733  TYR A CE2   1 
ATOM   5663  C  CZ    . TYR A 1 733 ? 130.969 119.696 108.015 1.00 28.78  ? 733  TYR A CZ    1 
ATOM   5664  O  OH    . TYR A 1 733 ? 130.698 120.732 107.155 1.00 36.47  ? 733  TYR A OH    1 
ATOM   5665  N  N     . ASN A 1 734 ? 129.978 114.118 108.536 1.00 24.44  ? 734  ASN A N     1 
ATOM   5666  C  CA    . ASN A 1 734 ? 129.913 113.576 107.179 1.00 29.66  ? 734  ASN A CA    1 
ATOM   5667  C  C     . ASN A 1 734 ? 131.068 112.607 106.913 1.00 36.26  ? 734  ASN A C     1 
ATOM   5668  O  O     . ASN A 1 734 ? 131.971 112.873 106.123 1.00 37.86  ? 734  ASN A O     1 
ATOM   5669  C  CB    . ASN A 1 734 ? 129.891 114.701 106.139 1.00 27.10  ? 734  ASN A CB    1 
ATOM   5670  C  CG    . ASN A 1 734 ? 128.536 115.360 106.026 1.00 34.71  ? 734  ASN A CG    1 
ATOM   5671  O  OD1   . ASN A 1 734 ? 127.614 114.807 105.430 1.00 34.50  ? 734  ASN A OD1   1 
ATOM   5672  N  ND2   . ASN A 1 734 ? 128.408 116.552 106.593 1.00 33.42  ? 734  ASN A ND2   1 
ATOM   5673  N  N     . ASP A 1 735 ? 131.022 111.491 107.640 1.00 32.74  ? 735  ASP A N     1 
ATOM   5674  C  CA    . ASP A 1 735 ? 131.911 110.332 107.549 1.00 29.51  ? 735  ASP A CA    1 
ATOM   5675  C  C     . ASP A 1 735 ? 133.292 110.584 108.165 1.00 30.62  ? 735  ASP A C     1 
ATOM   5676  O  O     . ASP A 1 735 ? 134.138 109.682 108.152 1.00 34.13  ? 735  ASP A O     1 
ATOM   5677  C  CB    . ASP A 1 735 ? 132.016 109.804 106.100 1.00 26.01  ? 735  ASP A CB    1 
ATOM   5678  C  CG    . ASP A 1 735 ? 133.386 110.005 105.462 1.00 27.66  ? 735  ASP A CG    1 
ATOM   5679  O  OD1   . ASP A 1 735 ? 133.830 111.157 105.282 1.00 30.71  ? 735  ASP A OD1   1 
ATOM   5680  O  OD2   . ASP A 1 735 ? 134.026 108.986 105.132 1.00 32.54  ? 735  ASP A OD2   1 
ATOM   5681  N  N     . ILE A 1 736 ? 133.528 111.744 108.767 1.00 26.98  ? 736  ILE A N     1 
ATOM   5682  C  CA    . ILE A 1 736 ? 134.743 111.977 109.540 1.00 30.97  ? 736  ILE A CA    1 
ATOM   5683  C  C     . ILE A 1 736 ? 134.494 111.561 110.984 1.00 34.79  ? 736  ILE A C     1 
ATOM   5684  O  O     . ILE A 1 736 ? 133.557 112.046 111.625 1.00 39.63  ? 736  ILE A O     1 
ATOM   5685  C  CB    . ILE A 1 736 ? 135.174 113.451 109.468 1.00 30.29  ? 736  ILE A CB    1 
ATOM   5686  C  CG1   . ILE A 1 736 ? 135.572 113.842 108.049 1.00 28.45  ? 736  ILE A CG1   1 
ATOM   5687  C  CG2   . ILE A 1 736 ? 136.328 113.714 110.413 1.00 25.29  ? 736  ILE A CG2   1 
ATOM   5688  C  CD1   . ILE A 1 736 ? 136.090 115.259 107.951 1.00 28.16  ? 736  ILE A CD1   1 
ATOM   5689  N  N     . LEU A 1 737 ? 135.336 110.668 111.503 1.00 36.05  ? 737  LEU A N     1 
ATOM   5690  C  CA    . LEU A 1 737 ? 135.279 110.262 112.908 1.00 27.05  ? 737  LEU A CA    1 
ATOM   5691  C  C     . LEU A 1 737 ? 136.114 111.250 113.709 1.00 31.26  ? 737  LEU A C     1 
ATOM   5692  O  O     . LEU A 1 737 ? 137.345 111.184 113.703 1.00 44.22  ? 737  LEU A O     1 
ATOM   5693  C  CB    . LEU A 1 737 ? 135.793 108.839 113.088 1.00 30.21  ? 737  LEU A CB    1 
ATOM   5694  C  CG    . LEU A 1 737 ? 135.113 107.720 112.307 1.00 38.19  ? 737  LEU A CG    1 
ATOM   5695  C  CD1   . LEU A 1 737 ? 135.791 106.396 112.599 1.00 35.48  ? 737  LEU A CD1   1 
ATOM   5696  C  CD2   . LEU A 1 737 ? 133.645 107.659 112.655 1.00 36.19  ? 737  LEU A CD2   1 
ATOM   5697  N  N     . VAL A 1 738 ? 135.449 112.164 114.413 1.00 23.93  ? 738  VAL A N     1 
ATOM   5698  C  CA    . VAL A 1 738 ? 136.150 113.269 115.057 1.00 22.77  ? 738  VAL A CA    1 
ATOM   5699  C  C     . VAL A 1 738 ? 136.593 112.891 116.465 1.00 26.73  ? 738  VAL A C     1 
ATOM   5700  O  O     . VAL A 1 738 ? 137.794 112.844 116.750 1.00 35.65  ? 738  VAL A O     1 
ATOM   5701  C  CB    . VAL A 1 738 ? 135.282 114.541 115.076 1.00 28.14  ? 738  VAL A CB    1 
ATOM   5702  C  CG1   . VAL A 1 738 ? 135.987 115.653 115.821 1.00 27.48  ? 738  VAL A CG1   1 
ATOM   5703  C  CG2   . VAL A 1 738 ? 134.966 114.980 113.659 1.00 30.99  ? 738  VAL A CG2   1 
ATOM   5704  N  N     . ARG A 1 739 ? 135.644 112.609 117.353 1.00 21.86  ? 739  ARG A N     1 
ATOM   5705  C  CA    . ARG A 1 739 ? 135.990 112.392 118.752 1.00 29.00  ? 739  ARG A CA    1 
ATOM   5706  C  C     . ARG A 1 739 ? 134.919 111.544 119.421 1.00 31.81  ? 739  ARG A C     1 
ATOM   5707  O  O     . ARG A 1 739 ? 133.831 111.335 118.882 1.00 28.38  ? 739  ARG A O     1 
ATOM   5708  C  CB    . ARG A 1 739 ? 136.167 113.719 119.493 1.00 28.30  ? 739  ARG A CB    1 
ATOM   5709  C  CG    . ARG A 1 739 ? 134.888 114.514 119.641 1.00 24.63  ? 739  ARG A CG    1 
ATOM   5710  C  CD    . ARG A 1 739 ? 135.156 115.890 120.212 1.00 28.05  ? 739  ARG A CD    1 
ATOM   5711  N  NE    . ARG A 1 739 ? 135.655 115.834 121.580 1.00 36.25  ? 739  ARG A NE    1 
ATOM   5712  C  CZ    . ARG A 1 739 ? 134.885 115.859 122.658 1.00 32.10  ? 739  ARG A CZ    1 
ATOM   5713  N  NH1   . ARG A 1 739 ? 133.569 115.920 122.564 1.00 34.05  ? 739  ARG A NH1   1 
ATOM   5714  N  NH2   . ARG A 1 739 ? 135.451 115.822 123.860 1.00 32.31  ? 739  ARG A NH2   1 
ATOM   5715  N  N     . ALA A 1 740 ? 135.253 111.056 120.612 1.00 32.75  ? 740  ALA A N     1 
ATOM   5716  C  CA    . ALA A 1 740 ? 134.338 110.300 121.454 1.00 28.20  ? 740  ALA A CA    1 
ATOM   5717  C  C     . ALA A 1 740 ? 133.915 111.165 122.630 1.00 31.13  ? 740  ALA A C     1 
ATOM   5718  O  O     . ALA A 1 740 ? 134.760 111.774 123.294 1.00 32.99  ? 740  ALA A O     1 
ATOM   5719  C  CB    . ALA A 1 740 ? 134.988 109.009 121.954 1.00 28.51  ? 740  ALA A CB    1 
ATOM   5720  N  N     . SER A 1 741 ? 132.613 111.221 122.884 1.00 31.98  ? 741  SER A N     1 
ATOM   5721  C  CA    . SER A 1 741 ? 132.073 112.013 123.977 1.00 29.97  ? 741  SER A CA    1 
ATOM   5722  C  C     . SER A 1 741 ? 131.181 111.136 124.843 1.00 30.10  ? 741  SER A C     1 
ATOM   5723  O  O     . SER A 1 741 ? 130.825 110.014 124.479 1.00 28.06  ? 741  SER A O     1 
ATOM   5724  C  CB    . SER A 1 741 ? 131.298 113.230 123.457 1.00 32.98  ? 741  SER A CB    1 
ATOM   5725  O  OG    . SER A 1 741 ? 130.301 112.844 122.529 1.00 34.49  ? 741  SER A OG    1 
ATOM   5726  N  N     . SER A 1 742 ? 130.823 111.664 126.006 1.00 30.16  ? 742  SER A N     1 
ATOM   5727  C  CA    . SER A 1 742 ? 130.042 110.926 126.985 1.00 32.47  ? 742  SER A CA    1 
ATOM   5728  C  C     . SER A 1 742 ? 128.579 111.339 126.917 1.00 36.35  ? 742  SER A C     1 
ATOM   5729  O  O     . SER A 1 742 ? 128.259 112.521 126.760 1.00 35.20  ? 742  SER A O     1 
ATOM   5730  C  CB    . SER A 1 742 ? 130.588 111.152 128.395 1.00 28.92  ? 742  SER A CB    1 
ATOM   5731  O  OG    . SER A 1 742 ? 130.607 112.528 128.717 1.00 28.07  ? 742  SER A OG    1 
ATOM   5732  N  N     . ARG A 1 743 ? 127.697 110.354 127.023 1.00 38.92  ? 743  ARG A N     1 
ATOM   5733  C  CA    . ARG A 1 743 ? 126.263 110.585 127.049 1.00 31.99  ? 743  ARG A CA    1 
ATOM   5734  C  C     . ARG A 1 743 ? 125.779 110.705 128.486 1.00 43.11  ? 743  ARG A C     1 
ATOM   5735  O  O     . ARG A 1 743 ? 126.333 110.094 129.403 1.00 46.88  ? 743  ARG A O     1 
ATOM   5736  C  CB    . ARG A 1 743 ? 125.524 109.445 126.351 1.00 34.67  ? 743  ARG A CB    1 
ATOM   5737  C  CG    . ARG A 1 743 ? 125.979 109.192 124.936 1.00 42.90  ? 743  ARG A CG    1 
ATOM   5738  C  CD    . ARG A 1 743 ? 125.786 107.742 124.544 1.00 36.01  ? 743  ARG A CD    1 
ATOM   5739  N  NE    . ARG A 1 743 ? 124.429 107.280 124.800 1.00 32.36  ? 743  ARG A NE    1 
ATOM   5740  C  CZ    . ARG A 1 743 ? 124.006 106.046 124.565 1.00 42.85  ? 743  ARG A CZ    1 
ATOM   5741  N  NH1   . ARG A 1 743 ? 124.810 105.126 124.061 1.00 47.63  ? 743  ARG A NH1   1 
ATOM   5742  N  NH2   . ARG A 1 743 ? 122.746 105.728 124.843 1.00 43.13  ? 743  ARG A NH2   1 
ATOM   5743  N  N     . LYS A 1 744 ? 124.734 111.508 128.678 1.00 45.00  ? 744  LYS A N     1 
ATOM   5744  C  CA    . LYS A 1 744 ? 124.126 111.615 129.997 1.00 42.21  ? 744  LYS A CA    1 
ATOM   5745  C  C     . LYS A 1 744 ? 123.256 110.410 130.326 1.00 45.11  ? 744  LYS A C     1 
ATOM   5746  O  O     . LYS A 1 744 ? 123.145 110.035 131.498 1.00 45.07  ? 744  LYS A O     1 
ATOM   5747  C  CB    . LYS A 1 744 ? 123.303 112.897 130.097 1.00 44.44  ? 744  LYS A CB    1 
ATOM   5748  C  CG    . LYS A 1 744 ? 124.140 114.153 130.219 1.00 44.21  ? 744  LYS A CG    1 
ATOM   5749  C  CD    . LYS A 1 744 ? 125.029 114.092 131.444 1.00 44.75  ? 744  LYS A CD    1 
ATOM   5750  C  CE    . LYS A 1 744 ? 125.695 115.430 131.697 1.00 43.90  ? 744  LYS A CE    1 
ATOM   5751  N  NZ    . LYS A 1 744 ? 124.691 116.508 131.899 1.00 42.68  ? 744  LYS A NZ    1 
ATOM   5752  N  N     . ASP A 1 745 ? 122.640 109.793 129.319 1.00 45.59  ? 745  ASP A N     1 
ATOM   5753  C  CA    . ASP A 1 745 ? 121.761 108.650 129.514 1.00 47.00  ? 745  ASP A CA    1 
ATOM   5754  C  C     . ASP A 1 745 ? 122.508 107.322 129.494 1.00 43.72  ? 745  ASP A C     1 
ATOM   5755  O  O     . ASP A 1 745 ? 121.901 106.282 129.216 1.00 42.58  ? 745  ASP A O     1 
ATOM   5756  C  CB    . ASP A 1 745 ? 120.659 108.649 128.454 1.00 46.39  ? 745  ASP A CB    1 
ATOM   5757  C  CG    . ASP A 1 745 ? 121.206 108.740 127.047 1.00 47.88  ? 745  ASP A CG    1 
ATOM   5758  O  OD1   . ASP A 1 745 ? 122.250 109.398 126.858 1.00 50.48  ? 745  ASP A OD1   1 
ATOM   5759  O  OD2   . ASP A 1 745 ? 120.593 108.156 126.129 1.00 48.87  ? 745  ASP A OD2   1 
ATOM   5760  N  N     . SER A 1 746 ? 123.805 107.334 129.776 1.00 40.85  ? 746  SER A N     1 
ATOM   5761  C  CA    . SER A 1 746 ? 124.614 106.126 129.825 1.00 40.30  ? 746  SER A CA    1 
ATOM   5762  C  C     . SER A 1 746 ? 124.813 105.704 131.273 1.00 46.29  ? 746  SER A C     1 
ATOM   5763  O  O     . SER A 1 746 ? 124.987 106.547 132.157 1.00 51.05  ? 746  SER A O     1 
ATOM   5764  C  CB    . SER A 1 746 ? 125.966 106.350 129.150 1.00 40.38  ? 746  SER A CB    1 
ATOM   5765  O  OG    . SER A 1 746 ? 126.608 107.500 129.668 1.00 44.09  ? 746  SER A OG    1 
ATOM   5766  N  N     . TRP A 1 747 ? 124.775 104.391 131.511 1.00 47.35  ? 747  TRP A N     1 
ATOM   5767  C  CA    . TRP A 1 747 ? 124.884 103.889 132.876 1.00 48.36  ? 747  TRP A CA    1 
ATOM   5768  C  C     . TRP A 1 747 ? 126.245 104.202 133.484 1.00 47.10  ? 747  TRP A C     1 
ATOM   5769  O  O     . TRP A 1 747 ? 126.338 104.467 134.687 1.00 52.15  ? 747  TRP A O     1 
ATOM   5770  C  CB    . TRP A 1 747 ? 124.607 102.385 132.913 1.00 52.05  ? 747  TRP A CB    1 
ATOM   5771  C  CG    . TRP A 1 747 ? 125.510 101.573 132.043 1.00 50.01  ? 747  TRP A CG    1 
ATOM   5772  C  CD1   . TRP A 1 747 ? 125.280 101.191 130.756 1.00 47.57  ? 747  TRP A CD1   1 
ATOM   5773  C  CD2   . TRP A 1 747 ? 126.791 101.037 132.398 1.00 49.27  ? 747  TRP A CD2   1 
ATOM   5774  N  NE1   . TRP A 1 747 ? 126.338 100.455 130.284 1.00 50.71  ? 747  TRP A NE1   1 
ATOM   5775  C  CE2   . TRP A 1 747 ? 127.280 100.347 131.273 1.00 50.13  ? 747  TRP A CE2   1 
ATOM   5776  C  CE3   . TRP A 1 747 ? 127.574 101.078 133.555 1.00 48.35  ? 747  TRP A CE3   1 
ATOM   5777  C  CZ2   . TRP A 1 747 ? 128.513 99.702  131.272 1.00 49.77  ? 747  TRP A CZ2   1 
ATOM   5778  C  CZ3   . TRP A 1 747 ? 128.798 100.439 133.551 1.00 51.30  ? 747  TRP A CZ3   1 
ATOM   5779  C  CH2   . TRP A 1 747 ? 129.255 99.760  132.418 1.00 50.92  ? 747  TRP A CH2   1 
ATOM   5780  N  N     . ASN A 1 748 ? 127.309 104.167 132.682 1.00 39.29  ? 748  ASN A N     1 
ATOM   5781  C  CA    . ASN A 1 748 ? 128.617 104.558 133.190 1.00 40.82  ? 748  ASN A CA    1 
ATOM   5782  C  C     . ASN A 1 748 ? 128.730 106.070 133.330 1.00 45.23  ? 748  ASN A C     1 
ATOM   5783  O  O     . ASN A 1 748 ? 129.277 106.565 134.321 1.00 44.06  ? 748  ASN A O     1 
ATOM   5784  C  CB    . ASN A 1 748 ? 129.719 104.015 132.280 1.00 40.51  ? 748  ASN A CB    1 
ATOM   5785  C  CG    . ASN A 1 748 ? 129.499 104.363 130.825 1.00 39.93  ? 748  ASN A CG    1 
ATOM   5786  O  OD1   . ASN A 1 748 ? 128.781 103.666 130.111 1.00 44.99  ? 748  ASN A OD1   1 
ATOM   5787  N  ND2   . ASN A 1 748 ? 130.120 105.445 130.376 1.00 45.41  ? 748  ASN A ND2   1 
ATOM   5788  N  N     . GLY A 1 749 ? 128.211 106.817 132.357 1.00 45.19  ? 749  GLY A N     1 
ATOM   5789  C  CA    . GLY A 1 749 ? 128.281 108.260 132.365 1.00 36.60  ? 749  GLY A CA    1 
ATOM   5790  C  C     . GLY A 1 749 ? 129.606 108.843 131.935 1.00 41.39  ? 749  GLY A C     1 
ATOM   5791  O  O     . GLY A 1 749 ? 129.654 110.019 131.559 1.00 50.98  ? 749  GLY A O     1 
ATOM   5792  N  N     . TYR A 1 750 ? 130.683 108.063 131.971 1.00 40.15  ? 750  TYR A N     1 
ATOM   5793  C  CA    . TYR A 1 750 ? 132.015 108.551 131.652 1.00 39.16  ? 750  TYR A CA    1 
ATOM   5794  C  C     . TYR A 1 750 ? 132.747 107.498 130.832 1.00 38.21  ? 750  TYR A C     1 
ATOM   5795  O  O     . TYR A 1 750 ? 132.416 106.311 130.872 1.00 46.25  ? 750  TYR A O     1 
ATOM   5796  C  CB    . TYR A 1 750 ? 132.800 108.890 132.927 1.00 37.13  ? 750  TYR A CB    1 
ATOM   5797  C  CG    . TYR A 1 750 ? 131.952 109.562 133.983 1.00 42.96  ? 750  TYR A CG    1 
ATOM   5798  C  CD1   . TYR A 1 750 ? 131.706 110.925 133.939 1.00 42.08  ? 750  TYR A CD1   1 
ATOM   5799  C  CD2   . TYR A 1 750 ? 131.378 108.830 135.010 1.00 43.22  ? 750  TYR A CD2   1 
ATOM   5800  C  CE1   . TYR A 1 750 ? 130.926 111.541 134.892 1.00 43.28  ? 750  TYR A CE1   1 
ATOM   5801  C  CE2   . TYR A 1 750 ? 130.595 109.438 135.968 1.00 42.06  ? 750  TYR A CE2   1 
ATOM   5802  C  CZ    . TYR A 1 750 ? 130.373 110.794 135.903 1.00 47.45  ? 750  TYR A CZ    1 
ATOM   5803  O  OH    . TYR A 1 750 ? 129.594 111.406 136.852 1.00 44.47  ? 750  TYR A OH    1 
ATOM   5804  N  N     . ILE A 1 751 ? 133.742 107.948 130.073 1.00 33.09  ? 751  ILE A N     1 
ATOM   5805  C  CA    . ILE A 1 751 ? 134.614 107.059 129.319 1.00 33.72  ? 751  ILE A CA    1 
ATOM   5806  C  C     . ILE A 1 751 ? 136.058 107.415 129.641 1.00 36.55  ? 751  ILE A C     1 
ATOM   5807  O  O     . ILE A 1 751 ? 136.376 108.561 129.973 1.00 37.88  ? 751  ILE A O     1 
ATOM   5808  C  CB    . ILE A 1 751 ? 134.351 107.127 127.798 1.00 30.21  ? 751  ILE A CB    1 
ATOM   5809  C  CG1   . ILE A 1 751 ? 134.465 108.561 127.293 1.00 31.44  ? 751  ILE A CG1   1 
ATOM   5810  C  CG2   . ILE A 1 751 ? 132.981 106.561 127.467 1.00 34.48  ? 751  ILE A CG2   1 
ATOM   5811  C  CD1   . ILE A 1 751 ? 134.195 108.704 125.816 1.00 36.11  ? 751  ILE A CD1   1 
ATOM   5812  N  N     . CYS A 1 752 ? 136.933 106.420 129.552 1.00 33.71  ? 752  CYS A N     1 
ATOM   5813  C  CA    . CYS A 1 752 ? 138.306 106.573 130.002 1.00 34.96  ? 752  CYS A CA    1 
ATOM   5814  C  C     . CYS A 1 752 ? 139.188 107.143 128.893 1.00 33.60  ? 752  CYS A C     1 
ATOM   5815  O  O     . CYS A 1 752 ? 138.807 107.201 127.723 1.00 39.09  ? 752  CYS A O     1 
ATOM   5816  C  CB    . CYS A 1 752 ? 138.856 105.236 130.499 1.00 36.64  ? 752  CYS A CB    1 
ATOM   5817  S  SG    . CYS A 1 752 ? 139.100 103.994 129.221 1.00 48.77  ? 752  CYS A SG    1 
ATOM   5818  N  N     . ASP A 1 753 ? 140.392 107.570 129.285 1.00 32.53  ? 753  ASP A N     1 
ATOM   5819  C  CA    . ASP A 1 753 ? 141.303 108.208 128.340 1.00 36.41  ? 753  ASP A CA    1 
ATOM   5820  C  C     . ASP A 1 753 ? 141.854 107.227 127.316 1.00 41.50  ? 753  ASP A C     1 
ATOM   5821  O  O     . ASP A 1 753 ? 142.217 107.640 126.209 1.00 42.02  ? 753  ASP A O     1 
ATOM   5822  C  CB    . ASP A 1 753 ? 142.454 108.882 129.082 1.00 41.46  ? 753  ASP A CB    1 
ATOM   5823  C  CG    . ASP A 1 753 ? 142.033 110.155 129.766 1.00 46.85  ? 753  ASP A CG    1 
ATOM   5824  O  OD1   . ASP A 1 753 ? 140.820 110.333 129.993 1.00 46.82  ? 753  ASP A OD1   1 
ATOM   5825  O  OD2   . ASP A 1 753 ? 142.915 110.984 130.068 1.00 50.78  ? 753  ASP A OD2   1 
ATOM   5826  N  N     . TYR A 1 754 ? 141.943 105.941 127.661 1.00 44.41  ? 754  TYR A N     1 
ATOM   5827  C  CA    . TYR A 1 754 ? 142.355 104.948 126.674 1.00 41.87  ? 754  TYR A CA    1 
ATOM   5828  C  C     . TYR A 1 754 ? 141.382 104.913 125.504 1.00 47.59  ? 754  TYR A C     1 
ATOM   5829  O  O     . TYR A 1 754 ? 141.791 104.981 124.340 1.00 56.10  ? 754  TYR A O     1 
ATOM   5830  C  CB    . TYR A 1 754 ? 142.464 103.564 127.317 1.00 47.55  ? 754  TYR A CB    1 
ATOM   5831  C  CG    . TYR A 1 754 ? 142.676 102.450 126.313 1.00 46.19  ? 754  TYR A CG    1 
ATOM   5832  C  CD1   . TYR A 1 754 ? 143.940 102.166 125.822 1.00 46.38  ? 754  TYR A CD1   1 
ATOM   5833  C  CD2   . TYR A 1 754 ? 141.611 101.684 125.855 1.00 44.76  ? 754  TYR A CD2   1 
ATOM   5834  C  CE1   . TYR A 1 754 ? 144.139 101.156 124.903 1.00 48.72  ? 754  TYR A CE1   1 
ATOM   5835  C  CE2   . TYR A 1 754 ? 141.802 100.674 124.935 1.00 44.86  ? 754  TYR A CE2   1 
ATOM   5836  C  CZ    . TYR A 1 754 ? 143.067 100.413 124.463 1.00 47.68  ? 754  TYR A CZ    1 
ATOM   5837  O  OH    . TYR A 1 754 ? 143.264 99.405  123.549 1.00 44.97  ? 754  TYR A OH    1 
ATOM   5838  N  N     . CYS A 1 755 ? 140.084 104.828 125.800 1.00 37.49  ? 755  CYS A N     1 
ATOM   5839  C  CA    . CYS A 1 755 ? 139.081 104.791 124.741 1.00 34.34  ? 755  CYS A CA    1 
ATOM   5840  C  C     . CYS A 1 755 ? 139.096 106.071 123.915 1.00 37.35  ? 755  CYS A C     1 
ATOM   5841  O  O     . CYS A 1 755 ? 139.027 106.022 122.682 1.00 41.42  ? 755  CYS A O     1 
ATOM   5842  C  CB    . CYS A 1 755 ? 137.697 104.560 125.345 1.00 33.62  ? 755  CYS A CB    1 
ATOM   5843  S  SG    . CYS A 1 755 ? 136.322 105.022 124.275 1.00 45.66  ? 755  CYS A SG    1 
ATOM   5844  N  N     . ARG A 1 756 ? 139.198 107.224 124.578 1.00 31.22  ? 756  ARG A N     1 
ATOM   5845  C  CA    . ARG A 1 756 ? 139.161 108.502 123.875 1.00 22.70  ? 756  ARG A CA    1 
ATOM   5846  C  C     . ARG A 1 756 ? 140.370 108.682 122.967 1.00 31.45  ? 756  ARG A C     1 
ATOM   5847  O  O     . ARG A 1 756 ? 140.230 109.085 121.807 1.00 39.81  ? 756  ARG A O     1 
ATOM   5848  C  CB    . ARG A 1 756 ? 139.094 109.653 124.878 1.00 26.74  ? 756  ARG A CB    1 
ATOM   5849  C  CG    . ARG A 1 756 ? 137.811 109.746 125.665 1.00 31.77  ? 756  ARG A CG    1 
ATOM   5850  C  CD    . ARG A 1 756 ? 137.833 110.967 126.563 1.00 30.45  ? 756  ARG A CD    1 
ATOM   5851  N  NE    . ARG A 1 756 ? 136.577 111.136 127.282 1.00 35.79  ? 756  ARG A NE    1 
ATOM   5852  C  CZ    . ARG A 1 756 ? 135.537 111.815 126.821 1.00 35.17  ? 756  ARG A CZ    1 
ATOM   5853  N  NH1   . ARG A 1 756 ? 135.565 112.403 125.636 1.00 28.99  ? 756  ARG A NH1   1 
ATOM   5854  N  NH2   . ARG A 1 756 ? 134.440 111.905 127.566 1.00 37.40  ? 756  ARG A NH2   1 
ATOM   5855  N  N     . PHE A 1 757 ? 141.566 108.394 123.476 1.00 41.51  ? 757  PHE A N     1 
ATOM   5856  C  CA    . PHE A 1 757 ? 142.797 108.827 122.826 1.00 38.90  ? 757  PHE A CA    1 
ATOM   5857  C  C     . PHE A 1 757 ? 143.521 107.716 122.080 1.00 37.60  ? 757  PHE A C     1 
ATOM   5858  O  O     . PHE A 1 757 ? 144.068 107.963 121.002 1.00 45.08  ? 757  PHE A O     1 
ATOM   5859  C  CB    . PHE A 1 757 ? 143.735 109.452 123.862 1.00 38.51  ? 757  PHE A CB    1 
ATOM   5860  C  CG    . PHE A 1 757 ? 143.106 110.564 124.649 1.00 41.14  ? 757  PHE A CG    1 
ATOM   5861  C  CD1   . PHE A 1 757 ? 142.172 111.404 124.065 1.00 35.26  ? 757  PHE A CD1   1 
ATOM   5862  C  CD2   . PHE A 1 757 ? 143.435 110.762 125.977 1.00 40.08  ? 757  PHE A CD2   1 
ATOM   5863  C  CE1   . PHE A 1 757 ? 141.588 112.420 124.788 1.00 33.27  ? 757  PHE A CE1   1 
ATOM   5864  C  CE2   . PHE A 1 757 ? 142.855 111.778 126.702 1.00 40.52  ? 757  PHE A CE2   1 
ATOM   5865  C  CZ    . PHE A 1 757 ? 141.930 112.607 126.107 1.00 41.52  ? 757  PHE A CZ    1 
ATOM   5866  N  N     . GLU A 1 758 ? 143.561 106.499 122.626 1.00 41.07  ? 758  GLU A N     1 
ATOM   5867  C  CA    . GLU A 1 758 ? 144.118 105.387 121.869 1.00 43.34  ? 758  GLU A CA    1 
ATOM   5868  C  C     . GLU A 1 758 ? 143.169 104.916 120.778 1.00 49.15  ? 758  GLU A C     1 
ATOM   5869  O  O     . GLU A 1 758 ? 143.616 104.288 119.813 1.00 53.76  ? 758  GLU A O     1 
ATOM   5870  C  CB    . GLU A 1 758 ? 144.463 104.231 122.806 1.00 43.59  ? 758  GLU A CB    1 
ATOM   5871  C  CG    . GLU A 1 758 ? 145.507 104.581 123.844 1.00 47.07  ? 758  GLU A CG    1 
ATOM   5872  C  CD    . GLU A 1 758 ? 146.866 104.849 123.239 1.00 52.58  ? 758  GLU A CD    1 
ATOM   5873  O  OE1   . GLU A 1 758 ? 147.181 104.252 122.188 1.00 55.33  ? 758  GLU A OE1   1 
ATOM   5874  O  OE2   . GLU A 1 758 ? 147.623 105.660 123.813 1.00 54.31  ? 758  GLU A OE2   1 
ATOM   5875  N  N     . ARG A 1 759 ? 141.878 105.210 120.917 1.00 35.29  ? 759  ARG A N     1 
ATOM   5876  C  CA    . ARG A 1 759 ? 140.840 104.990 119.916 1.00 35.35  ? 759  ARG A CA    1 
ATOM   5877  C  C     . ARG A 1 759 ? 140.758 103.549 119.426 1.00 40.65  ? 759  ARG A C     1 
ATOM   5878  O  O     . ARG A 1 759 ? 141.008 103.289 118.243 1.00 48.06  ? 759  ARG A O     1 
ATOM   5879  C  CB    . ARG A 1 759 ? 141.062 105.925 118.726 1.00 38.03  ? 759  ARG A CB    1 
ATOM   5880  C  CG    . ARG A 1 759 ? 140.751 107.374 119.029 1.00 36.06  ? 759  ARG A CG    1 
ATOM   5881  C  CD    . ARG A 1 759 ? 141.016 108.267 117.836 1.00 38.50  ? 759  ARG A CD    1 
ATOM   5882  N  NE    . ARG A 1 759 ? 140.340 109.551 117.969 1.00 46.85  ? 759  ARG A NE    1 
ATOM   5883  C  CZ    . ARG A 1 759 ? 140.778 110.556 118.714 1.00 42.25  ? 759  ARG A CZ    1 
ATOM   5884  N  NH1   . ARG A 1 759 ? 141.893 110.460 119.419 1.00 38.49  ? 759  ARG A NH1   1 
ATOM   5885  N  NH2   . ARG A 1 759 ? 140.081 111.687 118.753 1.00 43.31  ? 759  ARG A NH2   1 
ATOM   5886  N  N     . PRO A 1 760 ? 140.401 102.588 120.285 1.00 45.19  ? 760  PRO A N     1 
ATOM   5887  C  CA    . PRO A 1 760 ? 140.163 101.224 119.789 1.00 48.79  ? 760  PRO A CA    1 
ATOM   5888  C  C     . PRO A 1 760 ? 138.970 101.124 118.857 1.00 52.92  ? 760  PRO A C     1 
ATOM   5889  O  O     . PRO A 1 760 ? 138.870 100.147 118.107 1.00 54.21  ? 760  PRO A O     1 
ATOM   5890  C  CB    . PRO A 1 760 ? 139.935 100.420 121.074 1.00 48.08  ? 760  PRO A CB    1 
ATOM   5891  C  CG    . PRO A 1 760 ? 139.394 101.414 122.029 1.00 49.55  ? 760  PRO A CG    1 
ATOM   5892  C  CD    . PRO A 1 760 ? 140.111 102.700 121.725 1.00 46.27  ? 760  PRO A CD    1 
ATOM   5893  N  N     . TRP A 1 761 ? 138.066 102.102 118.885 1.00 43.93  ? 761  TRP A N     1 
ATOM   5894  C  CA    . TRP A 1 761 ? 136.899 102.109 118.015 1.00 44.05  ? 761  TRP A CA    1 
ATOM   5895  C  C     . TRP A 1 761 ? 137.205 102.616 116.612 1.00 45.78  ? 761  TRP A C     1 
ATOM   5896  O  O     . TRP A 1 761 ? 136.392 102.410 115.705 1.00 47.11  ? 761  TRP A O     1 
ATOM   5897  C  CB    . TRP A 1 761 ? 135.796 102.967 118.640 1.00 40.84  ? 761  TRP A CB    1 
ATOM   5898  C  CG    . TRP A 1 761 ? 136.312 104.238 119.265 1.00 41.00  ? 761  TRP A CG    1 
ATOM   5899  C  CD1   . TRP A 1 761 ? 136.764 104.397 120.541 1.00 42.35  ? 761  TRP A CD1   1 
ATOM   5900  C  CD2   . TRP A 1 761 ? 136.426 105.523 118.639 1.00 37.53  ? 761  TRP A CD2   1 
ATOM   5901  N  NE1   . TRP A 1 761 ? 137.154 105.696 120.748 1.00 35.15  ? 761  TRP A NE1   1 
ATOM   5902  C  CE2   . TRP A 1 761 ? 136.955 106.408 119.596 1.00 32.33  ? 761  TRP A CE2   1 
ATOM   5903  C  CE3   . TRP A 1 761 ? 136.129 106.010 117.363 1.00 41.01  ? 761  TRP A CE3   1 
ATOM   5904  C  CZ2   . TRP A 1 761 ? 137.195 107.750 119.318 1.00 37.38  ? 761  TRP A CZ2   1 
ATOM   5905  C  CZ3   . TRP A 1 761 ? 136.370 107.342 117.090 1.00 37.29  ? 761  TRP A CZ3   1 
ATOM   5906  C  CH2   . TRP A 1 761 ? 136.896 108.196 118.061 1.00 35.97  ? 761  TRP A CH2   1 
ATOM   5907  N  N     . ALA A 1 762 ? 138.352 103.264 116.408 1.00 48.00  ? 762  ALA A N     1 
ATOM   5908  C  CA    . ALA A 1 762 ? 138.691 103.882 115.132 1.00 50.46  ? 762  ALA A CA    1 
ATOM   5909  C  C     . ALA A 1 762 ? 139.894 103.222 114.467 1.00 57.00  ? 762  ALA A C     1 
ATOM   5910  O  O     . ALA A 1 762 ? 140.626 103.873 113.718 1.00 61.48  ? 762  ALA A O     1 
ATOM   5911  C  CB    . ALA A 1 762 ? 138.950 105.376 115.311 1.00 48.10  ? 762  ALA A CB    1 
ATOM   5912  N  N     . GLN A 1 763 ? 140.115 101.934 114.724 1.00 55.86  ? 763  GLN A N     1 
ATOM   5913  C  CA    . GLN A 1 763 ? 141.224 101.236 114.096 1.00 57.05  ? 763  GLN A CA    1 
ATOM   5914  C  C     . GLN A 1 763 ? 140.904 99.753  113.990 1.00 60.30  ? 763  GLN A C     1 
ATOM   5915  O  O     . GLN A 1 763 ? 140.053 99.224  114.709 1.00 61.85  ? 763  GLN A O     1 
ATOM   5916  C  CB    . GLN A 1 763 ? 142.531 101.456 114.864 1.00 57.22  ? 763  GLN A CB    1 
ATOM   5917  C  CG    . GLN A 1 763 ? 142.490 101.017 116.310 1.00 58.34  ? 763  GLN A CG    1 
ATOM   5918  C  CD    . GLN A 1 763 ? 143.676 101.533 117.099 1.00 60.79  ? 763  GLN A CD    1 
ATOM   5919  O  OE1   . GLN A 1 763 ? 144.316 102.509 116.710 1.00 61.12  ? 763  GLN A OE1   1 
ATOM   5920  N  NE2   . GLN A 1 763 ? 143.976 100.878 118.214 1.00 59.14  ? 763  GLN A NE2   1 
ATOM   5921  N  N     . ASP A 1 764 ? 141.601 99.094  113.071 1.00 78.01  ? 764  ASP A N     1 
ATOM   5922  C  CA    . ASP A 1 764 ? 141.475 97.662  112.824 1.00 79.17  ? 764  ASP A CA    1 
ATOM   5923  C  C     . ASP A 1 764 ? 142.714 97.217  112.054 1.00 81.78  ? 764  ASP A C     1 
ATOM   5924  O  O     . ASP A 1 764 ? 143.690 97.964  111.934 1.00 81.45  ? 764  ASP A O     1 
ATOM   5925  C  CB    . ASP A 1 764 ? 140.184 97.345  112.066 1.00 81.07  ? 764  ASP A CB    1 
ATOM   5926  C  CG    . ASP A 1 764 ? 140.152 97.971  110.687 1.00 81.78  ? 764  ASP A CG    1 
ATOM   5927  O  OD1   . ASP A 1 764 ? 140.738 99.060  110.513 1.00 78.58  ? 764  ASP A OD1   1 
ATOM   5928  O  OD2   . ASP A 1 764 ? 139.542 97.373  109.776 1.00 81.86  ? 764  ASP A OD2   1 
ATOM   5929  N  N     . ILE A 1 765 ? 142.677 95.997  111.525 1.00 94.08  ? 765  ILE A N     1 
ATOM   5930  C  CA    . ILE A 1 765 ? 143.756 95.470  110.697 1.00 94.62  ? 765  ILE A CA    1 
ATOM   5931  C  C     . ILE A 1 765 ? 143.325 95.533  109.240 1.00 95.84  ? 765  ILE A C     1 
ATOM   5932  O  O     . ILE A 1 765 ? 142.221 95.097  108.888 1.00 95.48  ? 765  ILE A O     1 
ATOM   5933  C  CB    . ILE A 1 765 ? 144.135 94.038  111.110 1.00 95.04  ? 765  ILE A CB    1 
ATOM   5934  C  CG1   . ILE A 1 765 ? 142.887 93.229  111.462 1.00 94.88  ? 765  ILE A CG1   1 
ATOM   5935  C  CG2   . ILE A 1 765 ? 145.108 94.063  112.278 1.00 94.69  ? 765  ILE A CG2   1 
ATOM   5936  C  CD1   . ILE A 1 765 ? 143.193 91.848  112.001 1.00 95.38  ? 765  ILE A CD1   1 
ATOM   5937  N  N     . ALA A 1 766 ? 144.195 96.088  108.392 1.00 105.95 ? 766  ALA A N     1 
ATOM   5938  C  CA    . ALA A 1 766 ? 143.821 96.360  107.008 1.00 106.29 ? 766  ALA A CA    1 
ATOM   5939  C  C     . ALA A 1 766 ? 143.770 95.087  106.172 1.00 108.52 ? 766  ALA A C     1 
ATOM   5940  O  O     . ALA A 1 766 ? 142.847 94.904  105.370 1.00 107.34 ? 766  ALA A O     1 
ATOM   5941  C  CB    . ALA A 1 766 ? 144.792 97.367  106.395 1.00 105.62 ? 766  ALA A CB    1 
ATOM   5942  N  N     . GLN A 1 767 ? 144.746 94.196  106.338 1.00 111.51 ? 767  GLN A N     1 
ATOM   5943  C  CA    . GLN A 1 767 ? 144.823 93.012  105.499 1.00 110.44 ? 767  GLN A CA    1 
ATOM   5944  C  C     . GLN A 1 767 ? 144.838 91.753  106.357 1.00 110.12 ? 767  GLN A C     1 
ATOM   5945  O  O     . GLN A 1 767 ? 145.319 91.781  107.493 1.00 110.10 ? 767  GLN A O     1 
ATOM   5946  C  CB    . GLN A 1 767 ? 146.079 93.039  104.620 1.00 109.62 ? 767  GLN A CB    1 
ATOM   5947  C  CG    . GLN A 1 767 ? 146.334 94.366  103.927 1.00 109.43 ? 767  GLN A CG    1 
ATOM   5948  C  CD    . GLN A 1 767 ? 145.326 94.665  102.841 1.00 110.14 ? 767  GLN A CD    1 
ATOM   5949  O  OE1   . GLN A 1 767 ? 144.663 93.765  102.328 1.00 109.76 ? 767  GLN A OE1   1 
ATOM   5950  N  NE2   . GLN A 1 767 ? 145.206 95.936  102.481 1.00 110.87 ? 767  GLN A NE2   1 
ATOM   5951  N  N     . PRO A 1 768 ? 144.305 90.640  105.850 1.00 110.13 ? 768  PRO A N     1 
ATOM   5952  C  CA    . PRO A 1 768 ? 144.345 89.391  106.620 1.00 109.12 ? 768  PRO A CA    1 
ATOM   5953  C  C     . PRO A 1 768 ? 145.775 88.927  106.854 1.00 109.17 ? 768  PRO A C     1 
ATOM   5954  O  O     . PRO A 1 768 ? 146.651 89.091  106.004 1.00 110.11 ? 768  PRO A O     1 
ATOM   5955  C  CB    . PRO A 1 768 ? 143.562 88.405  105.745 1.00 108.99 ? 768  PRO A CB    1 
ATOM   5956  C  CG    . PRO A 1 768 ? 143.544 89.012  104.387 1.00 110.02 ? 768  PRO A CG    1 
ATOM   5957  C  CD    . PRO A 1 768 ? 143.544 90.490  104.599 1.00 110.47 ? 768  PRO A CD    1 
ATOM   5958  N  N     . ILE A 1 769 ? 146.001 88.342  108.025 1.00 112.11 ? 769  ILE A N     1 
ATOM   5959  C  CA    . ILE A 1 769 ? 147.335 87.974  108.480 1.00 113.24 ? 769  ILE A CA    1 
ATOM   5960  C  C     . ILE A 1 769 ? 147.519 86.476  108.304 1.00 113.88 ? 769  ILE A C     1 
ATOM   5961  O  O     . ILE A 1 769 ? 146.711 85.680  108.795 1.00 113.48 ? 769  ILE A O     1 
ATOM   5962  C  CB    . ILE A 1 769 ? 147.557 88.385  109.945 1.00 113.84 ? 769  ILE A CB    1 
ATOM   5963  C  CG1   . ILE A 1 769 ? 147.481 89.906  110.088 1.00 113.50 ? 769  ILE A CG1   1 
ATOM   5964  C  CG2   . ILE A 1 769 ? 148.893 87.869  110.447 1.00 113.69 ? 769  ILE A CG2   1 
ATOM   5965  C  CD1   . ILE A 1 769 ? 147.695 90.397  111.502 1.00 111.99 ? 769  ILE A CD1   1 
ATOM   5966  N  N     . LEU A 1 770 ? 148.583 86.093  107.600 1.00 117.81 ? 770  LEU A N     1 
ATOM   5967  C  CA    . LEU A 1 770 ? 148.939 84.693  107.379 1.00 117.34 ? 770  LEU A CA    1 
ATOM   5968  C  C     . LEU A 1 770 ? 150.418 84.553  107.724 1.00 117.32 ? 770  LEU A C     1 
ATOM   5969  O  O     . LEU A 1 770 ? 151.278 84.764  106.865 1.00 117.33 ? 770  LEU A O     1 
ATOM   5970  C  CB    . LEU A 1 770 ? 148.646 84.267  105.946 1.00 117.21 ? 770  LEU A CB    1 
ATOM   5971  C  CG    . LEU A 1 770 ? 148.886 82.792  105.624 1.00 118.27 ? 770  LEU A CG    1 
ATOM   5972  C  CD1   . LEU A 1 770 ? 148.045 81.905  106.526 1.00 117.59 ? 770  LEU A CD1   1 
ATOM   5973  C  CD2   . LEU A 1 770 ? 148.590 82.508  104.161 1.00 117.90 ? 770  LEU A CD2   1 
ATOM   5974  N  N     . LYS A 1 771 ? 150.697 84.201  108.980 1.00 118.99 ? 771  LYS A N     1 
ATOM   5975  C  CA    . LYS A 1 771 ? 152.063 84.051  109.488 1.00 119.39 ? 771  LYS A CA    1 
ATOM   5976  C  C     . LYS A 1 771 ? 152.867 85.337  109.288 1.00 119.14 ? 771  LYS A C     1 
ATOM   5977  O  O     . LYS A 1 771 ? 153.999 85.326  108.801 1.00 119.05 ? 771  LYS A O     1 
ATOM   5978  C  CB    . LYS A 1 771 ? 152.763 82.851  108.840 1.00 118.18 ? 771  LYS A CB    1 
ATOM   5979  C  CG    . LYS A 1 771 ? 153.917 82.281  109.654 1.00 118.40 ? 771  LYS A CG    1 
ATOM   5980  C  CD    . LYS A 1 771 ? 154.728 81.285  108.840 1.00 119.09 ? 771  LYS A CD    1 
ATOM   5981  C  CE    . LYS A 1 771 ? 153.860 80.146  108.334 1.00 118.88 ? 771  LYS A CE    1 
ATOM   5982  N  NZ    . LYS A 1 771 ? 154.643 79.168  107.529 1.00 118.66 ? 771  LYS A NZ    1 
ATOM   5983  N  N     . GLY A 1 772 ? 152.261 86.460  109.662 1.00 116.32 ? 772  GLY A N     1 
ATOM   5984  C  CA    . GLY A 1 772 ? 152.925 87.743  109.558 1.00 115.87 ? 772  GLY A CA    1 
ATOM   5985  C  C     . GLY A 1 772 ? 152.985 88.325  108.166 1.00 115.50 ? 772  GLY A C     1 
ATOM   5986  O  O     . GLY A 1 772 ? 153.687 89.322  107.960 1.00 114.82 ? 772  GLY A O     1 
ATOM   5987  N  N     . ASN A 1 773 ? 152.277 87.741  107.206 1.00 115.05 ? 773  ASN A N     1 
ATOM   5988  C  CA    . ASN A 1 773 ? 152.274 88.209  105.828 1.00 115.03 ? 773  ASN A CA    1 
ATOM   5989  C  C     . ASN A 1 773 ? 150.946 88.884  105.526 1.00 114.81 ? 773  ASN A C     1 
ATOM   5990  O  O     . ASN A 1 773 ? 149.882 88.310  105.776 1.00 114.70 ? 773  ASN A O     1 
ATOM   5991  C  CB    . ASN A 1 773 ? 152.511 87.052  104.856 1.00 115.27 ? 773  ASN A CB    1 
ATOM   5992  C  CG    . ASN A 1 773 ? 153.813 86.324  105.123 1.00 115.74 ? 773  ASN A CG    1 
ATOM   5993  O  OD1   . ASN A 1 773 ? 154.855 86.667  104.565 1.00 115.88 ? 773  ASN A OD1   1 
ATOM   5994  N  ND2   . ASN A 1 773 ? 153.760 85.313  105.983 1.00 114.82 ? 773  ASN A ND2   1 
ATOM   5995  N  N     . ALA A 1 774 ? 151.012 90.099  104.984 1.00 114.89 ? 774  ALA A N     1 
ATOM   5996  C  CA    . ALA A 1 774 ? 149.813 90.858  104.630 1.00 115.17 ? 774  ALA A CA    1 
ATOM   5997  C  C     . ALA A 1 774 ? 149.317 90.397  103.260 1.00 114.88 ? 774  ALA A C     1 
ATOM   5998  O  O     . ALA A 1 774 ? 149.403 91.100  102.251 1.00 114.48 ? 774  ALA A O     1 
ATOM   5999  C  CB    . ALA A 1 774 ? 150.100 92.353  104.652 1.00 114.57 ? 774  ALA A CB    1 
ATOM   6000  N  N     . VAL A 1 775 ? 148.785 89.174  103.242 1.00 118.06 ? 775  VAL A N     1 
ATOM   6001  C  CA    . VAL A 1 775 ? 148.302 88.606  101.992 1.00 118.19 ? 775  VAL A CA    1 
ATOM   6002  C  C     . VAL A 1 775 ? 146.978 89.252  101.600 1.00 118.84 ? 775  VAL A C     1 
ATOM   6003  O  O     . VAL A 1 775 ? 146.276 89.862  102.415 1.00 118.91 ? 775  VAL A O     1 
ATOM   6004  C  CB    . VAL A 1 775 ? 148.162 87.079  102.101 1.00 118.28 ? 775  VAL A CB    1 
ATOM   6005  C  CG1   . VAL A 1 775 ? 149.436 86.469  102.665 1.00 118.24 ? 775  VAL A CG1   1 
ATOM   6006  C  CG2   . VAL A 1 775 ? 146.956 86.712  102.953 1.00 118.31 ? 775  VAL A CG2   1 
ATOM   6007  N  N     . SER A 1 776 ? 146.639 89.118  100.322 1.00 121.83 ? 776  SER A N     1 
ATOM   6008  C  CA    . SER A 1 776 ? 145.367 89.605  99.818  1.00 122.32 ? 776  SER A CA    1 
ATOM   6009  C  C     . SER A 1 776 ? 144.251 88.639  100.206 1.00 122.11 ? 776  SER A C     1 
ATOM   6010  O  O     . SER A 1 776 ? 144.484 87.580  100.796 1.00 122.36 ? 776  SER A O     1 
ATOM   6011  C  CB    . SER A 1 776 ? 145.435 89.797  98.306  1.00 121.97 ? 776  SER A CB    1 
ATOM   6012  O  OG    . SER A 1 776 ? 144.197 90.263  97.797  1.00 121.79 ? 776  SER A OG    1 
ATOM   6013  N  N     . TRP A 1 777 ? 143.014 89.008  99.873  1.00 118.14 ? 777  TRP A N     1 
ATOM   6014  C  CA    . TRP A 1 777 ? 141.877 88.167  100.218 1.00 118.16 ? 777  TRP A CA    1 
ATOM   6015  C  C     . TRP A 1 777 ? 141.759 86.933  99.336  1.00 119.03 ? 777  TRP A C     1 
ATOM   6016  O  O     . TRP A 1 777 ? 141.133 85.956  99.753  1.00 118.50 ? 777  TRP A O     1 
ATOM   6017  C  CB    . TRP A 1 777 ? 140.580 88.972  100.154 1.00 118.77 ? 777  TRP A CB    1 
ATOM   6018  C  CG    . TRP A 1 777 ? 140.176 89.512  101.484 1.00 119.95 ? 777  TRP A CG    1 
ATOM   6019  C  CD1   . TRP A 1 777 ? 139.346 88.921  102.390 1.00 118.79 ? 777  TRP A CD1   1 
ATOM   6020  C  CD2   . TRP A 1 777 ? 140.595 90.748  102.070 1.00 119.78 ? 777  TRP A CD2   1 
ATOM   6021  N  NE1   . TRP A 1 777 ? 139.217 89.714  103.502 1.00 118.10 ? 777  TRP A NE1   1 
ATOM   6022  C  CE2   . TRP A 1 777 ? 139.975 90.843  103.330 1.00 119.47 ? 777  TRP A CE2   1 
ATOM   6023  C  CE3   . TRP A 1 777 ? 141.431 91.786  101.650 1.00 118.31 ? 777  TRP A CE3   1 
ATOM   6024  C  CZ2   . TRP A 1 777 ? 140.164 91.934  104.171 1.00 119.13 ? 777  TRP A CZ2   1 
ATOM   6025  C  CZ3   . TRP A 1 777 ? 141.617 92.866  102.487 1.00 118.34 ? 777  TRP A CZ3   1 
ATOM   6026  C  CH2   . TRP A 1 777 ? 140.987 92.933  103.733 1.00 118.54 ? 777  TRP A CH2   1 
ATOM   6027  N  N     . GLU A 1 778 ? 142.337 86.950  98.134  1.00 123.50 ? 778  GLU A N     1 
ATOM   6028  C  CA    . GLU A 1 778 ? 142.337 85.749  97.305  1.00 123.20 ? 778  GLU A CA    1 
ATOM   6029  C  C     . GLU A 1 778 ? 143.194 84.656  97.933  1.00 123.18 ? 778  GLU A C     1 
ATOM   6030  O  O     . GLU A 1 778 ? 142.782 83.492  98.004  1.00 123.08 ? 778  GLU A O     1 
ATOM   6031  C  CB    . GLU A 1 778 ? 142.825 86.078  95.894  1.00 122.27 ? 778  GLU A CB    1 
ATOM   6032  C  CG    . GLU A 1 778 ? 141.878 86.955  95.086  1.00 122.63 ? 778  GLU A CG    1 
ATOM   6033  C  CD    . GLU A 1 778 ? 141.995 88.427  95.433  1.00 123.30 ? 778  GLU A CD    1 
ATOM   6034  O  OE1   . GLU A 1 778 ? 142.932 88.795  96.173  1.00 123.46 ? 778  GLU A OE1   1 
ATOM   6035  O  OE2   . GLU A 1 778 ? 141.148 89.218  94.966  1.00 122.59 ? 778  GLU A OE2   1 
ATOM   6036  N  N     . ASP A 1 779 ? 144.389 85.020  98.406  1.00 125.22 ? 779  ASP A N     1 
ATOM   6037  C  CA    . ASP A 1 779 ? 145.253 84.054  99.076  1.00 126.05 ? 779  ASP A CA    1 
ATOM   6038  C  C     . ASP A 1 779 ? 144.629 83.569  100.379 1.00 126.19 ? 779  ASP A C     1 
ATOM   6039  O  O     . ASP A 1 779 ? 144.731 82.384  100.722 1.00 126.08 ? 779  ASP A O     1 
ATOM   6040  C  CB    . ASP A 1 779 ? 146.624 84.675  99.335  1.00 125.30 ? 779  ASP A CB    1 
ATOM   6041  C  CG    . ASP A 1 779 ? 147.680 83.641  99.662  1.00 125.21 ? 779  ASP A CG    1 
ATOM   6042  O  OD1   . ASP A 1 779 ? 147.389 82.432  99.546  1.00 124.99 ? 779  ASP A OD1   1 
ATOM   6043  O  OD2   . ASP A 1 779 ? 148.805 84.037  100.033 1.00 125.11 ? 779  ASP A OD2   1 
ATOM   6044  N  N     . ALA A 1 780 ? 143.984 84.472  101.120 1.00 126.55 ? 780  ALA A N     1 
ATOM   6045  C  CA    . ALA A 1 780 ? 143.293 84.074  102.341 1.00 127.37 ? 780  ALA A CA    1 
ATOM   6046  C  C     . ALA A 1 780 ? 142.153 83.111  102.041 1.00 128.00 ? 780  ALA A C     1 
ATOM   6047  O  O     . ALA A 1 780 ? 141.941 82.140  102.776 1.00 129.00 ? 780  ALA A O     1 
ATOM   6048  C  CB    . ALA A 1 780 ? 142.775 85.310  103.077 1.00 127.54 ? 780  ALA A CB    1 
ATOM   6049  N  N     . GLU A 1 781 ? 141.403 83.366  100.967 1.00 126.17 ? 781  GLU A N     1 
ATOM   6050  C  CA    . GLU A 1 781 ? 140.327 82.460  100.581 1.00 126.37 ? 781  GLU A CA    1 
ATOM   6051  C  C     . GLU A 1 781 ? 140.875 81.103  100.161 1.00 126.88 ? 781  GLU A C     1 
ATOM   6052  O  O     . GLU A 1 781 ? 140.278 80.064  100.465 1.00 126.45 ? 781  GLU A O     1 
ATOM   6053  C  CB    . GLU A 1 781 ? 139.498 83.080  99.456  1.00 126.66 ? 781  GLU A CB    1 
ATOM   6054  C  CG    . GLU A 1 781 ? 138.282 82.260  99.050  1.00 126.70 ? 781  GLU A CG    1 
ATOM   6055  C  CD    . GLU A 1 781 ? 137.210 82.229  100.123 1.00 126.46 ? 781  GLU A CD    1 
ATOM   6056  O  OE1   . GLU A 1 781 ? 137.164 83.163  100.952 1.00 126.28 ? 781  GLU A OE1   1 
ATOM   6057  O  OE2   . GLU A 1 781 ? 136.411 81.270  100.137 1.00 126.29 ? 781  GLU A OE2   1 
ATOM   6058  N  N     . LYS A 1 782 ? 142.007 81.096  99.452  1.00 129.19 ? 782  LYS A N     1 
ATOM   6059  C  CA    . LYS A 1 782 ? 142.642 79.836  99.082  1.00 129.30 ? 782  LYS A CA    1 
ATOM   6060  C  C     . LYS A 1 782 ? 143.070 79.055  100.318 1.00 129.45 ? 782  LYS A C     1 
ATOM   6061  O  O     . LYS A 1 782 ? 142.871 77.836  100.393 1.00 129.26 ? 782  LYS A O     1 
ATOM   6062  C  CB    . LYS A 1 782 ? 143.839 80.102  98.171  1.00 128.50 ? 782  LYS A CB    1 
ATOM   6063  C  CG    . LYS A 1 782 ? 144.595 78.853  97.756  1.00 128.93 ? 782  LYS A CG    1 
ATOM   6064  C  CD    . LYS A 1 782 ? 145.783 79.197  96.872  1.00 128.68 ? 782  LYS A CD    1 
ATOM   6065  C  CE    . LYS A 1 782 ? 146.547 77.948  96.464  1.00 128.79 ? 782  LYS A CE    1 
ATOM   6066  N  NZ    . LYS A 1 782 ? 147.715 78.269  95.598  1.00 128.83 ? 782  LYS A NZ    1 
ATOM   6067  N  N     . PHE A 1 783 ? 143.650 79.745  101.303 1.00 127.54 ? 783  PHE A N     1 
ATOM   6068  C  CA    . PHE A 1 783 ? 144.026 79.090  102.552 1.00 127.74 ? 783  PHE A CA    1 
ATOM   6069  C  C     . PHE A 1 783 ? 142.806 78.537  103.277 1.00 128.07 ? 783  PHE A C     1 
ATOM   6070  O  O     . PHE A 1 783 ? 142.844 77.422  103.811 1.00 128.18 ? 783  PHE A O     1 
ATOM   6071  C  CB    . PHE A 1 783 ? 144.783 80.070  103.448 1.00 128.09 ? 783  PHE A CB    1 
ATOM   6072  C  CG    . PHE A 1 783 ? 145.161 79.505  104.791 1.00 128.44 ? 783  PHE A CG    1 
ATOM   6073  C  CD1   . PHE A 1 783 ? 146.350 78.818  104.957 1.00 128.57 ? 783  PHE A CD1   1 
ATOM   6074  C  CD2   . PHE A 1 783 ? 144.336 79.677  105.891 1.00 127.71 ? 783  PHE A CD2   1 
ATOM   6075  C  CE1   . PHE A 1 783 ? 146.703 78.305  106.190 1.00 128.26 ? 783  PHE A CE1   1 
ATOM   6076  C  CE2   . PHE A 1 783 ? 144.683 79.163  107.123 1.00 127.73 ? 783  PHE A CE2   1 
ATOM   6077  C  CZ    . PHE A 1 783 ? 145.867 78.479  107.274 1.00 127.70 ? 783  PHE A CZ    1 
ATOM   6078  N  N     . LEU A 1 784 ? 141.718 79.308  103.319 1.00 130.13 ? 784  LEU A N     1 
ATOM   6079  C  CA    . LEU A 1 784 ? 140.523 78.872  104.036 1.00 130.33 ? 784  LEU A CA    1 
ATOM   6080  C  C     . LEU A 1 784 ? 139.871 77.672  103.362 1.00 131.03 ? 784  LEU A C     1 
ATOM   6081  O  O     . LEU A 1 784 ? 139.415 76.746  104.042 1.00 130.38 ? 784  LEU A O     1 
ATOM   6082  C  CB    . LEU A 1 784 ? 139.528 80.025  104.147 1.00 130.07 ? 784  LEU A CB    1 
ATOM   6083  C  CG    . LEU A 1 784 ? 138.179 79.687  104.785 1.00 130.26 ? 784  LEU A CG    1 
ATOM   6084  C  CD1   . LEU A 1 784 ? 138.369 79.186  106.208 1.00 130.33 ? 784  LEU A CD1   1 
ATOM   6085  C  CD2   . LEU A 1 784 ? 137.253 80.891  104.755 1.00 130.21 ? 784  LEU A CD2   1 
ATOM   6086  N  N     . GLU A 1 785 ? 139.809 77.670  102.031 1.00 129.28 ? 785  GLU A N     1 
ATOM   6087  C  CA    . GLU A 1 785 ? 139.156 76.572  101.327 1.00 128.51 ? 785  GLU A CA    1 
ATOM   6088  C  C     . GLU A 1 785 ? 140.024 75.319  101.301 1.00 127.87 ? 785  GLU A C     1 
ATOM   6089  O  O     . GLU A 1 785 ? 139.504 74.201  101.392 1.00 127.33 ? 785  GLU A O     1 
ATOM   6090  C  CB    . GLU A 1 785 ? 138.794 77.002  99.904  1.00 128.05 ? 785  GLU A CB    1 
ATOM   6091  C  CG    . GLU A 1 785 ? 138.053 75.942  99.105  1.00 128.05 ? 785  GLU A CG    1 
ATOM   6092  C  CD    . GLU A 1 785 ? 136.747 75.526  99.755  1.00 128.16 ? 785  GLU A CD    1 
ATOM   6093  O  OE1   . GLU A 1 785 ? 136.057 76.398  100.324 1.00 128.09 ? 785  GLU A OE1   1 
ATOM   6094  O  OE2   . GLU A 1 785 ? 136.412 74.325  99.701  1.00 128.55 ? 785  GLU A OE2   1 
ATOM   6095  N  N     . GLU A 1 786 ? 141.344 75.485  101.177 1.00 129.04 ? 786  GLU A N     1 
ATOM   6096  C  CA    . GLU A 1 786 ? 142.231 74.331  101.063 1.00 129.06 ? 786  GLU A CA    1 
ATOM   6097  C  C     . GLU A 1 786 ? 142.233 73.493  102.336 1.00 129.00 ? 786  GLU A C     1 
ATOM   6098  O  O     . GLU A 1 786 ? 142.223 72.258  102.271 1.00 128.49 ? 786  GLU A O     1 
ATOM   6099  C  CB    . GLU A 1 786 ? 143.647 74.797  100.726 1.00 129.05 ? 786  GLU A CB    1 
ATOM   6100  C  CG    . GLU A 1 786 ? 144.656 73.671  100.579 1.00 128.89 ? 786  GLU A CG    1 
ATOM   6101  C  CD    . GLU A 1 786 ? 146.049 74.177  100.264 1.00 129.40 ? 786  GLU A CD    1 
ATOM   6102  O  OE1   . GLU A 1 786 ? 146.223 75.408  100.147 1.00 129.04 ? 786  GLU A OE1   1 
ATOM   6103  O  OE2   . GLU A 1 786 ? 146.970 73.343  100.134 1.00 129.18 ? 786  GLU A OE2   1 
ATOM   6104  N  N     . LYS A 1 787 ? 142.241 74.137  103.497 1.00 130.58 ? 787  LYS A N     1 
ATOM   6105  C  CA    . LYS A 1 787 ? 142.349 73.446  104.772 1.00 130.43 ? 787  LYS A CA    1 
ATOM   6106  C  C     . LYS A 1 787 ? 141.019 73.474  105.511 1.00 130.86 ? 787  LYS A C     1 
ATOM   6107  O  O     . LYS A 1 787 ? 140.199 74.375  105.318 1.00 131.53 ? 787  LYS A O     1 
ATOM   6108  C  CB    . LYS A 1 787 ? 143.438 74.074  105.644 1.00 129.59 ? 787  LYS A CB    1 
ATOM   6109  C  CG    . LYS A 1 787 ? 144.789 74.165  104.965 1.00 129.86 ? 787  LYS A CG    1 
ATOM   6110  C  CD    . LYS A 1 787 ? 145.822 74.793  105.876 1.00 130.38 ? 787  LYS A CD    1 
ATOM   6111  C  CE    . LYS A 1 787 ? 147.159 74.918  105.172 1.00 130.09 ? 787  LYS A CE    1 
ATOM   6112  N  NZ    . LYS A 1 787 ? 147.660 73.597  104.705 1.00 130.27 ? 787  LYS A NZ    1 
ATOM   6113  N  N     . GLU A 1 788 ? 140.812 72.472  106.358 1.00 130.54 ? 788  GLU A N     1 
ATOM   6114  C  CA    . GLU A 1 788 ? 139.625 72.407  107.211 1.00 131.53 ? 788  GLU A CA    1 
ATOM   6115  C  C     . GLU A 1 788 ? 139.930 73.000  108.586 1.00 131.61 ? 788  GLU A C     1 
ATOM   6116  O  O     . GLU A 1 788 ? 139.914 72.321  109.613 1.00 130.98 ? 788  GLU A O     1 
ATOM   6117  C  CB    . GLU A 1 788 ? 139.131 70.968  107.320 1.00 130.55 ? 788  GLU A CB    1 
ATOM   6118  C  CG    . GLU A 1 788 ? 138.771 70.335  105.987 1.00 130.31 ? 788  GLU A CG    1 
ATOM   6119  C  CD    . GLU A 1 788 ? 137.586 71.007  105.319 1.00 130.57 ? 788  GLU A CD    1 
ATOM   6120  O  OE1   . GLU A 1 788 ? 136.714 71.537  106.040 1.00 130.45 ? 788  GLU A OE1   1 
ATOM   6121  O  OE2   . GLU A 1 788 ? 137.528 71.007  104.072 1.00 130.37 ? 788  GLU A OE2   1 
ATOM   6122  N  N     . CYS A 1 789 ? 140.215 74.299  108.584 1.00 126.95 ? 789  CYS A N     1 
ATOM   6123  C  CA    . CYS A 1 789 ? 140.578 74.995  109.808 1.00 126.32 ? 789  CYS A CA    1 
ATOM   6124  C  C     . CYS A 1 789 ? 139.369 75.158  110.719 1.00 126.40 ? 789  CYS A C     1 
ATOM   6125  O  O     . CYS A 1 789 ? 138.220 75.171  110.270 1.00 126.83 ? 789  CYS A O     1 
ATOM   6126  C  CB    . CYS A 1 789 ? 141.166 76.368  109.486 1.00 126.41 ? 789  CYS A CB    1 
ATOM   6127  S  SG    . CYS A 1 789 ? 142.527 76.347  108.301 1.00 130.65 ? 789  CYS A SG    1 
ATOM   6128  N  N     . ALA A 1 790 ? 139.640 75.282  112.014 1.00 119.01 ? 790  ALA A N     1 
ATOM   6129  C  CA    . ALA A 1 790 ? 138.588 75.562  112.975 1.00 118.71 ? 790  ALA A CA    1 
ATOM   6130  C  C     . ALA A 1 790 ? 138.294 77.056  113.011 1.00 118.40 ? 790  ALA A C     1 
ATOM   6131  O  O     . ALA A 1 790 ? 139.100 77.886  112.583 1.00 117.75 ? 790  ALA A O     1 
ATOM   6132  C  CB    . ALA A 1 790 ? 138.979 75.067  114.366 1.00 117.37 ? 790  ALA A CB    1 
ATOM   6133  N  N     . LEU A 1 791 ? 137.122 77.396  113.536 1.00 110.12 ? 791  LEU A N     1 
ATOM   6134  C  CA    . LEU A 1 791 ? 136.645 78.774  113.562 1.00 109.59 ? 791  LEU A CA    1 
ATOM   6135  C  C     . LEU A 1 791 ? 136.812 79.332  114.973 1.00 109.05 ? 791  LEU A C     1 
ATOM   6136  O  O     . LEU A 1 791 ? 136.083 78.945  115.892 1.00 107.81 ? 791  LEU A O     1 
ATOM   6137  C  CB    . LEU A 1 791 ? 135.191 78.841  113.103 1.00 109.13 ? 791  LEU A CB    1 
ATOM   6138  C  CG    . LEU A 1 791 ? 134.713 80.160  112.498 1.00 109.43 ? 791  LEU A CG    1 
ATOM   6139  C  CD1   . LEU A 1 791 ? 135.636 80.597  111.372 1.00 107.81 ? 791  LEU A CD1   1 
ATOM   6140  C  CD2   . LEU A 1 791 ? 133.282 80.016  112.000 1.00 108.57 ? 791  LEU A CD2   1 
ATOM   6141  N  N     . ILE A 1 792 ? 137.767 80.246  115.138 1.00 106.25 ? 792  ILE A N     1 
ATOM   6142  C  CA    . ILE A 1 792 ? 138.064 80.876  116.420 1.00 106.08 ? 792  ILE A CA    1 
ATOM   6143  C  C     . ILE A 1 792 ? 137.595 82.322  116.358 1.00 106.82 ? 792  ILE A C     1 
ATOM   6144  O  O     . ILE A 1 792 ? 137.903 83.040  115.400 1.00 107.35 ? 792  ILE A O     1 
ATOM   6145  C  CB    . ILE A 1 792 ? 139.563 80.796  116.753 1.00 107.00 ? 792  ILE A CB    1 
ATOM   6146  C  CG1   . ILE A 1 792 ? 140.028 79.342  116.748 1.00 107.46 ? 792  ILE A CG1   1 
ATOM   6147  C  CG2   . ILE A 1 792 ? 139.845 81.429  118.103 1.00 106.24 ? 792  ILE A CG2   1 
ATOM   6148  C  CD1   . ILE A 1 792 ? 139.252 78.462  117.689 1.00 106.35 ? 792  ILE A CD1   1 
ATOM   6149  N  N     . LEU A 1 793 ? 136.847 82.747  117.373 1.00 94.36  ? 793  LEU A N     1 
ATOM   6150  C  CA    . LEU A 1 793 ? 136.195 84.052  117.387 1.00 92.67  ? 793  LEU A CA    1 
ATOM   6151  C  C     . LEU A 1 793 ? 136.783 84.911  118.499 1.00 91.58  ? 793  LEU A C     1 
ATOM   6152  O  O     . LEU A 1 793 ? 136.803 84.497  119.662 1.00 92.47  ? 793  LEU A O     1 
ATOM   6153  C  CB    . LEU A 1 793 ? 134.685 83.899  117.574 1.00 90.00  ? 793  LEU A CB    1 
ATOM   6154  C  CG    . LEU A 1 793 ? 133.780 83.783  116.343 1.00 89.70  ? 793  LEU A CG    1 
ATOM   6155  C  CD1   . LEU A 1 793 ? 134.317 82.797  115.326 1.00 90.78  ? 793  LEU A CD1   1 
ATOM   6156  C  CD2   . LEU A 1 793 ? 132.378 83.383  116.763 1.00 89.13  ? 793  LEU A CD2   1 
ATOM   6157  N  N     . THR A 1 794 ? 137.259 86.099  118.142 1.00 88.42  ? 794  THR A N     1 
ATOM   6158  C  CA    . THR A 1 794 ? 137.645 87.084  119.138 1.00 90.21  ? 794  THR A CA    1 
ATOM   6159  C  C     . THR A 1 794 ? 136.404 87.811  119.649 1.00 91.18  ? 794  THR A C     1 
ATOM   6160  O  O     . THR A 1 794 ? 135.387 87.883  118.955 1.00 91.84  ? 794  THR A O     1 
ATOM   6161  C  CB    . THR A 1 794 ? 138.644 88.072  118.545 1.00 91.95  ? 794  THR A CB    1 
ATOM   6162  O  OG1   . THR A 1 794 ? 138.057 88.730  117.416 1.00 94.31  ? 794  THR A OG1   1 
ATOM   6163  C  CG2   . THR A 1 794 ? 139.903 87.348  118.110 1.00 91.41  ? 794  THR A CG2   1 
ATOM   6164  N  N     . PRO A 1 795 ? 136.452 88.360  120.871 1.00 81.73  ? 795  PRO A N     1 
ATOM   6165  C  CA    . PRO A 1 795 ? 135.233 88.930  121.460 1.00 79.65  ? 795  PRO A CA    1 
ATOM   6166  C  C     . PRO A 1 795 ? 134.926 90.339  120.974 1.00 82.68  ? 795  PRO A C     1 
ATOM   6167  O  O     . PRO A 1 795 ? 134.137 91.054  121.600 1.00 85.31  ? 795  PRO A O     1 
ATOM   6168  C  CB    . PRO A 1 795 ? 135.532 88.918  122.966 1.00 80.59  ? 795  PRO A CB    1 
ATOM   6169  C  CG    . PRO A 1 795 ? 136.822 88.154  123.128 1.00 82.38  ? 795  PRO A CG    1 
ATOM   6170  C  CD    . PRO A 1 795 ? 137.550 88.341  121.849 1.00 83.45  ? 795  PRO A CD    1 
ATOM   6171  N  N     . SER A 1 796 ? 135.540 90.752  119.865 1.00 77.11  ? 796  SER A N     1 
ATOM   6172  C  CA    . SER A 1 796 ? 135.333 92.078  119.298 1.00 75.73  ? 796  SER A CA    1 
ATOM   6173  C  C     . SER A 1 796 ? 134.302 92.069  118.174 1.00 70.77  ? 796  SER A C     1 
ATOM   6174  O  O     . SER A 1 796 ? 134.426 92.830  117.210 1.00 71.66  ? 796  SER A O     1 
ATOM   6175  C  CB    . SER A 1 796 ? 136.658 92.656  118.804 1.00 75.20  ? 796  SER A CB    1 
ATOM   6176  O  OG    . SER A 1 796 ? 137.573 92.812  119.875 1.00 73.86  ? 796  SER A OG    1 
ATOM   6177  N  N     . LEU A 1 797 ? 133.291 91.210  118.278 1.00 71.80  ? 797  LEU A N     1 
ATOM   6178  C  CA    . LEU A 1 797 ? 132.246 91.088  117.272 1.00 75.06  ? 797  LEU A CA    1 
ATOM   6179  C  C     . LEU A 1 797 ? 130.883 91.162  117.944 1.00 75.32  ? 797  LEU A C     1 
ATOM   6180  O  O     . LEU A 1 797 ? 130.696 90.633  119.042 1.00 76.79  ? 797  LEU A O     1 
ATOM   6181  C  CB    . LEU A 1 797 ? 132.370 89.770  116.490 1.00 79.15  ? 797  LEU A CB    1 
ATOM   6182  C  CG    . LEU A 1 797 ? 133.478 89.642  115.438 1.00 78.19  ? 797  LEU A CG    1 
ATOM   6183  C  CD1   . LEU A 1 797 ? 134.831 89.334  116.063 1.00 75.91  ? 797  LEU A CD1   1 
ATOM   6184  C  CD2   . LEU A 1 797 ? 133.111 88.585  114.410 1.00 78.64  ? 797  LEU A CD2   1 
ATOM   6185  N  N     . THR A 1 798 ? 129.931 91.810  117.277 1.00 73.94  ? 798  THR A N     1 
ATOM   6186  C  CA    . THR A 1 798 ? 128.596 91.960  117.835 1.00 71.53  ? 798  THR A CA    1 
ATOM   6187  C  C     . THR A 1 798 ? 127.860 90.623  117.838 1.00 75.78  ? 798  THR A C     1 
ATOM   6188  O  O     . THR A 1 798 ? 128.324 89.622  117.288 1.00 80.95  ? 798  THR A O     1 
ATOM   6189  C  CB    . THR A 1 798 ? 127.794 92.998  117.054 1.00 72.96  ? 798  THR A CB    1 
ATOM   6190  O  OG1   . THR A 1 798 ? 127.860 92.702  115.654 1.00 77.11  ? 798  THR A OG1   1 
ATOM   6191  C  CG2   . THR A 1 798 ? 128.340 94.392  117.307 1.00 75.63  ? 798  THR A CG2   1 
ATOM   6192  N  N     . ASN A 1 799 ? 126.684 90.622  118.471 1.00 72.49  ? 799  ASN A N     1 
ATOM   6193  C  CA    . ASN A 1 799 ? 125.929 89.384  118.642 1.00 75.38  ? 799  ASN A CA    1 
ATOM   6194  C  C     . ASN A 1 799 ? 125.462 88.819  117.306 1.00 79.50  ? 799  ASN A C     1 
ATOM   6195  O  O     . ASN A 1 799 ? 125.452 87.597  117.115 1.00 81.04  ? 799  ASN A O     1 
ATOM   6196  C  CB    . ASN A 1 799 ? 124.739 89.620  119.570 1.00 74.51  ? 799  ASN A CB    1 
ATOM   6197  C  CG    . ASN A 1 799 ? 125.158 89.869  121.004 1.00 73.03  ? 799  ASN A CG    1 
ATOM   6198  O  OD1   . ASN A 1 799 ? 126.310 90.204  121.277 1.00 68.74  ? 799  ASN A OD1   1 
ATOM   6199  N  ND2   . ASN A 1 799 ? 124.221 89.710  121.929 1.00 74.14  ? 799  ASN A ND2   1 
ATOM   6200  N  N     . GLU A 1 800 ? 125.061 89.686  116.375 1.00 87.56  ? 800  GLU A N     1 
ATOM   6201  C  CA    . GLU A 1 800 ? 124.600 89.208  115.075 1.00 87.21  ? 800  GLU A CA    1 
ATOM   6202  C  C     . GLU A 1 800 ? 125.725 88.535  114.300 1.00 86.26  ? 800  GLU A C     1 
ATOM   6203  O  O     . GLU A 1 800 ? 125.506 87.515  113.638 1.00 87.69  ? 800  GLU A O     1 
ATOM   6204  C  CB    . GLU A 1 800 ? 124.005 90.361  114.270 1.00 88.42  ? 800  GLU A CB    1 
ATOM   6205  C  CG    . GLU A 1 800 ? 123.152 89.911  113.101 1.00 88.12  ? 800  GLU A CG    1 
ATOM   6206  C  CD    . GLU A 1 800 ? 121.883 89.212  113.543 1.00 89.28  ? 800  GLU A CD    1 
ATOM   6207  O  OE1   . GLU A 1 800 ? 121.415 89.477  114.670 1.00 89.08  ? 800  GLU A OE1   1 
ATOM   6208  O  OE2   . GLU A 1 800 ? 121.352 88.394  112.764 1.00 88.11  ? 800  GLU A OE2   1 
ATOM   6209  N  N     . GLU A 1 801 ? 126.937 89.090  114.373 1.00 85.53  ? 801  GLU A N     1 
ATOM   6210  C  CA    . GLU A 1 801 ? 128.084 88.455  113.732 1.00 83.82  ? 801  GLU A CA    1 
ATOM   6211  C  C     . GLU A 1 801 ? 128.374 87.090  114.344 1.00 86.08  ? 801  GLU A C     1 
ATOM   6212  O  O     . GLU A 1 801 ? 128.664 86.127  113.622 1.00 88.12  ? 801  GLU A O     1 
ATOM   6213  C  CB    . GLU A 1 801 ? 129.308 89.364  113.832 1.00 83.24  ? 801  GLU A CB    1 
ATOM   6214  C  CG    . GLU A 1 801 ? 129.161 90.671  113.072 1.00 85.73  ? 801  GLU A CG    1 
ATOM   6215  C  CD    . GLU A 1 801 ? 130.422 91.511  113.093 1.00 87.07  ? 801  GLU A CD    1 
ATOM   6216  O  OE1   . GLU A 1 801 ? 131.097 91.546  114.140 1.00 86.86  ? 801  GLU A OE1   1 
ATOM   6217  O  OE2   . GLU A 1 801 ? 130.742 92.135  112.061 1.00 84.95  ? 801  GLU A OE2   1 
ATOM   6218  N  N     . ILE A 1 802 ? 128.299 86.986  115.674 1.00 90.13  ? 802  ILE A N     1 
ATOM   6219  C  CA    . ILE A 1 802 ? 128.537 85.706  116.338 1.00 92.09  ? 802  ILE A CA    1 
ATOM   6220  C  C     . ILE A 1 802 ? 127.497 84.682  115.906 1.00 92.01  ? 802  ILE A C     1 
ATOM   6221  O  O     . ILE A 1 802 ? 127.828 83.527  115.608 1.00 92.67  ? 802  ILE A O     1 
ATOM   6222  C  CB    . ILE A 1 802 ? 128.549 85.883  117.868 1.00 90.59  ? 802  ILE A CB    1 
ATOM   6223  C  CG1   . ILE A 1 802 ? 129.586 86.925  118.285 1.00 87.96  ? 802  ILE A CG1   1 
ATOM   6224  C  CG2   . ILE A 1 802 ? 128.843 84.562  118.551 1.00 91.25  ? 802  ILE A CG2   1 
ATOM   6225  C  CD1   . ILE A 1 802 ? 130.995 86.595  117.865 1.00 90.59  ? 802  ILE A CD1   1 
ATOM   6226  N  N     . MET A 1 803 ? 126.225 85.088  115.861 1.00 94.80  ? 803  MET A N     1 
ATOM   6227  C  CA    . MET A 1 803 ? 125.174 84.171  115.435 1.00 97.28  ? 803  MET A CA    1 
ATOM   6228  C  C     . MET A 1 803 ? 125.365 83.741  113.986 1.00 99.43  ? 803  MET A C     1 
ATOM   6229  O  O     . MET A 1 803 ? 125.148 82.573  113.646 1.00 100.08 ? 803  MET A O     1 
ATOM   6230  C  CB    . MET A 1 803 ? 123.800 84.810  115.625 1.00 96.01  ? 803  MET A CB    1 
ATOM   6231  C  CG    . MET A 1 803 ? 123.402 85.007  117.074 1.00 97.31  ? 803  MET A CG    1 
ATOM   6232  S  SD    . MET A 1 803 ? 121.620 85.184  117.273 1.00 102.74 ? 803  MET A SD    1 
ATOM   6233  C  CE    . MET A 1 803 ? 121.269 86.460  116.068 1.00 96.67  ? 803  MET A CE    1 
ATOM   6234  N  N     . PHE A 1 804 ? 125.770 84.670  113.117 1.00 103.38 ? 804  PHE A N     1 
ATOM   6235  C  CA    . PHE A 1 804 ? 125.972 84.327  111.714 1.00 102.55 ? 804  PHE A CA    1 
ATOM   6236  C  C     . PHE A 1 804 ? 127.115 83.332  111.549 1.00 103.00 ? 804  PHE A C     1 
ATOM   6237  O  O     . PHE A 1 804 ? 126.992 82.345  110.813 1.00 105.34 ? 804  PHE A O     1 
ATOM   6238  C  CB    . PHE A 1 804 ? 126.235 85.592  110.901 1.00 103.67 ? 804  PHE A CB    1 
ATOM   6239  C  CG    . PHE A 1 804 ? 126.171 85.382  109.420 1.00 104.78 ? 804  PHE A CG    1 
ATOM   6240  C  CD1   . PHE A 1 804 ? 124.951 85.289  108.775 1.00 103.66 ? 804  PHE A CD1   1 
ATOM   6241  C  CD2   . PHE A 1 804 ? 127.329 85.283  108.671 1.00 104.62 ? 804  PHE A CD2   1 
ATOM   6242  C  CE1   . PHE A 1 804 ? 124.888 85.098  107.412 1.00 103.42 ? 804  PHE A CE1   1 
ATOM   6243  C  CE2   . PHE A 1 804 ? 127.272 85.094  107.309 1.00 104.89 ? 804  PHE A CE2   1 
ATOM   6244  C  CZ    . PHE A 1 804 ? 126.050 85.000  106.678 1.00 104.39 ? 804  PHE A CZ    1 
ATOM   6245  N  N     . LEU A 1 805 ? 128.232 83.570  112.239 1.00 99.86  ? 805  LEU A N     1 
ATOM   6246  C  CA    . LEU A 1 805 ? 129.360 82.647  112.152 1.00 100.80 ? 805  LEU A CA    1 
ATOM   6247  C  C     . LEU A 1 805 ? 129.005 81.279  112.726 1.00 102.02 ? 805  LEU A C     1 
ATOM   6248  O  O     . LEU A 1 805 ? 129.384 80.244  112.163 1.00 102.43 ? 805  LEU A O     1 
ATOM   6249  C  CB    . LEU A 1 805 ? 130.571 83.241  112.865 1.00 101.37 ? 805  LEU A CB    1 
ATOM   6250  C  CG    . LEU A 1 805 ? 131.061 84.564  112.273 1.00 101.07 ? 805  LEU A CG    1 
ATOM   6251  C  CD1   . LEU A 1 805 ? 131.996 85.268  113.233 1.00 101.21 ? 805  LEU A CD1   1 
ATOM   6252  C  CD2   . LEU A 1 805 ? 131.735 84.344  110.931 1.00 100.98 ? 805  LEU A CD2   1 
ATOM   6253  N  N     . LYS A 1 806 ? 128.263 81.252  113.837 1.00 105.50 ? 806  LYS A N     1 
ATOM   6254  C  CA    . LYS A 1 806 ? 127.864 79.980  114.430 1.00 105.42 ? 806  LYS A CA    1 
ATOM   6255  C  C     . LYS A 1 806 ? 126.918 79.207  113.517 1.00 105.99 ? 806  LYS A C     1 
ATOM   6256  O  O     . LYS A 1 806 ? 127.058 77.989  113.362 1.00 106.63 ? 806  LYS A O     1 
ATOM   6257  C  CB    . LYS A 1 806 ? 127.219 80.219  115.793 1.00 104.88 ? 806  LYS A CB    1 
ATOM   6258  C  CG    . LYS A 1 806 ? 126.907 78.948  116.558 1.00 106.00 ? 806  LYS A CG    1 
ATOM   6259  C  CD    . LYS A 1 806 ? 126.190 79.252  117.861 1.00 106.06 ? 806  LYS A CD    1 
ATOM   6260  C  CE    . LYS A 1 806 ? 124.892 80.004  117.613 1.00 106.39 ? 806  LYS A CE    1 
ATOM   6261  N  NZ    . LYS A 1 806 ? 123.974 79.252  116.716 1.00 106.56 ? 806  LYS A NZ    1 
ATOM   6262  N  N     . GLU A 1 807 ? 125.949 79.894  112.906 1.00 108.67 ? 807  GLU A N     1 
ATOM   6263  C  CA    . GLU A 1 807 ? 125.026 79.222  111.996 1.00 109.93 ? 807  GLU A CA    1 
ATOM   6264  C  C     . GLU A 1 807 ? 125.747 78.710  110.754 1.00 109.05 ? 807  GLU A C     1 
ATOM   6265  O  O     . GLU A 1 807 ? 125.440 77.618  110.258 1.00 108.71 ? 807  GLU A O     1 
ATOM   6266  C  CB    . GLU A 1 807 ? 123.887 80.168  111.617 1.00 110.20 ? 807  GLU A CB    1 
ATOM   6267  C  CG    . GLU A 1 807 ? 122.691 79.488  110.971 1.00 109.15 ? 807  GLU A CG    1 
ATOM   6268  C  CD    . GLU A 1 807 ? 122.813 79.388  109.465 1.00 109.48 ? 807  GLU A CD    1 
ATOM   6269  O  OE1   . GLU A 1 807 ? 123.688 80.067  108.890 1.00 109.25 ? 807  GLU A OE1   1 
ATOM   6270  O  OE2   . GLU A 1 807 ? 122.032 78.629  108.855 1.00 109.03 ? 807  GLU A OE2   1 
ATOM   6271  N  N     . LEU A 1 808 ? 126.702 79.487  110.233 1.00 112.07 ? 808  LEU A N     1 
ATOM   6272  C  CA    . LEU A 1 808 ? 127.497 79.014  109.104 1.00 111.86 ? 808  LEU A CA    1 
ATOM   6273  C  C     . LEU A 1 808 ? 128.298 77.775  109.474 1.00 113.03 ? 808  LEU A C     1 
ATOM   6274  O  O     . LEU A 1 808 ? 128.365 76.817  108.697 1.00 114.11 ? 808  LEU A O     1 
ATOM   6275  C  CB    . LEU A 1 808 ? 128.433 80.116  108.612 1.00 113.38 ? 808  LEU A CB    1 
ATOM   6276  C  CG    . LEU A 1 808 ? 127.866 81.120  107.612 1.00 114.08 ? 808  LEU A CG    1 
ATOM   6277  C  CD1   . LEU A 1 808 ? 128.982 82.002  107.079 1.00 112.82 ? 808  LEU A CD1   1 
ATOM   6278  C  CD2   . LEU A 1 808 ? 127.160 80.398  106.478 1.00 113.18 ? 808  LEU A CD2   1 
ATOM   6279  N  N     . ALA A 1 809 ? 128.915 77.774  110.659 1.00 112.99 ? 809  ALA A N     1 
ATOM   6280  C  CA    . ALA A 1 809 ? 129.679 76.607  111.087 1.00 113.22 ? 809  ALA A CA    1 
ATOM   6281  C  C     . ALA A 1 809 ? 128.774 75.397  111.275 1.00 112.22 ? 809  ALA A C     1 
ATOM   6282  O  O     . ALA A 1 809 ? 129.169 74.264  110.977 1.00 110.34 ? 809  ALA A O     1 
ATOM   6283  C  CB    . ALA A 1 809 ? 130.437 76.919  112.376 1.00 113.17 ? 809  ALA A CB    1 
ATOM   6284  N  N     . GLU A 1 810 ? 127.557 75.619  111.774 1.00 112.04 ? 810  GLU A N     1 
ATOM   6285  C  CA    . GLU A 1 810 ? 126.623 74.517  111.972 1.00 112.43 ? 810  GLU A CA    1 
ATOM   6286  C  C     . GLU A 1 810 ? 126.189 73.911  110.643 1.00 112.45 ? 810  GLU A C     1 
ATOM   6287  O  O     . GLU A 1 810 ? 126.226 72.687  110.468 1.00 112.38 ? 810  GLU A O     1 
ATOM   6288  C  CB    . GLU A 1 810 ? 125.407 74.996  112.763 1.00 111.85 ? 810  GLU A CB    1 
ATOM   6289  C  CG    . GLU A 1 810 ? 124.294 73.967  112.864 1.00 111.79 ? 810  GLU A CG    1 
ATOM   6290  C  CD    . GLU A 1 810 ? 123.077 74.495  113.596 1.00 112.31 ? 810  GLU A CD    1 
ATOM   6291  O  OE1   . GLU A 1 810 ? 123.105 75.664  114.034 1.00 113.16 ? 810  GLU A OE1   1 
ATOM   6292  O  OE2   . GLU A 1 810 ? 122.091 73.740  113.732 1.00 111.65 ? 810  GLU A OE2   1 
ATOM   6293  N  N     . ARG A 1 811 ? 125.775 74.749  109.690 1.00 112.28 ? 811  ARG A N     1 
ATOM   6294  C  CA    . ARG A 1 811 ? 125.283 74.217  108.424 1.00 111.81 ? 811  ARG A CA    1 
ATOM   6295  C  C     . ARG A 1 811 ? 126.404 73.746  107.505 1.00 112.00 ? 811  ARG A C     1 
ATOM   6296  O  O     . ARG A 1 811 ? 126.144 72.960  106.588 1.00 111.89 ? 811  ARG A O     1 
ATOM   6297  C  CB    . ARG A 1 811 ? 124.414 75.253  107.705 1.00 111.74 ? 811  ARG A CB    1 
ATOM   6298  C  CG    . ARG A 1 811 ? 125.082 75.956  106.537 1.00 110.81 ? 811  ARG A CG    1 
ATOM   6299  C  CD    . ARG A 1 811 ? 124.051 76.384  105.510 1.00 111.98 ? 811  ARG A CD    1 
ATOM   6300  N  NE    . ARG A 1 811 ? 124.658 77.076  104.380 1.00 111.59 ? 811  ARG A NE    1 
ATOM   6301  C  CZ    . ARG A 1 811 ? 124.739 78.394  104.266 1.00 111.30 ? 811  ARG A CZ    1 
ATOM   6302  N  NH1   . ARG A 1 811 ? 124.253 79.199  105.196 1.00 111.07 ? 811  ARG A NH1   1 
ATOM   6303  N  NH2   . ARG A 1 811 ? 125.321 78.918  103.191 1.00 111.35 ? 811  ARG A NH2   1 
ATOM   6304  N  N     . LYS A 1 812 ? 127.639 74.192  107.730 1.00 113.59 ? 812  LYS A N     1 
ATOM   6305  C  CA    . LYS A 1 812 ? 128.784 73.734  106.957 1.00 113.26 ? 812  LYS A CA    1 
ATOM   6306  C  C     . LYS A 1 812 ? 129.611 72.686  107.687 1.00 114.13 ? 812  LYS A C     1 
ATOM   6307  O  O     . LYS A 1 812 ? 130.565 72.159  107.108 1.00 113.62 ? 812  LYS A O     1 
ATOM   6308  C  CB    . LYS A 1 812 ? 129.674 74.920  106.576 1.00 112.85 ? 812  LYS A CB    1 
ATOM   6309  C  CG    . LYS A 1 812 ? 129.031 75.881  105.596 1.00 112.80 ? 812  LYS A CG    1 
ATOM   6310  C  CD    . LYS A 1 812 ? 130.002 76.968  105.176 1.00 113.65 ? 812  LYS A CD    1 
ATOM   6311  C  CE    . LYS A 1 812 ? 129.387 77.878  104.126 1.00 113.29 ? 812  LYS A CE    1 
ATOM   6312  N  NZ    . LYS A 1 812 ? 130.339 78.931  103.678 1.00 113.79 ? 812  LYS A NZ    1 
ATOM   6313  N  N     . GLY A 1 813 ? 129.271 72.370  108.932 1.00 113.98 ? 813  GLY A N     1 
ATOM   6314  C  CA    . GLY A 1 813 ? 129.971 71.332  109.670 1.00 113.67 ? 813  GLY A CA    1 
ATOM   6315  C  C     . GLY A 1 813 ? 131.421 71.628  109.989 1.00 113.78 ? 813  GLY A C     1 
ATOM   6316  O  O     . GLY A 1 813 ? 132.279 70.752  109.817 1.00 113.35 ? 813  GLY A O     1 
ATOM   6317  N  N     . ILE A 1 814 ? 131.718 72.835  110.444 1.00 114.33 ? 814  ILE A N     1 
ATOM   6318  C  CA    . ILE A 1 814 ? 133.065 73.235  110.846 1.00 113.83 ? 814  ILE A CA    1 
ATOM   6319  C  C     . ILE A 1 814 ? 133.064 73.437  112.356 1.00 114.02 ? 814  ILE A C     1 
ATOM   6320  O  O     . ILE A 1 814 ? 132.139 74.067  112.881 1.00 113.71 ? 814  ILE A O     1 
ATOM   6321  C  CB    . ILE A 1 814 ? 133.520 74.520  110.128 1.00 112.86 ? 814  ILE A CB    1 
ATOM   6322  C  CG1   . ILE A 1 814 ? 133.462 74.333  108.612 1.00 112.21 ? 814  ILE A CG1   1 
ATOM   6323  C  CG2   . ILE A 1 814 ? 134.923 74.908  110.554 1.00 111.78 ? 814  ILE A CG2   1 
ATOM   6324  C  CD1   . ILE A 1 814 ? 133.907 75.548  107.835 1.00 111.85 ? 814  ILE A CD1   1 
ATOM   6325  N  N     . PRO A 1 815 ? 134.044 72.905  113.085 1.00 112.29 ? 815  PRO A N     1 
ATOM   6326  C  CA    . PRO A 1 815 ? 134.126 73.185  114.524 1.00 111.54 ? 815  PRO A CA    1 
ATOM   6327  C  C     . PRO A 1 815 ? 134.307 74.674  114.791 1.00 112.50 ? 815  PRO A C     1 
ATOM   6328  O  O     . PRO A 1 815 ? 135.001 75.377  114.054 1.00 112.53 ? 815  PRO A O     1 
ATOM   6329  C  CB    . PRO A 1 815 ? 135.346 72.374  114.976 1.00 111.00 ? 815  PRO A CB    1 
ATOM   6330  C  CG    . PRO A 1 815 ? 136.112 72.085  113.719 1.00 111.85 ? 815  PRO A CG    1 
ATOM   6331  C  CD    . PRO A 1 815 ? 135.082 71.959  112.646 1.00 111.00 ? 815  PRO A CD    1 
ATOM   6332  N  N     . ILE A 1 816 ? 133.675 75.146  115.864 1.00 109.84 ? 816  ILE A N     1 
ATOM   6333  C  CA    . ILE A 1 816 ? 133.581 76.568  116.176 1.00 109.46 ? 816  ILE A CA    1 
ATOM   6334  C  C     . ILE A 1 816 ? 134.134 76.800  117.576 1.00 108.73 ? 816  ILE A C     1 
ATOM   6335  O  O     . ILE A 1 816 ? 133.822 76.046  118.506 1.00 107.63 ? 816  ILE A O     1 
ATOM   6336  C  CB    . ILE A 1 816 ? 132.128 77.070  116.055 1.00 108.09 ? 816  ILE A CB    1 
ATOM   6337  C  CG1   . ILE A 1 816 ? 131.990 78.496  116.592 1.00 108.67 ? 816  ILE A CG1   1 
ATOM   6338  C  CG2   . ILE A 1 816 ? 131.159 76.121  116.752 1.00 107.38 ? 816  ILE A CG2   1 
ATOM   6339  C  CD1   . ILE A 1 816 ? 132.746 79.523  115.787 1.00 108.48 ? 816  ILE A CD1   1 
ATOM   6340  N  N     . GLY A 1 817 ? 134.967 77.830  117.720 1.00 105.19 ? 817  GLY A N     1 
ATOM   6341  C  CA    . GLY A 1 817 ? 135.572 78.148  119.000 1.00 105.84 ? 817  GLY A CA    1 
ATOM   6342  C  C     . GLY A 1 817 ? 135.846 79.626  119.191 1.00 105.09 ? 817  GLY A C     1 
ATOM   6343  O  O     . GLY A 1 817 ? 135.470 80.446  118.349 1.00 105.43 ? 817  GLY A O     1 
ATOM   6344  N  N     . SER A 1 818 ? 136.502 79.981  120.296 1.00 102.87 ? 818  SER A N     1 
ATOM   6345  C  CA    . SER A 1 818 ? 136.793 81.374  120.602 1.00 102.33 ? 818  SER A CA    1 
ATOM   6346  C  C     . SER A 1 818 ? 138.113 81.462  121.350 1.00 103.92 ? 818  SER A C     1 
ATOM   6347  O  O     . SER A 1 818 ? 138.615 80.471  121.886 1.00 105.61 ? 818  SER A O     1 
ATOM   6348  C  CB    . SER A 1 818 ? 135.680 82.018  121.433 1.00 101.09 ? 818  SER A CB    1 
ATOM   6349  O  OG    . SER A 1 818 ? 135.601 81.432  122.719 1.00 101.59 ? 818  SER A OG    1 
ATOM   6350  N  N     . THR A 1 819 ? 138.669 82.674  121.386 1.00 100.44 ? 819  THR A N     1 
ATOM   6351  C  CA    . THR A 1 819 ? 139.946 82.898  122.051 1.00 100.81 ? 819  THR A CA    1 
ATOM   6352  C  C     . THR A 1 819 ? 139.847 82.848  123.569 1.00 101.22 ? 819  THR A C     1 
ATOM   6353  O  O     . THR A 1 819 ? 140.884 82.739  124.232 1.00 101.70 ? 819  THR A O     1 
ATOM   6354  C  CB    . THR A 1 819 ? 140.531 84.246  121.631 1.00 100.17 ? 819  THR A CB    1 
ATOM   6355  O  OG1   . THR A 1 819 ? 141.703 84.522  122.407 1.00 100.40 ? 819  THR A OG1   1 
ATOM   6356  C  CG2   . THR A 1 819 ? 139.524 85.346  121.861 1.00 100.09 ? 819  THR A CG2   1 
ATOM   6357  N  N     . ILE A 1 820 ? 138.646 82.927  124.134 1.00 100.20 ? 820  ILE A N     1 
ATOM   6358  C  CA    . ILE A 1 820 ? 138.470 82.935  125.579 1.00 100.58 ? 820  ILE A CA    1 
ATOM   6359  C  C     . ILE A 1 820 ? 137.401 81.919  125.953 1.00 99.73  ? 820  ILE A C     1 
ATOM   6360  O  O     . ILE A 1 820 ? 136.412 81.732  125.237 1.00 99.14  ? 820  ILE A O     1 
ATOM   6361  C  CB    . ILE A 1 820 ? 138.114 84.348  126.106 1.00 101.09 ? 820  ILE A CB    1 
ATOM   6362  C  CG1   . ILE A 1 820 ? 138.070 84.366  127.636 1.00 100.75 ? 820  ILE A CG1   1 
ATOM   6363  C  CG2   . ILE A 1 820 ? 136.798 84.839  125.520 1.00 98.93  ? 820  ILE A CG2   1 
ATOM   6364  C  CD1   . ILE A 1 820 ? 139.365 83.939  128.292 1.00 100.20 ? 820  ILE A CD1   1 
ATOM   6365  N  N     . ASP A 1 821 ? 137.624 81.235  127.073 1.00 102.39 ? 821  ASP A N     1 
ATOM   6366  C  CA    . ASP A 1 821 ? 136.682 80.262  127.601 1.00 102.68 ? 821  ASP A CA    1 
ATOM   6367  C  C     . ASP A 1 821 ? 136.381 80.588  129.056 1.00 103.34 ? 821  ASP A C     1 
ATOM   6368  O  O     . ASP A 1 821 ? 137.215 81.157  129.766 1.00 103.36 ? 821  ASP A O     1 
ATOM   6369  C  CB    . ASP A 1 821 ? 137.225 78.832  127.484 1.00 102.66 ? 821  ASP A CB    1 
ATOM   6370  C  CG    . ASP A 1 821 ? 138.624 78.691  128.053 1.00 103.71 ? 821  ASP A CG    1 
ATOM   6371  O  OD1   . ASP A 1 821 ? 139.258 79.726  128.346 1.00 104.19 ? 821  ASP A OD1   1 
ATOM   6372  O  OD2   . ASP A 1 821 ? 139.090 77.542  128.207 1.00 103.39 ? 821  ASP A OD2   1 
ATOM   6373  N  N     . GLY A 1 822 ? 135.182 80.232  129.491 1.00 101.71 ? 822  GLY A N     1 
ATOM   6374  C  CA    . GLY A 1 822 ? 134.786 80.470  130.862 1.00 101.79 ? 822  GLY A CA    1 
ATOM   6375  C  C     . GLY A 1 822 ? 133.282 80.622  130.972 1.00 100.99 ? 822  GLY A C     1 
ATOM   6376  O  O     . GLY A 1 822 ? 132.537 80.342  130.033 1.00 100.45 ? 822  GLY A O     1 
ATOM   6377  N  N     . GLU A 1 823 ? 132.859 81.072  132.150 1.00 94.44  ? 823  GLU A N     1 
ATOM   6378  C  CA    . GLU A 1 823 ? 131.448 81.275  132.444 1.00 95.31  ? 823  GLU A CA    1 
ATOM   6379  C  C     . GLU A 1 823 ? 131.344 82.136  133.694 1.00 95.56  ? 823  GLU A C     1 
ATOM   6380  O  O     . GLU A 1 823 ? 132.303 82.267  134.457 1.00 94.90  ? 823  GLU A O     1 
ATOM   6381  C  CB    . GLU A 1 823 ? 130.720 79.938  132.637 1.00 95.27  ? 823  GLU A CB    1 
ATOM   6382  C  CG    . GLU A 1 823 ? 129.208 80.001  132.479 1.00 96.74  ? 823  GLU A CG    1 
ATOM   6383  C  CD    . GLU A 1 823 ? 128.540 78.666  132.747 1.00 97.04  ? 823  GLU A CD    1 
ATOM   6384  O  OE1   . GLU A 1 823 ? 129.258 77.691  133.052 1.00 95.58  ? 823  GLU A OE1   1 
ATOM   6385  O  OE2   . GLU A 1 823 ? 127.297 78.592  132.652 1.00 95.82  ? 823  GLU A OE2   1 
ATOM   6386  N  N     . GLY A 1 824 ? 130.169 82.730  133.890 1.00 92.90  ? 824  GLY A N     1 
ATOM   6387  C  CA    . GLY A 1 824 ? 129.904 83.452  135.119 1.00 92.26  ? 824  GLY A CA    1 
ATOM   6388  C  C     . GLY A 1 824 ? 129.302 84.831  134.952 1.00 92.65  ? 824  GLY A C     1 
ATOM   6389  O  O     . GLY A 1 824 ? 128.323 85.007  134.219 1.00 91.56  ? 824  GLY A O     1 
ATOM   6390  N  N     . SER A 1 825 ? 129.888 85.812  135.643 1.00 89.28  ? 825  SER A N     1 
ATOM   6391  C  CA    . SER A 1 825 ? 129.405 87.192  135.674 1.00 87.11  ? 825  SER A CA    1 
ATOM   6392  C  C     . SER A 1 825 ? 127.958 87.246  136.168 1.00 86.78  ? 825  SER A C     1 
ATOM   6393  O  O     . SER A 1 825 ? 127.031 87.624  135.449 1.00 88.07  ? 825  SER A O     1 
ATOM   6394  C  CB    . SER A 1 825 ? 129.560 87.868  134.307 1.00 84.30  ? 825  SER A CB    1 
ATOM   6395  O  OG    . SER A 1 825 ? 129.702 89.271  134.449 1.00 85.19  ? 825  SER A OG    1 
ATOM   6396  N  N     . THR A 1 826 ? 127.783 86.840  137.422 1.00 91.29  ? 826  THR A N     1 
ATOM   6397  C  CA    . THR A 1 826 ? 126.483 86.844  138.076 1.00 92.79  ? 826  THR A CA    1 
ATOM   6398  C  C     . THR A 1 826 ? 126.193 88.143  138.812 1.00 92.29  ? 826  THR A C     1 
ATOM   6399  O  O     . THR A 1 826 ? 125.159 88.241  139.480 1.00 92.40  ? 826  THR A O     1 
ATOM   6400  C  CB    . THR A 1 826 ? 126.383 85.674  139.059 1.00 94.34  ? 826  THR A CB    1 
ATOM   6401  O  OG1   . THR A 1 826 ? 127.328 85.860  140.119 1.00 93.47  ? 826  THR A OG1   1 
ATOM   6402  C  CG2   . THR A 1 826 ? 126.675 84.360  138.351 1.00 93.04  ? 826  THR A CG2   1 
ATOM   6403  N  N     . ALA A 1 827 ? 127.074 89.135  138.711 1.00 87.65  ? 827  ALA A N     1 
ATOM   6404  C  CA    . ALA A 1 827 ? 126.898 90.399  139.411 1.00 87.14  ? 827  ALA A CA    1 
ATOM   6405  C  C     . ALA A 1 827 ? 126.353 91.457  138.462 1.00 87.02  ? 827  ALA A C     1 
ATOM   6406  O  O     . ALA A 1 827 ? 126.934 91.710  137.403 1.00 86.90  ? 827  ALA A O     1 
ATOM   6407  C  CB    . ALA A 1 827 ? 128.220 90.869  140.016 1.00 88.15  ? 827  ALA A CB    1 
ATOM   6408  N  N     . THR A 1 828 ? 125.238 92.070  138.846 1.00 90.30  ? 828  THR A N     1 
ATOM   6409  C  CA    . THR A 1 828 ? 124.691 93.202  138.118 1.00 91.49  ? 828  THR A CA    1 
ATOM   6410  C  C     . THR A 1 828 ? 125.315 94.501  138.622 1.00 90.31  ? 828  THR A C     1 
ATOM   6411  O  O     . THR A 1 828 ? 126.035 94.530  139.621 1.00 91.92  ? 828  THR A O     1 
ATOM   6412  C  CB    . THR A 1 828 ? 123.170 93.250  138.262 1.00 90.27  ? 828  THR A CB    1 
ATOM   6413  O  OG1   . THR A 1 828 ? 122.827 93.565  139.616 1.00 90.29  ? 828  THR A OG1   1 
ATOM   6414  C  CG2   . THR A 1 828 ? 122.560 91.908  137.894 1.00 89.91  ? 828  THR A CG2   1 
ATOM   6415  N  N     . LEU A 1 829 ? 125.037 95.591  137.903 1.00 88.18  ? 829  LEU A N     1 
ATOM   6416  C  CA    . LEU A 1 829 ? 125.523 96.899  138.331 1.00 88.92  ? 829  LEU A CA    1 
ATOM   6417  C  C     . LEU A 1 829 ? 124.881 97.321  139.646 1.00 90.31  ? 829  LEU A C     1 
ATOM   6418  O  O     . LEU A 1 829 ? 125.537 97.932  140.499 1.00 89.84  ? 829  LEU A O     1 
ATOM   6419  C  CB    . LEU A 1 829 ? 125.257 97.939  137.244 1.00 87.99  ? 829  LEU A CB    1 
ATOM   6420  C  CG    . LEU A 1 829 ? 125.542 99.400  137.598 1.00 86.11  ? 829  LEU A CG    1 
ATOM   6421  C  CD1   . LEU A 1 829 ? 126.999 99.592  137.978 1.00 85.85  ? 829  LEU A CD1   1 
ATOM   6422  C  CD2   . LEU A 1 829 ? 125.161 100.312 136.446 1.00 86.46  ? 829  LEU A CD2   1 
ATOM   6423  N  N     . GLU A 1 830 ? 123.596 97.004  139.823 1.00 95.86  ? 830  GLU A N     1 
ATOM   6424  C  CA    . GLU A 1 830 ? 122.910 97.351  141.062 1.00 95.19  ? 830  GLU A CA    1 
ATOM   6425  C  C     . GLU A 1 830 ? 123.538 96.642  142.253 1.00 94.23  ? 830  GLU A C     1 
ATOM   6426  O  O     . GLU A 1 830 ? 123.611 97.205  143.351 1.00 96.08  ? 830  GLU A O     1 
ATOM   6427  C  CB    . GLU A 1 830 ? 121.425 97.009  140.949 1.00 95.28  ? 830  GLU A CB    1 
ATOM   6428  C  CG    . GLU A 1 830 ? 120.595 97.423  142.150 1.00 95.87  ? 830  GLU A CG    1 
ATOM   6429  C  CD    . GLU A 1 830 ? 119.144 97.008  142.023 1.00 96.41  ? 830  GLU A CD    1 
ATOM   6430  O  OE1   . GLU A 1 830 ? 118.783 96.411  140.987 1.00 95.90  ? 830  GLU A OE1   1 
ATOM   6431  O  OE2   . GLU A 1 830 ? 118.363 97.277  142.960 1.00 97.45  ? 830  GLU A OE2   1 
ATOM   6432  N  N     . ASP A 1 831 ? 123.995 95.404  142.055 1.00 90.63  ? 831  ASP A N     1 
ATOM   6433  C  CA    . ASP A 1 831 ? 124.678 94.688  143.127 1.00 91.50  ? 831  ASP A CA    1 
ATOM   6434  C  C     . ASP A 1 831 ? 125.988 95.369  143.499 1.00 92.15  ? 831  ASP A C     1 
ATOM   6435  O  O     . ASP A 1 831 ? 126.309 95.502  144.684 1.00 92.56  ? 831  ASP A O     1 
ATOM   6436  C  CB    . ASP A 1 831 ? 124.926 93.239  142.715 1.00 92.30  ? 831  ASP A CB    1 
ATOM   6437  C  CG    . ASP A 1 831 ? 123.643 92.470  142.504 1.00 92.70  ? 831  ASP A CG    1 
ATOM   6438  O  OD1   . ASP A 1 831 ? 122.637 92.805  143.161 1.00 92.72  ? 831  ASP A OD1   1 
ATOM   6439  O  OD2   . ASP A 1 831 ? 123.639 91.530  141.682 1.00 91.75  ? 831  ASP A OD2   1 
ATOM   6440  N  N     . ILE A 1 832 ? 126.757 95.808  142.500 1.00 87.66  ? 832  ILE A N     1 
ATOM   6441  C  CA    . ILE A 1 832 ? 128.010 96.502  142.780 1.00 86.89  ? 832  ILE A CA    1 
ATOM   6442  C  C     . ILE A 1 832 ? 127.740 97.822  143.486 1.00 85.71  ? 832  ILE A C     1 
ATOM   6443  O  O     . ILE A 1 832 ? 128.530 98.256  144.331 1.00 87.13  ? 832  ILE A O     1 
ATOM   6444  C  CB    . ILE A 1 832 ? 128.812 96.703  141.480 1.00 85.83  ? 832  ILE A CB    1 
ATOM   6445  C  CG1   . ILE A 1 832 ? 129.064 95.360  140.795 1.00 86.51  ? 832  ILE A CG1   1 
ATOM   6446  C  CG2   . ILE A 1 832 ? 130.139 97.385  141.762 1.00 84.32  ? 832  ILE A CG2   1 
ATOM   6447  C  CD1   . ILE A 1 832 ? 129.953 94.429  141.585 1.00 86.64  ? 832  ILE A CD1   1 
ATOM   6448  N  N     . ARG A 1 833 ? 126.623 98.474  143.165 1.00 92.44  ? 833  ARG A N     1 
ATOM   6449  C  CA    . ARG A 1 833 ? 126.300 99.746  143.802 1.00 94.79  ? 833  ARG A CA    1 
ATOM   6450  C  C     . ARG A 1 833 ? 125.830 99.552  145.242 1.00 95.60  ? 833  ARG A C     1 
ATOM   6451  O  O     . ARG A 1 833 ? 126.192 100.335 146.128 1.00 94.47  ? 833  ARG A O     1 
ATOM   6452  C  CB    . ARG A 1 833 ? 125.241 100.474 142.977 1.00 95.82  ? 833  ARG A CB    1 
ATOM   6453  C  CG    . ARG A 1 833 ? 124.999 101.910 143.382 1.00 95.80  ? 833  ARG A CG    1 
ATOM   6454  C  CD    . ARG A 1 833 ? 124.270 102.651 142.279 1.00 95.88  ? 833  ARG A CD    1 
ATOM   6455  N  NE    . ARG A 1 833 ? 125.015 102.608 141.026 1.00 96.66  ? 833  ARG A NE    1 
ATOM   6456  C  CZ    . ARG A 1 833 ? 124.638 103.211 139.908 1.00 97.96  ? 833  ARG A CZ    1 
ATOM   6457  N  NH1   . ARG A 1 833 ? 123.519 103.913 139.845 1.00 97.00  ? 833  ARG A NH1   1 
ATOM   6458  N  NH2   . ARG A 1 833 ? 125.404 103.110 138.826 1.00 95.60  ? 833  ARG A NH2   1 
ATOM   6459  N  N     . ASN A 1 834 ? 125.028 98.515  145.496 1.00 97.68  ? 834  ASN A N     1 
ATOM   6460  C  CA    . ASN A 1 834 ? 124.433 98.330  146.816 1.00 96.10  ? 834  ASN A CA    1 
ATOM   6461  C  C     . ASN A 1 834 ? 125.355 97.600  147.784 1.00 95.75  ? 834  ASN A C     1 
ATOM   6462  O  O     . ASN A 1 834 ? 125.276 97.835  148.994 1.00 96.43  ? 834  ASN A O     1 
ATOM   6463  C  CB    . ASN A 1 834 ? 123.113 97.567  146.700 1.00 95.58  ? 834  ASN A CB    1 
ATOM   6464  C  CG    . ASN A 1 834 ? 122.040 98.365  145.994 1.00 97.04  ? 834  ASN A CG    1 
ATOM   6465  O  OD1   . ASN A 1 834 ? 122.334 99.228  145.169 1.00 98.76  ? 834  ASN A OD1   1 
ATOM   6466  N  ND2   . ASN A 1 834 ? 120.785 98.083  146.319 1.00 97.77  ? 834  ASN A ND2   1 
ATOM   6467  N  N     . ALA A 1 835 ? 126.213 96.713  147.287 1.00 97.39  ? 835  ALA A N     1 
ATOM   6468  C  CA    . ALA A 1 835 ? 127.099 95.962  148.164 1.00 99.70  ? 835  ALA A CA    1 
ATOM   6469  C  C     . ALA A 1 835 ? 128.116 96.882  148.825 1.00 99.70  ? 835  ALA A C     1 
ATOM   6470  O  O     . ALA A 1 835 ? 128.527 97.900  148.263 1.00 99.16  ? 835  ALA A O     1 
ATOM   6471  C  CB    . ALA A 1 835 ? 127.823 94.862  147.389 1.00 99.07  ? 835  ALA A CB    1 
ATOM   6472  N  N     . LYS A 1 836 ? 128.520 96.511  150.037 1.00 100.80 ? 836  LYS A N     1 
ATOM   6473  C  CA    . LYS A 1 836 ? 129.450 97.318  150.815 1.00 100.02 ? 836  LYS A CA    1 
ATOM   6474  C  C     . LYS A 1 836 ? 130.861 96.751  150.850 1.00 99.92  ? 836  LYS A C     1 
ATOM   6475  O  O     . LYS A 1 836 ? 131.819 97.521  150.969 1.00 97.59  ? 836  LYS A O     1 
ATOM   6476  C  CB    . LYS A 1 836 ? 128.939 97.473  152.250 1.00 100.72 ? 836  LYS A CB    1 
ATOM   6477  C  CG    . LYS A 1 836 ? 127.517 97.995  152.347 1.00 100.51 ? 836  LYS A CG    1 
ATOM   6478  C  CD    . LYS A 1 836 ? 127.400 99.393  151.769 1.00 100.35 ? 836  LYS A CD    1 
ATOM   6479  C  CE    . LYS A 1 836 ? 128.246 100.384 152.551 1.00 101.10 ? 836  LYS A CE    1 
ATOM   6480  N  NZ    . LYS A 1 836 ? 128.146 101.761 151.993 1.00 101.35 ? 836  LYS A NZ    1 
ATOM   6481  N  N     . ARG A 1 837 ? 131.016 95.434  150.742 1.00 104.95 ? 837  ARG A N     1 
ATOM   6482  C  CA    . ARG A 1 837 ? 132.315 94.781  150.841 1.00 105.24 ? 837  ARG A CA    1 
ATOM   6483  C  C     . ARG A 1 837 ? 132.651 94.108  149.519 1.00 105.29 ? 837  ARG A C     1 
ATOM   6484  O  O     . ARG A 1 837 ? 131.815 93.399  148.950 1.00 105.23 ? 837  ARG A O     1 
ATOM   6485  C  CB    . ARG A 1 837 ? 132.323 93.758  151.979 1.00 106.25 ? 837  ARG A CB    1 
ATOM   6486  C  CG    . ARG A 1 837 ? 132.310 94.383  153.366 1.00 106.37 ? 837  ARG A CG    1 
ATOM   6487  C  CD    . ARG A 1 837 ? 131.885 93.388  154.434 1.00 104.00 ? 837  ARG A CD    1 
ATOM   6488  N  NE    . ARG A 1 837 ? 130.436 93.239  154.499 1.00 104.58 ? 837  ARG A NE    1 
ATOM   6489  C  CZ    . ARG A 1 837 ? 129.749 92.283  153.890 1.00 105.91 ? 837  ARG A CZ    1 
ATOM   6490  N  NH1   . ARG A 1 837 ? 130.348 91.359  153.157 1.00 106.20 ? 837  ARG A NH1   1 
ATOM   6491  N  NH2   . ARG A 1 837 ? 128.425 92.251  154.020 1.00 105.43 ? 837  ARG A NH2   1 
ATOM   6492  N  N     . VAL A 1 838 ? 133.873 94.331  149.034 1.00 104.99 ? 838  VAL A N     1 
ATOM   6493  C  CA    . VAL A 1 838 ? 134.318 93.791  147.756 1.00 104.15 ? 838  VAL A CA    1 
ATOM   6494  C  C     . VAL A 1 838 ? 135.626 93.037  147.955 1.00 104.38 ? 838  VAL A C     1 
ATOM   6495  O  O     . VAL A 1 838 ? 136.379 93.295  148.900 1.00 104.21 ? 838  VAL A O     1 
ATOM   6496  C  CB    . VAL A 1 838 ? 134.494 94.892  146.680 1.00 103.36 ? 838  VAL A CB    1 
ATOM   6497  C  CG1   . VAL A 1 838 ? 133.236 95.739  146.558 1.00 103.45 ? 838  VAL A CG1   1 
ATOM   6498  C  CG2   . VAL A 1 838 ? 135.703 95.764  146.983 1.00 102.13 ? 838  VAL A CG2   1 
ATOM   6499  N  N     . LEU A 1 839 ? 135.885 92.090  147.057 1.00 99.82  ? 839  LEU A N     1 
ATOM   6500  C  CA    . LEU A 1 839 ? 137.148 91.364  147.005 1.00 98.61  ? 839  LEU A CA    1 
ATOM   6501  C  C     . LEU A 1 839 ? 137.842 91.714  145.699 1.00 97.51  ? 839  LEU A C     1 
ATOM   6502  O  O     . LEU A 1 839 ? 137.281 91.501  144.620 1.00 97.22  ? 839  LEU A O     1 
ATOM   6503  C  CB    . LEU A 1 839 ? 136.931 89.854  147.109 1.00 100.14 ? 839  LEU A CB    1 
ATOM   6504  C  CG    . LEU A 1 839 ? 138.177 89.010  146.843 1.00 99.63  ? 839  LEU A CG    1 
ATOM   6505  C  CD1   . LEU A 1 839 ? 139.259 89.313  147.866 1.00 99.09  ? 839  LEU A CD1   1 
ATOM   6506  C  CD2   . LEU A 1 839 ? 137.837 87.530  146.834 1.00 98.53  ? 839  LEU A CD2   1 
ATOM   6507  N  N     . LEU A 1 840 ? 139.062 92.227  145.798 1.00 99.96  ? 840  LEU A N     1 
ATOM   6508  C  CA    . LEU A 1 840 ? 139.773 92.811  144.668 1.00 100.37 ? 840  LEU A CA    1 
ATOM   6509  C  C     . LEU A 1 840 ? 140.944 91.909  144.299 1.00 100.54 ? 840  LEU A C     1 
ATOM   6510  O  O     . LEU A 1 840 ? 141.947 91.857  145.019 1.00 101.01 ? 840  LEU A O     1 
ATOM   6511  C  CB    . LEU A 1 840 ? 140.244 94.220  145.022 1.00 100.23 ? 840  LEU A CB    1 
ATOM   6512  C  CG    . LEU A 1 840 ? 140.687 95.201  143.939 1.00 99.37  ? 840  LEU A CG    1 
ATOM   6513  C  CD1   . LEU A 1 840 ? 140.431 96.611  144.426 1.00 99.78  ? 840  LEU A CD1   1 
ATOM   6514  C  CD2   . LEU A 1 840 ? 142.156 95.023  143.612 1.00 99.64  ? 840  LEU A CD2   1 
ATOM   6515  N  N     . LYS A 1 841 ? 140.818 91.201  143.181 1.00 101.26 ? 841  LYS A N     1 
ATOM   6516  C  CA    . LYS A 1 841 ? 141.909 90.405  142.636 1.00 101.10 ? 841  LYS A CA    1 
ATOM   6517  C  C     . LYS A 1 841 ? 142.457 90.958  141.332 1.00 101.49 ? 841  LYS A C     1 
ATOM   6518  O  O     . LYS A 1 841 ? 143.667 90.908  141.109 1.00 100.60 ? 841  LYS A O     1 
ATOM   6519  C  CB    . LYS A 1 841 ? 141.458 88.957  142.416 1.00 98.65  ? 841  LYS A CB    1 
ATOM   6520  C  CG    . LYS A 1 841 ? 140.979 88.259  143.674 1.00 99.95  ? 841  LYS A CG    1 
ATOM   6521  C  CD    . LYS A 1 841 ? 141.446 86.814  143.708 1.00 101.35 ? 841  LYS A CD    1 
ATOM   6522  C  CE    . LYS A 1 841 ? 141.108 86.089  142.419 1.00 101.18 ? 841  LYS A CE    1 
ATOM   6523  N  NZ    . LYS A 1 841 ? 141.590 84.681  142.432 1.00 99.87  ? 841  LYS A NZ    1 
ATOM   6524  N  N     . VAL A 1 842 ? 141.594 91.484  140.463 1.00 101.81 ? 842  VAL A N     1 
ATOM   6525  C  CA    . VAL A 1 842 ? 142.059 92.090  139.225 1.00 101.56 ? 842  VAL A CA    1 
ATOM   6526  C  C     . VAL A 1 842 ? 142.830 93.365  139.537 1.00 101.24 ? 842  VAL A C     1 
ATOM   6527  O  O     . VAL A 1 842 ? 142.600 94.029  140.555 1.00 100.75 ? 842  VAL A O     1 
ATOM   6528  C  CB    . VAL A 1 842 ? 140.881 92.377  138.276 1.00 101.02 ? 842  VAL A CB    1 
ATOM   6529  C  CG1   . VAL A 1 842 ? 140.154 91.100  137.940 1.00 99.27  ? 842  VAL A CG1   1 
ATOM   6530  C  CG2   . VAL A 1 842 ? 139.930 93.383  138.896 1.00 99.51  ? 842  VAL A CG2   1 
ATOM   6531  N  N     . ASN A 1 843 ? 143.769 93.703  138.661 1.00 105.38 ? 843  ASN A N     1 
ATOM   6532  C  CA    . ASN A 1 843 ? 144.473 94.967  138.793 1.00 106.15 ? 843  ASN A CA    1 
ATOM   6533  C  C     . ASN A 1 843 ? 143.512 96.112  138.502 1.00 105.59 ? 843  ASN A C     1 
ATOM   6534  O  O     . ASN A 1 843 ? 142.835 96.120  137.470 1.00 105.00 ? 843  ASN A O     1 
ATOM   6535  C  CB    . ASN A 1 843 ? 145.669 95.012  137.845 1.00 105.13 ? 843  ASN A CB    1 
ATOM   6536  C  CG    . ASN A 1 843 ? 146.586 96.181  138.123 1.00 105.27 ? 843  ASN A CG    1 
ATOM   6537  O  OD1   . ASN A 1 843 ? 146.560 96.759  139.208 1.00 105.24 ? 843  ASN A OD1   1 
ATOM   6538  N  ND2   . ASN A 1 843 ? 147.408 96.535  137.143 1.00 104.67 ? 843  ASN A ND2   1 
ATOM   6539  N  N     . ILE A 1 844 ? 143.442 97.072  139.425 1.00 102.64 ? 844  ILE A N     1 
ATOM   6540  C  CA    . ILE A 1 844 ? 142.527 98.199  139.266 1.00 103.63 ? 844  ILE A CA    1 
ATOM   6541  C  C     . ILE A 1 844 ? 142.928 99.054  138.071 1.00 103.89 ? 844  ILE A C     1 
ATOM   6542  O  O     . ILE A 1 844 ? 142.073 99.507  137.300 1.00 104.27 ? 844  ILE A O     1 
ATOM   6543  C  CB    . ILE A 1 844 ? 142.469 99.019  140.568 1.00 103.91 ? 844  ILE A CB    1 
ATOM   6544  C  CG1   . ILE A 1 844 ? 141.394 98.458  141.493 1.00 103.52 ? 844  ILE A CG1   1 
ATOM   6545  C  CG2   . ILE A 1 844 ? 142.207 100.494 140.288 1.00 101.63 ? 844  ILE A CG2   1 
ATOM   6546  C  CD1   . ILE A 1 844 ? 140.006 98.511  140.905 1.00 102.35 ? 844  ILE A CD1   1 
ATOM   6547  N  N     . GLU A 1 845 ? 144.232 99.275  137.889 1.00 102.92 ? 845  GLU A N     1 
ATOM   6548  C  CA    . GLU A 1 845 ? 144.699 100.176 136.841 1.00 102.65 ? 845  GLU A CA    1 
ATOM   6549  C  C     . GLU A 1 845 ? 144.335 99.677  135.449 1.00 102.01 ? 845  GLU A C     1 
ATOM   6550  O  O     . GLU A 1 845 ? 144.153 100.486 134.532 1.00 99.70  ? 845  GLU A O     1 
ATOM   6551  C  CB    . GLU A 1 845 ? 146.210 100.365 136.958 1.00 102.91 ? 845  GLU A CB    1 
ATOM   6552  C  CG    . GLU A 1 845 ? 146.668 100.809 138.333 1.00 103.45 ? 845  GLU A CG    1 
ATOM   6553  C  CD    . GLU A 1 845 ? 148.166 101.017 138.406 1.00 103.87 ? 845  GLU A CD    1 
ATOM   6554  O  OE1   . GLU A 1 845 ? 148.842 100.845 137.371 1.00 102.91 ? 845  GLU A OE1   1 
ATOM   6555  O  OE2   . GLU A 1 845 ? 148.669 101.353 139.499 1.00 102.95 ? 845  GLU A OE2   1 
ATOM   6556  N  N     . LYS A 1 846 ? 144.228 98.359  135.265 1.00 98.66  ? 846  LYS A N     1 
ATOM   6557  C  CA    . LYS A 1 846 ? 143.918 97.827  133.941 1.00 97.39  ? 846  LYS A CA    1 
ATOM   6558  C  C     . LYS A 1 846 ? 142.494 98.153  133.516 1.00 97.10  ? 846  LYS A C     1 
ATOM   6559  O  O     . LYS A 1 846 ? 142.245 98.401  132.332 1.00 98.14  ? 846  LYS A O     1 
ATOM   6560  C  CB    . LYS A 1 846 ? 144.146 96.317  133.906 1.00 97.50  ? 846  LYS A CB    1 
ATOM   6561  C  CG    . LYS A 1 846 ? 145.606 95.912  133.863 1.00 97.45  ? 846  LYS A CG    1 
ATOM   6562  C  CD    . LYS A 1 846 ? 145.753 94.422  133.621 1.00 97.97  ? 846  LYS A CD    1 
ATOM   6563  C  CE    . LYS A 1 846 ? 145.131 94.021  132.296 1.00 97.78  ? 846  LYS A CE    1 
ATOM   6564  N  NZ    . LYS A 1 846 ? 145.247 92.558  132.048 1.00 97.48  ? 846  LYS A NZ    1 
ATOM   6565  N  N     . TYR A 1 847 ? 141.551 98.158  134.453 1.00 85.90  ? 847  TYR A N     1 
ATOM   6566  C  CA    . TYR A 1 847 ? 140.153 98.463  134.153 1.00 83.33  ? 847  TYR A CA    1 
ATOM   6567  C  C     . TYR A 1 847 ? 139.768 99.755  134.856 1.00 82.20  ? 847  TYR A C     1 
ATOM   6568  O  O     . TYR A 1 847 ? 139.474 99.747  136.065 1.00 80.70  ? 847  TYR A O     1 
ATOM   6569  C  CB    . TYR A 1 847 ? 139.251 97.310  134.580 1.00 83.77  ? 847  TYR A CB    1 
ATOM   6570  C  CG    . TYR A 1 847 ? 139.757 95.979  134.081 1.00 85.23  ? 847  TYR A CG    1 
ATOM   6571  C  CD1   . TYR A 1 847 ? 139.621 95.622  132.748 1.00 85.54  ? 847  TYR A CD1   1 
ATOM   6572  C  CD2   . TYR A 1 847 ? 140.388 95.089  134.936 1.00 84.49  ? 847  TYR A CD2   1 
ATOM   6573  C  CE1   . TYR A 1 847 ? 140.090 94.413  132.283 1.00 86.08  ? 847  TYR A CE1   1 
ATOM   6574  C  CE2   . TYR A 1 847 ? 140.859 93.876  134.479 1.00 85.13  ? 847  TYR A CE2   1 
ATOM   6575  C  CZ    . TYR A 1 847 ? 140.708 93.544  133.153 1.00 85.22  ? 847  TYR A CZ    1 
ATOM   6576  O  OH    . TYR A 1 847 ? 141.176 92.338  132.691 1.00 84.65  ? 847  TYR A OH    1 
ATOM   6577  N  N     . PRO A 1 848 ? 139.758 100.888 134.148 1.00 72.69  ? 848  PRO A N     1 
ATOM   6578  C  CA    . PRO A 1 848 ? 139.614 102.182 134.829 1.00 71.29  ? 848  PRO A CA    1 
ATOM   6579  C  C     . PRO A 1 848 ? 138.213 102.496 135.322 1.00 72.16  ? 848  PRO A C     1 
ATOM   6580  O  O     . PRO A 1 848 ? 138.076 103.366 136.192 1.00 72.40  ? 848  PRO A O     1 
ATOM   6581  C  CB    . PRO A 1 848 ? 140.048 103.193 133.756 1.00 71.98  ? 848  PRO A CB    1 
ATOM   6582  C  CG    . PRO A 1 848 ? 140.758 102.384 132.711 1.00 71.56  ? 848  PRO A CG    1 
ATOM   6583  C  CD    . PRO A 1 848 ? 140.088 101.055 132.726 1.00 72.22  ? 848  PRO A CD    1 
ATOM   6584  N  N     . LEU A 1 849 ? 137.169 101.847 134.801 1.00 62.72  ? 849  LEU A N     1 
ATOM   6585  C  CA    . LEU A 1 849 ? 135.827 102.150 135.286 1.00 57.03  ? 849  LEU A CA    1 
ATOM   6586  C  C     . LEU A 1 849 ? 135.615 101.626 136.700 1.00 58.56  ? 849  LEU A C     1 
ATOM   6587  O  O     . LEU A 1 849 ? 134.801 102.178 137.450 1.00 59.90  ? 849  LEU A O     1 
ATOM   6588  C  CB    . LEU A 1 849 ? 134.770 101.580 134.341 1.00 58.11  ? 849  LEU A CB    1 
ATOM   6589  C  CG    . LEU A 1 849 ? 133.344 102.060 134.630 1.00 58.89  ? 849  LEU A CG    1 
ATOM   6590  C  CD1   . LEU A 1 849 ? 133.248 103.565 134.453 1.00 58.94  ? 849  LEU A CD1   1 
ATOM   6591  C  CD2   . LEU A 1 849 ? 132.324 101.351 133.762 1.00 60.75  ? 849  LEU A CD2   1 
ATOM   6592  N  N     . LEU A 1 850 ? 136.343 100.573 137.084 1.00 66.83  ? 850  LEU A N     1 
ATOM   6593  C  CA    . LEU A 1 850 ? 136.281 100.079 138.454 1.00 65.88  ? 850  LEU A CA    1 
ATOM   6594  C  C     . LEU A 1 850 ? 136.736 101.125 139.459 1.00 63.91  ? 850  LEU A C     1 
ATOM   6595  O  O     . LEU A 1 850 ? 136.366 101.043 140.633 1.00 66.24  ? 850  LEU A O     1 
ATOM   6596  C  CB    . LEU A 1 850 ? 137.131 98.819  138.602 1.00 65.23  ? 850  LEU A CB    1 
ATOM   6597  C  CG    . LEU A 1 850 ? 136.561 97.529  138.017 1.00 62.75  ? 850  LEU A CG    1 
ATOM   6598  C  CD1   . LEU A 1 850 ? 137.505 96.374  138.277 1.00 64.69  ? 850  LEU A CD1   1 
ATOM   6599  C  CD2   . LEU A 1 850 ? 135.190 97.242  138.598 1.00 62.78  ? 850  LEU A CD2   1 
ATOM   6600  N  N     . LYS A 1 851 ? 137.537 102.099 139.023 1.00 56.41  ? 851  LYS A N     1 
ATOM   6601  C  CA    . LYS A 1 851 ? 137.912 103.206 139.894 1.00 59.16  ? 851  LYS A CA    1 
ATOM   6602  C  C     . LYS A 1 851 ? 136.690 104.018 140.305 1.00 59.87  ? 851  LYS A C     1 
ATOM   6603  O  O     . LYS A 1 851 ? 136.551 104.395 141.474 1.00 61.79  ? 851  LYS A O     1 
ATOM   6604  C  CB    . LYS A 1 851 ? 138.938 104.087 139.183 1.00 59.97  ? 851  LYS A CB    1 
ATOM   6605  C  CG    . LYS A 1 851 ? 139.687 105.050 140.074 1.00 58.95  ? 851  LYS A CG    1 
ATOM   6606  C  CD    . LYS A 1 851 ? 140.840 105.677 139.316 1.00 60.52  ? 851  LYS A CD    1 
ATOM   6607  C  CE    . LYS A 1 851 ? 141.758 106.444 140.245 1.00 58.01  ? 851  LYS A CE    1 
ATOM   6608  N  NZ    . LYS A 1 851 ? 142.995 106.891 139.549 1.00 58.93  ? 851  LYS A NZ    1 
ATOM   6609  N  N     . LEU A 1 852 ? 135.792 104.294 139.357 1.00 52.76  ? 852  LEU A N     1 
ATOM   6610  C  CA    . LEU A 1 852 ? 134.571 105.031 139.669 1.00 49.40  ? 852  LEU A CA    1 
ATOM   6611  C  C     . LEU A 1 852 ? 133.531 104.150 140.348 1.00 47.44  ? 852  LEU A C     1 
ATOM   6612  O  O     . LEU A 1 852 ? 132.809 104.613 141.237 1.00 48.72  ? 852  LEU A O     1 
ATOM   6613  C  CB    . LEU A 1 852 ? 133.979 105.636 138.398 1.00 47.69  ? 852  LEU A CB    1 
ATOM   6614  C  CG    . LEU A 1 852 ? 134.910 106.427 137.486 1.00 47.13  ? 852  LEU A CG    1 
ATOM   6615  C  CD1   . LEU A 1 852 ? 134.119 107.043 136.352 1.00 47.31  ? 852  LEU A CD1   1 
ATOM   6616  C  CD2   . LEU A 1 852 ? 135.640 107.488 138.265 1.00 46.47  ? 852  LEU A CD2   1 
ATOM   6617  N  N     . LEU A 1 853 ? 133.426 102.886 139.932 1.00 57.05  ? 853  LEU A N     1 
ATOM   6618  C  CA    . LEU A 1 853 ? 132.373 102.025 140.460 1.00 60.04  ? 853  LEU A CA    1 
ATOM   6619  C  C     . LEU A 1 853 ? 132.653 101.585 141.890 1.00 64.36  ? 853  LEU A C     1 
ATOM   6620  O  O     . LEU A 1 853 ? 131.715 101.417 142.677 1.00 64.73  ? 853  LEU A O     1 
ATOM   6621  C  CB    . LEU A 1 853 ? 132.188 100.805 139.561 1.00 60.89  ? 853  LEU A CB    1 
ATOM   6622  C  CG    . LEU A 1 853 ? 131.441 101.037 138.251 1.00 62.10  ? 853  LEU A CG    1 
ATOM   6623  C  CD1   . LEU A 1 853 ? 131.270 99.731  137.508 1.00 62.41  ? 853  LEU A CD1   1 
ATOM   6624  C  CD2   . LEU A 1 853 ? 130.093 101.681 138.513 1.00 63.92  ? 853  LEU A CD2   1 
ATOM   6625  N  N     . LEU A 1 854 ? 133.921 101.391 142.246 1.00 62.93  ? 854  LEU A N     1 
ATOM   6626  C  CA    . LEU A 1 854 ? 134.297 100.896 143.563 1.00 59.27  ? 854  LEU A CA    1 
ATOM   6627  C  C     . LEU A 1 854 ? 134.811 101.998 144.479 1.00 59.74  ? 854  LEU A C     1 
ATOM   6628  O  O     . LEU A 1 854 ? 135.465 101.703 145.484 1.00 60.59  ? 854  LEU A O     1 
ATOM   6629  C  CB    . LEU A 1 854 ? 135.345 99.793  143.435 1.00 57.28  ? 854  LEU A CB    1 
ATOM   6630  C  CG    . LEU A 1 854 ? 134.908 98.536  142.689 1.00 58.72  ? 854  LEU A CG    1 
ATOM   6631  C  CD1   . LEU A 1 854 ? 135.988 97.478  142.779 1.00 61.96  ? 854  LEU A CD1   1 
ATOM   6632  C  CD2   . LEU A 1 854 ? 133.595 98.018  143.243 1.00 59.06  ? 854  LEU A CD2   1 
ATOM   6633  N  N     . LYS A 1 855 ? 134.538 103.256 144.153 1.00 59.08  ? 855  LYS A N     1 
ATOM   6634  C  CA    . LYS A 1 855 ? 134.964 104.355 145.007 1.00 60.83  ? 855  LYS A CA    1 
ATOM   6635  C  C     . LYS A 1 855 ? 134.178 104.342 146.312 1.00 63.41  ? 855  LYS A C     1 
ATOM   6636  O  O     . LYS A 1 855 ? 132.945 104.289 146.309 1.00 64.21  ? 855  LYS A O     1 
ATOM   6637  C  CB    . LYS A 1 855 ? 134.780 105.687 144.284 1.00 59.48  ? 855  LYS A CB    1 
ATOM   6638  C  CG    . LYS A 1 855 ? 135.071 106.903 145.138 1.00 57.90  ? 855  LYS A CG    1 
ATOM   6639  C  CD    . LYS A 1 855 ? 133.804 107.682 145.434 1.00 56.80  ? 855  LYS A CD    1 
ATOM   6640  C  CE    . LYS A 1 855 ? 134.061 108.781 146.444 1.00 58.35  ? 855  LYS A CE    1 
ATOM   6641  N  NZ    . LYS A 1 855 ? 132.835 109.576 146.716 1.00 62.69  ? 855  LYS A NZ    1 
ATOM   6642  N  N     . GLY A 1 856 ? 134.896 104.398 147.427 1.00 73.29  ? 856  GLY A N     1 
ATOM   6643  C  CA    . GLY A 1 856 ? 134.261 104.411 148.732 1.00 72.62  ? 856  GLY A CA    1 
ATOM   6644  C  C     . GLY A 1 856 ? 133.531 103.138 149.099 1.00 75.50  ? 856  GLY A C     1 
ATOM   6645  O  O     . GLY A 1 856 ? 132.406 103.201 149.611 1.00 76.29  ? 856  GLY A O     1 
ATOM   6646  N  N     . LYS A 1 857 ? 134.136 101.980 148.845 1.00 83.85  ? 857  LYS A N     1 
ATOM   6647  C  CA    . LYS A 1 857 ? 133.564 100.706 149.251 1.00 84.03  ? 857  LYS A CA    1 
ATOM   6648  C  C     . LYS A 1 857 ? 134.655 99.840  149.862 1.00 86.38  ? 857  LYS A C     1 
ATOM   6649  O  O     . LYS A 1 857 ? 135.836 99.980  149.535 1.00 85.01  ? 857  LYS A O     1 
ATOM   6650  C  CB    . LYS A 1 857 ? 132.891 99.986  148.080 1.00 82.63  ? 857  LYS A CB    1 
ATOM   6651  C  CG    . LYS A 1 857 ? 131.571 100.618 147.689 1.00 83.97  ? 857  LYS A CG    1 
ATOM   6652  C  CD    . LYS A 1 857 ? 130.847 99.829  146.626 1.00 84.92  ? 857  LYS A CD    1 
ATOM   6653  C  CE    . LYS A 1 857 ? 129.510 100.473 146.326 1.00 85.27  ? 857  LYS A CE    1 
ATOM   6654  N  NZ    . LYS A 1 857 ? 128.620 100.471 147.516 1.00 85.94  ? 857  LYS A NZ    1 
ATOM   6655  N  N     . GLU A 1 858 ? 134.245 98.943  150.755 1.00 101.65 ? 858  GLU A N     1 
ATOM   6656  C  CA    . GLU A 1 858 ? 135.189 98.188  151.570 1.00 102.14 ? 858  GLU A CA    1 
ATOM   6657  C  C     . GLU A 1 858 ? 135.856 97.102  150.736 1.00 103.12 ? 858  GLU A C     1 
ATOM   6658  O  O     . GLU A 1 858 ? 135.174 96.269  150.130 1.00 101.64 ? 858  GLU A O     1 
ATOM   6659  C  CB    . GLU A 1 858 ? 134.477 97.577  152.775 1.00 101.66 ? 858  GLU A CB    1 
ATOM   6660  C  CG    . GLU A 1 858 ? 133.681 98.576  153.601 1.00 102.44 ? 858  GLU A CG    1 
ATOM   6661  C  CD    . GLU A 1 858 ? 134.562 99.572  154.330 1.00 103.30 ? 858  GLU A CD    1 
ATOM   6662  O  OE1   . GLU A 1 858 ? 135.738 99.247  154.600 1.00 104.47 ? 858  GLU A OE1   1 
ATOM   6663  O  OE2   . GLU A 1 858 ? 134.077 100.682 154.635 1.00 101.27 ? 858  GLU A OE2   1 
ATOM   6664  N  N     . ILE A 1 859 ? 137.184 97.106  150.718 1.00 110.89 ? 859  ILE A N     1 
ATOM   6665  C  CA    . ILE A 1 859 ? 137.974 96.090  150.033 1.00 110.85 ? 859  ILE A CA    1 
ATOM   6666  C  C     . ILE A 1 859 ? 138.522 95.148  151.097 1.00 110.45 ? 859  ILE A C     1 
ATOM   6667  O  O     . ILE A 1 859 ? 139.447 95.501  151.836 1.00 109.49 ? 859  ILE A O     1 
ATOM   6668  C  CB    . ILE A 1 859 ? 139.104 96.716  149.207 1.00 110.66 ? 859  ILE A CB    1 
ATOM   6669  C  CG1   . ILE A 1 859 ? 138.545 97.769  148.252 1.00 109.37 ? 859  ILE A CG1   1 
ATOM   6670  C  CG2   . ILE A 1 859 ? 139.853 95.643  148.440 1.00 109.88 ? 859  ILE A CG2   1 
ATOM   6671  C  CD1   . ILE A 1 859 ? 139.608 98.526  147.491 1.00 107.70 ? 859  ILE A CD1   1 
ATOM   6672  N  N     . VAL A 1 860 ? 137.959 93.941  151.174 1.00 111.08 ? 860  VAL A N     1 
ATOM   6673  C  CA    . VAL A 1 860 ? 138.301 92.984  152.216 1.00 111.59 ? 860  VAL A CA    1 
ATOM   6674  C  C     . VAL A 1 860 ? 138.649 91.648  151.576 1.00 111.56 ? 860  VAL A C     1 
ATOM   6675  O  O     . VAL A 1 860 ? 138.275 91.358  150.438 1.00 111.16 ? 860  VAL A O     1 
ATOM   6676  C  CB    . VAL A 1 860 ? 137.160 92.805  153.240 1.00 111.29 ? 860  VAL A CB    1 
ATOM   6677  C  CG1   . VAL A 1 860 ? 136.946 94.086  154.031 1.00 110.21 ? 860  VAL A CG1   1 
ATOM   6678  C  CG2   . VAL A 1 860 ? 135.880 92.388  152.535 1.00 110.48 ? 860  VAL A CG2   1 
ATOM   6679  N  N     . GLU A 1 861 ? 139.377 90.830  152.335 1.00 111.79 ? 861  GLU A N     1 
ATOM   6680  C  CA    . GLU A 1 861 ? 139.800 89.519  151.858 1.00 111.99 ? 861  GLU A CA    1 
ATOM   6681  C  C     . GLU A 1 861 ? 138.818 88.412  152.211 1.00 111.65 ? 861  GLU A C     1 
ATOM   6682  O  O     . GLU A 1 861 ? 138.749 87.408  151.494 1.00 110.85 ? 861  GLU A O     1 
ATOM   6683  C  CB    . GLU A 1 861 ? 141.179 89.172  152.424 1.00 110.88 ? 861  GLU A CB    1 
ATOM   6684  C  CG    . GLU A 1 861 ? 142.302 90.056  151.911 1.00 110.76 ? 861  GLU A CG    1 
ATOM   6685  C  CD    . GLU A 1 861 ? 142.627 89.798  150.453 1.00 111.83 ? 861  GLU A CD    1 
ATOM   6686  O  OE1   . GLU A 1 861 ? 142.328 88.689  149.961 1.00 112.19 ? 861  GLU A OE1   1 
ATOM   6687  O  OE2   . GLU A 1 861 ? 143.181 90.705  149.797 1.00 111.40 ? 861  GLU A OE2   1 
ATOM   6688  N  N     . GLU A 1 862 ? 138.060 88.566  153.294 1.00 111.23 ? 862  GLU A N     1 
ATOM   6689  C  CA    . GLU A 1 862 ? 137.113 87.554  153.731 1.00 110.75 ? 862  GLU A CA    1 
ATOM   6690  C  C     . GLU A 1 862 ? 135.794 88.222  154.092 1.00 110.92 ? 862  GLU A C     1 
ATOM   6691  O  O     . GLU A 1 862 ? 135.749 89.402  154.448 1.00 110.08 ? 862  GLU A O     1 
ATOM   6692  C  CB    . GLU A 1 862 ? 137.656 86.756  154.926 1.00 110.86 ? 862  GLU A CB    1 
ATOM   6693  C  CG    . GLU A 1 862 ? 136.968 85.418  155.156 1.00 111.37 ? 862  GLU A CG    1 
ATOM   6694  C  CD    . GLU A 1 862 ? 137.569 84.645  156.313 1.00 111.71 ? 862  GLU A CD    1 
ATOM   6695  O  OE1   . GLU A 1 862 ? 138.522 85.153  156.940 1.00 110.89 ? 862  GLU A OE1   1 
ATOM   6696  O  OE2   . GLU A 1 862 ? 137.088 83.527  156.596 1.00 112.01 ? 862  GLU A OE2   1 
ATOM   6697  N  N     . GLY A 1 863 ? 134.713 87.451  153.993 1.00 111.61 ? 863  GLY A N     1 
ATOM   6698  C  CA    . GLY A 1 863 ? 133.391 87.990  154.236 1.00 110.76 ? 863  GLY A CA    1 
ATOM   6699  C  C     . GLY A 1 863 ? 132.874 88.892  153.143 1.00 111.53 ? 863  GLY A C     1 
ATOM   6700  O  O     . GLY A 1 863 ? 131.908 89.625  153.368 1.00 111.04 ? 863  GLY A O     1 
ATOM   6701  N  N     . TYR A 1 864 ? 133.493 88.858  151.968 1.00 110.51 ? 864  TYR A N     1 
ATOM   6702  C  CA    . TYR A 1 864 ? 133.132 89.758  150.884 1.00 109.20 ? 864  TYR A CA    1 
ATOM   6703  C  C     . TYR A 1 864 ? 131.739 89.451  150.352 1.00 109.36 ? 864  TYR A C     1 
ATOM   6704  O  O     . TYR A 1 864 ? 131.352 88.289  150.201 1.00 110.86 ? 864  TYR A O     1 
ATOM   6705  C  CB    . TYR A 1 864 ? 134.159 89.652  149.757 1.00 108.85 ? 864  TYR A CB    1 
ATOM   6706  C  CG    . TYR A 1 864 ? 134.597 88.233  149.468 1.00 108.48 ? 864  TYR A CG    1 
ATOM   6707  C  CD1   . TYR A 1 864 ? 133.873 87.423  148.604 1.00 108.26 ? 864  TYR A CD1   1 
ATOM   6708  C  CD2   . TYR A 1 864 ? 135.738 87.704  150.058 1.00 109.41 ? 864  TYR A CD2   1 
ATOM   6709  C  CE1   . TYR A 1 864 ? 134.269 86.127  148.338 1.00 109.28 ? 864  TYR A CE1   1 
ATOM   6710  C  CE2   . TYR A 1 864 ? 136.142 86.409  149.799 1.00 109.89 ? 864  TYR A CE2   1 
ATOM   6711  C  CZ    . TYR A 1 864 ? 135.404 85.626  148.938 1.00 109.46 ? 864  TYR A CZ    1 
ATOM   6712  O  OH    . TYR A 1 864 ? 135.803 84.336  148.676 1.00 108.78 ? 864  TYR A OH    1 
ATOM   6713  N  N     . GLU A 1 865 ? 130.978 90.510  150.073 1.00 105.54 ? 865  GLU A N     1 
ATOM   6714  C  CA    . GLU A 1 865 ? 129.673 90.339  149.448 1.00 105.60 ? 865  GLU A CA    1 
ATOM   6715  C  C     . GLU A 1 865 ? 129.799 90.126  147.945 1.00 106.94 ? 865  GLU A C     1 
ATOM   6716  O  O     . GLU A 1 865 ? 129.066 89.317  147.367 1.00 107.91 ? 865  GLU A O     1 
ATOM   6717  C  CB    . GLU A 1 865 ? 128.786 91.548  149.747 1.00 106.38 ? 865  GLU A CB    1 
ATOM   6718  C  CG    . GLU A 1 865 ? 127.430 91.521  149.059 1.00 106.66 ? 865  GLU A CG    1 
ATOM   6719  C  CD    . GLU A 1 865 ? 126.527 90.420  149.578 1.00 106.16 ? 865  GLU A CD    1 
ATOM   6720  O  OE1   . GLU A 1 865 ? 126.731 89.966  150.723 1.00 105.30 ? 865  GLU A OE1   1 
ATOM   6721  O  OE2   . GLU A 1 865 ? 125.609 90.010  148.838 1.00 105.73 ? 865  GLU A OE2   1 
ATOM   6722  N  N     . VAL A 1 866 ? 130.721 90.840  147.295 1.00 103.61 ? 866  VAL A N     1 
ATOM   6723  C  CA    . VAL A 1 866 ? 130.945 90.718  145.862 1.00 102.27 ? 866  VAL A CA    1 
ATOM   6724  C  C     . VAL A 1 866 ? 132.444 90.642  145.603 1.00 101.80 ? 866  VAL A C     1 
ATOM   6725  O  O     . VAL A 1 866 ? 133.263 91.046  146.430 1.00 100.86 ? 866  VAL A O     1 
ATOM   6726  C  CB    . VAL A 1 866 ? 130.319 91.885  145.069 1.00 102.56 ? 866  VAL A CB    1 
ATOM   6727  C  CG1   . VAL A 1 866 ? 128.801 91.783  145.077 1.00 100.51 ? 866  VAL A CG1   1 
ATOM   6728  C  CG2   . VAL A 1 866 ? 130.766 93.214  145.647 1.00 101.38 ? 866  VAL A CG2   1 
ATOM   6729  N  N     . ALA A 1 867 ? 132.797 90.113  144.433 1.00 98.28  ? 867  ALA A N     1 
ATOM   6730  C  CA    . ALA A 1 867 ? 134.192 89.909  144.071 1.00 97.77  ? 867  ALA A CA    1 
ATOM   6731  C  C     . ALA A 1 867 ? 134.413 90.273  142.610 1.00 96.45  ? 867  ALA A C     1 
ATOM   6732  O  O     . ALA A 1 867 ? 133.488 90.229  141.795 1.00 94.14  ? 867  ALA A O     1 
ATOM   6733  C  CB    . ALA A 1 867 ? 134.629 88.460  144.317 1.00 96.43  ? 867  ALA A CB    1 
ATOM   6734  N  N     . ILE A 1 868 ? 135.652 90.637  142.290 1.00 92.25  ? 868  ILE A N     1 
ATOM   6735  C  CA    . ILE A 1 868 ? 136.076 90.895  140.918 1.00 90.52  ? 868  ILE A CA    1 
ATOM   6736  C  C     . ILE A 1 868 ? 137.251 89.975  140.608 1.00 90.65  ? 868  ILE A C     1 
ATOM   6737  O  O     . ILE A 1 868 ? 138.271 89.997  141.308 1.00 92.61  ? 868  ILE A O     1 
ATOM   6738  C  CB    . ILE A 1 868 ? 136.434 92.375  140.689 1.00 91.08  ? 868  ILE A CB    1 
ATOM   6739  C  CG1   . ILE A 1 868 ? 137.365 92.908  141.777 1.00 91.28  ? 868  ILE A CG1   1 
ATOM   6740  C  CG2   . ILE A 1 868 ? 135.177 93.220  140.664 1.00 90.52  ? 868  ILE A CG2   1 
ATOM   6741  C  CD1   . ILE A 1 868 ? 137.647 94.388  141.660 1.00 90.23  ? 868  ILE A CD1   1 
ATOM   6742  N  N     . ILE A 1 869 ? 137.100 89.152  139.569 1.00 91.29  ? 869  ILE A N     1 
ATOM   6743  C  CA    . ILE A 1 869 ? 138.096 88.158  139.197 1.00 90.95  ? 869  ILE A CA    1 
ATOM   6744  C  C     . ILE A 1 869 ? 138.351 88.248  137.699 1.00 91.88  ? 869  ILE A C     1 
ATOM   6745  O  O     . ILE A 1 869 ? 137.556 88.800  136.938 1.00 93.14  ? 869  ILE A O     1 
ATOM   6746  C  CB    . ILE A 1 869 ? 137.670 86.727  139.589 1.00 91.00  ? 869  ILE A CB    1 
ATOM   6747  C  CG1   . ILE A 1 869 ? 136.267 86.422  139.066 1.00 90.25  ? 869  ILE A CG1   1 
ATOM   6748  C  CG2   . ILE A 1 869 ? 137.725 86.550  141.096 1.00 93.07  ? 869  ILE A CG2   1 
ATOM   6749  C  CD1   . ILE A 1 869 ? 135.700 85.121  139.579 1.00 90.71  ? 869  ILE A CD1   1 
ATOM   6750  N  N     . GLU A 1 870 ? 139.489 87.703  137.284 1.00 94.17  ? 870  GLU A N     1 
ATOM   6751  C  CA    . GLU A 1 870 ? 139.972 87.833  135.917 1.00 93.78  ? 870  GLU A CA    1 
ATOM   6752  C  C     . GLU A 1 870 ? 139.718 86.544  135.150 1.00 94.00  ? 870  GLU A C     1 
ATOM   6753  O  O     . GLU A 1 870 ? 139.986 85.450  135.658 1.00 93.60  ? 870  GLU A O     1 
ATOM   6754  C  CB    . GLU A 1 870 ? 141.464 88.169  135.905 1.00 95.06  ? 870  GLU A CB    1 
ATOM   6755  C  CG    . GLU A 1 870 ? 142.079 88.251  134.520 1.00 94.10  ? 870  GLU A CG    1 
ATOM   6756  C  CD    . GLU A 1 870 ? 141.727 89.533  133.800 1.00 94.73  ? 870  GLU A CD    1 
ATOM   6757  O  OE1   . GLU A 1 870 ? 141.240 90.475  134.458 1.00 93.48  ? 870  GLU A OE1   1 
ATOM   6758  O  OE2   . GLU A 1 870 ? 141.941 89.602  132.573 1.00 95.66  ? 870  GLU A OE2   1 
ATOM   6759  N  N     . GLY A 1 871 ? 139.202 86.677  133.932 1.00 94.86  ? 871  GLY A N     1 
ATOM   6760  C  CA    . GLY A 1 871 ? 138.959 85.541  133.080 1.00 95.93  ? 871  GLY A CA    1 
ATOM   6761  C  C     . GLY A 1 871 ? 140.244 84.843  132.684 1.00 96.75  ? 871  GLY A C     1 
ATOM   6762  O  O     . GLY A 1 871 ? 141.292 85.474  132.521 1.00 95.96  ? 871  GLY A O     1 
ATOM   6763  N  N     . PRO A 1 872 ? 140.191 83.515  132.527 1.00 102.16 ? 872  PRO A N     1 
ATOM   6764  C  CA    . PRO A 1 872 ? 139.037 82.626  132.725 1.00 102.24 ? 872  PRO A CA    1 
ATOM   6765  C  C     . PRO A 1 872 ? 138.748 82.397  134.203 1.00 102.88 ? 872  PRO A C     1 
ATOM   6766  O  O     . PRO A 1 872 ? 139.668 82.352  135.015 1.00 102.82 ? 872  PRO A O     1 
ATOM   6767  C  CB    . PRO A 1 872 ? 139.478 81.340  132.018 1.00 102.05 ? 872  PRO A CB    1 
ATOM   6768  C  CG    . PRO A 1 872 ? 140.965 81.322  132.203 1.00 101.50 ? 872  PRO A CG    1 
ATOM   6769  C  CD    . PRO A 1 872 ? 141.390 82.767  132.108 1.00 101.07 ? 872  PRO A CD    1 
ATOM   6770  N  N     . ALA A 1 873 ? 137.482 82.250  134.586 1.00 99.90  ? 873  ALA A N     1 
ATOM   6771  C  CA    . ALA A 1 873 ? 137.140 82.115  135.993 1.00 99.12  ? 873  ALA A CA    1 
ATOM   6772  C  C     . ALA A 1 873 ? 135.793 81.422  136.120 1.00 99.03  ? 873  ALA A C     1 
ATOM   6773  O  O     . ALA A 1 873 ? 135.010 81.360  135.168 1.00 98.57  ? 873  ALA A O     1 
ATOM   6774  C  CB    . ALA A 1 873 ? 137.116 83.475  136.694 1.00 97.44  ? 873  ALA A CB    1 
ATOM   6775  N  N     . GLU A 1 874 ? 135.536 80.904  137.319 1.00 102.70 ? 874  GLU A N     1 
ATOM   6776  C  CA    . GLU A 1 874 ? 134.307 80.199  137.640 1.00 103.24 ? 874  GLU A CA    1 
ATOM   6777  C  C     . GLU A 1 874 ? 133.453 81.049  138.565 1.00 104.85 ? 874  GLU A C     1 
ATOM   6778  O  O     . GLU A 1 874 ? 133.979 81.607  139.537 1.00 103.93 ? 874  GLU A O     1 
ATOM   6779  C  CB    . GLU A 1 874 ? 134.620 78.854  138.306 1.00 103.38 ? 874  GLU A CB    1 
ATOM   6780  C  CG    . GLU A 1 874 ? 133.395 78.032  138.676 1.00 103.82 ? 874  GLU A CG    1 
ATOM   6781  C  CD    . GLU A 1 874 ? 133.755 76.704  139.312 1.00 104.98 ? 874  GLU A CD    1 
ATOM   6782  O  OE1   . GLU A 1 874 ? 134.962 76.424  139.465 1.00 104.92 ? 874  GLU A OE1   1 
ATOM   6783  O  OE2   . GLU A 1 874 ? 132.830 75.940  139.659 1.00 104.28 ? 874  GLU A OE2   1 
ATOM   6784  N  N     . PRO A 1 875 ? 132.154 81.186  138.295 1.00 105.95 ? 875  PRO A N     1 
ATOM   6785  C  CA    . PRO A 1 875 ? 131.305 82.015  139.159 1.00 104.18 ? 875  PRO A CA    1 
ATOM   6786  C  C     . PRO A 1 875 ? 131.239 81.471  140.579 1.00 104.91 ? 875  PRO A C     1 
ATOM   6787  O  O     . PRO A 1 875 ? 131.225 80.259  140.804 1.00 105.66 ? 875  PRO A O     1 
ATOM   6788  C  CB    . PRO A 1 875 ? 129.936 81.961  138.471 1.00 101.93 ? 875  PRO A CB    1 
ATOM   6789  C  CG    . PRO A 1 875 ? 129.977 80.733  137.628 1.00 101.90 ? 875  PRO A CG    1 
ATOM   6790  C  CD    . PRO A 1 875 ? 131.397 80.607  137.172 1.00 103.41 ? 875  PRO A CD    1 
ATOM   6791  N  N     . MET A 1 876 ? 131.201 82.388  141.539 1.00 107.37 ? 876  MET A N     1 
ATOM   6792  C  CA    . MET A 1 876 ? 131.150 82.055  142.953 1.00 107.33 ? 876  MET A CA    1 
ATOM   6793  C  C     . MET A 1 876 ? 129.720 82.154  143.470 1.00 107.27 ? 876  MET A C     1 
ATOM   6794  O  O     . MET A 1 876 ? 128.809 82.619  142.780 1.00 106.05 ? 876  MET A O     1 
ATOM   6795  C  CB    . MET A 1 876 ? 132.072 82.979  143.754 1.00 106.14 ? 876  MET A CB    1 
ATOM   6796  C  CG    . MET A 1 876 ? 133.500 83.025  143.244 1.00 106.08 ? 876  MET A CG    1 
ATOM   6797  S  SD    . MET A 1 876 ? 134.518 84.193  144.163 1.00 108.16 ? 876  MET A SD    1 
ATOM   6798  C  CE    . MET A 1 876 ? 136.085 84.011  143.317 1.00 106.11 ? 876  MET A CE    1 
ATOM   6799  N  N     . ASP A 1 877 ? 129.529 81.694  144.709 1.00 110.94 ? 877  ASP A N     1 
ATOM   6800  C  CA    . ASP A 1 877 ? 128.226 81.828  145.353 1.00 110.62 ? 877  ASP A CA    1 
ATOM   6801  C  C     . ASP A 1 877 ? 127.861 83.294  145.547 1.00 110.83 ? 877  ASP A C     1 
ATOM   6802  O  O     . ASP A 1 877 ? 126.713 83.692  145.320 1.00 110.68 ? 877  ASP A O     1 
ATOM   6803  C  CB    . ASP A 1 877 ? 128.224 81.090  146.691 1.00 110.56 ? 877  ASP A CB    1 
ATOM   6804  C  CG    . ASP A 1 877 ? 128.551 79.617  146.544 1.00 111.71 ? 877  ASP A CG    1 
ATOM   6805  O  OD1   . ASP A 1 877 ? 128.793 79.172  145.403 1.00 111.56 ? 877  ASP A OD1   1 
ATOM   6806  O  OD2   . ASP A 1 877 ? 128.566 78.904  147.570 1.00 111.74 ? 877  ASP A OD2   1 
ATOM   6807  N  N     . VAL A 1 878 ? 128.824 84.108  145.965 1.00 107.95 ? 878  VAL A N     1 
ATOM   6808  C  CA    . VAL A 1 878 ? 128.638 85.551  146.081 1.00 106.65 ? 878  VAL A CA    1 
ATOM   6809  C  C     . VAL A 1 878 ? 128.541 86.131  144.675 1.00 107.48 ? 878  VAL A C     1 
ATOM   6810  O  O     . VAL A 1 878 ? 129.075 85.535  143.728 1.00 107.36 ? 878  VAL A O     1 
ATOM   6811  C  CB    . VAL A 1 878 ? 129.782 86.196  146.879 1.00 107.54 ? 878  VAL A CB    1 
ATOM   6812  C  CG1   . VAL A 1 878 ? 129.723 85.760  148.332 1.00 107.47 ? 878  VAL A CG1   1 
ATOM   6813  C  CG2   . VAL A 1 878 ? 131.123 85.830  146.270 1.00 108.17 ? 878  VAL A CG2   1 
ATOM   6814  N  N     . PRO A 1 879 ? 127.855 87.258  144.481 1.00 103.55 ? 879  PRO A N     1 
ATOM   6815  C  CA    . PRO A 1 879 ? 127.822 87.885  143.149 1.00 102.69 ? 879  PRO A CA    1 
ATOM   6816  C  C     . PRO A 1 879 ? 129.220 88.269  142.692 1.00 101.80 ? 879  PRO A C     1 
ATOM   6817  O  O     . PRO A 1 879 ? 129.883 89.112  143.298 1.00 99.90  ? 879  PRO A O     1 
ATOM   6818  C  CB    . PRO A 1 879 ? 126.931 89.113  143.361 1.00 100.26 ? 879  PRO A CB    1 
ATOM   6819  C  CG    . PRO A 1 879 ? 126.064 88.748  144.512 1.00 100.57 ? 879  PRO A CG    1 
ATOM   6820  C  CD    . PRO A 1 879 ? 126.920 87.906  145.416 1.00 101.63 ? 879  PRO A CD    1 
ATOM   6821  N  N     . THR A 1 880 ? 129.662 87.642  141.609 1.00 94.31  ? 880  THR A N     1 
ATOM   6822  C  CA    . THR A 1 880 ? 131.026 87.770  141.126 1.00 94.77  ? 880  THR A CA    1 
ATOM   6823  C  C     . THR A 1 880 ? 131.064 88.535  139.811 1.00 95.73  ? 880  THR A C     1 
ATOM   6824  O  O     . THR A 1 880 ? 130.160 88.427  138.978 1.00 94.99  ? 880  THR A O     1 
ATOM   6825  C  CB    . THR A 1 880 ? 131.668 86.396  140.931 1.00 93.59  ? 880  THR A CB    1 
ATOM   6826  O  OG1   . THR A 1 880 ? 132.873 86.536  140.172 1.00 95.12  ? 880  THR A OG1   1 
ATOM   6827  C  CG2   . THR A 1 880 ? 130.719 85.473  140.194 1.00 92.64  ? 880  THR A CG2   1 
ATOM   6828  N  N     . LEU A 1 881 ? 132.124 89.315  139.637 1.00 90.11  ? 881  LEU A N     1 
ATOM   6829  C  CA    . LEU A 1 881 ? 132.390 90.024  138.395 1.00 87.70  ? 881  LEU A CA    1 
ATOM   6830  C  C     . LEU A 1 881 ? 133.638 89.425  137.764 1.00 88.79  ? 881  LEU A C     1 
ATOM   6831  O  O     . LEU A 1 881 ? 134.709 89.424  138.380 1.00 91.51  ? 881  LEU A O     1 
ATOM   6832  C  CB    . LEU A 1 881 ? 132.569 91.521  138.645 1.00 88.15  ? 881  LEU A CB    1 
ATOM   6833  C  CG    . LEU A 1 881 ? 132.890 92.388  137.426 1.00 87.76  ? 881  LEU A CG    1 
ATOM   6834  C  CD1   . LEU A 1 881 ? 131.827 92.207  136.357 1.00 89.10  ? 881  LEU A CD1   1 
ATOM   6835  C  CD2   . LEU A 1 881 ? 133.008 93.849  137.815 1.00 85.68  ? 881  LEU A CD2   1 
ATOM   6836  N  N     . ILE A 1 882 ? 133.501 88.911  136.548 1.00 84.67  ? 882  ILE A N     1 
ATOM   6837  C  CA    . ILE A 1 882 ? 134.625 88.383  135.788 1.00 83.32  ? 882  ILE A CA    1 
ATOM   6838  C  C     . ILE A 1 882 ? 134.853 89.306  134.600 1.00 84.04  ? 882  ILE A C     1 
ATOM   6839  O  O     . ILE A 1 882 ? 133.945 89.528  133.789 1.00 86.09  ? 882  ILE A O     1 
ATOM   6840  C  CB    . ILE A 1 882 ? 134.389 86.928  135.350 1.00 84.52  ? 882  ILE A CB    1 
ATOM   6841  C  CG1   . ILE A 1 882 ? 135.382 86.520  134.263 1.00 85.48  ? 882  ILE A CG1   1 
ATOM   6842  C  CG2   . ILE A 1 882 ? 132.966 86.721  134.887 1.00 83.41  ? 882  ILE A CG2   1 
ATOM   6843  C  CD1   . ILE A 1 882 ? 135.258 85.073  133.853 1.00 87.43  ? 882  ILE A CD1   1 
ATOM   6844  N  N     . LEU A 1 883 ? 136.056 89.860  134.508 1.00 86.50  ? 883  LEU A N     1 
ATOM   6845  C  CA    . LEU A 1 883 ? 136.402 90.823  133.472 1.00 87.45  ? 883  LEU A CA    1 
ATOM   6846  C  C     . LEU A 1 883 ? 137.355 90.175  132.481 1.00 88.75  ? 883  LEU A C     1 
ATOM   6847  O  O     . LEU A 1 883 ? 138.474 89.797  132.844 1.00 91.05  ? 883  LEU A O     1 
ATOM   6848  C  CB    . LEU A 1 883 ? 137.035 92.076  134.075 1.00 86.56  ? 883  LEU A CB    1 
ATOM   6849  C  CG    . LEU A 1 883 ? 136.143 92.963  134.941 1.00 86.49  ? 883  LEU A CG    1 
ATOM   6850  C  CD1   . LEU A 1 883 ? 136.858 94.257  135.269 1.00 85.60  ? 883  LEU A CD1   1 
ATOM   6851  C  CD2   . LEU A 1 883 ? 134.825 93.242  134.242 1.00 89.69  ? 883  LEU A CD2   1 
ATOM   6852  N  N     . HIS A 1 884 ? 136.911 90.047  131.238 1.00 83.37  ? 884  HIS A N     1 
ATOM   6853  C  CA    . HIS A 1 884 ? 137.780 89.653  130.144 1.00 83.13  ? 884  HIS A CA    1 
ATOM   6854  C  C     . HIS A 1 884 ? 138.351 90.914  129.499 1.00 84.77  ? 884  HIS A C     1 
ATOM   6855  O  O     . HIS A 1 884 ? 138.258 92.015  130.048 1.00 83.45  ? 884  HIS A O     1 
ATOM   6856  C  CB    . HIS A 1 884 ? 137.023 88.790  129.140 1.00 83.26  ? 884  HIS A CB    1 
ATOM   6857  C  CG    . HIS A 1 884 ? 136.350 87.600  129.749 1.00 84.34  ? 884  HIS A CG    1 
ATOM   6858  N  ND1   . HIS A 1 884 ? 137.023 86.437  130.049 1.00 84.65  ? 884  HIS A ND1   1 
ATOM   6859  C  CD2   . HIS A 1 884 ? 135.060 87.390  130.102 1.00 85.88  ? 884  HIS A CD2   1 
ATOM   6860  C  CE1   . HIS A 1 884 ? 136.179 85.563  130.566 1.00 85.48  ? 884  HIS A CE1   1 
ATOM   6861  N  NE2   . HIS A 1 884 ? 134.981 86.116  130.610 1.00 86.92  ? 884  HIS A NE2   1 
ATOM   6862  N  N     . ASP A 1 885 ? 138.959 90.769  128.322 1.00 82.91  ? 885  ASP A N     1 
ATOM   6863  C  CA    . ASP A 1 885 ? 139.496 91.910  127.591 1.00 83.07  ? 885  ASP A CA    1 
ATOM   6864  C  C     . ASP A 1 885 ? 138.761 92.145  126.275 1.00 81.51  ? 885  ASP A C     1 
ATOM   6865  O  O     . ASP A 1 885 ? 139.246 92.894  125.423 1.00 79.81  ? 885  ASP A O     1 
ATOM   6866  C  CB    . ASP A 1 885 ? 140.994 91.726  127.343 1.00 83.53  ? 885  ASP A CB    1 
ATOM   6867  C  CG    . ASP A 1 885 ? 141.735 93.043  127.262 1.00 84.37  ? 885  ASP A CG    1 
ATOM   6868  O  OD1   . ASP A 1 885 ? 141.097 94.097  127.464 1.00 84.44  ? 885  ASP A OD1   1 
ATOM   6869  O  OD2   . ASP A 1 885 ? 142.956 93.026  126.997 1.00 83.59  ? 885  ASP A OD2   1 
ATOM   6870  N  N     . GLY A 1 886 ? 137.603 91.530  126.095 1.00 77.24  ? 886  GLY A N     1 
ATOM   6871  C  CA    . GLY A 1 886 ? 136.825 91.678  124.874 1.00 79.28  ? 886  GLY A CA    1 
ATOM   6872  C  C     . GLY A 1 886 ? 135.479 92.317  125.153 1.00 77.08  ? 886  GLY A C     1 
ATOM   6873  O  O     . GLY A 1 886 ? 134.854 92.037  126.177 1.00 76.29  ? 886  GLY A O     1 
ATOM   6874  N  N     . VAL A 1 887 ? 135.035 93.168  124.225 1.00 68.42  ? 887  VAL A N     1 
ATOM   6875  C  CA    . VAL A 1 887 ? 133.805 93.931  124.429 1.00 69.47  ? 887  VAL A CA    1 
ATOM   6876  C  C     . VAL A 1 887 ? 132.602 93.000  124.516 1.00 68.38  ? 887  VAL A C     1 
ATOM   6877  O  O     . VAL A 1 887 ? 131.758 93.125  125.411 1.00 70.65  ? 887  VAL A O     1 
ATOM   6878  C  CB    . VAL A 1 887 ? 133.636 94.978  123.313 1.00 69.28  ? 887  VAL A CB    1 
ATOM   6879  C  CG1   . VAL A 1 887 ? 134.045 94.398  121.969 1.00 68.99  ? 887  VAL A CG1   1 
ATOM   6880  C  CG2   . VAL A 1 887 ? 132.203 95.488  123.267 1.00 70.53  ? 887  VAL A CG2   1 
ATOM   6881  N  N     . ASN A 1 888 ? 132.511 92.044  123.596 1.00 72.24  ? 888  ASN A N     1 
ATOM   6882  C  CA    . ASN A 1 888 ? 131.428 91.066  123.585 1.00 72.64  ? 888  ASN A CA    1 
ATOM   6883  C  C     . ASN A 1 888 ? 131.901 89.716  124.102 1.00 73.51  ? 888  ASN A C     1 
ATOM   6884  O  O     . ASN A 1 888 ? 131.502 88.664  123.596 1.00 76.03  ? 888  ASN A O     1 
ATOM   6885  C  CB    . ASN A 1 888 ? 130.843 90.938  122.183 1.00 70.54  ? 888  ASN A CB    1 
ATOM   6886  C  CG    . ASN A 1 888 ? 129.447 90.354  122.186 1.00 70.81  ? 888  ASN A CG    1 
ATOM   6887  O  OD1   . ASN A 1 888 ? 128.758 90.369  123.205 1.00 69.63  ? 888  ASN A OD1   1 
ATOM   6888  N  ND2   . ASN A 1 888 ? 129.021 89.834  121.042 1.00 74.97  ? 888  ASN A ND2   1 
ATOM   6889  N  N     . ALA A 1 889 ? 132.770 89.730  125.115 1.00 71.80  ? 889  ALA A N     1 
ATOM   6890  C  CA    . ALA A 1 889 ? 133.240 88.491  125.718 1.00 72.51  ? 889  ALA A CA    1 
ATOM   6891  C  C     . ALA A 1 889 ? 132.119 87.724  126.399 1.00 72.25  ? 889  ALA A C     1 
ATOM   6892  O  O     . ALA A 1 889 ? 132.266 86.523  126.647 1.00 73.10  ? 889  ALA A O     1 
ATOM   6893  C  CB    . ALA A 1 889 ? 134.356 88.785  126.718 1.00 74.35  ? 889  ALA A CB    1 
ATOM   6894  N  N     . THR A 1 890 ? 131.006 88.386  126.709 1.00 70.79  ? 890  THR A N     1 
ATOM   6895  C  CA    . THR A 1 890 ? 129.820 87.720  127.221 1.00 72.88  ? 890  THR A CA    1 
ATOM   6896  C  C     . THR A 1 890 ? 128.927 87.196  126.098 1.00 72.28  ? 890  THR A C     1 
ATOM   6897  O  O     . THR A 1 890 ? 127.739 86.940  126.323 1.00 76.90  ? 890  THR A O     1 
ATOM   6898  C  CB    . THR A 1 890 ? 129.044 88.668  128.139 1.00 72.04  ? 890  THR A CB    1 
ATOM   6899  O  OG1   . THR A 1 890 ? 129.958 89.594  128.739 1.00 72.17  ? 890  THR A OG1   1 
ATOM   6900  C  CG2   . THR A 1 890 ? 128.350 87.893  129.250 1.00 73.27  ? 890  THR A CG2   1 
ATOM   6901  N  N     . GLY A 1 891 ? 129.474 87.037  124.893 1.00 72.08  ? 891  GLY A N     1 
ATOM   6902  C  CA    . GLY A 1 891 ? 128.760 86.386  123.811 1.00 75.69  ? 891  GLY A CA    1 
ATOM   6903  C  C     . GLY A 1 891 ? 128.680 84.883  123.930 1.00 75.51  ? 891  GLY A C     1 
ATOM   6904  O  O     . GLY A 1 891 ? 127.982 84.243  123.138 1.00 72.43  ? 891  GLY A O     1 
ATOM   6905  N  N     . LEU A 1 892 ? 129.386 84.309  124.904 1.00 78.64  ? 892  LEU A N     1 
ATOM   6906  C  CA    . LEU A 1 892 ? 129.295 82.888  125.208 1.00 78.67  ? 892  LEU A CA    1 
ATOM   6907  C  C     . LEU A 1 892 ? 128.142 82.552  126.144 1.00 82.29  ? 892  LEU A C     1 
ATOM   6908  O  O     . LEU A 1 892 ? 127.891 81.367  126.387 1.00 85.31  ? 892  LEU A O     1 
ATOM   6909  C  CB    . LEU A 1 892 ? 130.614 82.404  125.817 1.00 81.16  ? 892  LEU A CB    1 
ATOM   6910  C  CG    . LEU A 1 892 ? 131.411 83.405  126.662 1.00 83.05  ? 892  LEU A CG    1 
ATOM   6911  C  CD1   . LEU A 1 892 ? 130.751 83.685  128.003 1.00 82.74  ? 892  LEU A CD1   1 
ATOM   6912  C  CD2   . LEU A 1 892 ? 132.836 82.919  126.862 1.00 83.87  ? 892  LEU A CD2   1 
ATOM   6913  N  N     . ILE A 1 893 ? 127.439 83.557  126.674 1.00 79.62  ? 893  ILE A N     1 
ATOM   6914  C  CA    . ILE A 1 893 ? 126.345 83.292  127.599 1.00 78.67  ? 893  ILE A CA    1 
ATOM   6915  C  C     . ILE A 1 893 ? 125.133 82.708  126.885 1.00 78.11  ? 893  ILE A C     1 
ATOM   6916  O  O     . ILE A 1 893 ? 124.272 82.099  127.530 1.00 79.04  ? 893  ILE A O     1 
ATOM   6917  C  CB    . ILE A 1 893 ? 125.969 84.574  128.367 1.00 78.52  ? 893  ILE A CB    1 
ATOM   6918  C  CG1   . ILE A 1 893 ? 125.270 84.227  129.683 1.00 78.53  ? 893  ILE A CG1   1 
ATOM   6919  C  CG2   . ILE A 1 893 ? 125.080 85.472  127.523 1.00 79.63  ? 893  ILE A CG2   1 
ATOM   6920  C  CD1   . ILE A 1 893 ? 126.116 83.397  130.624 1.00 80.00  ? 893  ILE A CD1   1 
ATOM   6921  N  N     . LYS A 1 894 ? 125.044 82.866  125.569 1.00 78.61  ? 894  LYS A N     1 
ATOM   6922  C  CA    . LYS A 1 894 ? 123.953 82.297  124.787 1.00 79.77  ? 894  LYS A CA    1 
ATOM   6923  C  C     . LYS A 1 894 ? 124.423 81.321  123.722 1.00 82.54  ? 894  LYS A C     1 
ATOM   6924  O  O     . LYS A 1 894 ? 123.784 80.287  123.515 1.00 84.00  ? 894  LYS A O     1 
ATOM   6925  C  CB    . LYS A 1 894 ? 123.136 83.415  124.124 1.00 80.01  ? 894  LYS A CB    1 
ATOM   6926  C  CG    . LYS A 1 894 ? 121.783 83.661  124.767 1.00 78.61  ? 894  LYS A CG    1 
ATOM   6927  C  CD    . LYS A 1 894 ? 121.924 84.065  126.220 1.00 81.09  ? 894  LYS A CD    1 
ATOM   6928  C  CE    . LYS A 1 894 ? 120.571 84.363  126.841 1.00 81.34  ? 894  LYS A CE    1 
ATOM   6929  N  NZ    . LYS A 1 894 ? 120.692 84.762  128.270 1.00 82.32  ? 894  LYS A NZ    1 
ATOM   6930  N  N     . ALA A 1 895 ? 125.523 81.624  123.033 1.00 83.58  ? 895  ALA A N     1 
ATOM   6931  C  CA    . ALA A 1 895 ? 126.013 80.727  121.994 1.00 83.31  ? 895  ALA A CA    1 
ATOM   6932  C  C     . ALA A 1 895 ? 126.718 79.512  122.583 1.00 83.70  ? 895  ALA A C     1 
ATOM   6933  O  O     . ALA A 1 895 ? 126.614 78.409  122.036 1.00 83.14  ? 895  ALA A O     1 
ATOM   6934  C  CB    . ALA A 1 895 ? 126.949 81.478  121.049 1.00 83.50  ? 895  ALA A CB    1 
ATOM   6935  N  N     . GLY A 1 896 ? 127.425 79.688  123.698 1.00 84.93  ? 896  GLY A N     1 
ATOM   6936  C  CA    . GLY A 1 896 ? 128.233 78.615  124.241 1.00 83.35  ? 896  GLY A CA    1 
ATOM   6937  C  C     . GLY A 1 896 ? 129.337 78.239  123.278 1.00 83.19  ? 896  GLY A C     1 
ATOM   6938  O  O     . GLY A 1 896 ? 129.560 77.059  122.995 1.00 83.10  ? 896  GLY A O     1 
ATOM   6939  N  N     . VAL A 1 897 ? 130.029 79.256  122.760 1.00 89.43  ? 897  VAL A N     1 
ATOM   6940  C  CA    . VAL A 1 897 ? 130.962 79.070  121.656 1.00 91.50  ? 897  VAL A CA    1 
ATOM   6941  C  C     . VAL A 1 897 ? 132.185 78.245  122.055 1.00 92.58  ? 897  VAL A C     1 
ATOM   6942  O  O     . VAL A 1 897 ? 132.908 77.758  121.177 1.00 92.30  ? 897  VAL A O     1 
ATOM   6943  C  CB    . VAL A 1 897 ? 131.354 80.457  121.104 1.00 88.30  ? 897  VAL A CB    1 
ATOM   6944  C  CG1   . VAL A 1 897 ? 132.277 81.176  122.068 1.00 88.77  ? 897  VAL A CG1   1 
ATOM   6945  C  CG2   . VAL A 1 897 ? 131.964 80.352  119.717 1.00 89.73  ? 897  VAL A CG2   1 
ATOM   6946  N  N     . THR A 1 898 ? 132.426 78.062  123.357 1.00 97.94  ? 898  THR A N     1 
ATOM   6947  C  CA    . THR A 1 898 ? 133.544 77.282  123.893 1.00 99.67  ? 898  THR A CA    1 
ATOM   6948  C  C     . THR A 1 898 ? 134.898 77.811  123.431 1.00 99.55  ? 898  THR A C     1 
ATOM   6949  O  O     . THR A 1 898 ? 134.988 78.901  122.858 1.00 98.86  ? 898  THR A O     1 
ATOM   6950  C  CB    . THR A 1 898 ? 133.421 75.796  123.528 1.00 100.10 ? 898  THR A CB    1 
ATOM   6951  O  OG1   . THR A 1 898 ? 133.587 75.624  122.115 1.00 100.38 ? 898  THR A OG1   1 
ATOM   6952  C  CG2   . THR A 1 898 ? 132.067 75.248  123.952 1.00 99.51  ? 898  THR A CG2   1 
ATOM   6953  N  N     . GLY A 1 899 ? 135.957 77.049  123.690 1.00 106.09 ? 899  GLY A N     1 
ATOM   6954  C  CA    . GLY A 1 899 ? 137.312 77.471  123.416 1.00 107.13 ? 899  GLY A CA    1 
ATOM   6955  C  C     . GLY A 1 899 ? 137.898 76.828  122.176 1.00 107.29 ? 899  GLY A C     1 
ATOM   6956  O  O     . GLY A 1 899 ? 137.184 76.329  121.299 1.00 105.40 ? 899  GLY A O     1 
ATOM   6957  N  N     . ILE A 1 900 ? 139.226 76.845  122.105 1.00 111.49 ? 900  ILE A N     1 
ATOM   6958  C  CA    . ILE A 1 900 ? 139.974 76.296  120.977 1.00 110.97 ? 900  ILE A CA    1 
ATOM   6959  C  C     . ILE A 1 900 ? 139.748 74.790  120.925 1.00 111.37 ? 900  ILE A C     1 
ATOM   6960  O  O     . ILE A 1 900 ? 140.025 74.089  121.909 1.00 110.77 ? 900  ILE A O     1 
ATOM   6961  C  CB    . ILE A 1 900 ? 141.473 76.616  121.095 1.00 111.05 ? 900  ILE A CB    1 
ATOM   6962  C  CG1   . ILE A 1 900 ? 141.689 78.027  121.644 1.00 110.37 ? 900  ILE A CG1   1 
ATOM   6963  C  CG2   . ILE A 1 900 ? 142.160 76.457  119.747 1.00 111.38 ? 900  ILE A CG2   1 
ATOM   6964  C  CD1   . ILE A 1 900 ? 141.361 79.125  120.666 1.00 110.42 ? 900  ILE A CD1   1 
ATOM   6965  N  N     . PRO A 1 901 ? 139.257 74.246  119.811 1.00 115.81 ? 901  PRO A N     1 
ATOM   6966  C  CA    . PRO A 1 901 ? 139.002 72.805  119.725 1.00 116.45 ? 901  PRO A CA    1 
ATOM   6967  C  C     . PRO A 1 901 ? 140.216 71.964  119.363 1.00 116.76 ? 901  PRO A C     1 
ATOM   6968  O  O     . PRO A 1 901 ? 140.052 70.767  119.111 1.00 117.10 ? 901  PRO A O     1 
ATOM   6969  C  CB    . PRO A 1 901 ? 137.937 72.725  118.622 1.00 116.67 ? 901  PRO A CB    1 
ATOM   6970  C  CG    . PRO A 1 901 ? 138.269 73.858  117.727 1.00 115.96 ? 901  PRO A CG    1 
ATOM   6971  C  CD    . PRO A 1 901 ? 138.795 74.961  118.609 1.00 116.03 ? 901  PRO A CD    1 
ATOM   6972  N  N     . GLU A 1 902 ? 141.411 72.557  119.325 1.00 120.39 ? 902  GLU A N     1 
ATOM   6973  C  CA    . GLU A 1 902 ? 142.664 71.844  119.070 1.00 120.70 ? 902  GLU A CA    1 
ATOM   6974  C  C     . GLU A 1 902 ? 142.626 71.120  117.720 1.00 121.33 ? 902  GLU A C     1 
ATOM   6975  O  O     . GLU A 1 902 ? 142.664 69.892  117.635 1.00 121.05 ? 902  GLU A O     1 
ATOM   6976  C  CB    . GLU A 1 902 ? 142.984 70.875  120.215 1.00 120.37 ? 902  GLU A CB    1 
ATOM   6977  C  CG    . GLU A 1 902 ? 144.426 70.392  120.246 1.00 120.43 ? 902  GLU A CG    1 
ATOM   6978  C  CD    . GLU A 1 902 ? 144.705 69.467  121.413 1.00 121.24 ? 902  GLU A CD    1 
ATOM   6979  O  OE1   . GLU A 1 902 ? 143.768 69.193  122.193 1.00 121.39 ? 902  GLU A OE1   1 
ATOM   6980  O  OE2   . GLU A 1 902 ? 145.860 69.013  121.551 1.00 121.19 ? 902  GLU A OE2   1 
ATOM   6981  N  N     . ALA A 1 903 ? 142.539 71.913  116.658 1.00 121.52 ? 903  ALA A N     1 
ATOM   6982  C  CA    . ALA A 1 903 ? 142.528 71.411  115.292 1.00 121.05 ? 903  ALA A CA    1 
ATOM   6983  C  C     . ALA A 1 903 ? 143.824 71.797  114.586 1.00 121.12 ? 903  ALA A C     1 
ATOM   6984  O  O     . ALA A 1 903 ? 144.729 72.396  115.173 1.00 120.15 ? 903  ALA A O     1 
ATOM   6985  C  CB    . ALA A 1 903 ? 141.307 71.936  114.534 1.00 120.67 ? 903  ALA A CB    1 
ATOM   6986  N  N     . LYS A 1 904 ? 143.907 71.443  113.305 1.00 118.88 ? 904  LYS A N     1 
ATOM   6987  C  CA    . LYS A 1 904 ? 145.077 71.727  112.481 1.00 118.55 ? 904  LYS A CA    1 
ATOM   6988  C  C     . LYS A 1 904 ? 144.806 72.996  111.682 1.00 118.24 ? 904  LYS A C     1 
ATOM   6989  O  O     . LYS A 1 904 ? 143.946 73.002  110.795 1.00 117.14 ? 904  LYS A O     1 
ATOM   6990  C  CB    . LYS A 1 904 ? 145.391 70.551  111.559 1.00 117.07 ? 904  LYS A CB    1 
ATOM   6991  C  CG    . LYS A 1 904 ? 146.592 70.776  110.656 1.00 116.83 ? 904  LYS A CG    1 
ATOM   6992  C  CD    . LYS A 1 904 ? 146.916 69.528  109.851 1.00 117.27 ? 904  LYS A CD    1 
ATOM   6993  C  CE    . LYS A 1 904 ? 145.739 69.104  108.988 1.00 117.30 ? 904  LYS A CE    1 
ATOM   6994  N  NZ    . LYS A 1 904 ? 146.039 67.870  108.210 1.00 117.31 ? 904  LYS A NZ    1 
ATOM   6995  N  N     . ALA A 1 905 ? 145.531 74.068  112.020 1.00 121.45 ? 905  ALA A N     1 
ATOM   6996  C  CA    . ALA A 1 905 ? 145.403 75.402  111.432 1.00 121.13 ? 905  ALA A CA    1 
ATOM   6997  C  C     . ALA A 1 905 ? 144.060 76.033  111.782 1.00 121.21 ? 905  ALA A C     1 
ATOM   6998  O  O     . ALA A 1 905 ? 143.061 75.333  111.969 1.00 121.29 ? 905  ALA A O     1 
ATOM   6999  C  CB    . ALA A 1 905 ? 145.610 75.367  109.915 1.00 120.97 ? 905  ALA A CB    1 
ATOM   7000  N  N     . TYR A 1 906 ? 144.021 77.359  111.883 1.00 119.29 ? 906  TYR A N     1 
ATOM   7001  C  CA    . TYR A 1 906 ? 142.820 78.042  112.337 1.00 118.85 ? 906  TYR A CA    1 
ATOM   7002  C  C     . TYR A 1 906 ? 142.606 79.316  111.539 1.00 118.46 ? 906  TYR A C     1 
ATOM   7003  O  O     . TYR A 1 906 ? 143.553 79.921  111.030 1.00 118.42 ? 906  TYR A O     1 
ATOM   7004  C  CB    . TYR A 1 906 ? 142.892 78.398  113.829 1.00 118.75 ? 906  TYR A CB    1 
ATOM   7005  C  CG    . TYR A 1 906 ? 143.229 77.243  114.743 1.00 119.42 ? 906  TYR A CG    1 
ATOM   7006  C  CD1   . TYR A 1 906 ? 142.243 76.378  115.196 1.00 119.14 ? 906  TYR A CD1   1 
ATOM   7007  C  CD2   . TYR A 1 906 ? 144.534 77.027  115.164 1.00 118.95 ? 906  TYR A CD2   1 
ATOM   7008  C  CE1   . TYR A 1 906 ? 142.547 75.328  116.035 1.00 118.55 ? 906  TYR A CE1   1 
ATOM   7009  C  CE2   . TYR A 1 906 ? 144.847 75.979  116.002 1.00 118.83 ? 906  TYR A CE2   1 
ATOM   7010  C  CZ    . TYR A 1 906 ? 143.852 75.134  116.435 1.00 119.08 ? 906  TYR A CZ    1 
ATOM   7011  O  OH    . TYR A 1 906 ? 144.167 74.090  117.269 1.00 119.60 ? 906  TYR A OH    1 
ATOM   7012  N  N     . VAL A 1 907 ? 141.344 79.719  111.442 1.00 114.86 ? 907  VAL A N     1 
ATOM   7013  C  CA    . VAL A 1 907 ? 140.965 81.047  110.980 1.00 114.99 ? 907  VAL A CA    1 
ATOM   7014  C  C     . VAL A 1 907 ? 140.347 81.774  112.169 1.00 115.99 ? 907  VAL A C     1 
ATOM   7015  O  O     . VAL A 1 907 ? 139.345 81.320  112.736 1.00 115.29 ? 907  VAL A O     1 
ATOM   7016  C  CB    . VAL A 1 907 ? 140.007 80.986  109.779 1.00 115.12 ? 907  VAL A CB    1 
ATOM   7017  C  CG1   . VAL A 1 907 ? 139.007 79.853  109.942 1.00 115.27 ? 907  VAL A CG1   1 
ATOM   7018  C  CG2   . VAL A 1 907 ? 139.293 82.313  109.594 1.00 114.04 ? 907  VAL A CG2   1 
ATOM   7019  N  N     . VAL A 1 908 ? 140.963 82.883  112.566 1.00 113.38 ? 908  VAL A N     1 
ATOM   7020  C  CA    . VAL A 1 908 ? 140.554 83.641  113.742 1.00 112.27 ? 908  VAL A CA    1 
ATOM   7021  C  C     . VAL A 1 908 ? 140.186 85.050  113.296 1.00 112.07 ? 908  VAL A C     1 
ATOM   7022  O  O     . VAL A 1 908 ? 140.962 85.710  112.597 1.00 112.41 ? 908  VAL A O     1 
ATOM   7023  C  CB    . VAL A 1 908 ? 141.659 83.658  114.816 1.00 111.86 ? 908  VAL A CB    1 
ATOM   7024  C  CG1   . VAL A 1 908 ? 143.020 83.917  114.189 1.00 111.49 ? 908  VAL A CG1   1 
ATOM   7025  C  CG2   . VAL A 1 908 ? 141.355 84.691  115.887 1.00 110.80 ? 908  VAL A CG2   1 
ATOM   7026  N  N     . ILE A 1 909 ? 138.999 85.501  113.687 1.00 104.25 ? 909  ILE A N     1 
ATOM   7027  C  CA    . ILE A 1 909 ? 138.451 86.775  113.237 1.00 105.17 ? 909  ILE A CA    1 
ATOM   7028  C  C     . ILE A 1 909 ? 138.763 87.812  114.309 1.00 103.64 ? 909  ILE A C     1 
ATOM   7029  O  O     . ILE A 1 909 ? 138.061 87.912  115.318 1.00 104.46 ? 909  ILE A O     1 
ATOM   7030  C  CB    . ILE A 1 909 ? 136.951 86.671  112.962 1.00 104.10 ? 909  ILE A CB    1 
ATOM   7031  C  CG1   . ILE A 1 909 ? 136.668 85.423  112.127 1.00 103.42 ? 909  ILE A CG1   1 
ATOM   7032  C  CG2   . ILE A 1 909 ? 136.457 87.921  112.258 1.00 104.80 ? 909  ILE A CG2   1 
ATOM   7033  C  CD1   . ILE A 1 909 ? 135.245 85.303  111.666 1.00 102.57 ? 909  ILE A CD1   1 
ATOM   7034  N  N     . GLY A 1 910 ? 139.805 88.596  114.083 1.00 98.28  ? 910  GLY A N     1 
ATOM   7035  C  CA    . GLY A 1 910 ? 140.294 89.555  115.049 1.00 98.03  ? 910  GLY A CA    1 
ATOM   7036  C  C     . GLY A 1 910 ? 141.650 89.151  115.606 1.00 98.37  ? 910  GLY A C     1 
ATOM   7037  O  O     . GLY A 1 910 ? 142.049 87.984  115.581 1.00 99.46  ? 910  GLY A O     1 
ATOM   7038  N  N     . ASN A 1 911 ? 142.369 90.146  116.117 1.00 101.86 ? 911  ASN A N     1 
ATOM   7039  C  CA    . ASN A 1 911 ? 143.708 89.941  116.654 1.00 102.28 ? 911  ASN A CA    1 
ATOM   7040  C  C     . ASN A 1 911 ? 143.670 89.980  118.176 1.00 102.56 ? 911  ASN A C     1 
ATOM   7041  O  O     . ASN A 1 911 ? 143.110 90.909  118.767 1.00 103.25 ? 911  ASN A O     1 
ATOM   7042  C  CB    . ASN A 1 911 ? 144.682 90.991  116.116 1.00 103.05 ? 911  ASN A CB    1 
ATOM   7043  C  CG    . ASN A 1 911 ? 144.223 92.408  116.386 1.00 104.02 ? 911  ASN A CG    1 
ATOM   7044  O  OD1   . ASN A 1 911 ? 144.557 92.996  117.414 1.00 103.27 ? 911  ASN A OD1   1 
ATOM   7045  N  ND2   . ASN A 1 911 ? 143.454 92.968  115.459 1.00 103.95 ? 911  ASN A ND2   1 
ATOM   7046  N  N     . SER A 1 912 ? 144.254 88.968  118.801 1.00 105.46 ? 912  SER A N     1 
ATOM   7047  C  CA    . SER A 1 912 ? 144.314 88.843  120.247 1.00 106.39 ? 912  SER A CA    1 
ATOM   7048  C  C     . SER A 1 912 ? 145.680 88.304  120.636 1.00 106.67 ? 912  SER A C     1 
ATOM   7049  O  O     . SER A 1 912 ? 146.345 87.645  119.829 1.00 106.71 ? 912  SER A O     1 
ATOM   7050  C  CB    . SER A 1 912 ? 143.211 87.916  120.779 1.00 106.45 ? 912  SER A CB    1 
ATOM   7051  O  OG    . SER A 1 912 ? 141.925 88.445  120.510 1.00 106.16 ? 912  SER A OG    1 
ATOM   7052  N  N     . PRO A 1 913 ? 146.136 88.582  121.860 1.00 107.92 ? 913  PRO A N     1 
ATOM   7053  C  CA    . PRO A 1 913 ? 147.415 88.005  122.307 1.00 107.14 ? 913  PRO A CA    1 
ATOM   7054  C  C     . PRO A 1 913 ? 147.409 86.489  122.368 1.00 107.98 ? 913  PRO A C     1 
ATOM   7055  O  O     . PRO A 1 913 ? 148.476 85.870  122.266 1.00 108.26 ? 913  PRO A O     1 
ATOM   7056  C  CB    . PRO A 1 913 ? 147.609 88.626  123.697 1.00 106.56 ? 913  PRO A CB    1 
ATOM   7057  C  CG    . PRO A 1 913 ? 146.814 89.882  123.661 1.00 106.24 ? 913  PRO A CG    1 
ATOM   7058  C  CD    . PRO A 1 913 ? 145.617 89.574  122.816 1.00 107.63 ? 913  PRO A CD    1 
ATOM   7059  N  N     . ALA A 1 914 ? 146.240 85.868  122.524 1.00 112.31 ? 914  ALA A N     1 
ATOM   7060  C  CA    . ALA A 1 914 ? 146.147 84.416  122.625 1.00 112.72 ? 914  ALA A CA    1 
ATOM   7061  C  C     . ALA A 1 914 ? 146.336 83.712  121.289 1.00 112.97 ? 914  ALA A C     1 
ATOM   7062  O  O     . ALA A 1 914 ? 146.321 82.477  121.256 1.00 112.98 ? 914  ALA A O     1 
ATOM   7063  C  CB    . ALA A 1 914 ? 144.803 84.017  123.235 1.00 112.07 ? 914  ALA A CB    1 
ATOM   7064  N  N     . ILE A 1 915 ? 146.497 84.460  120.195 1.00 111.89 ? 915  ILE A N     1 
ATOM   7065  C  CA    . ILE A 1 915 ? 146.765 83.847  118.899 1.00 110.95 ? 915  ILE A CA    1 
ATOM   7066  C  C     . ILE A 1 915 ? 148.108 83.132  118.912 1.00 112.26 ? 915  ILE A C     1 
ATOM   7067  O  O     . ILE A 1 915 ? 148.268 82.081  118.278 1.00 112.71 ? 915  ILE A O     1 
ATOM   7068  C  CB    . ILE A 1 915 ? 146.687 84.916  117.791 1.00 111.61 ? 915  ILE A CB    1 
ATOM   7069  C  CG1   . ILE A 1 915 ? 145.265 85.470  117.701 1.00 112.56 ? 915  ILE A CG1   1 
ATOM   7070  C  CG2   . ILE A 1 915 ? 147.113 84.349  116.448 1.00 112.30 ? 915  ILE A CG2   1 
ATOM   7071  C  CD1   . ILE A 1 915 ? 145.079 86.502  116.620 1.00 112.08 ? 915  ILE A CD1   1 
ATOM   7072  N  N     . SER A 1 916 ? 149.087 83.674  119.641 1.00 113.36 ? 916  SER A N     1 
ATOM   7073  C  CA    . SER A 1 916 ? 150.393 83.030  119.737 1.00 113.51 ? 916  SER A CA    1 
ATOM   7074  C  C     . SER A 1 916 ? 150.298 81.645  120.365 1.00 113.71 ? 916  SER A C     1 
ATOM   7075  O  O     . SER A 1 916 ? 151.136 80.779  120.088 1.00 112.63 ? 916  SER A O     1 
ATOM   7076  C  CB    . SER A 1 916 ? 151.351 83.908  120.541 1.00 113.00 ? 916  SER A CB    1 
ATOM   7077  O  OG    . SER A 1 916 ? 150.850 84.139  121.846 1.00 112.50 ? 916  SER A OG    1 
ATOM   7078  N  N     . LYS A 1 917 ? 149.288 81.414  121.204 1.00 112.59 ? 917  LYS A N     1 
ATOM   7079  C  CA    . LYS A 1 917 ? 149.094 80.107  121.815 1.00 111.81 ? 917  LYS A CA    1 
ATOM   7080  C  C     . LYS A 1 917 ? 148.611 79.054  120.826 1.00 112.30 ? 917  LYS A C     1 
ATOM   7081  O  O     . LYS A 1 917 ? 148.641 77.864  121.157 1.00 111.98 ? 917  LYS A O     1 
ATOM   7082  C  CB    . LYS A 1 917 ? 148.101 80.214  122.973 1.00 111.67 ? 917  LYS A CB    1 
ATOM   7083  C  CG    . LYS A 1 917 ? 148.546 81.147  124.087 1.00 112.17 ? 917  LYS A CG    1 
ATOM   7084  C  CD    . LYS A 1 917 ? 147.501 81.229  125.189 1.00 112.67 ? 917  LYS A CD    1 
ATOM   7085  C  CE    . LYS A 1 917 ? 147.230 79.861  125.796 1.00 111.97 ? 917  LYS A CE    1 
ATOM   7086  N  NZ    . LYS A 1 917 ? 146.196 79.923  126.866 1.00 111.56 ? 917  LYS A NZ    1 
ATOM   7087  N  N     . LEU A 1 918 ? 148.168 79.453  119.638 1.00 114.14 ? 918  LEU A N     1 
ATOM   7088  C  CA    . LEU A 1 918 ? 147.671 78.494  118.663 1.00 114.54 ? 918  LEU A CA    1 
ATOM   7089  C  C     . LEU A 1 918 ? 148.803 77.634  118.113 1.00 114.87 ? 918  LEU A C     1 
ATOM   7090  O  O     . LEU A 1 918 ? 149.944 78.082  117.967 1.00 113.95 ? 918  LEU A O     1 
ATOM   7091  C  CB    . LEU A 1 918 ? 146.963 79.212  117.514 1.00 114.31 ? 918  LEU A CB    1 
ATOM   7092  C  CG    . LEU A 1 918 ? 145.640 79.904  117.840 1.00 114.71 ? 918  LEU A CG    1 
ATOM   7093  C  CD1   . LEU A 1 918 ? 145.072 80.575  116.599 1.00 114.70 ? 918  LEU A CD1   1 
ATOM   7094  C  CD2   . LEU A 1 918 ? 144.646 78.909  118.418 1.00 113.23 ? 918  LEU A CD2   1 
ATOM   7095  N  N     . LYS A 1 919 ? 148.472 76.384  117.804 1.00 119.66 ? 919  LYS A N     1 
ATOM   7096  C  CA    . LYS A 1 919 ? 149.407 75.442  117.206 1.00 119.67 ? 919  LYS A CA    1 
ATOM   7097  C  C     . LYS A 1 919 ? 149.092 75.313  115.721 1.00 119.76 ? 919  LYS A C     1 
ATOM   7098  O  O     . LYS A 1 919 ? 147.980 74.922  115.350 1.00 119.58 ? 919  LYS A O     1 
ATOM   7099  C  CB    . LYS A 1 919 ? 149.326 74.082  117.896 1.00 118.40 ? 919  LYS A CB    1 
ATOM   7100  C  CG    . LYS A 1 919 ? 149.576 74.133  119.393 1.00 118.43 ? 919  LYS A CG    1 
ATOM   7101  C  CD    . LYS A 1 919 ? 149.424 72.759  120.025 1.00 119.36 ? 919  LYS A CD    1 
ATOM   7102  C  CE    . LYS A 1 919 ? 149.646 72.814  121.528 1.00 119.51 ? 919  LYS A CE    1 
ATOM   7103  N  NZ    . LYS A 1 919 ? 149.486 71.476  122.161 1.00 118.92 ? 919  LYS A NZ    1 
ATOM   7104  N  N     . GLY A 1 920 ? 150.068 75.634  114.880 1.00 123.88 ? 920  GLY A N     1 
ATOM   7105  C  CA    . GLY A 1 920 ? 149.894 75.614  113.444 1.00 123.62 ? 920  GLY A CA    1 
ATOM   7106  C  C     . GLY A 1 920 ? 149.716 77.009  112.869 1.00 123.31 ? 920  GLY A C     1 
ATOM   7107  O  O     . GLY A 1 920 ? 149.577 78.006  113.581 1.00 123.51 ? 920  GLY A O     1 
ATOM   7108  N  N     . GLU A 1 921 ? 149.732 77.066  111.541 1.00 121.67 ? 921  GLU A N     1 
ATOM   7109  C  CA    . GLU A 1 921 ? 149.568 78.334  110.844 1.00 122.40 ? 921  GLU A CA    1 
ATOM   7110  C  C     . GLU A 1 921 ? 148.148 78.857  111.017 1.00 122.58 ? 921  GLU A C     1 
ATOM   7111  O  O     . GLU A 1 921 ? 147.177 78.098  110.957 1.00 122.56 ? 921  GLU A O     1 
ATOM   7112  C  CB    . GLU A 1 921 ? 149.892 78.170  109.362 1.00 122.38 ? 921  GLU A CB    1 
ATOM   7113  C  CG    . GLU A 1 921 ? 151.286 77.635  109.092 1.00 122.08 ? 921  GLU A CG    1 
ATOM   7114  C  CD    . GLU A 1 921 ? 151.569 77.472  107.611 1.00 121.99 ? 921  GLU A CD    1 
ATOM   7115  O  OE1   . GLU A 1 921 ? 150.673 77.776  106.797 1.00 122.16 ? 921  GLU A OE1   1 
ATOM   7116  O  OE2   . GLU A 1 921 ? 152.688 77.040  107.262 1.00 121.30 ? 921  GLU A OE2   1 
ATOM   7117  N  N     . TYR A 1 922 ? 148.031 80.165  111.226 1.00 115.72 ? 922  TYR A N     1 
ATOM   7118  C  CA    . TYR A 1 922 ? 146.754 80.801  111.516 1.00 115.04 ? 922  TYR A CA    1 
ATOM   7119  C  C     . TYR A 1 922 ? 146.487 81.917  110.517 1.00 114.63 ? 922  TYR A C     1 
ATOM   7120  O  O     . TYR A 1 922 ? 147.396 82.666  110.150 1.00 114.53 ? 922  TYR A O     1 
ATOM   7121  C  CB    . TYR A 1 922 ? 146.728 81.358  112.946 1.00 114.69 ? 922  TYR A CB    1 
ATOM   7122  C  CG    . TYR A 1 922 ? 147.933 82.203  113.298 1.00 115.12 ? 922  TYR A CG    1 
ATOM   7123  C  CD1   . TYR A 1 922 ? 147.951 83.567  113.037 1.00 114.50 ? 922  TYR A CD1   1 
ATOM   7124  C  CD2   . TYR A 1 922 ? 149.050 81.638  113.897 1.00 114.82 ? 922  TYR A CD2   1 
ATOM   7125  C  CE1   . TYR A 1 922 ? 149.048 84.340  113.355 1.00 114.33 ? 922  TYR A CE1   1 
ATOM   7126  C  CE2   . TYR A 1 922 ? 150.151 82.406  114.220 1.00 115.29 ? 922  TYR A CE2   1 
ATOM   7127  C  CZ    . TYR A 1 922 ? 150.144 83.756  113.947 1.00 115.26 ? 922  TYR A CZ    1 
ATOM   7128  O  OH    . TYR A 1 922 ? 151.237 84.526  114.267 1.00 114.63 ? 922  TYR A OH    1 
ATOM   7129  N  N     . LEU A 1 923 ? 145.239 82.014  110.075 1.00 113.73 ? 923  LEU A N     1 
ATOM   7130  C  CA    . LEU A 1 923 ? 144.788 83.094  109.205 1.00 113.67 ? 923  LEU A CA    1 
ATOM   7131  C  C     . LEU A 1 923 ? 143.920 84.028  110.036 1.00 113.25 ? 923  LEU A C     1 
ATOM   7132  O  O     . LEU A 1 923 ? 142.800 83.671  110.416 1.00 111.65 ? 923  LEU A O     1 
ATOM   7133  C  CB    . LEU A 1 923 ? 144.018 82.556  108.003 1.00 112.88 ? 923  LEU A CB    1 
ATOM   7134  C  CG    . LEU A 1 923 ? 143.503 83.611  107.023 1.00 112.54 ? 923  LEU A CG    1 
ATOM   7135  C  CD1   . LEU A 1 923 ? 144.662 84.327  106.356 1.00 112.58 ? 923  LEU A CD1   1 
ATOM   7136  C  CD2   . LEU A 1 923 ? 142.587 82.986  105.987 1.00 112.68 ? 923  LEU A CD2   1 
ATOM   7137  N  N     . ILE A 1 924 ? 144.436 85.218  110.320 1.00 113.43 ? 924  ILE A N     1 
ATOM   7138  C  CA    . ILE A 1 924 ? 143.708 86.213  111.095 1.00 113.24 ? 924  ILE A CA    1 
ATOM   7139  C  C     . ILE A 1 924 ? 142.847 87.016  110.128 1.00 113.60 ? 924  ILE A C     1 
ATOM   7140  O  O     . ILE A 1 924 ? 143.354 87.863  109.390 1.00 114.41 ? 924  ILE A O     1 
ATOM   7141  C  CB    . ILE A 1 924 ? 144.658 87.128  111.877 1.00 112.54 ? 924  ILE A CB    1 
ATOM   7142  C  CG1   . ILE A 1 924 ? 145.601 86.307  112.752 1.00 113.01 ? 924  ILE A CG1   1 
ATOM   7143  C  CG2   . ILE A 1 924 ? 143.870 88.108  112.728 1.00 112.39 ? 924  ILE A CG2   1 
ATOM   7144  C  CD1   . ILE A 1 924 ? 146.682 87.136  113.406 1.00 113.01 ? 924  ILE A CD1   1 
ATOM   7145  N  N     . LEU A 1 925 ? 141.558 86.745  110.119 1.00 107.14 ? 925  LEU A N     1 
ATOM   7146  C  CA    . LEU A 1 925 ? 140.694 87.617  109.340 1.00 105.73 ? 925  LEU A CA    1 
ATOM   7147  C  C     . LEU A 1 925 ? 140.475 88.928  110.090 1.00 106.26 ? 925  LEU A C     1 
ATOM   7148  O  O     . LEU A 1 925 ? 140.359 88.928  111.318 1.00 107.11 ? 925  LEU A O     1 
ATOM   7149  C  CB    . LEU A 1 925 ? 139.350 86.950  109.065 1.00 105.15 ? 925  LEU A CB    1 
ATOM   7150  C  CG    . LEU A 1 925 ? 139.337 85.780  108.084 1.00 107.47 ? 925  LEU A CG    1 
ATOM   7151  C  CD1   . LEU A 1 925 ? 137.906 85.412  107.720 1.00 107.46 ? 925  LEU A CD1   1 
ATOM   7152  C  CD2   . LEU A 1 925 ? 140.142 86.115  106.842 1.00 107.78 ? 925  LEU A CD2   1 
ATOM   7153  N  N     . PRO A 1 926 ? 140.431 90.055  109.387 1.00 104.24 ? 926  PRO A N     1 
ATOM   7154  C  CA    . PRO A 1 926 ? 140.120 91.320  110.059 1.00 103.95 ? 926  PRO A CA    1 
ATOM   7155  C  C     . PRO A 1 926 ? 138.700 91.324  110.602 1.00 104.16 ? 926  PRO A C     1 
ATOM   7156  O  O     . PRO A 1 926 ? 137.763 90.854  109.953 1.00 104.08 ? 926  PRO A O     1 
ATOM   7157  C  CB    . PRO A 1 926 ? 140.304 92.365  108.953 1.00 104.07 ? 926  PRO A CB    1 
ATOM   7158  C  CG    . PRO A 1 926 ? 140.123 91.605  107.687 1.00 104.07 ? 926  PRO A CG    1 
ATOM   7159  C  CD    . PRO A 1 926 ? 140.679 90.238  107.948 1.00 104.51 ? 926  PRO A CD    1 
ATOM   7160  N  N     . SER A 1 927 ? 138.550 91.866  111.807 1.00 91.01  ? 927  SER A N     1 
ATOM   7161  C  CA    . SER A 1 927 ? 137.260 91.945  112.476 1.00 89.24  ? 927  SER A CA    1 
ATOM   7162  C  C     . SER A 1 927 ? 136.470 93.185  112.091 1.00 88.22  ? 927  SER A C     1 
ATOM   7163  O  O     . SER A 1 927 ? 135.352 93.367  112.581 1.00 90.71  ? 927  SER A O     1 
ATOM   7164  C  CB    . SER A 1 927 ? 137.452 91.913  113.994 1.00 89.16  ? 927  SER A CB    1 
ATOM   7165  O  OG    . SER A 1 927 ? 138.268 92.989  114.422 1.00 88.88  ? 927  SER A OG    1 
ATOM   7166  N  N     . GLY A 1 928 ? 137.025 94.042  111.240 1.00 78.91  ? 928  GLY A N     1 
ATOM   7167  C  CA    . GLY A 1 928 ? 136.341 95.234  110.793 1.00 78.97  ? 928  GLY A CA    1 
ATOM   7168  C  C     . GLY A 1 928 ? 136.517 96.405  111.742 1.00 78.56  ? 928  GLY A C     1 
ATOM   7169  O  O     . GLY A 1 928 ? 136.956 96.272  112.886 1.00 78.21  ? 928  GLY A O     1 
ATOM   7170  N  N     . LEU A 1 929 ? 136.168 97.583  111.237 1.00 69.87  ? 929  LEU A N     1 
ATOM   7171  C  CA    . LEU A 1 929 ? 136.195 98.784  112.057 1.00 66.90  ? 929  LEU A CA    1 
ATOM   7172  C  C     . LEU A 1 929 ? 135.012 98.777  113.016 1.00 66.57  ? 929  LEU A C     1 
ATOM   7173  O  O     . LEU A 1 929 ? 133.872 98.532  112.610 1.00 66.90  ? 929  LEU A O     1 
ATOM   7174  C  CB    . LEU A 1 929 ? 136.168 100.027 111.170 1.00 65.29  ? 929  LEU A CB    1 
ATOM   7175  C  CG    . LEU A 1 929 ? 136.363 101.370 111.868 1.00 63.99  ? 929  LEU A CG    1 
ATOM   7176  C  CD1   . LEU A 1 929 ? 137.559 101.301 112.775 1.00 65.99  ? 929  LEU A CD1   1 
ATOM   7177  C  CD2   . LEU A 1 929 ? 136.543 102.479 110.850 1.00 65.88  ? 929  LEU A CD2   1 
ATOM   7178  N  N     . TRP A 1 930 ? 135.288 99.033  114.295 1.00 51.57  ? 930  TRP A N     1 
ATOM   7179  C  CA    . TRP A 1 930 ? 134.246 98.947  115.314 1.00 50.80  ? 930  TRP A CA    1 
ATOM   7180  C  C     . TRP A 1 930 ? 133.187 100.025 115.126 1.00 56.71  ? 930  TRP A C     1 
ATOM   7181  O  O     . TRP A 1 930 ? 131.991 99.766  115.303 1.00 56.05  ? 930  TRP A O     1 
ATOM   7182  C  CB    . TRP A 1 930 ? 134.873 99.039  116.705 1.00 57.90  ? 930  TRP A CB    1 
ATOM   7183  C  CG    . TRP A 1 930 ? 133.898 98.872  117.825 1.00 56.10  ? 930  TRP A CG    1 
ATOM   7184  C  CD1   . TRP A 1 930 ? 133.471 99.834  118.690 1.00 50.90  ? 930  TRP A CD1   1 
ATOM   7185  C  CD2   . TRP A 1 930 ? 133.229 97.666  118.205 1.00 53.03  ? 930  TRP A CD2   1 
ATOM   7186  N  NE1   . TRP A 1 930 ? 132.578 99.303  119.586 1.00 51.54  ? 930  TRP A NE1   1 
ATOM   7187  C  CE2   . TRP A 1 930 ? 132.412 97.972  119.308 1.00 52.49  ? 930  TRP A CE2   1 
ATOM   7188  C  CE3   . TRP A 1 930 ? 133.242 96.356  117.719 1.00 52.61  ? 930  TRP A CE3   1 
ATOM   7189  C  CZ2   . TRP A 1 930 ? 131.614 97.019  119.932 1.00 56.53  ? 930  TRP A CZ2   1 
ATOM   7190  C  CZ3   . TRP A 1 930 ? 132.451 95.413  118.340 1.00 54.29  ? 930  TRP A CZ3   1 
ATOM   7191  C  CH2   . TRP A 1 930 ? 131.648 95.748  119.434 1.00 54.09  ? 930  TRP A CH2   1 
ATOM   7192  N  N     . ALA A 1 931 ? 133.604 101.239 114.759 1.00 60.69  ? 931  ALA A N     1 
ATOM   7193  C  CA    . ALA A 1 931 ? 132.676 102.351 114.600 1.00 54.58  ? 931  ALA A CA    1 
ATOM   7194  C  C     . ALA A 1 931 ? 131.743 102.188 113.408 1.00 56.91  ? 931  ALA A C     1 
ATOM   7195  O  O     . ALA A 1 931 ? 130.759 102.928 113.311 1.00 55.26  ? 931  ALA A O     1 
ATOM   7196  C  CB    . ALA A 1 931 ? 133.452 103.662 114.471 1.00 50.93  ? 931  ALA A CB    1 
ATOM   7197  N  N     . GLU A 1 932 ? 132.018 101.244 112.508 1.00 67.83  ? 932  GLU A N     1 
ATOM   7198  C  CA    . GLU A 1 932 ? 131.217 101.033 111.312 1.00 66.12  ? 932  GLU A CA    1 
ATOM   7199  C  C     . GLU A 1 932 ? 130.258 99.858  111.448 1.00 68.36  ? 932  GLU A C     1 
ATOM   7200  O  O     . GLU A 1 932 ? 129.718 99.388  110.441 1.00 71.40  ? 932  GLU A O     1 
ATOM   7201  C  CB    . GLU A 1 932 ? 132.122 100.818 110.100 1.00 65.30  ? 932  GLU A CB    1 
ATOM   7202  C  CG    . GLU A 1 932 ? 133.016 101.988 109.763 1.00 65.91  ? 932  GLU A CG    1 
ATOM   7203  C  CD    . GLU A 1 932 ? 133.911 101.695 108.578 1.00 71.14  ? 932  GLU A CD    1 
ATOM   7204  O  OE1   . GLU A 1 932 ? 134.129 100.502 108.280 1.00 73.09  ? 932  GLU A OE1   1 
ATOM   7205  O  OE2   . GLU A 1 932 ? 134.393 102.652 107.941 1.00 70.85  ? 932  GLU A OE2   1 
ATOM   7206  N  N     . LYS A 1 933 ? 130.037 99.370  112.662 1.00 63.26  ? 933  LYS A N     1 
ATOM   7207  C  CA    . LYS A 1 933 ? 129.246 98.172  112.887 1.00 62.80  ? 933  LYS A CA    1 
ATOM   7208  C  C     . LYS A 1 933 ? 127.958 98.514  113.620 1.00 64.04  ? 933  LYS A C     1 
ATOM   7209  O  O     . LYS A 1 933 ? 127.946 99.363  114.517 1.00 69.02  ? 933  LYS A O     1 
ATOM   7210  C  CB    . LYS A 1 933 ? 130.043 97.139  113.684 1.00 65.98  ? 933  LYS A CB    1 
ATOM   7211  C  CG    . LYS A 1 933 ? 129.468 95.743  113.637 1.00 64.54  ? 933  LYS A CG    1 
ATOM   7212  C  CD    . LYS A 1 933 ? 130.391 94.760  114.325 1.00 64.66  ? 933  LYS A CD    1 
ATOM   7213  C  CE    . LYS A 1 933 ? 131.769 94.770  113.699 1.00 65.40  ? 933  LYS A CE    1 
ATOM   7214  N  NZ    . LYS A 1 933 ? 132.655 93.753  114.317 1.00 68.64  ? 933  LYS A NZ    1 
ATOM   7215  N  N     . GLU A 1 934 ? 126.873 97.853  113.230 1.00 59.77  ? 934  GLU A N     1 
ATOM   7216  C  CA    . GLU A 1 934 ? 125.589 97.982  113.901 1.00 57.84  ? 934  GLU A CA    1 
ATOM   7217  C  C     . GLU A 1 934 ? 125.211 96.636  114.497 1.00 63.63  ? 934  GLU A C     1 
ATOM   7218  O  O     . GLU A 1 934 ? 125.264 95.610  113.811 1.00 68.07  ? 934  GLU A O     1 
ATOM   7219  C  CB    . GLU A 1 934 ? 124.501 98.464  112.942 1.00 57.81  ? 934  GLU A CB    1 
ATOM   7220  C  CG    . GLU A 1 934 ? 123.144 98.620  113.593 1.00 58.09  ? 934  GLU A CG    1 
ATOM   7221  C  CD    . GLU A 1 934 ? 122.129 99.261  112.674 1.00 66.66  ? 934  GLU A CD    1 
ATOM   7222  O  OE1   . GLU A 1 934 ? 122.501 99.630  111.541 1.00 66.50  ? 934  GLU A OE1   1 
ATOM   7223  O  OE2   . GLU A 1 934 ? 120.958 99.398  113.085 1.00 68.83  ? 934  GLU A OE2   1 
ATOM   7224  N  N     . GLY A 1 935 ? 124.840 96.643  115.768 1.00 63.16  ? 935  GLY A N     1 
ATOM   7225  C  CA    . GLY A 1 935 ? 124.469 95.419  116.443 1.00 62.49  ? 935  GLY A CA    1 
ATOM   7226  C  C     . GLY A 1 935 ? 124.297 95.668  117.924 1.00 63.52  ? 935  GLY A C     1 
ATOM   7227  O  O     . GLY A 1 935 ? 124.370 96.803  118.404 1.00 62.62  ? 935  GLY A O     1 
ATOM   7228  N  N     . THR A 1 936 ? 124.061 94.577  118.640 1.00 64.42  ? 936  THR A N     1 
ATOM   7229  C  CA    . THR A 1 936 ? 123.909 94.601  120.085 1.00 60.85  ? 936  THR A CA    1 
ATOM   7230  C  C     . THR A 1 936 ? 125.047 93.815  120.719 1.00 64.64  ? 936  THR A C     1 
ATOM   7231  O  O     . THR A 1 936 ? 125.465 92.780  120.191 1.00 72.86  ? 936  THR A O     1 
ATOM   7232  C  CB    . THR A 1 936 ? 122.560 94.013  120.506 1.00 61.78  ? 936  THR A CB    1 
ATOM   7233  O  OG1   . THR A 1 936 ? 121.526 94.537  119.664 1.00 64.09  ? 936  THR A OG1   1 
ATOM   7234  C  CG2   . THR A 1 936 ? 122.248 94.378  121.941 1.00 62.11  ? 936  THR A CG2   1 
ATOM   7235  N  N     . VAL A 1 937 ? 125.563 94.318  121.838 1.00 60.76  ? 937  VAL A N     1 
ATOM   7236  C  CA    . VAL A 1 937 ? 126.629 93.645  122.565 1.00 64.41  ? 937  VAL A CA    1 
ATOM   7237  C  C     . VAL A 1 937 ? 126.185 93.439  124.006 1.00 65.64  ? 937  VAL A C     1 
ATOM   7238  O  O     . VAL A 1 937 ? 125.315 94.142  124.525 1.00 68.45  ? 937  VAL A O     1 
ATOM   7239  C  CB    . VAL A 1 937 ? 127.961 94.423  122.516 1.00 65.94  ? 937  VAL A CB    1 
ATOM   7240  C  CG1   . VAL A 1 937 ? 128.408 94.634  121.078 1.00 66.12  ? 937  VAL A CG1   1 
ATOM   7241  C  CG2   . VAL A 1 937 ? 127.834 95.749  123.244 1.00 59.68  ? 937  VAL A CG2   1 
ATOM   7242  N  N     . THR A 1 938 ? 126.794 92.449  124.650 1.00 65.50  ? 938  THR A N     1 
ATOM   7243  C  CA    . THR A 1 938 ? 126.569 92.164  126.061 1.00 63.99  ? 938  THR A CA    1 
ATOM   7244  C  C     . THR A 1 938 ? 127.867 92.417  126.814 1.00 63.29  ? 938  THR A C     1 
ATOM   7245  O  O     . THR A 1 938 ? 128.908 91.848  126.470 1.00 68.62  ? 938  THR A O     1 
ATOM   7246  C  CB    . THR A 1 938 ? 126.093 90.727  126.268 1.00 69.00  ? 938  THR A CB    1 
ATOM   7247  O  OG1   . THR A 1 938 ? 124.895 90.505  125.516 1.00 66.89  ? 938  THR A OG1   1 
ATOM   7248  C  CG2   . THR A 1 938 ? 125.809 90.469  127.738 1.00 69.47  ? 938  THR A CG2   1 
ATOM   7249  N  N     . ASN A 1 939 ? 127.802 93.267  127.831 1.00 60.42  ? 939  ASN A N     1 
ATOM   7250  C  CA    . ASN A 1 939 ? 128.975 93.658  128.594 1.00 63.47  ? 939  ASN A CA    1 
ATOM   7251  C  C     . ASN A 1 939 ? 129.150 92.728  129.793 1.00 66.13  ? 939  ASN A C     1 
ATOM   7252  O  O     . ASN A 1 939 ? 128.531 91.664  129.880 1.00 69.83  ? 939  ASN A O     1 
ATOM   7253  C  CB    . ASN A 1 939 ? 128.861 95.119  129.015 1.00 61.74  ? 939  ASN A CB    1 
ATOM   7254  C  CG    . ASN A 1 939 ? 127.728 95.357  129.986 1.00 64.48  ? 939  ASN A CG    1 
ATOM   7255  O  OD1   . ASN A 1 939 ? 126.797 94.557  130.078 1.00 66.42  ? 939  ASN A OD1   1 
ATOM   7256  N  ND2   . ASN A 1 939 ? 127.798 96.463  130.717 1.00 61.03  ? 939  ASN A ND2   1 
ATOM   7257  N  N     . ALA A 1 940 ? 130.016 93.123  130.729 1.00 67.33  ? 940  ALA A N     1 
ATOM   7258  C  CA    . ALA A 1 940 ? 130.245 92.317  131.923 1.00 66.92  ? 940  ALA A CA    1 
ATOM   7259  C  C     . ALA A 1 940 ? 128.984 92.205  132.771 1.00 67.37  ? 940  ALA A C     1 
ATOM   7260  O  O     . ALA A 1 940 ? 128.683 91.133  133.310 1.00 71.03  ? 940  ALA A O     1 
ATOM   7261  C  CB    . ALA A 1 940 ? 131.389 92.912  132.743 1.00 67.28  ? 940  ALA A CB    1 
ATOM   7262  N  N     . PHE A 1 941 ? 128.232 93.295  132.899 1.00 66.55  ? 941  PHE A N     1 
ATOM   7263  C  CA    . PHE A 1 941 ? 127.050 93.315  133.750 1.00 66.64  ? 941  PHE A CA    1 
ATOM   7264  C  C     . PHE A 1 941 ? 125.839 92.655  133.108 1.00 67.31  ? 941  PHE A C     1 
ATOM   7265  O  O     . PHE A 1 941 ? 124.756 92.681  133.702 1.00 69.25  ? 941  PHE A O     1 
ATOM   7266  C  CB    . PHE A 1 941 ? 126.702 94.754  134.136 1.00 68.28  ? 941  PHE A CB    1 
ATOM   7267  C  CG    . PHE A 1 941 ? 127.831 95.492  134.785 1.00 68.80  ? 941  PHE A CG    1 
ATOM   7268  C  CD1   . PHE A 1 941 ? 128.188 95.221  136.094 1.00 72.31  ? 941  PHE A CD1   1 
ATOM   7269  C  CD2   . PHE A 1 941 ? 128.538 96.455  134.089 1.00 65.51  ? 941  PHE A CD2   1 
ATOM   7270  C  CE1   . PHE A 1 941 ? 129.229 95.896  136.694 1.00 71.66  ? 941  PHE A CE1   1 
ATOM   7271  C  CE2   . PHE A 1 941 ? 129.579 97.133  134.685 1.00 64.15  ? 941  PHE A CE2   1 
ATOM   7272  C  CZ    . PHE A 1 941 ? 129.924 96.853  135.987 1.00 66.20  ? 941  PHE A CZ    1 
ATOM   7273  N  N     . GLY A 1 942 ? 125.990 92.072  131.925 1.00 64.90  ? 942  GLY A N     1 
ATOM   7274  C  CA    . GLY A 1 942 ? 124.887 91.384  131.283 1.00 66.89  ? 942  GLY A CA    1 
ATOM   7275  C  C     . GLY A 1 942 ? 123.746 92.281  130.859 1.00 66.95  ? 942  GLY A C     1 
ATOM   7276  O  O     . GLY A 1 942 ? 122.578 91.929  131.067 1.00 67.15  ? 942  GLY A O     1 
ATOM   7277  N  N     . MET A 1 943 ? 124.051 93.437  130.278 1.00 62.46  ? 943  MET A N     1 
ATOM   7278  C  CA    . MET A 1 943 ? 123.040 94.319  129.713 1.00 64.75  ? 943  MET A CA    1 
ATOM   7279  C  C     . MET A 1 943 ? 123.303 94.469  128.222 1.00 60.96  ? 943  MET A C     1 
ATOM   7280  O  O     . MET A 1 943 ? 124.451 94.647  127.802 1.00 62.52  ? 943  MET A O     1 
ATOM   7281  C  CB    . MET A 1 943 ? 123.026 95.684  130.414 1.00 66.29  ? 943  MET A CB    1 
ATOM   7282  C  CG    . MET A 1 943 ? 124.329 96.460  130.364 1.00 62.79  ? 943  MET A CG    1 
ATOM   7283  S  SD    . MET A 1 943 ? 124.803 97.128  131.968 1.00 62.42  ? 943  MET A SD    1 
ATOM   7284  C  CE    . MET A 1 943 ? 123.314 98.012  132.417 1.00 61.07  ? 943  MET A CE    1 
ATOM   7285  N  N     . ASP A 1 944 ? 122.242 94.370  127.426 1.00 62.51  ? 944  ASP A N     1 
ATOM   7286  C  CA    . ASP A 1 944 ? 122.358 94.431  125.974 1.00 65.04  ? 944  ASP A CA    1 
ATOM   7287  C  C     . ASP A 1 944 ? 122.400 95.891  125.542 1.00 65.07  ? 944  ASP A C     1 
ATOM   7288  O  O     . ASP A 1 944 ? 121.424 96.627  125.715 1.00 66.00  ? 944  ASP A O     1 
ATOM   7289  C  CB    . ASP A 1 944 ? 121.194 93.692  125.321 1.00 65.00  ? 944  ASP A CB    1 
ATOM   7290  C  CG    . ASP A 1 944 ? 121.153 92.226  125.697 1.00 65.82  ? 944  ASP A CG    1 
ATOM   7291  O  OD1   . ASP A 1 944 ? 122.052 91.779  126.439 1.00 65.23  ? 944  ASP A OD1   1 
ATOM   7292  O  OD2   . ASP A 1 944 ? 120.223 91.522  125.253 1.00 66.74  ? 944  ASP A OD2   1 
ATOM   7293  N  N     . LEU A 1 945 ? 123.528 96.310  124.978 1.00 56.88  ? 945  LEU A N     1 
ATOM   7294  C  CA    . LEU A 1 945 ? 123.746 97.692  124.581 1.00 55.30  ? 945  LEU A CA    1 
ATOM   7295  C  C     . LEU A 1 945 ? 123.828 97.789  123.065 1.00 60.64  ? 945  LEU A C     1 
ATOM   7296  O  O     . LEU A 1 945 ? 124.502 96.983  122.417 1.00 64.67  ? 945  LEU A O     1 
ATOM   7297  C  CB    . LEU A 1 945 ? 125.026 98.244  125.211 1.00 54.50  ? 945  LEU A CB    1 
ATOM   7298  C  CG    . LEU A 1 945 ? 125.139 98.095  126.727 1.00 50.31  ? 945  LEU A CG    1 
ATOM   7299  C  CD1   . LEU A 1 945 ? 126.400 98.766  127.240 1.00 52.86  ? 945  LEU A CD1   1 
ATOM   7300  C  CD2   . LEU A 1 945 ? 123.909 98.663  127.411 1.00 56.56  ? 945  LEU A CD2   1 
ATOM   7301  N  N     . LYS A 1 946 ? 123.139 98.778  122.505 1.00 61.67  ? 946  LYS A N     1 
ATOM   7302  C  CA    . LYS A 1 946 ? 123.080 98.936  121.061 1.00 60.42  ? 946  LYS A CA    1 
ATOM   7303  C  C     . LYS A 1 946 ? 124.347 99.590  120.530 1.00 60.55  ? 946  LYS A C     1 
ATOM   7304  O  O     . LYS A 1 946 ? 124.902 100.503 121.148 1.00 58.65  ? 946  LYS A O     1 
ATOM   7305  C  CB    . LYS A 1 946 ? 121.862 99.768  120.661 1.00 57.44  ? 946  LYS A CB    1 
ATOM   7306  C  CG    . LYS A 1 946 ? 120.534 99.107  120.969 1.00 58.01  ? 946  LYS A CG    1 
ATOM   7307  C  CD    . LYS A 1 946 ? 119.373 99.977  120.526 1.00 60.47  ? 946  LYS A CD    1 
ATOM   7308  C  CE    . LYS A 1 946 ? 118.041 99.337  120.879 1.00 62.45  ? 946  LYS A CE    1 
ATOM   7309  N  NZ    . LYS A 1 946 ? 117.880 98.003  120.237 1.00 60.10  ? 946  LYS A NZ    1 
ATOM   7310  N  N     . VAL A 1 947 ? 124.801 99.108  119.378 1.00 56.69  ? 947  VAL A N     1 
ATOM   7311  C  CA    . VAL A 1 947 ? 125.902 99.704  118.632 1.00 55.79  ? 947  VAL A CA    1 
ATOM   7312  C  C     . VAL A 1 947 ? 125.337 100.203 117.311 1.00 54.45  ? 947  VAL A C     1 
ATOM   7313  O  O     . VAL A 1 947 ? 124.609 99.474  116.629 1.00 58.42  ? 947  VAL A O     1 
ATOM   7314  C  CB    . VAL A 1 947 ? 127.043 98.697  118.403 1.00 52.87  ? 947  VAL A CB    1 
ATOM   7315  C  CG1   . VAL A 1 947 ? 128.270 99.395  117.846 1.00 50.81  ? 947  VAL A CG1   1 
ATOM   7316  C  CG2   . VAL A 1 947 ? 127.378 97.972  119.690 1.00 56.20  ? 947  VAL A CG2   1 
ATOM   7317  N  N     . LYS A 1 948 ? 125.650 101.447 116.962 1.00 54.67  ? 948  LYS A N     1 
ATOM   7318  C  CA    . LYS A 1 948 ? 125.176 102.048 115.726 1.00 56.37  ? 948  LYS A CA    1 
ATOM   7319  C  C     . LYS A 1 948 ? 126.356 102.519 114.889 1.00 56.61  ? 948  LYS A C     1 
ATOM   7320  O  O     . LYS A 1 948 ? 127.428 102.830 115.414 1.00 56.33  ? 948  LYS A O     1 
ATOM   7321  C  CB    . LYS A 1 948 ? 124.232 103.221 115.995 1.00 54.03  ? 948  LYS A CB    1 
ATOM   7322  C  CG    . LYS A 1 948 ? 122.909 102.817 116.609 1.00 55.79  ? 948  LYS A CG    1 
ATOM   7323  C  CD    . LYS A 1 948 ? 121.985 104.009 116.748 1.00 58.79  ? 948  LYS A CD    1 
ATOM   7324  C  CE    . LYS A 1 948 ? 120.643 103.593 117.318 1.00 57.35  ? 948  LYS A CE    1 
ATOM   7325  N  NZ    . LYS A 1 948 ? 119.980 102.569 116.466 1.00 56.92  ? 948  LYS A NZ    1 
ATOM   7326  N  N     . LYS A 1 949 ? 126.143 102.565 113.578 1.00 56.35  ? 949  LYS A N     1 
ATOM   7327  C  CA    . LYS A 1 949 ? 127.204 102.915 112.646 1.00 53.79  ? 949  LYS A CA    1 
ATOM   7328  C  C     . LYS A 1 949 ? 127.348 104.426 112.547 1.00 54.15  ? 949  LYS A C     1 
ATOM   7329  O  O     . LYS A 1 949 ? 126.363 105.143 112.349 1.00 60.05  ? 949  LYS A O     1 
ATOM   7330  C  CB    . LYS A 1 949 ? 126.915 102.331 111.265 1.00 56.15  ? 949  LYS A CB    1 
ATOM   7331  C  CG    . LYS A 1 949 ? 126.727 100.831 111.244 1.00 56.64  ? 949  LYS A CG    1 
ATOM   7332  C  CD    . LYS A 1 949 ? 126.520 100.332 109.830 1.00 57.48  ? 949  LYS A CD    1 
ATOM   7333  C  CE    . LYS A 1 949 ? 125.379 101.067 109.155 1.00 60.21  ? 949  LYS A CE    1 
ATOM   7334  N  NZ    . LYS A 1 949 ? 124.113 100.948 109.926 1.00 57.71  ? 949  LYS A NZ    1 
ATOM   7335  N  N     . ALA A 1 950 ? 128.579 104.909 112.689 1.00 50.59  ? 950  ALA A N     1 
ATOM   7336  C  CA    . ALA A 1 950 ? 128.850 106.309 112.397 1.00 51.23  ? 950  ALA A CA    1 
ATOM   7337  C  C     . ALA A 1 950 ? 128.876 106.562 110.895 1.00 56.83  ? 950  ALA A C     1 
ATOM   7338  O  O     . ALA A 1 950 ? 128.340 107.570 110.422 1.00 58.29  ? 950  ALA A O     1 
ATOM   7339  C  CB    . ALA A 1 950 ? 130.172 106.730 113.034 1.00 51.01  ? 950  ALA A CB    1 
ATOM   7340  N  N     . ARG A 1 951 ? 129.485 105.656 110.136 1.00 59.74  ? 951  ARG A N     1 
ATOM   7341  C  CA    . ARG A 1 951 ? 129.619 105.770 108.693 1.00 52.13  ? 951  ARG A CA    1 
ATOM   7342  C  C     . ARG A 1 951 ? 129.132 104.481 108.046 1.00 58.37  ? 951  ARG A C     1 
ATOM   7343  O  O     . ARG A 1 951 ? 128.733 103.530 108.724 1.00 59.91  ? 951  ARG A O     1 
ATOM   7344  C  CB    . ARG A 1 951 ? 131.070 106.056 108.290 1.00 49.69  ? 951  ARG A CB    1 
ATOM   7345  C  CG    . ARG A 1 951 ? 131.943 106.519 109.434 1.00 50.73  ? 951  ARG A CG    1 
ATOM   7346  C  CD    . ARG A 1 951 ? 133.364 106.778 108.989 1.00 53.91  ? 951  ARG A CD    1 
ATOM   7347  N  NE    . ARG A 1 951 ? 134.079 105.560 108.636 1.00 58.51  ? 951  ARG A NE    1 
ATOM   7348  C  CZ    . ARG A 1 951 ? 135.382 105.508 108.397 1.00 58.12  ? 951  ARG A CZ    1 
ATOM   7349  N  NH1   . ARG A 1 951 ? 136.140 106.590 108.468 1.00 55.70  ? 951  ARG A NH1   1 
ATOM   7350  N  NH2   . ARG A 1 951 ? 135.938 104.343 108.082 1.00 55.74  ? 951  ARG A NH2   1 
ATOM   7351  N  N     . LYS A 1 952 ? 129.168 104.451 106.719 1.00 75.21  ? 952  LYS A N     1 
ATOM   7352  C  CA    . LYS A 1 952 ? 128.824 103.245 105.984 1.00 74.09  ? 952  LYS A CA    1 
ATOM   7353  C  C     . LYS A 1 952 ? 129.975 102.252 106.040 1.00 73.67  ? 952  LYS A C     1 
ATOM   7354  O  O     . LYS A 1 952 ? 131.147 102.631 105.965 1.00 72.38  ? 952  LYS A O     1 
ATOM   7355  C  CB    . LYS A 1 952 ? 128.485 103.582 104.533 1.00 75.35  ? 952  LYS A CB    1 
ATOM   7356  C  CG    . LYS A 1 952 ? 127.290 104.504 104.381 1.00 74.21  ? 952  LYS A CG    1 
ATOM   7357  C  CD    . LYS A 1 952 ? 126.036 103.880 104.968 1.00 74.80  ? 952  LYS A CD    1 
ATOM   7358  C  CE    . LYS A 1 952 ? 125.644 102.615 104.220 1.00 75.17  ? 952  LYS A CE    1 
ATOM   7359  N  NZ    . LYS A 1 952 ? 124.418 101.992 104.790 1.00 73.80  ? 952  LYS A NZ    1 
ATOM   7360  N  N     . ALA A 1 953 ? 129.634 100.974 106.175 1.00 83.24  ? 953  ALA A N     1 
ATOM   7361  C  CA    . ALA A 1 953 ? 130.644 99.935  106.316 1.00 84.53  ? 953  ALA A CA    1 
ATOM   7362  C  C     . ALA A 1 953 ? 131.339 99.699  104.982 1.00 87.63  ? 953  ALA A C     1 
ATOM   7363  O  O     . ALA A 1 953 ? 130.691 99.359  103.987 1.00 87.88  ? 953  ALA A O     1 
ATOM   7364  C  CB    . ALA A 1 953 ? 130.007 98.646  106.826 1.00 84.36  ? 953  ALA A CB    1 
ATOM   7365  N  N     . HIS A 1 954 ? 132.661 99.882  104.962 1.00 94.30  ? 954  HIS A N     1 
ATOM   7366  C  CA    . HIS A 1 954 ? 133.417 99.676  103.732 1.00 92.81  ? 954  HIS A CA    1 
ATOM   7367  C  C     . HIS A 1 954 ? 133.484 98.199  103.366 1.00 92.93  ? 954  HIS A C     1 
ATOM   7368  O  O     . HIS A 1 954 ? 133.237 97.824  102.214 1.00 92.67  ? 954  HIS A O     1 
ATOM   7369  C  CB    . HIS A 1 954 ? 134.818 100.267 103.875 1.00 93.93  ? 954  HIS A CB    1 
ATOM   7370  C  CG    . HIS A 1 954 ? 134.838 101.762 103.938 1.00 94.19  ? 954  HIS A CG    1 
ATOM   7371  N  ND1   . HIS A 1 954 ? 134.124 102.477 104.875 1.00 92.50  ? 954  HIS A ND1   1 
ATOM   7372  C  CD2   . HIS A 1 954 ? 135.483 102.678 103.178 1.00 93.24  ? 954  HIS A CD2   1 
ATOM   7373  C  CE1   . HIS A 1 954 ? 134.330 103.769 104.690 1.00 93.42  ? 954  HIS A CE1   1 
ATOM   7374  N  NE2   . HIS A 1 954 ? 135.151 103.917 103.666 1.00 93.83  ? 954  HIS A NE2   1 
ATOM   7375  N  N     . TYR A 1 955 ? 133.813 97.343  104.331 1.00 99.45  ? 955  TYR A N     1 
ATOM   7376  C  CA    . TYR A 1 955 ? 133.810 95.906  104.109 1.00 100.21 ? 955  TYR A CA    1 
ATOM   7377  C  C     . TYR A 1 955 ? 133.171 95.217  105.304 1.00 98.85  ? 955  TYR A C     1 
ATOM   7378  O  O     . TYR A 1 955 ? 133.308 95.662  106.446 1.00 98.93  ? 955  TYR A O     1 
ATOM   7379  C  CB    . TYR A 1 955 ? 135.225 95.358  103.859 1.00 100.34 ? 955  TYR A CB    1 
ATOM   7380  C  CG    . TYR A 1 955 ? 136.124 95.320  105.074 1.00 100.22 ? 955  TYR A CG    1 
ATOM   7381  C  CD1   . TYR A 1 955 ? 136.712 96.477  105.564 1.00 99.55  ? 955  TYR A CD1   1 
ATOM   7382  C  CD2   . TYR A 1 955 ? 136.402 94.121  105.716 1.00 98.14  ? 955  TYR A CD2   1 
ATOM   7383  C  CE1   . TYR A 1 955 ? 137.538 96.444  106.668 1.00 99.51  ? 955  TYR A CE1   1 
ATOM   7384  C  CE2   . TYR A 1 955 ? 137.228 94.078  106.819 1.00 98.46  ? 955  TYR A CE2   1 
ATOM   7385  C  CZ    . TYR A 1 955 ? 137.793 95.243  107.290 1.00 98.80  ? 955  TYR A CZ    1 
ATOM   7386  O  OH    . TYR A 1 955 ? 138.618 95.208  108.390 1.00 98.47  ? 955  TYR A OH    1 
ATOM   7387  N  N     . ASP A 1 956 ? 132.476 94.120  105.027 1.00 110.02 ? 956  ASP A N     1 
ATOM   7388  C  CA    . ASP A 1 956 ? 131.674 93.418  106.016 1.00 110.79 ? 956  ASP A CA    1 
ATOM   7389  C  C     . ASP A 1 956 ? 132.359 92.121  106.420 1.00 111.26 ? 956  ASP A C     1 
ATOM   7390  O  O     . ASP A 1 956 ? 132.925 91.417  105.579 1.00 111.32 ? 956  ASP A O     1 
ATOM   7391  C  CB    . ASP A 1 956 ? 130.274 93.125  105.470 1.00 111.77 ? 956  ASP A CB    1 
ATOM   7392  C  CG    . ASP A 1 956 ? 129.293 92.730  106.555 1.00 111.89 ? 956  ASP A CG    1 
ATOM   7393  O  OD1   . ASP A 1 956 ? 129.698 92.651  107.733 1.00 111.94 ? 956  ASP A OD1   1 
ATOM   7394  O  OD2   . ASP A 1 956 ? 128.110 92.503  106.227 1.00 112.29 ? 956  ASP A OD2   1 
ATOM   7395  N  N     . VAL A 1 957 ? 132.305 91.817  107.719 1.00 113.36 ? 957  VAL A N     1 
ATOM   7396  C  CA    . VAL A 1 957 ? 132.919 90.598  108.237 1.00 113.90 ? 957  VAL A CA    1 
ATOM   7397  C  C     . VAL A 1 957 ? 132.146 89.368  107.781 1.00 114.77 ? 957  VAL A C     1 
ATOM   7398  O  O     . VAL A 1 957 ? 132.737 88.331  107.456 1.00 114.78 ? 957  VAL A O     1 
ATOM   7399  C  CB    . VAL A 1 957 ? 133.011 90.666  109.771 1.00 112.66 ? 957  VAL A CB    1 
ATOM   7400  C  CG1   . VAL A 1 957 ? 133.705 89.433  110.319 1.00 113.84 ? 957  VAL A CG1   1 
ATOM   7401  C  CG2   . VAL A 1 957 ? 133.734 91.928  110.196 1.00 111.48 ? 957  VAL A CG2   1 
ATOM   7402  N  N     . LYS A 1 958 ? 130.815 89.459  107.756 1.00 113.94 ? 958  LYS A N     1 
ATOM   7403  C  CA    . LYS A 1 958 ? 129.993 88.301  107.421 1.00 114.44 ? 958  LYS A CA    1 
ATOM   7404  C  C     . LYS A 1 958 ? 130.181 87.864  105.974 1.00 115.24 ? 958  LYS A C     1 
ATOM   7405  O  O     . LYS A 1 958 ? 129.995 86.685  105.657 1.00 114.84 ? 958  LYS A O     1 
ATOM   7406  C  CB    . LYS A 1 958 ? 128.523 88.616  107.688 1.00 113.31 ? 958  LYS A CB    1 
ATOM   7407  C  CG    . LYS A 1 958 ? 128.269 89.279  109.026 1.00 112.49 ? 958  LYS A CG    1 
ATOM   7408  C  CD    . LYS A 1 958 ? 126.819 89.703  109.152 1.00 112.39 ? 958  LYS A CD    1 
ATOM   7409  C  CE    . LYS A 1 958 ? 126.585 90.481  110.429 1.00 112.73 ? 958  LYS A CE    1 
ATOM   7410  N  NZ    . LYS A 1 958 ? 125.179 90.951  110.537 1.00 113.83 ? 958  LYS A NZ    1 
ATOM   7411  N  N     . SER A 1 959 ? 130.550 88.787  105.090 1.00 120.55 ? 959  SER A N     1 
ATOM   7412  C  CA    . SER A 1 959 ? 130.718 88.490  103.675 1.00 120.54 ? 959  SER A CA    1 
ATOM   7413  C  C     . SER A 1 959 ? 132.142 88.086  103.318 1.00 120.75 ? 959  SER A C     1 
ATOM   7414  O  O     . SER A 1 959 ? 132.441 87.900  102.134 1.00 120.33 ? 959  SER A O     1 
ATOM   7415  C  CB    . SER A 1 959 ? 130.298 89.695  102.831 1.00 120.20 ? 959  SER A CB    1 
ATOM   7416  O  OG    . SER A 1 959 ? 131.136 90.810  103.083 1.00 119.62 ? 959  SER A OG    1 
ATOM   7417  N  N     . LEU A 1 960 ? 133.024 87.953  104.301 1.00 122.06 ? 960  LEU A N     1 
ATOM   7418  C  CA    . LEU A 1 960 ? 134.408 87.579  104.036 1.00 121.91 ? 960  LEU A CA    1 
ATOM   7419  C  C     . LEU A 1 960 ? 134.513 86.115  103.620 1.00 122.19 ? 960  LEU A C     1 
ATOM   7420  O  O     . LEU A 1 960 ? 133.548 85.359  103.725 1.00 121.89 ? 960  LEU A O     1 
ATOM   7421  C  CB    . LEU A 1 960 ? 135.281 87.840  105.267 1.00 122.20 ? 960  LEU A CB    1 
ATOM   7422  C  CG    . LEU A 1 960 ? 135.392 89.292  105.739 1.00 122.68 ? 960  LEU A CG    1 
ATOM   7423  C  CD1   . LEU A 1 960 ? 136.275 89.392  106.973 1.00 122.74 ? 960  LEU A CD1   1 
ATOM   7424  C  CD2   . LEU A 1 960 ? 135.916 90.188  104.629 1.00 122.18 ? 960  LEU A CD2   1 
ATOM   7425  N  N     . SER B 2 2   ? 139.375 149.008 202.670 1.00 108.47 ? 2    SER B N     1 
ATOM   7426  C  CA    . SER B 2 2   ? 140.371 148.463 203.584 1.00 108.68 ? 2    SER B CA    1 
ATOM   7427  C  C     . SER B 2 2   ? 141.777 148.629 203.022 1.00 107.69 ? 2    SER B C     1 
ATOM   7428  O  O     . SER B 2 2   ? 142.025 149.506 202.195 1.00 106.37 ? 2    SER B O     1 
ATOM   7429  C  CB    . SER B 2 2   ? 140.090 146.986 203.867 1.00 107.36 ? 2    SER B CB    1 
ATOM   7430  O  OG    . SER B 2 2   ? 138.807 146.812 204.443 1.00 107.80 ? 2    SER B OG    1 
ATOM   7431  N  N     . GLU B 2 3   ? 142.695 147.783 203.479 1.00 103.94 ? 3    GLU B N     1 
ATOM   7432  C  CA    . GLU B 2 3   ? 144.066 147.835 202.997 1.00 104.79 ? 3    GLU B CA    1 
ATOM   7433  C  C     . GLU B 2 3   ? 144.140 147.355 201.552 1.00 105.38 ? 3    GLU B C     1 
ATOM   7434  O  O     . GLU B 2 3   ? 143.334 146.535 201.104 1.00 105.21 ? 3    GLU B O     1 
ATOM   7435  C  CB    . GLU B 2 3   ? 144.976 146.989 203.890 1.00 103.79 ? 3    GLU B CB    1 
ATOM   7436  C  CG    . GLU B 2 3   ? 146.474 147.177 203.661 1.00 104.82 ? 3    GLU B CG    1 
ATOM   7437  C  CD    . GLU B 2 3   ? 146.993 148.519 204.153 1.00 105.27 ? 3    GLU B CD    1 
ATOM   7438  O  OE1   . GLU B 2 3   ? 146.632 149.562 203.568 1.00 104.61 ? 3    GLU B OE1   1 
ATOM   7439  O  OE2   . GLU B 2 3   ? 147.768 148.528 205.133 1.00 104.51 ? 3    GLU B OE2   1 
ATOM   7440  N  N     . ILE B 2 4   ? 145.117 147.885 200.820 1.00 98.26  ? 4    ILE B N     1 
ATOM   7441  C  CA    . ILE B 2 4   ? 145.265 147.574 199.403 1.00 96.06  ? 4    ILE B CA    1 
ATOM   7442  C  C     . ILE B 2 4   ? 145.698 146.123 199.250 1.00 97.21  ? 4    ILE B C     1 
ATOM   7443  O  O     . ILE B 2 4   ? 146.765 145.722 199.728 1.00 98.85  ? 4    ILE B O     1 
ATOM   7444  C  CB    . ILE B 2 4   ? 146.263 148.531 198.742 1.00 97.08  ? 4    ILE B CB    1 
ATOM   7445  C  CG1   . ILE B 2 4   ? 145.712 149.954 198.791 1.00 96.80  ? 4    ILE B CG1   1 
ATOM   7446  C  CG2   . ILE B 2 4   ? 146.545 148.102 197.316 1.00 96.79  ? 4    ILE B CG2   1 
ATOM   7447  C  CD1   . ILE B 2 4   ? 146.694 151.002 198.381 1.00 96.60  ? 4    ILE B CD1   1 
ATOM   7448  N  N     . LYS B 2 5   ? 144.871 145.330 198.573 1.00 94.96  ? 5    LYS B N     1 
ATOM   7449  C  CA    . LYS B 2 5   ? 145.095 143.896 198.463 1.00 95.15  ? 5    LYS B CA    1 
ATOM   7450  C  C     . LYS B 2 5   ? 145.702 143.474 197.135 1.00 94.57  ? 5    LYS B C     1 
ATOM   7451  O  O     . LYS B 2 5   ? 146.380 142.443 197.082 1.00 92.88  ? 5    LYS B O     1 
ATOM   7452  C  CB    . LYS B 2 5   ? 143.780 143.138 198.665 1.00 94.86  ? 5    LYS B CB    1 
ATOM   7453  C  CG    . LYS B 2 5   ? 143.018 143.537 199.913 1.00 95.42  ? 5    LYS B CG    1 
ATOM   7454  C  CD    . LYS B 2 5   ? 143.819 143.251 201.171 1.00 95.00  ? 5    LYS B CD    1 
ATOM   7455  C  CE    . LYS B 2 5   ? 144.060 141.761 201.345 1.00 95.02  ? 5    LYS B CE    1 
ATOM   7456  N  NZ    . LYS B 2 5   ? 142.783 141.003 201.450 1.00 95.95  ? 5    LYS B NZ    1 
ATOM   7457  N  N     . ALA B 2 6   ? 145.479 144.229 196.064 1.00 90.57  ? 6    ALA B N     1 
ATOM   7458  C  CA    . ALA B 2 6   ? 145.941 143.801 194.754 1.00 90.58  ? 6    ALA B CA    1 
ATOM   7459  C  C     . ALA B 2 6   ? 146.190 145.005 193.861 1.00 87.51  ? 6    ALA B C     1 
ATOM   7460  O  O     . ALA B 2 6   ? 145.530 146.040 193.982 1.00 86.69  ? 6    ALA B O     1 
ATOM   7461  C  CB    . ALA B 2 6   ? 144.935 142.857 194.088 1.00 88.46  ? 6    ALA B CB    1 
ATOM   7462  N  N     . ILE B 2 7   ? 147.157 144.851 192.964 1.00 81.88  ? 7    ILE B N     1 
ATOM   7463  C  CA    . ILE B 2 7   ? 147.424 145.802 191.894 1.00 80.38  ? 7    ILE B CA    1 
ATOM   7464  C  C     . ILE B 2 7   ? 147.224 145.059 190.583 1.00 80.03  ? 7    ILE B C     1 
ATOM   7465  O  O     . ILE B 2 7   ? 147.827 144.002 190.367 1.00 81.29  ? 7    ILE B O     1 
ATOM   7466  C  CB    . ILE B 2 7   ? 148.838 146.392 191.994 1.00 80.50  ? 7    ILE B CB    1 
ATOM   7467  C  CG1   . ILE B 2 7   ? 148.979 147.204 193.282 1.00 82.52  ? 7    ILE B CG1   1 
ATOM   7468  C  CG2   . ILE B 2 7   ? 149.144 147.246 190.782 1.00 78.39  ? 7    ILE B CG2   1 
ATOM   7469  C  CD1   . ILE B 2 7   ? 150.316 147.870 193.439 1.00 82.61  ? 7    ILE B CD1   1 
ATOM   7470  N  N     . ALA B 2 8   ? 146.366 145.593 189.720 1.00 74.39  ? 8    ALA B N     1 
ATOM   7471  C  CA    . ALA B 2 8   ? 145.946 144.891 188.517 1.00 72.31  ? 8    ALA B CA    1 
ATOM   7472  C  C     . ALA B 2 8   ? 146.125 145.780 187.298 1.00 74.29  ? 8    ALA B C     1 
ATOM   7473  O  O     . ALA B 2 8   ? 145.902 146.992 187.363 1.00 78.36  ? 8    ALA B O     1 
ATOM   7474  C  CB    . ALA B 2 8   ? 144.486 144.439 188.623 1.00 72.92  ? 8    ALA B CB    1 
ATOM   7475  N  N     . VAL B 2 9   ? 146.524 145.168 186.187 1.00 64.28  ? 9    VAL B N     1 
ATOM   7476  C  CA    . VAL B 2 9   ? 146.732 145.867 184.927 1.00 61.95  ? 9    VAL B CA    1 
ATOM   7477  C  C     . VAL B 2 9   ? 146.026 145.095 183.820 1.00 61.28  ? 9    VAL B C     1 
ATOM   7478  O  O     . VAL B 2 9   ? 146.101 143.863 183.763 1.00 69.02  ? 9    VAL B O     1 
ATOM   7479  C  CB    . VAL B 2 9   ? 148.237 146.046 184.624 1.00 63.07  ? 9    VAL B CB    1 
ATOM   7480  C  CG1   . VAL B 2 9   ? 148.980 144.730 184.773 1.00 64.58  ? 9    VAL B CG1   1 
ATOM   7481  C  CG2   . VAL B 2 9   ? 148.450 146.638 183.242 1.00 64.71  ? 9    VAL B CG2   1 
ATOM   7482  N  N     . GLY B 2 10  ? 145.315 145.818 182.957 1.00 55.24  ? 10   GLY B N     1 
ATOM   7483  C  CA    . GLY B 2 10  ? 144.579 145.186 181.878 1.00 58.34  ? 10   GLY B CA    1 
ATOM   7484  C  C     . GLY B 2 10  ? 145.518 144.657 180.813 1.00 60.19  ? 10   GLY B C     1 
ATOM   7485  O  O     . GLY B 2 10  ? 146.228 145.439 180.161 1.00 63.30  ? 10   GLY B O     1 
ATOM   7486  N  N     . MET B 2 11  ? 145.523 143.342 180.608 1.00 52.91  ? 11   MET B N     1 
ATOM   7487  C  CA    . MET B 2 11  ? 146.480 142.681 179.730 1.00 54.94  ? 11   MET B CA    1 
ATOM   7488  C  C     . MET B 2 11  ? 145.777 141.961 178.584 1.00 55.06  ? 11   MET B C     1 
ATOM   7489  O  O     . MET B 2 11  ? 146.104 140.823 178.245 1.00 54.98  ? 11   MET B O     1 
ATOM   7490  C  CB    . MET B 2 11  ? 147.358 141.714 180.521 1.00 56.04  ? 11   MET B CB    1 
ATOM   7491  C  CG    . MET B 2 11  ? 148.686 141.371 179.860 1.00 60.02  ? 11   MET B CG    1 
ATOM   7492  S  SD    . MET B 2 11  ? 149.797 142.779 179.756 1.00 63.29  ? 11   MET B SD    1 
ATOM   7493  C  CE    . MET B 2 11  ? 149.868 143.245 181.478 1.00 54.78  ? 11   MET B CE    1 
ATOM   7494  N  N     . ASN B 2 12  ? 144.796 142.611 177.972 1.00 54.85  ? 12   ASN B N     1 
ATOM   7495  C  CA    . ASN B 2 12  ? 144.237 142.108 176.725 1.00 52.03  ? 12   ASN B CA    1 
ATOM   7496  C  C     . ASN B 2 12  ? 145.127 142.573 175.574 1.00 56.13  ? 12   ASN B C     1 
ATOM   7497  O  O     . ASN B 2 12  ? 146.183 143.176 175.782 1.00 61.45  ? 12   ASN B O     1 
ATOM   7498  C  CB    . ASN B 2 12  ? 142.786 142.553 176.567 1.00 50.43  ? 12   ASN B CB    1 
ATOM   7499  C  CG    . ASN B 2 12  ? 141.810 141.589 177.209 1.00 48.29  ? 12   ASN B CG    1 
ATOM   7500  O  OD1   . ASN B 2 12  ? 142.202 140.706 177.969 1.00 53.29  ? 12   ASN B OD1   1 
ATOM   7501  N  ND2   . ASN B 2 12  ? 140.530 141.754 176.908 1.00 47.43  ? 12   ASN B ND2   1 
ATOM   7502  N  N     . SER B 2 13  ? 144.713 142.289 174.339 1.00 54.98  ? 13   SER B N     1 
ATOM   7503  C  CA    . SER B 2 13  ? 145.508 142.694 173.185 1.00 53.98  ? 13   SER B CA    1 
ATOM   7504  C  C     . SER B 2 13  ? 145.591 144.211 173.076 1.00 55.39  ? 13   SER B C     1 
ATOM   7505  O  O     . SER B 2 13  ? 146.646 144.761 172.735 1.00 57.55  ? 13   SER B O     1 
ATOM   7506  C  CB    . SER B 2 13  ? 144.923 142.091 171.911 1.00 53.34  ? 13   SER B CB    1 
ATOM   7507  O  OG    . SER B 2 13  ? 144.973 140.677 171.955 1.00 55.78  ? 13   SER B OG    1 
ATOM   7508  N  N     . CYS B 2 14  ? 144.488 144.904 173.366 1.00 59.10  ? 14   CYS B N     1 
ATOM   7509  C  CA    . CYS B 2 14  ? 144.496 146.363 173.338 1.00 59.87  ? 14   CYS B CA    1 
ATOM   7510  C  C     . CYS B 2 14  ? 145.442 146.933 174.387 1.00 60.50  ? 14   CYS B C     1 
ATOM   7511  O  O     . CYS B 2 14  ? 146.161 147.902 174.123 1.00 63.61  ? 14   CYS B O     1 
ATOM   7512  C  CB    . CYS B 2 14  ? 143.080 146.898 173.545 1.00 64.30  ? 14   CYS B CB    1 
ATOM   7513  S  SG    . CYS B 2 14  ? 142.281 146.344 175.069 1.00 66.64  ? 14   CYS B SG    1 
ATOM   7514  N  N     . GLY B 2 15  ? 145.449 146.350 175.587 1.00 62.68  ? 15   GLY B N     1 
ATOM   7515  C  CA    . GLY B 2 15  ? 146.363 146.814 176.617 1.00 64.83  ? 15   GLY B CA    1 
ATOM   7516  C  C     . GLY B 2 15  ? 147.818 146.557 176.273 1.00 65.62  ? 15   GLY B C     1 
ATOM   7517  O  O     . GLY B 2 15  ? 148.678 147.411 176.502 1.00 67.97  ? 15   GLY B O     1 
ATOM   7518  N  N     . ILE B 2 16  ? 148.113 145.378 175.720 1.00 60.14  ? 16   ILE B N     1 
ATOM   7519  C  CA    . ILE B 2 16  ? 149.483 145.054 175.331 1.00 57.33  ? 16   ILE B CA    1 
ATOM   7520  C  C     . ILE B 2 16  ? 149.959 145.992 174.232 1.00 62.19  ? 16   ILE B C     1 
ATOM   7521  O  O     . ILE B 2 16  ? 151.095 146.480 174.261 1.00 66.54  ? 16   ILE B O     1 
ATOM   7522  C  CB    . ILE B 2 16  ? 149.585 143.579 174.901 1.00 61.36  ? 16   ILE B CB    1 
ATOM   7523  C  CG1   . ILE B 2 16  ? 149.315 142.657 176.086 1.00 60.60  ? 16   ILE B CG1   1 
ATOM   7524  C  CG2   . ILE B 2 16  ? 150.954 143.282 174.317 1.00 64.61  ? 16   ILE B CG2   1 
ATOM   7525  C  CD1   . ILE B 2 16  ? 149.285 141.199 175.715 1.00 57.59  ? 16   ILE B CD1   1 
ATOM   7526  N  N     . ALA B 2 17  ? 149.096 146.263 173.248 1.00 63.20  ? 17   ALA B N     1 
ATOM   7527  C  CA    . ALA B 2 17  ? 149.468 147.167 172.165 1.00 61.91  ? 17   ALA B CA    1 
ATOM   7528  C  C     . ALA B 2 17  ? 149.776 148.566 172.679 1.00 62.31  ? 17   ALA B C     1 
ATOM   7529  O  O     . ALA B 2 17  ? 150.658 149.243 172.141 1.00 62.37  ? 17   ALA B O     1 
ATOM   7530  C  CB    . ALA B 2 17  ? 148.355 147.217 171.119 1.00 62.84  ? 17   ALA B CB    1 
ATOM   7531  N  N     . ALA B 2 18  ? 149.068 149.015 173.715 1.00 65.28  ? 18   ALA B N     1 
ATOM   7532  C  CA    . ALA B 2 18  ? 149.345 150.313 174.313 1.00 64.79  ? 18   ALA B CA    1 
ATOM   7533  C  C     . ALA B 2 18  ? 150.578 150.305 175.208 1.00 65.96  ? 18   ALA B C     1 
ATOM   7534  O  O     . ALA B 2 18  ? 151.163 151.367 175.439 1.00 67.40  ? 18   ALA B O     1 
ATOM   7535  C  CB    . ALA B 2 18  ? 148.135 150.790 175.113 1.00 62.72  ? 18   ALA B CB    1 
ATOM   7536  N  N     . GLY B 2 19  ? 150.989 149.144 175.711 1.00 69.77  ? 19   GLY B N     1 
ATOM   7537  C  CA    . GLY B 2 19  ? 152.150 149.082 176.575 1.00 70.64  ? 19   GLY B CA    1 
ATOM   7538  C  C     . GLY B 2 19  ? 151.868 148.599 177.983 1.00 72.58  ? 19   GLY B C     1 
ATOM   7539  O  O     . GLY B 2 19  ? 152.520 149.040 178.933 1.00 72.54  ? 19   GLY B O     1 
ATOM   7540  N  N     . ALA B 2 20  ? 150.893 147.701 178.141 1.00 70.35  ? 20   ALA B N     1 
ATOM   7541  C  CA    . ALA B 2 20  ? 150.607 147.159 179.464 1.00 66.70  ? 20   ALA B CA    1 
ATOM   7542  C  C     . ALA B 2 20  ? 151.666 146.173 179.933 1.00 67.98  ? 20   ALA B C     1 
ATOM   7543  O  O     . ALA B 2 20  ? 151.772 145.933 181.138 1.00 68.46  ? 20   ALA B O     1 
ATOM   7544  C  CB    . ALA B 2 20  ? 149.238 146.483 179.485 1.00 65.82  ? 20   ALA B CB    1 
ATOM   7545  N  N     . ARG B 2 21  ? 152.437 145.584 179.017 1.00 74.07  ? 21   ARG B N     1 
ATOM   7546  C  CA    . ARG B 2 21  ? 153.528 144.705 179.426 1.00 72.28  ? 21   ARG B CA    1 
ATOM   7547  C  C     . ARG B 2 21  ? 154.596 145.482 180.182 1.00 72.28  ? 21   ARG B C     1 
ATOM   7548  O  O     . ARG B 2 21  ? 155.082 145.038 181.230 1.00 73.56  ? 21   ARG B O     1 
ATOM   7549  C  CB    . ARG B 2 21  ? 154.131 144.014 178.205 1.00 72.11  ? 21   ARG B CB    1 
ATOM   7550  C  CG    . ARG B 2 21  ? 153.315 142.850 177.693 1.00 71.45  ? 21   ARG B CG    1 
ATOM   7551  C  CD    . ARG B 2 21  ? 153.519 141.620 178.554 1.00 73.01  ? 21   ARG B CD    1 
ATOM   7552  N  NE    . ARG B 2 21  ? 152.557 140.573 178.236 1.00 74.15  ? 21   ARG B NE    1 
ATOM   7553  C  CZ    . ARG B 2 21  ? 152.651 139.762 177.193 1.00 73.42  ? 21   ARG B CZ    1 
ATOM   7554  N  NH1   . ARG B 2 21  ? 153.650 139.855 176.332 1.00 72.20  ? 21   ARG B NH1   1 
ATOM   7555  N  NH2   . ARG B 2 21  ? 151.716 138.835 177.007 1.00 70.89  ? 21   ARG B NH2   1 
ATOM   7556  N  N     . GLU B 2 22  ? 154.966 146.654 179.664 1.00 76.89  ? 22   GLU B N     1 
ATOM   7557  C  CA    . GLU B 2 22  ? 155.938 147.496 180.350 1.00 78.84  ? 22   GLU B CA    1 
ATOM   7558  C  C     . GLU B 2 22  ? 155.406 147.960 181.697 1.00 80.17  ? 22   GLU B C     1 
ATOM   7559  O  O     . GLU B 2 22  ? 156.154 148.015 182.678 1.00 82.21  ? 22   GLU B O     1 
ATOM   7560  C  CB    . GLU B 2 22  ? 156.308 148.695 179.477 1.00 78.36  ? 22   GLU B CB    1 
ATOM   7561  C  CG    . GLU B 2 22  ? 157.352 148.398 178.418 1.00 81.89  ? 22   GLU B CG    1 
ATOM   7562  C  CD    . GLU B 2 22  ? 156.819 147.547 177.287 1.00 80.81  ? 22   GLU B CD    1 
ATOM   7563  O  OE1   . GLU B 2 22  ? 155.587 147.525 177.087 1.00 80.64  ? 22   GLU B OE1   1 
ATOM   7564  O  OE2   . GLU B 2 22  ? 157.632 146.898 176.598 1.00 78.12  ? 22   GLU B OE2   1 
ATOM   7565  N  N     . THR B 2 23  ? 154.116 148.294 181.764 1.00 79.87  ? 23   THR B N     1 
ATOM   7566  C  CA    . THR B 2 23  ? 153.514 148.688 183.034 1.00 78.15  ? 23   THR B CA    1 
ATOM   7567  C  C     . THR B 2 23  ? 153.547 147.543 184.039 1.00 80.25  ? 23   THR B C     1 
ATOM   7568  O  O     . THR B 2 23  ? 153.867 147.748 185.213 1.00 83.13  ? 23   THR B O     1 
ATOM   7569  C  CB    . THR B 2 23  ? 152.078 149.159 182.806 1.00 79.98  ? 23   THR B CB    1 
ATOM   7570  O  OG1   . THR B 2 23  ? 152.074 150.248 181.876 1.00 82.27  ? 23   THR B OG1   1 
ATOM   7571  C  CG2   . THR B 2 23  ? 151.451 149.616 184.110 1.00 79.68  ? 23   THR B CG2   1 
ATOM   7572  N  N     . TYR B 2 24  ? 153.222 146.330 183.588 1.00 79.75  ? 24   TYR B N     1 
ATOM   7573  C  CA    . TYR B 2 24  ? 153.248 145.152 184.450 1.00 77.08  ? 24   TYR B CA    1 
ATOM   7574  C  C     . TYR B 2 24  ? 154.652 144.900 184.991 1.00 79.26  ? 24   TYR B C     1 
ATOM   7575  O  O     . TYR B 2 24  ? 154.838 144.667 186.194 1.00 80.11  ? 24   TYR B O     1 
ATOM   7576  C  CB    . TYR B 2 24  ? 152.735 143.954 183.646 1.00 77.86  ? 24   TYR B CB    1 
ATOM   7577  C  CG    . TYR B 2 24  ? 152.586 142.629 184.363 1.00 77.85  ? 24   TYR B CG    1 
ATOM   7578  C  CD1   . TYR B 2 24  ? 152.580 142.542 185.745 1.00 77.20  ? 24   TYR B CD1   1 
ATOM   7579  C  CD2   . TYR B 2 24  ? 152.443 141.455 183.636 1.00 78.93  ? 24   TYR B CD2   1 
ATOM   7580  C  CE1   . TYR B 2 24  ? 152.445 141.323 186.377 1.00 79.77  ? 24   TYR B CE1   1 
ATOM   7581  C  CE2   . TYR B 2 24  ? 152.306 140.238 184.260 1.00 78.89  ? 24   TYR B CE2   1 
ATOM   7582  C  CZ    . TYR B 2 24  ? 152.306 140.177 185.631 1.00 78.48  ? 24   TYR B CZ    1 
ATOM   7583  O  OH    . TYR B 2 24  ? 152.168 138.963 186.261 1.00 77.02  ? 24   TYR B OH    1 
ATOM   7584  N  N     . GLU B 2 25  ? 155.657 144.965 184.114 1.00 86.17  ? 25   GLU B N     1 
ATOM   7585  C  CA    . GLU B 2 25  ? 157.033 144.757 184.552 1.00 86.20  ? 25   GLU B CA    1 
ATOM   7586  C  C     . GLU B 2 25  ? 157.485 145.856 185.506 1.00 88.23  ? 25   GLU B C     1 
ATOM   7587  O  O     . GLU B 2 25  ? 158.187 145.584 186.486 1.00 88.76  ? 25   GLU B O     1 
ATOM   7588  C  CB    . GLU B 2 25  ? 157.967 144.676 183.345 1.00 86.35  ? 25   GLU B CB    1 
ATOM   7589  C  CG    . GLU B 2 25  ? 157.618 143.576 182.360 1.00 87.05  ? 25   GLU B CG    1 
ATOM   7590  C  CD    . GLU B 2 25  ? 157.522 142.213 183.008 1.00 89.28  ? 25   GLU B CD    1 
ATOM   7591  O  OE1   . GLU B 2 25  ? 158.363 141.901 183.877 1.00 88.81  ? 25   GLU B OE1   1 
ATOM   7592  O  OE2   . GLU B 2 25  ? 156.602 141.450 182.648 1.00 88.52  ? 25   GLU B OE2   1 
ATOM   7593  N  N     . ALA B 2 26  ? 157.091 147.103 185.237 1.00 89.15  ? 26   ALA B N     1 
ATOM   7594  C  CA    . ALA B 2 26  ? 157.453 148.204 186.122 1.00 89.43  ? 26   ALA B CA    1 
ATOM   7595  C  C     . ALA B 2 26  ? 156.819 148.042 187.496 1.00 90.70  ? 26   ALA B C     1 
ATOM   7596  O  O     . ALA B 2 26  ? 157.461 148.307 188.517 1.00 92.31  ? 26   ALA B O     1 
ATOM   7597  C  CB    . ALA B 2 26  ? 157.046 149.535 185.492 1.00 88.47  ? 26   ALA B CB    1 
ATOM   7598  N  N     . VAL B 2 27  ? 155.558 147.606 187.543 1.00 90.16  ? 27   VAL B N     1 
ATOM   7599  C  CA    . VAL B 2 27  ? 154.894 147.386 188.824 1.00 90.19  ? 27   VAL B CA    1 
ATOM   7600  C  C     . VAL B 2 27  ? 155.571 146.258 189.590 1.00 90.91  ? 27   VAL B C     1 
ATOM   7601  O  O     . VAL B 2 27  ? 155.772 146.353 190.806 1.00 90.17  ? 27   VAL B O     1 
ATOM   7602  C  CB    . VAL B 2 27  ? 153.392 147.111 188.617 1.00 89.79  ? 27   VAL B CB    1 
ATOM   7603  C  CG1   . VAL B 2 27  ? 152.742 146.712 189.925 1.00 90.20  ? 27   VAL B CG1   1 
ATOM   7604  C  CG2   . VAL B 2 27  ? 152.704 148.335 188.066 1.00 90.02  ? 27   VAL B CG2   1 
ATOM   7605  N  N     . LYS B 2 28  ? 155.927 145.171 188.898 1.00 96.57  ? 28   LYS B N     1 
ATOM   7606  C  CA    . LYS B 2 28  ? 156.622 144.071 189.562 1.00 95.83  ? 28   LYS B CA    1 
ATOM   7607  C  C     . LYS B 2 28  ? 157.970 144.521 190.113 1.00 97.07  ? 28   LYS B C     1 
ATOM   7608  O  O     . LYS B 2 28  ? 158.327 144.198 191.254 1.00 96.17  ? 28   LYS B O     1 
ATOM   7609  C  CB    . LYS B 2 28  ? 156.798 142.905 188.590 1.00 95.63  ? 28   LYS B CB    1 
ATOM   7610  C  CG    . LYS B 2 28  ? 157.390 141.655 189.210 1.00 97.13  ? 28   LYS B CG    1 
ATOM   7611  C  CD    . LYS B 2 28  ? 157.727 140.619 188.149 1.00 96.38  ? 28   LYS B CD    1 
ATOM   7612  C  CE    . LYS B 2 28  ? 156.492 140.175 187.390 1.00 95.69  ? 28   LYS B CE    1 
ATOM   7613  N  NZ    . LYS B 2 28  ? 155.495 139.539 188.288 1.00 95.78  ? 28   LYS B NZ    1 
ATOM   7614  N  N     . GLU B 2 29  ? 158.718 145.295 189.323 1.00 99.01  ? 29   GLU B N     1 
ATOM   7615  C  CA    . GLU B 2 29  ? 160.003 145.809 189.781 1.00 98.98  ? 29   GLU B CA    1 
ATOM   7616  C  C     . GLU B 2 29  ? 159.839 146.738 190.975 1.00 99.71  ? 29   GLU B C     1 
ATOM   7617  O  O     . GLU B 2 29  ? 160.652 146.709 191.902 1.00 100.74 ? 29   GLU B O     1 
ATOM   7618  C  CB    . GLU B 2 29  ? 160.716 146.534 188.642 1.00 98.87  ? 29   GLU B CB    1 
ATOM   7619  C  CG    . GLU B 2 29  ? 161.300 145.618 187.592 1.00 98.45  ? 29   GLU B CG    1 
ATOM   7620  C  CD    . GLU B 2 29  ? 162.008 146.385 186.498 1.00 99.34  ? 29   GLU B CD    1 
ATOM   7621  O  OE1   . GLU B 2 29  ? 161.988 147.633 186.544 1.00 99.41  ? 29   GLU B OE1   1 
ATOM   7622  O  OE2   . GLU B 2 29  ? 162.584 145.744 185.595 1.00 100.15 ? 29   GLU B OE2   1 
ATOM   7623  N  N     . GLU B 2 30  ? 158.807 147.583 190.962 1.00 103.43 ? 30   GLU B N     1 
ATOM   7624  C  CA    . GLU B 2 30  ? 158.611 148.518 192.066 1.00 104.38 ? 30   GLU B CA    1 
ATOM   7625  C  C     . GLU B 2 30  ? 158.172 147.797 193.334 1.00 105.39 ? 30   GLU B C     1 
ATOM   7626  O  O     . GLU B 2 30  ? 158.579 148.173 194.439 1.00 105.65 ? 30   GLU B O     1 
ATOM   7627  C  CB    . GLU B 2 30  ? 157.595 149.587 191.675 1.00 104.72 ? 30   GLU B CB    1 
ATOM   7628  C  CG    . GLU B 2 30  ? 157.464 150.709 192.689 1.00 105.11 ? 30   GLU B CG    1 
ATOM   7629  C  CD    . GLU B 2 30  ? 158.704 151.575 192.771 1.00 105.69 ? 30   GLU B CD    1 
ATOM   7630  O  OE1   . GLU B 2 30  ? 159.460 151.631 191.779 1.00 106.51 ? 30   GLU B OE1   1 
ATOM   7631  O  OE2   . GLU B 2 30  ? 158.922 152.202 193.828 1.00 106.06 ? 30   GLU B OE2   1 
ATOM   7632  N  N     . LEU B 2 31  ? 157.338 146.764 193.199 1.00 104.89 ? 31   LEU B N     1 
ATOM   7633  C  CA    . LEU B 2 31  ? 156.975 145.960 194.360 1.00 104.88 ? 31   LEU B CA    1 
ATOM   7634  C  C     . LEU B 2 31  ? 158.173 145.193 194.899 1.00 104.60 ? 31   LEU B C     1 
ATOM   7635  O  O     . LEU B 2 31  ? 158.240 144.915 196.101 1.00 103.29 ? 31   LEU B O     1 
ATOM   7636  C  CB    . LEU B 2 31  ? 155.839 145.000 194.008 1.00 104.63 ? 31   LEU B CB    1 
ATOM   7637  C  CG    . LEU B 2 31  ? 154.460 145.617 193.763 1.00 103.59 ? 31   LEU B CG    1 
ATOM   7638  C  CD1   . LEU B 2 31  ? 153.442 144.542 193.434 1.00 103.26 ? 31   LEU B CD1   1 
ATOM   7639  C  CD2   . LEU B 2 31  ? 154.008 146.426 194.964 1.00 102.52 ? 31   LEU B CD2   1 
ATOM   7640  N  N     . GLU B 2 32  ? 159.117 144.827 194.030 1.00 111.26 ? 32   GLU B N     1 
ATOM   7641  C  CA    . GLU B 2 32  ? 160.345 144.198 194.505 1.00 111.75 ? 32   GLU B CA    1 
ATOM   7642  C  C     . GLU B 2 32  ? 161.242 145.201 195.223 1.00 111.30 ? 32   GLU B C     1 
ATOM   7643  O  O     . GLU B 2 32  ? 161.760 144.919 196.309 1.00 111.77 ? 32   GLU B O     1 
ATOM   7644  C  CB    . GLU B 2 32  ? 161.088 143.554 193.334 1.00 111.40 ? 32   GLU B CB    1 
ATOM   7645  C  CG    . GLU B 2 32  ? 162.407 142.905 193.715 1.00 111.69 ? 32   GLU B CG    1 
ATOM   7646  C  CD    . GLU B 2 32  ? 162.228 141.675 194.585 1.00 112.33 ? 32   GLU B CD    1 
ATOM   7647  O  OE1   . GLU B 2 32  ? 161.153 141.044 194.516 1.00 112.17 ? 32   GLU B OE1   1 
ATOM   7648  O  OE2   . GLU B 2 32  ? 163.165 141.339 195.340 1.00 112.41 ? 32   GLU B OE2   1 
ATOM   7649  N  N     . LYS B 2 33  ? 161.435 146.380 194.628 1.00 110.84 ? 33   LYS B N     1 
ATOM   7650  C  CA    . LYS B 2 33  ? 162.385 147.350 195.166 1.00 112.05 ? 33   LYS B CA    1 
ATOM   7651  C  C     . LYS B 2 33  ? 161.900 147.922 196.491 1.00 112.78 ? 33   LYS B C     1 
ATOM   7652  O  O     . LYS B 2 33  ? 162.650 147.965 197.473 1.00 112.64 ? 33   LYS B O     1 
ATOM   7653  C  CB    . LYS B 2 33  ? 162.622 148.463 194.147 1.00 111.57 ? 33   LYS B CB    1 
ATOM   7654  C  CG    . LYS B 2 33  ? 163.775 149.382 194.491 1.00 112.31 ? 33   LYS B CG    1 
ATOM   7655  C  CD    . LYS B 2 33  ? 164.016 150.392 193.385 1.00 111.86 ? 33   LYS B CD    1 
ATOM   7656  C  CE    . LYS B 2 33  ? 165.212 151.276 193.697 1.00 112.65 ? 33   LYS B CE    1 
ATOM   7657  N  NZ    . LYS B 2 33  ? 166.461 150.481 193.854 1.00 112.23 ? 33   LYS B NZ    1 
ATOM   7658  N  N     . ARG B 2 34  ? 160.650 148.368 196.538 1.00 113.47 ? 34   ARG B N     1 
ATOM   7659  C  CA    . ARG B 2 34  ? 159.996 148.720 197.794 1.00 113.61 ? 34   ARG B CA    1 
ATOM   7660  C  C     . ARG B 2 34  ? 159.268 147.469 198.259 1.00 113.01 ? 34   ARG B C     1 
ATOM   7661  O  O     . ARG B 2 34  ? 158.200 147.137 197.743 1.00 112.01 ? 34   ARG B O     1 
ATOM   7662  C  CB    . ARG B 2 34  ? 159.043 149.893 197.602 1.00 113.27 ? 34   ARG B CB    1 
ATOM   7663  C  CG    . ARG B 2 34  ? 159.682 151.106 196.960 1.00 112.72 ? 34   ARG B CG    1 
ATOM   7664  C  CD    . ARG B 2 34  ? 160.682 151.751 197.896 1.00 113.02 ? 34   ARG B CD    1 
ATOM   7665  N  NE    . ARG B 2 34  ? 160.033 152.256 199.099 1.00 114.24 ? 34   ARG B NE    1 
ATOM   7666  C  CZ    . ARG B 2 34  ? 159.470 153.452 199.195 1.00 113.35 ? 34   ARG B CZ    1 
ATOM   7667  N  NH1   . ARG B 2 34  ? 159.463 154.295 198.176 1.00 112.71 ? 34   ARG B NH1   1 
ATOM   7668  N  NH2   . ARG B 2 34  ? 158.900 153.812 200.341 1.00 112.94 ? 34   ARG B NH2   1 
ATOM   7669  N  N     . ASN B 2 35  ? 159.845 146.773 199.239 1.00 115.51 ? 35   ASN B N     1 
ATOM   7670  C  CA    . ASN B 2 35  ? 159.395 145.425 199.568 1.00 116.52 ? 35   ASN B CA    1 
ATOM   7671  C  C     . ASN B 2 35  ? 157.965 145.422 200.089 1.00 115.49 ? 35   ASN B C     1 
ATOM   7672  O  O     . ASN B 2 35  ? 157.706 145.799 201.235 1.00 113.59 ? 35   ASN B O     1 
ATOM   7673  C  CB    . ASN B 2 35  ? 160.330 144.785 200.595 1.00 116.32 ? 35   ASN B CB    1 
ATOM   7674  C  CG    . ASN B 2 35  ? 160.010 143.326 200.838 1.00 116.07 ? 35   ASN B CG    1 
ATOM   7675  O  OD1   . ASN B 2 35  ? 159.214 142.991 201.715 1.00 115.14 ? 35   ASN B OD1   1 
ATOM   7676  N  ND2   . ASN B 2 35  ? 160.628 142.447 200.058 1.00 115.28 ? 35   ASN B ND2   1 
ATOM   7677  N  N     . LEU B 2 36  ? 157.036 144.986 199.243 1.00 112.78 ? 36   LEU B N     1 
ATOM   7678  C  CA    . LEU B 2 36  ? 155.618 144.957 199.567 1.00 112.49 ? 36   LEU B CA    1 
ATOM   7679  C  C     . LEU B 2 36  ? 155.050 143.612 199.149 1.00 111.72 ? 36   LEU B C     1 
ATOM   7680  O  O     . LEU B 2 36  ? 155.316 143.143 198.039 1.00 110.29 ? 36   LEU B O     1 
ATOM   7681  C  CB    . LEU B 2 36  ? 154.866 146.091 198.863 1.00 111.99 ? 36   LEU B CB    1 
ATOM   7682  C  CG    . LEU B 2 36  ? 155.300 147.514 199.205 1.00 111.66 ? 36   LEU B CG    1 
ATOM   7683  C  CD1   . LEU B 2 36  ? 154.731 148.496 198.200 1.00 111.13 ? 36   LEU B CD1   1 
ATOM   7684  C  CD2   . LEU B 2 36  ? 154.867 147.876 200.616 1.00 111.97 ? 36   LEU B CD2   1 
ATOM   7685  N  N     . ASP B 2 37  ? 154.279 142.997 200.036 1.00 107.55 ? 37   ASP B N     1 
ATOM   7686  C  CA    . ASP B 2 37  ? 153.628 141.723 199.743 1.00 107.05 ? 37   ASP B CA    1 
ATOM   7687  C  C     . ASP B 2 37  ? 152.190 141.959 199.286 1.00 106.29 ? 37   ASP B C     1 
ATOM   7688  O  O     . ASP B 2 37  ? 151.222 141.576 199.940 1.00 106.53 ? 37   ASP B O     1 
ATOM   7689  C  CB    . ASP B 2 37  ? 153.683 140.809 200.963 1.00 107.55 ? 37   ASP B CB    1 
ATOM   7690  C  CG    . ASP B 2 37  ? 153.337 139.371 200.630 1.00 108.64 ? 37   ASP B CG    1 
ATOM   7691  O  OD1   . ASP B 2 37  ? 153.210 139.050 199.430 1.00 107.11 ? 37   ASP B OD1   1 
ATOM   7692  O  OD2   . ASP B 2 37  ? 153.191 138.561 201.570 1.00 108.31 ? 37   ASP B OD2   1 
ATOM   7693  N  N     . ILE B 2 38  ? 152.067 142.611 198.135 1.00 100.40 ? 38   ILE B N     1 
ATOM   7694  C  CA    . ILE B 2 38  ? 150.779 142.913 197.526 1.00 99.34  ? 38   ILE B CA    1 
ATOM   7695  C  C     . ILE B 2 38  ? 150.681 142.138 196.222 1.00 99.08  ? 38   ILE B C     1 
ATOM   7696  O  O     . ILE B 2 38  ? 151.612 142.158 195.408 1.00 99.98  ? 38   ILE B O     1 
ATOM   7697  C  CB    . ILE B 2 38  ? 150.603 144.423 197.294 1.00 101.16 ? 38   ILE B CB    1 
ATOM   7698  C  CG1   . ILE B 2 38  ? 150.696 145.174 198.623 1.00 101.23 ? 38   ILE B CG1   1 
ATOM   7699  C  CG2   . ILE B 2 38  ? 149.275 144.707 196.621 1.00 99.06  ? 38   ILE B CG2   1 
ATOM   7700  C  CD1   . ILE B 2 38  ? 150.495 146.663 198.499 1.00 100.96 ? 38   ILE B CD1   1 
ATOM   7701  N  N     . LYS B 2 39  ? 149.563 141.443 196.037 1.00 92.15  ? 39   LYS B N     1 
ATOM   7702  C  CA    . LYS B 2 39  ? 149.378 140.596 194.868 1.00 91.91  ? 39   LYS B CA    1 
ATOM   7703  C  C     . LYS B 2 39  ? 149.349 141.429 193.594 1.00 90.25  ? 39   LYS B C     1 
ATOM   7704  O  O     . LYS B 2 39  ? 148.803 142.535 193.564 1.00 91.77  ? 39   LYS B O     1 
ATOM   7705  C  CB    . LYS B 2 39  ? 148.084 139.796 195.008 1.00 92.77  ? 39   LYS B CB    1 
ATOM   7706  C  CG    . LYS B 2 39  ? 147.852 138.770 193.920 1.00 92.27  ? 39   LYS B CG    1 
ATOM   7707  C  CD    . LYS B 2 39  ? 146.530 138.057 194.124 1.00 92.70  ? 39   LYS B CD    1 
ATOM   7708  C  CE    . LYS B 2 39  ? 146.488 137.361 195.470 1.00 91.85  ? 39   LYS B CE    1 
ATOM   7709  N  NZ    . LYS B 2 39  ? 147.584 136.365 195.606 1.00 90.91  ? 39   LYS B NZ    1 
ATOM   7710  N  N     . LEU B 2 40  ? 149.946 140.892 192.535 1.00 81.78  ? 40   LEU B N     1 
ATOM   7711  C  CA    . LEU B 2 40  ? 150.026 141.571 191.244 1.00 82.14  ? 40   LEU B CA    1 
ATOM   7712  C  C     . LEU B 2 40  ? 149.437 140.645 190.187 1.00 82.37  ? 40   LEU B C     1 
ATOM   7713  O  O     . LEU B 2 40  ? 150.102 139.715 189.722 1.00 84.67  ? 40   LEU B O     1 
ATOM   7714  C  CB    . LEU B 2 40  ? 151.464 141.952 190.920 1.00 83.21  ? 40   LEU B CB    1 
ATOM   7715  C  CG    . LEU B 2 40  ? 151.734 142.563 189.549 1.00 80.90  ? 40   LEU B CG    1 
ATOM   7716  C  CD1   . LEU B 2 40  ? 150.811 143.726 189.270 1.00 81.04  ? 40   LEU B CD1   1 
ATOM   7717  C  CD2   . LEU B 2 40  ? 153.173 143.005 189.473 1.00 81.90  ? 40   LEU B CD2   1 
ATOM   7718  N  N     . LYS B 2 41  ? 148.193 140.900 189.810 1.00 71.43  ? 41   LYS B N     1 
ATOM   7719  C  CA    . LYS B 2 41  ? 147.490 140.089 188.833 1.00 70.97  ? 41   LYS B CA    1 
ATOM   7720  C  C     . LYS B 2 41  ? 147.241 140.894 187.567 1.00 72.27  ? 41   LYS B C     1 
ATOM   7721  O  O     . LYS B 2 41  ? 147.384 142.118 187.533 1.00 77.10  ? 41   LYS B O     1 
ATOM   7722  C  CB    . LYS B 2 41  ? 146.170 139.568 189.411 1.00 72.03  ? 41   LYS B CB    1 
ATOM   7723  C  CG    . LYS B 2 41  ? 145.201 140.651 189.843 1.00 70.18  ? 41   LYS B CG    1 
ATOM   7724  C  CD    . LYS B 2 41  ? 143.930 140.036 190.398 1.00 69.65  ? 41   LYS B CD    1 
ATOM   7725  C  CE    . LYS B 2 41  ? 142.856 141.079 190.614 1.00 69.46  ? 41   LYS B CE    1 
ATOM   7726  N  NZ    . LYS B 2 41  ? 141.606 140.474 191.138 1.00 68.23  ? 41   LYS B NZ    1 
ATOM   7727  N  N     . ILE B 2 42  ? 146.876 140.185 186.510 1.00 58.18  ? 42   ILE B N     1 
ATOM   7728  C  CA    . ILE B 2 42  ? 146.494 140.812 185.256 1.00 54.74  ? 42   ILE B CA    1 
ATOM   7729  C  C     . ILE B 2 42  ? 145.003 140.601 185.056 1.00 60.04  ? 42   ILE B C     1 
ATOM   7730  O  O     . ILE B 2 42  ? 144.439 139.574 185.447 1.00 63.32  ? 42   ILE B O     1 
ATOM   7731  C  CB    . ILE B 2 42  ? 147.304 140.272 184.059 1.00 55.13  ? 42   ILE B CB    1 
ATOM   7732  C  CG1   . ILE B 2 42  ? 147.219 138.748 183.984 1.00 59.49  ? 42   ILE B CG1   1 
ATOM   7733  C  CG2   . ILE B 2 42  ? 148.747 140.716 184.159 1.00 59.96  ? 42   ILE B CG2   1 
ATOM   7734  C  CD1   . ILE B 2 42  ? 146.340 138.242 182.868 1.00 58.99  ? 42   ILE B CD1   1 
ATOM   7735  N  N     . VAL B 2 43  ? 144.357 141.602 184.468 1.00 62.47  ? 43   VAL B N     1 
ATOM   7736  C  CA    . VAL B 2 43  ? 142.933 141.527 184.173 1.00 59.09  ? 43   VAL B CA    1 
ATOM   7737  C  C     . VAL B 2 43  ? 142.733 141.788 182.688 1.00 60.23  ? 43   VAL B C     1 
ATOM   7738  O  O     . VAL B 2 43  ? 143.697 142.027 181.953 1.00 58.60  ? 43   VAL B O     1 
ATOM   7739  C  CB    . VAL B 2 43  ? 142.128 142.520 185.030 1.00 57.19  ? 43   VAL B CB    1 
ATOM   7740  C  CG1   . VAL B 2 43  ? 142.218 142.145 186.497 1.00 57.64  ? 43   VAL B CG1   1 
ATOM   7741  C  CG2   . VAL B 2 43  ? 142.629 143.933 184.811 1.00 58.83  ? 43   VAL B CG2   1 
ATOM   7742  N  N     . GLY B 2 44  ? 141.486 141.735 182.235 1.00 60.36  ? 44   GLY B N     1 
ATOM   7743  C  CA    . GLY B 2 44  ? 141.166 142.013 180.855 1.00 58.53  ? 44   GLY B CA    1 
ATOM   7744  C  C     . GLY B 2 44  ? 141.030 143.501 180.598 1.00 58.26  ? 44   GLY B C     1 
ATOM   7745  O  O     . GLY B 2 44  ? 141.413 144.348 181.406 1.00 59.07  ? 44   GLY B O     1 
ATOM   7746  N  N     . CYS B 2 45  ? 140.476 143.817 179.434 1.00 63.65  ? 45   CYS B N     1 
ATOM   7747  C  CA    . CYS B 2 45  ? 140.193 145.200 179.086 1.00 63.48  ? 45   CYS B CA    1 
ATOM   7748  C  C     . CYS B 2 45  ? 138.867 145.616 179.705 1.00 65.57  ? 45   CYS B C     1 
ATOM   7749  O  O     . CYS B 2 45  ? 137.841 144.961 179.494 1.00 66.27  ? 45   CYS B O     1 
ATOM   7750  C  CB    . CYS B 2 45  ? 140.154 145.374 177.569 1.00 64.80  ? 45   CYS B CB    1 
ATOM   7751  S  SG    . CYS B 2 45  ? 139.744 147.043 177.018 1.00 70.45  ? 45   CYS B SG    1 
ATOM   7752  N  N     . VAL B 2 46  ? 138.892 146.702 180.481 1.00 68.48  ? 46   VAL B N     1 
ATOM   7753  C  CA    . VAL B 2 46  ? 137.683 147.158 181.160 1.00 66.66  ? 46   VAL B CA    1 
ATOM   7754  C  C     . VAL B 2 46  ? 136.655 147.652 180.151 1.00 66.69  ? 46   VAL B C     1 
ATOM   7755  O  O     . VAL B 2 46  ? 135.453 147.397 180.290 1.00 66.61  ? 46   VAL B O     1 
ATOM   7756  C  CB    . VAL B 2 46  ? 138.030 148.245 182.191 1.00 66.82  ? 46   VAL B CB    1 
ATOM   7757  C  CG1   . VAL B 2 46  ? 136.847 148.502 183.104 1.00 66.82  ? 46   VAL B CG1   1 
ATOM   7758  C  CG2   . VAL B 2 46  ? 139.256 147.841 182.990 1.00 65.77  ? 46   VAL B CG2   1 
ATOM   7759  N  N     . GLY B 2 47  ? 137.109 148.353 179.119 1.00 70.50  ? 47   GLY B N     1 
ATOM   7760  C  CA    . GLY B 2 47  ? 136.221 148.925 178.130 1.00 69.84  ? 47   GLY B CA    1 
ATOM   7761  C  C     . GLY B 2 47  ? 136.697 150.290 177.687 1.00 71.62  ? 47   GLY B C     1 
ATOM   7762  O  O     . GLY B 2 47  ? 136.392 150.736 176.578 1.00 74.45  ? 47   GLY B O     1 
ATOM   7763  N  N     . MET B 2 48  ? 137.457 150.961 178.552 1.00 75.17  ? 48   MET B N     1 
ATOM   7764  C  CA    . MET B 2 48  ? 138.007 152.281 178.248 1.00 77.47  ? 48   MET B CA    1 
ATOM   7765  C  C     . MET B 2 48  ? 139.293 152.102 177.448 1.00 77.18  ? 48   MET B C     1 
ATOM   7766  O  O     . MET B 2 48  ? 140.409 152.244 177.953 1.00 79.40  ? 48   MET B O     1 
ATOM   7767  C  CB    . MET B 2 48  ? 138.250 153.073 179.525 1.00 77.35  ? 48   MET B CB    1 
ATOM   7768  C  CG    . MET B 2 48  ? 136.991 153.481 180.252 1.00 78.11  ? 48   MET B CG    1 
ATOM   7769  S  SD    . MET B 2 48  ? 137.332 154.641 181.584 1.00 80.42  ? 48   MET B SD    1 
ATOM   7770  C  CE    . MET B 2 48  ? 138.413 153.654 182.612 1.00 76.91  ? 48   MET B CE    1 
ATOM   7771  N  N     . CYS B 2 49  ? 139.123 151.792 176.163 1.00 72.00  ? 49   CYS B N     1 
ATOM   7772  C  CA    . CYS B 2 49  ? 140.265 151.572 175.285 1.00 74.89  ? 49   CYS B CA    1 
ATOM   7773  C  C     . CYS B 2 49  ? 141.025 152.851 174.964 1.00 77.26  ? 49   CYS B C     1 
ATOM   7774  O  O     . CYS B 2 49  ? 142.127 152.771 174.413 1.00 79.44  ? 49   CYS B O     1 
ATOM   7775  C  CB    . CYS B 2 49  ? 139.809 150.907 173.986 1.00 74.36  ? 49   CYS B CB    1 
ATOM   7776  S  SG    . CYS B 2 49  ? 139.101 149.258 174.194 1.00 78.62  ? 49   CYS B SG    1 
ATOM   7777  N  N     . TYR B 2 50  ? 140.477 154.017 175.293 1.00 72.10  ? 50   TYR B N     1 
ATOM   7778  C  CA    . TYR B 2 50  ? 141.100 155.290 174.959 1.00 71.55  ? 50   TYR B CA    1 
ATOM   7779  C  C     . TYR B 2 50  ? 141.990 155.828 176.072 1.00 72.02  ? 50   TYR B C     1 
ATOM   7780  O  O     . TYR B 2 50  ? 142.475 156.957 175.966 1.00 73.87  ? 50   TYR B O     1 
ATOM   7781  C  CB    . TYR B 2 50  ? 140.029 156.324 174.597 1.00 71.34  ? 50   TYR B CB    1 
ATOM   7782  C  CG    . TYR B 2 50  ? 139.078 156.668 175.720 1.00 72.78  ? 50   TYR B CG    1 
ATOM   7783  C  CD1   . TYR B 2 50  ? 137.979 155.868 175.996 1.00 72.75  ? 50   TYR B CD1   1 
ATOM   7784  C  CD2   . TYR B 2 50  ? 139.270 157.803 176.493 1.00 72.80  ? 50   TYR B CD2   1 
ATOM   7785  C  CE1   . TYR B 2 50  ? 137.110 156.180 177.016 1.00 71.68  ? 50   TYR B CE1   1 
ATOM   7786  C  CE2   . TYR B 2 50  ? 138.404 158.122 177.516 1.00 72.58  ? 50   TYR B CE2   1 
ATOM   7787  C  CZ    . TYR B 2 50  ? 137.326 157.307 177.773 1.00 72.33  ? 50   TYR B CZ    1 
ATOM   7788  O  OH    . TYR B 2 50  ? 136.458 157.621 178.791 1.00 73.52  ? 50   TYR B OH    1 
ATOM   7789  N  N     . ARG B 2 51  ? 142.217 155.050 177.135 1.00 76.67  ? 51   ARG B N     1 
ATOM   7790  C  CA    . ARG B 2 51  ? 143.068 155.483 178.237 1.00 76.62  ? 51   ARG B CA    1 
ATOM   7791  C  C     . ARG B 2 51  ? 144.073 154.413 178.650 1.00 76.87  ? 51   ARG B C     1 
ATOM   7792  O  O     . ARG B 2 51  ? 144.619 154.483 179.756 1.00 78.49  ? 51   ARG B O     1 
ATOM   7793  C  CB    . ARG B 2 51  ? 142.222 155.896 179.442 1.00 75.22  ? 51   ARG B CB    1 
ATOM   7794  C  CG    . ARG B 2 51  ? 141.426 157.159 179.211 1.00 76.90  ? 51   ARG B CG    1 
ATOM   7795  C  CD    . ARG B 2 51  ? 140.738 157.620 180.471 1.00 77.54  ? 51   ARG B CD    1 
ATOM   7796  N  NE    . ARG B 2 51  ? 140.124 158.929 180.297 1.00 76.72  ? 51   ARG B NE    1 
ATOM   7797  C  CZ    . ARG B 2 51  ? 140.783 160.077 180.369 1.00 76.36  ? 51   ARG B CZ    1 
ATOM   7798  N  NH1   . ARG B 2 51  ? 142.083 160.113 180.604 1.00 77.06  ? 51   ARG B NH1   1 
ATOM   7799  N  NH2   . ARG B 2 51  ? 140.120 161.216 180.196 1.00 75.41  ? 51   ARG B NH2   1 
ATOM   7800  N  N     . GLU B 2 52  ? 144.330 153.433 177.789 1.00 72.12  ? 52   GLU B N     1 
ATOM   7801  C  CA    . GLU B 2 52  ? 145.239 152.351 178.130 1.00 73.72  ? 52   GLU B CA    1 
ATOM   7802  C  C     . GLU B 2 52  ? 146.677 152.863 178.219 1.00 74.67  ? 52   GLU B C     1 
ATOM   7803  O  O     . GLU B 2 52  ? 147.065 153.770 177.479 1.00 76.37  ? 52   GLU B O     1 
ATOM   7804  C  CB    . GLU B 2 52  ? 145.147 151.240 177.088 1.00 75.34  ? 52   GLU B CB    1 
ATOM   7805  C  CG    . GLU B 2 52  ? 143.733 150.784 176.776 1.00 73.07  ? 52   GLU B CG    1 
ATOM   7806  C  CD    . GLU B 2 52  ? 143.244 149.692 177.703 1.00 73.40  ? 52   GLU B CD    1 
ATOM   7807  O  OE1   . GLU B 2 52  ? 143.879 149.466 178.753 1.00 74.35  ? 52   GLU B OE1   1 
ATOM   7808  O  OE2   . GLU B 2 52  ? 142.226 149.050 177.376 1.00 75.19  ? 52   GLU B OE2   1 
ATOM   7809  N  N     . PRO B 2 53  ? 147.500 152.289 179.112 1.00 76.86  ? 53   PRO B N     1 
ATOM   7810  C  CA    . PRO B 2 53  ? 147.233 151.187 180.054 1.00 77.65  ? 53   PRO B CA    1 
ATOM   7811  C  C     . PRO B 2 53  ? 146.425 151.606 181.277 1.00 77.51  ? 53   PRO B C     1 
ATOM   7812  O  O     . PRO B 2 53  ? 146.441 152.764 181.680 1.00 80.93  ? 53   PRO B O     1 
ATOM   7813  C  CB    . PRO B 2 53  ? 148.646 150.730 180.468 1.00 77.82  ? 53   PRO B CB    1 
ATOM   7814  C  CG    . PRO B 2 53  ? 149.603 151.400 179.514 1.00 76.78  ? 53   PRO B CG    1 
ATOM   7815  C  CD    . PRO B 2 53  ? 148.919 152.669 179.130 1.00 77.20  ? 53   PRO B CD    1 
ATOM   7816  N  N     . LEU B 2 54  ? 145.715 150.666 181.891 1.00 67.06  ? 54   LEU B N     1 
ATOM   7817  C  CA    . LEU B 2 54  ? 144.917 150.922 183.083 1.00 67.61  ? 54   LEU B CA    1 
ATOM   7818  C  C     . LEU B 2 54  ? 145.498 150.147 184.256 1.00 69.40  ? 54   LEU B C     1 
ATOM   7819  O  O     . LEU B 2 54  ? 145.728 148.938 184.152 1.00 71.61  ? 54   LEU B O     1 
ATOM   7820  C  CB    . LEU B 2 54  ? 143.455 150.527 182.865 1.00 68.48  ? 54   LEU B CB    1 
ATOM   7821  C  CG    . LEU B 2 54  ? 142.489 151.552 182.265 1.00 69.01  ? 54   LEU B CG    1 
ATOM   7822  C  CD1   . LEU B 2 54  ? 142.830 151.864 180.827 1.00 70.91  ? 54   LEU B CD1   1 
ATOM   7823  C  CD2   . LEU B 2 54  ? 141.063 151.051 182.368 1.00 68.71  ? 54   LEU B CD2   1 
ATOM   7824  N  N     . LEU B 2 55  ? 145.729 150.842 185.366 1.00 75.96  ? 55   LEU B N     1 
ATOM   7825  C  CA    . LEU B 2 55  ? 146.251 150.240 186.585 1.00 75.14  ? 55   LEU B CA    1 
ATOM   7826  C  C     . LEU B 2 55  ? 145.192 150.348 187.670 1.00 75.66  ? 55   LEU B C     1 
ATOM   7827  O  O     . LEU B 2 55  ? 144.655 151.433 187.914 1.00 78.67  ? 55   LEU B O     1 
ATOM   7828  C  CB    . LEU B 2 55  ? 147.551 150.921 187.025 1.00 77.17  ? 55   LEU B CB    1 
ATOM   7829  C  CG    . LEU B 2 55  ? 148.461 150.204 188.026 1.00 75.61  ? 55   LEU B CG    1 
ATOM   7830  C  CD1   . LEU B 2 55  ? 149.889 150.652 187.827 1.00 76.92  ? 55   LEU B CD1   1 
ATOM   7831  C  CD2   . LEU B 2 55  ? 148.039 150.467 189.458 1.00 76.43  ? 55   LEU B CD2   1 
ATOM   7832  N  N     . ASP B 2 56  ? 144.900 149.230 188.322 1.00 80.60  ? 56   ASP B N     1 
ATOM   7833  C  CA    . ASP B 2 56  ? 143.858 149.164 189.332 1.00 81.57  ? 56   ASP B CA    1 
ATOM   7834  C  C     . ASP B 2 56  ? 144.471 149.009 190.715 1.00 82.88  ? 56   ASP B C     1 
ATOM   7835  O  O     . ASP B 2 56  ? 145.396 148.216 190.911 1.00 86.17  ? 56   ASP B O     1 
ATOM   7836  C  CB    . ASP B 2 56  ? 142.899 148.003 189.061 1.00 84.00  ? 56   ASP B CB    1 
ATOM   7837  C  CG    . ASP B 2 56  ? 142.239 148.099 187.701 1.00 86.21  ? 56   ASP B CG    1 
ATOM   7838  O  OD1   . ASP B 2 56  ? 142.108 149.225 187.181 1.00 85.17  ? 56   ASP B OD1   1 
ATOM   7839  O  OD2   . ASP B 2 56  ? 141.849 147.047 187.152 1.00 85.93  ? 56   ASP B OD2   1 
ATOM   7840  N  N     . ILE B 2 57  ? 143.957 149.780 191.666 1.00 82.29  ? 57   ILE B N     1 
ATOM   7841  C  CA    . ILE B 2 57  ? 144.263 149.612 193.079 1.00 82.51  ? 57   ILE B CA    1 
ATOM   7842  C  C     . ILE B 2 57  ? 143.008 149.066 193.744 1.00 83.37  ? 57   ILE B C     1 
ATOM   7843  O  O     . ILE B 2 57  ? 141.966 149.732 193.758 1.00 82.26  ? 57   ILE B O     1 
ATOM   7844  C  CB    . ILE B 2 57  ? 144.710 150.930 193.724 1.00 81.63  ? 57   ILE B CB    1 
ATOM   7845  C  CG1   . ILE B 2 57  ? 145.922 151.500 192.985 1.00 82.98  ? 57   ILE B CG1   1 
ATOM   7846  C  CG2   . ILE B 2 57  ? 145.036 150.713 195.180 1.00 82.64  ? 57   ILE B CG2   1 
ATOM   7847  C  CD1   . ILE B 2 57  ? 147.165 150.659 193.111 1.00 81.59  ? 57   ILE B CD1   1 
ATOM   7848  N  N     . ILE B 2 58  ? 143.104 147.858 194.288 1.00 92.73  ? 58   ILE B N     1 
ATOM   7849  C  CA    . ILE B 2 58  ? 141.945 147.121 194.778 1.00 91.19  ? 58   ILE B CA    1 
ATOM   7850  C  C     . ILE B 2 58  ? 142.005 147.067 196.297 1.00 92.86  ? 58   ILE B C     1 
ATOM   7851  O  O     . ILE B 2 58  ? 143.002 146.618 196.874 1.00 95.66  ? 58   ILE B O     1 
ATOM   7852  C  CB    . ILE B 2 58  ? 141.883 145.706 194.184 1.00 90.04  ? 58   ILE B CB    1 
ATOM   7853  C  CG1   . ILE B 2 58  ? 141.884 145.768 192.658 1.00 89.73  ? 58   ILE B CG1   1 
ATOM   7854  C  CG2   . ILE B 2 58  ? 140.651 144.974 194.681 1.00 90.67  ? 58   ILE B CG2   1 
ATOM   7855  C  CD1   . ILE B 2 58  ? 141.841 144.415 191.998 1.00 90.09  ? 58   ILE B CD1   1 
ATOM   7856  N  N     . THR B 2 59  ? 140.941 147.526 196.939 1.00 96.02  ? 59   THR B N     1 
ATOM   7857  C  CA    . THR B 2 59  ? 140.715 147.329 198.361 1.00 96.78  ? 59   THR B CA    1 
ATOM   7858  C  C     . THR B 2 59  ? 139.479 146.455 198.542 1.00 97.22  ? 59   THR B C     1 
ATOM   7859  O  O     . THR B 2 59  ? 138.878 145.980 197.575 1.00 95.61  ? 59   THR B O     1 
ATOM   7860  C  CB    . THR B 2 59  ? 140.563 148.668 199.083 1.00 98.23  ? 59   THR B CB    1 
ATOM   7861  O  OG1   . THR B 2 59  ? 139.329 149.283 198.698 1.00 96.91  ? 59   THR B OG1   1 
ATOM   7862  C  CG2   . THR B 2 59  ? 141.709 149.594 198.728 1.00 95.58  ? 59   THR B CG2   1 
ATOM   7863  N  N     . ASP B 2 60  ? 139.098 146.238 199.799 1.00 104.34 ? 60   ASP B N     1 
ATOM   7864  C  CA    . ASP B 2 60  ? 137.940 145.396 200.072 1.00 103.95 ? 60   ASP B CA    1 
ATOM   7865  C  C     . ASP B 2 60  ? 136.629 146.068 199.694 1.00 104.87 ? 60   ASP B C     1 
ATOM   7866  O  O     . ASP B 2 60  ? 135.619 145.376 199.528 1.00 104.39 ? 60   ASP B O     1 
ATOM   7867  C  CB    . ASP B 2 60  ? 137.912 145.000 201.548 1.00 104.86 ? 60   ASP B CB    1 
ATOM   7868  C  CG    . ASP B 2 60  ? 139.102 144.151 201.945 1.00 105.57 ? 60   ASP B CG    1 
ATOM   7869  O  OD1   . ASP B 2 60  ? 139.939 143.852 201.068 1.00 105.64 ? 60   ASP B OD1   1 
ATOM   7870  O  OD2   . ASP B 2 60  ? 139.201 143.781 203.134 1.00 105.45 ? 60   ASP B OD2   1 
ATOM   7871  N  N     . ASN B 2 61  ? 136.619 147.391 199.548 1.00 105.76 ? 61   ASN B N     1 
ATOM   7872  C  CA    . ASN B 2 61  ? 135.385 148.128 199.313 1.00 105.37 ? 61   ASN B CA    1 
ATOM   7873  C  C     . ASN B 2 61  ? 135.420 149.052 198.104 1.00 103.27 ? 61   ASN B C     1 
ATOM   7874  O  O     . ASN B 2 61  ? 134.346 149.430 197.622 1.00 104.77 ? 61   ASN B O     1 
ATOM   7875  C  CB    . ASN B 2 61  ? 135.017 148.954 200.555 1.00 106.29 ? 61   ASN B CB    1 
ATOM   7876  C  CG    . ASN B 2 61  ? 133.579 149.426 200.538 1.00 105.99 ? 61   ASN B CG    1 
ATOM   7877  O  OD1   . ASN B 2 61  ? 133.279 150.527 200.076 1.00 104.84 ? 61   ASN B OD1   1 
ATOM   7878  N  ND2   . ASN B 2 61  ? 132.677 148.593 201.044 1.00 106.19 ? 61   ASN B ND2   1 
ATOM   7879  N  N     . GLU B 2 62  ? 136.590 149.428 197.595 1.00 93.87  ? 62   GLU B N     1 
ATOM   7880  C  CA    . GLU B 2 62  ? 136.654 150.338 196.462 1.00 94.06  ? 62   GLU B CA    1 
ATOM   7881  C  C     . GLU B 2 62  ? 137.785 149.943 195.524 1.00 94.24  ? 62   GLU B C     1 
ATOM   7882  O  O     . GLU B 2 62  ? 138.790 149.362 195.940 1.00 97.07  ? 62   GLU B O     1 
ATOM   7883  C  CB    . GLU B 2 62  ? 136.839 151.794 196.913 1.00 96.25  ? 62   GLU B CB    1 
ATOM   7884  C  CG    . GLU B 2 62  ? 138.167 152.082 197.587 1.00 97.74  ? 62   GLU B CG    1 
ATOM   7885  C  CD    . GLU B 2 62  ? 138.310 153.534 197.994 1.00 97.37  ? 62   GLU B CD    1 
ATOM   7886  O  OE1   . GLU B 2 62  ? 137.373 154.320 197.738 1.00 95.08  ? 62   GLU B OE1   1 
ATOM   7887  O  OE2   . GLU B 2 62  ? 139.360 153.891 198.569 1.00 97.33  ? 62   GLU B OE2   1 
ATOM   7888  N  N     . ILE B 2 63  ? 137.601 150.266 194.247 1.00 83.07  ? 63   ILE B N     1 
ATOM   7889  C  CA    . ILE B 2 63  ? 138.609 150.071 193.212 1.00 81.52  ? 63   ILE B CA    1 
ATOM   7890  C  C     . ILE B 2 63  ? 138.863 151.424 192.566 1.00 80.96  ? 63   ILE B C     1 
ATOM   7891  O  O     . ILE B 2 63  ? 137.926 152.073 192.086 1.00 85.07  ? 63   ILE B O     1 
ATOM   7892  C  CB    . ILE B 2 63  ? 138.167 149.040 192.162 1.00 80.22  ? 63   ILE B CB    1 
ATOM   7893  C  CG1   . ILE B 2 63  ? 137.952 147.671 192.804 1.00 81.18  ? 63   ILE B CG1   1 
ATOM   7894  C  CG2   . ILE B 2 63  ? 139.188 148.948 191.044 1.00 80.90  ? 63   ILE B CG2   1 
ATOM   7895  C  CD1   . ILE B 2 63  ? 137.507 146.610 191.830 1.00 82.16  ? 63   ILE B CD1   1 
ATOM   7896  N  N     . ILE B 2 64  ? 140.120 151.847 192.554 1.00 77.89  ? 64   ILE B N     1 
ATOM   7897  C  CA    . ILE B 2 64  ? 140.511 153.136 192.000 1.00 78.96  ? 64   ILE B CA    1 
ATOM   7898  C  C     . ILE B 2 64  ? 141.398 152.861 190.796 1.00 79.99  ? 64   ILE B C     1 
ATOM   7899  O  O     . ILE B 2 64  ? 142.515 152.352 190.938 1.00 82.06  ? 64   ILE B O     1 
ATOM   7900  C  CB    . ILE B 2 64  ? 141.226 154.009 193.039 1.00 81.02  ? 64   ILE B CB    1 
ATOM   7901  C  CG1   . ILE B 2 64  ? 140.368 154.138 194.297 1.00 81.56  ? 64   ILE B CG1   1 
ATOM   7902  C  CG2   . ILE B 2 64  ? 141.513 155.376 192.469 1.00 81.68  ? 64   ILE B CG2   1 
ATOM   7903  C  CD1   . ILE B 2 64  ? 140.969 155.017 195.358 1.00 81.88  ? 64   ILE B CD1   1 
ATOM   7904  N  N     . THR B 2 65  ? 140.903 153.202 189.610 1.00 79.83  ? 65   THR B N     1 
ATOM   7905  C  CA    . THR B 2 65  ? 141.576 152.897 188.355 1.00 81.32  ? 65   THR B CA    1 
ATOM   7906  C  C     . THR B 2 65  ? 142.257 154.147 187.819 1.00 81.83  ? 65   THR B C     1 
ATOM   7907  O  O     . THR B 2 65  ? 141.647 155.219 187.761 1.00 83.94  ? 65   THR B O     1 
ATOM   7908  C  CB    . THR B 2 65  ? 140.583 152.353 187.325 1.00 80.39  ? 65   THR B CB    1 
ATOM   7909  O  OG1   . THR B 2 65  ? 140.050 151.105 187.784 1.00 80.48  ? 65   THR B OG1   1 
ATOM   7910  C  CG2   . THR B 2 65  ? 141.255 152.143 185.980 1.00 79.83  ? 65   THR B CG2   1 
ATOM   7911  N  N     . TYR B 2 66  ? 143.518 154.002 187.425 1.00 83.33  ? 66   TYR B N     1 
ATOM   7912  C  CA    . TYR B 2 66  ? 144.311 155.087 186.869 1.00 81.92  ? 66   TYR B CA    1 
ATOM   7913  C  C     . TYR B 2 66  ? 144.535 154.830 185.384 1.00 83.47  ? 66   TYR B C     1 
ATOM   7914  O  O     . TYR B 2 66  ? 144.851 153.705 184.987 1.00 86.61  ? 66   TYR B O     1 
ATOM   7915  C  CB    . TYR B 2 66  ? 145.646 155.213 187.608 1.00 82.46  ? 66   TYR B CB    1 
ATOM   7916  C  CG    . TYR B 2 66  ? 145.507 155.674 189.045 1.00 85.14  ? 66   TYR B CG    1 
ATOM   7917  C  CD1   . TYR B 2 66  ? 145.029 154.820 190.029 1.00 85.02  ? 66   TYR B CD1   1 
ATOM   7918  C  CD2   . TYR B 2 66  ? 145.854 156.965 189.414 1.00 86.47  ? 66   TYR B CD2   1 
ATOM   7919  C  CE1   . TYR B 2 66  ? 144.901 155.238 191.336 1.00 87.04  ? 66   TYR B CE1   1 
ATOM   7920  C  CE2   . TYR B 2 66  ? 145.728 157.391 190.720 1.00 85.45  ? 66   TYR B CE2   1 
ATOM   7921  C  CZ    . TYR B 2 66  ? 145.249 156.525 191.675 1.00 85.83  ? 66   TYR B CZ    1 
ATOM   7922  O  OH    . TYR B 2 66  ? 145.123 156.945 192.977 1.00 86.74  ? 66   TYR B OH    1 
ATOM   7923  N  N     . GLY B 2 67  ? 144.354 155.867 184.567 1.00 78.32  ? 67   GLY B N     1 
ATOM   7924  C  CA    . GLY B 2 67  ? 144.527 155.757 183.136 1.00 79.35  ? 67   GLY B CA    1 
ATOM   7925  C  C     . GLY B 2 67  ? 145.835 156.357 182.653 1.00 80.76  ? 67   GLY B C     1 
ATOM   7926  O  O     . GLY B 2 67  ? 146.443 157.183 183.328 1.00 83.46  ? 67   GLY B O     1 
ATOM   7927  N  N     . HIS B 2 68  ? 146.252 155.925 181.458 1.00 81.59  ? 68   HIS B N     1 
ATOM   7928  C  CA    . HIS B 2 68  ? 147.504 156.365 180.830 1.00 83.09  ? 68   HIS B CA    1 
ATOM   7929  C  C     . HIS B 2 68  ? 148.713 156.095 181.724 1.00 82.22  ? 68   HIS B C     1 
ATOM   7930  O  O     . HIS B 2 68  ? 149.593 156.943 181.877 1.00 84.18  ? 68   HIS B O     1 
ATOM   7931  C  CB    . HIS B 2 68  ? 147.450 157.848 180.446 1.00 83.08  ? 68   HIS B CB    1 
ATOM   7932  C  CG    . HIS B 2 68  ? 146.506 158.157 179.327 1.00 82.14  ? 68   HIS B CG    1 
ATOM   7933  N  ND1   . HIS B 2 68  ? 146.759 157.806 178.019 1.00 82.44  ? 68   HIS B ND1   1 
ATOM   7934  C  CD2   . HIS B 2 68  ? 145.319 158.808 179.318 1.00 81.85  ? 68   HIS B CD2   1 
ATOM   7935  C  CE1   . HIS B 2 68  ? 145.762 158.214 177.255 1.00 82.83  ? 68   HIS B CE1   1 
ATOM   7936  N  NE2   . HIS B 2 68  ? 144.876 158.826 178.019 1.00 83.39  ? 68   HIS B NE2   1 
ATOM   7937  N  N     . VAL B 2 69  ? 148.768 154.902 182.311 1.00 80.40  ? 69   VAL B N     1 
ATOM   7938  C  CA    . VAL B 2 69  ? 149.804 154.569 183.292 1.00 81.34  ? 69   VAL B CA    1 
ATOM   7939  C  C     . VAL B 2 69  ? 150.995 154.008 182.521 1.00 82.86  ? 69   VAL B C     1 
ATOM   7940  O  O     . VAL B 2 69  ? 151.094 152.809 182.262 1.00 83.19  ? 69   VAL B O     1 
ATOM   7941  C  CB    . VAL B 2 69  ? 149.294 153.603 184.356 1.00 81.66  ? 69   VAL B CB    1 
ATOM   7942  C  CG1   . VAL B 2 69  ? 150.355 153.390 185.415 1.00 82.66  ? 69   VAL B CG1   1 
ATOM   7943  C  CG2   . VAL B 2 69  ? 148.032 154.139 184.984 1.00 80.90  ? 69   VAL B CG2   1 
ATOM   7944  N  N     . THR B 2 70  ? 151.909 154.892 182.150 1.00 89.72  ? 70   THR B N     1 
ATOM   7945  C  CA    . THR B 2 70  ? 153.182 154.497 181.572 1.00 88.97  ? 70   THR B CA    1 
ATOM   7946  C  C     . THR B 2 70  ? 154.124 154.056 182.687 1.00 89.90  ? 70   THR B C     1 
ATOM   7947  O  O     . THR B 2 70  ? 153.837 154.254 183.868 1.00 92.35  ? 70   THR B O     1 
ATOM   7948  C  CB    . THR B 2 70  ? 153.756 155.657 180.759 1.00 90.14  ? 70   THR B CB    1 
ATOM   7949  O  OG1   . THR B 2 70  ? 153.677 156.865 181.523 1.00 90.20  ? 70   THR B OG1   1 
ATOM   7950  C  CG2   . THR B 2 70  ? 152.985 155.830 179.465 1.00 89.10  ? 70   THR B CG2   1 
ATOM   7951  N  N     . PRO B 2 71  ? 155.250 153.417 182.351 1.00 89.27  ? 71   PRO B N     1 
ATOM   7952  C  CA    . PRO B 2 71  ? 156.211 153.043 183.401 1.00 89.21  ? 71   PRO B CA    1 
ATOM   7953  C  C     . PRO B 2 71  ? 156.758 154.215 184.198 1.00 89.57  ? 71   PRO B C     1 
ATOM   7954  O  O     . PRO B 2 71  ? 157.214 154.008 185.328 1.00 89.69  ? 71   PRO B O     1 
ATOM   7955  C  CB    . PRO B 2 71  ? 157.326 152.341 182.616 1.00 89.81  ? 71   PRO B CB    1 
ATOM   7956  C  CG    . PRO B 2 71  ? 156.640 151.773 181.449 1.00 90.13  ? 71   PRO B CG    1 
ATOM   7957  C  CD    . PRO B 2 71  ? 155.571 152.755 181.073 1.00 90.60  ? 71   PRO B CD    1 
ATOM   7958  N  N     . ASP B 2 72  ? 156.732 155.435 183.657 1.00 93.50  ? 72   ASP B N     1 
ATOM   7959  C  CA    . ASP B 2 72  ? 157.332 156.559 184.368 1.00 94.37  ? 72   ASP B CA    1 
ATOM   7960  C  C     . ASP B 2 72  ? 156.482 157.013 185.550 1.00 94.64  ? 72   ASP B C     1 
ATOM   7961  O  O     . ASP B 2 72  ? 157.028 157.477 186.557 1.00 94.66  ? 72   ASP B O     1 
ATOM   7962  C  CB    . ASP B 2 72  ? 157.574 157.724 183.406 1.00 93.80  ? 72   ASP B CB    1 
ATOM   7963  C  CG    . ASP B 2 72  ? 156.289 158.358 182.921 1.00 94.32  ? 72   ASP B CG    1 
ATOM   7964  O  OD1   . ASP B 2 72  ? 155.265 157.651 182.853 1.00 93.91  ? 72   ASP B OD1   1 
ATOM   7965  O  OD2   . ASP B 2 72  ? 156.302 159.567 182.608 1.00 94.51  ? 72   ASP B OD2   1 
ATOM   7966  N  N     . ARG B 2 73  ? 155.161 156.896 185.455 1.00 91.97  ? 73   ARG B N     1 
ATOM   7967  C  CA    . ARG B 2 73  ? 154.274 157.320 186.530 1.00 91.17  ? 73   ARG B CA    1 
ATOM   7968  C  C     . ARG B 2 73  ? 153.922 156.198 187.499 1.00 91.69  ? 73   ARG B C     1 
ATOM   7969  O  O     . ARG B 2 73  ? 153.225 156.450 188.486 1.00 93.01  ? 73   ARG B O     1 
ATOM   7970  C  CB    . ARG B 2 73  ? 152.996 157.927 185.946 1.00 91.68  ? 73   ARG B CB    1 
ATOM   7971  C  CG    . ARG B 2 73  ? 152.567 157.319 184.626 1.00 92.04  ? 73   ARG B CG    1 
ATOM   7972  C  CD    . ARG B 2 73  ? 151.866 158.349 183.753 1.00 92.36  ? 73   ARG B CD    1 
ATOM   7973  N  NE    . ARG B 2 73  ? 150.514 158.646 184.211 1.00 91.68  ? 73   ARG B NE    1 
ATOM   7974  C  CZ    . ARG B 2 73  ? 149.722 159.552 183.655 1.00 92.12  ? 73   ARG B CZ    1 
ATOM   7975  N  NH1   . ARG B 2 73  ? 150.124 160.284 182.629 1.00 91.86  ? 73   ARG B NH1   1 
ATOM   7976  N  NH2   . ARG B 2 73  ? 148.496 159.727 184.139 1.00 92.43  ? 73   ARG B NH2   1 
ATOM   7977  N  N     . VAL B 2 74  ? 154.377 154.970 187.236 1.00 94.86  ? 74   VAL B N     1 
ATOM   7978  C  CA    . VAL B 2 74  ? 154.184 153.884 188.203 1.00 95.37  ? 74   VAL B CA    1 
ATOM   7979  C  C     . VAL B 2 74  ? 154.861 154.165 189.539 1.00 96.77  ? 74   VAL B C     1 
ATOM   7980  O  O     . VAL B 2 74  ? 154.246 153.896 190.583 1.00 96.07  ? 74   VAL B O     1 
ATOM   7981  C  CB    . VAL B 2 74  ? 154.598 152.543 187.582 1.00 95.89  ? 74   VAL B CB    1 
ATOM   7982  C  CG1   . VAL B 2 74  ? 154.574 151.441 188.622 1.00 94.94  ? 74   VAL B CG1   1 
ATOM   7983  C  CG2   . VAL B 2 74  ? 153.676 152.197 186.429 1.00 94.57  ? 74   VAL B CG2   1 
ATOM   7984  N  N     . PRO B 2 75  ? 156.107 154.666 189.604 1.00 102.92 ? 75   PRO B N     1 
ATOM   7985  C  CA    . PRO B 2 75  ? 156.669 154.992 190.928 1.00 102.89 ? 75   PRO B CA    1 
ATOM   7986  C  C     . PRO B 2 75  ? 155.833 155.982 191.716 1.00 101.58 ? 75   PRO B C     1 
ATOM   7987  O  O     . PRO B 2 75  ? 155.664 155.816 192.931 1.00 101.48 ? 75   PRO B O     1 
ATOM   7988  C  CB    . PRO B 2 75  ? 158.049 155.568 190.586 1.00 101.88 ? 75   PRO B CB    1 
ATOM   7989  C  CG    . PRO B 2 75  ? 158.409 154.926 189.316 1.00 100.25 ? 75   PRO B CG    1 
ATOM   7990  C  CD    . PRO B 2 75  ? 157.129 154.812 188.549 1.00 101.43 ? 75   PRO B CD    1 
ATOM   7991  N  N     . ARG B 2 76  ? 155.282 156.996 191.048 1.00 100.19 ? 76   ARG B N     1 
ATOM   7992  C  CA    . ARG B 2 76  ? 154.485 157.993 191.751 1.00 100.92 ? 76   ARG B CA    1 
ATOM   7993  C  C     . ARG B 2 76  ? 153.198 157.395 192.299 1.00 100.68 ? 76   ARG B C     1 
ATOM   7994  O  O     . ARG B 2 76  ? 152.825 157.670 193.443 1.00 100.64 ? 76   ARG B O     1 
ATOM   7995  C  CB    . ARG B 2 76  ? 154.177 159.171 190.829 1.00 100.66 ? 76   ARG B CB    1 
ATOM   7996  C  CG    . ARG B 2 76  ? 153.368 160.265 191.495 1.00 99.82  ? 76   ARG B CG    1 
ATOM   7997  C  CD    . ARG B 2 76  ? 153.317 161.511 190.641 1.00 100.16 ? 76   ARG B CD    1 
ATOM   7998  N  NE    . ARG B 2 76  ? 152.487 162.545 191.246 1.00 100.99 ? 76   ARG B NE    1 
ATOM   7999  C  CZ    . ARG B 2 76  ? 152.233 163.721 190.690 1.00 101.08 ? 76   ARG B CZ    1 
ATOM   8000  N  NH1   . ARG B 2 76  ? 152.731 164.049 189.509 1.00 100.72 ? 76   ARG B NH1   1 
ATOM   8001  N  NH2   . ARG B 2 76  ? 151.457 164.588 191.333 1.00 100.87 ? 76   ARG B NH2   1 
ATOM   8002  N  N     . ILE B 2 77  ? 152.504 156.576 191.506 1.00 99.15  ? 77   ILE B N     1 
ATOM   8003  C  CA    . ILE B 2 77  ? 151.253 156.005 191.991 1.00 98.31  ? 77   ILE B CA    1 
ATOM   8004  C  C     . ILE B 2 77  ? 151.525 155.009 193.111 1.00 97.85  ? 77   ILE B C     1 
ATOM   8005  O  O     . ILE B 2 77  ? 150.782 154.957 194.097 1.00 97.92  ? 77   ILE B O     1 
ATOM   8006  C  CB    . ILE B 2 77  ? 150.436 155.386 190.839 1.00 97.65  ? 77   ILE B CB    1 
ATOM   8007  C  CG1   . ILE B 2 77  ? 149.120 154.815 191.365 1.00 97.39  ? 77   ILE B CG1   1 
ATOM   8008  C  CG2   . ILE B 2 77  ? 151.201 154.310 190.119 1.00 97.20  ? 77   ILE B CG2   1 
ATOM   8009  C  CD1   . ILE B 2 77  ? 148.377 153.996 190.352 1.00 98.07  ? 77   ILE B CD1   1 
ATOM   8010  N  N     . ILE B 2 78  ? 152.618 154.247 193.012 1.00 101.30 ? 78   ILE B N     1 
ATOM   8011  C  CA    . ILE B 2 78  ? 152.990 153.349 194.104 1.00 102.64 ? 78   ILE B CA    1 
ATOM   8012  C  C     . ILE B 2 78  ? 153.216 154.145 195.384 1.00 102.81 ? 78   ILE B C     1 
ATOM   8013  O  O     . ILE B 2 78  ? 152.540 153.927 196.397 1.00 102.20 ? 78   ILE B O     1 
ATOM   8014  C  CB    . ILE B 2 78  ? 154.233 152.523 193.732 1.00 102.07 ? 78   ILE B CB    1 
ATOM   8015  C  CG1   . ILE B 2 78  ? 153.886 151.488 192.663 1.00 102.59 ? 78   ILE B CG1   1 
ATOM   8016  C  CG2   . ILE B 2 78  ? 154.799 151.836 194.959 1.00 101.63 ? 78   ILE B CG2   1 
ATOM   8017  C  CD1   . ILE B 2 78  ? 152.875 150.471 193.112 1.00 101.28 ? 78   ILE B CD1   1 
ATOM   8018  N  N     . GLU B 2 79  ? 154.108 155.138 195.321 1.00 105.08 ? 79   GLU B N     1 
ATOM   8019  C  CA    . GLU B 2 79  ? 154.457 155.913 196.508 1.00 104.69 ? 79   GLU B CA    1 
ATOM   8020  C  C     . GLU B 2 79  ? 153.244 156.618 197.101 1.00 104.88 ? 79   GLU B C     1 
ATOM   8021  O  O     . GLU B 2 79  ? 153.050 156.610 198.321 1.00 104.50 ? 79   GLU B O     1 
ATOM   8022  C  CB    . GLU B 2 79  ? 155.541 156.931 196.159 1.00 104.83 ? 79   GLU B CB    1 
ATOM   8023  C  CG    . GLU B 2 79  ? 156.957 156.436 196.350 1.00 105.36 ? 79   GLU B CG    1 
ATOM   8024  C  CD    . GLU B 2 79  ? 157.487 156.731 197.736 1.00 107.08 ? 79   GLU B CD    1 
ATOM   8025  O  OE1   . GLU B 2 79  ? 156.703 157.198 198.587 1.00 107.03 ? 79   GLU B OE1   1 
ATOM   8026  O  OE2   . GLU B 2 79  ? 158.691 156.504 197.973 1.00 107.37 ? 79   GLU B OE2   1 
ATOM   8027  N  N     . GLU B 2 80  ? 152.410 157.224 196.257 1.00 103.54 ? 80   GLU B N     1 
ATOM   8028  C  CA    . GLU B 2 80  ? 151.305 158.024 196.762 1.00 103.19 ? 80   GLU B CA    1 
ATOM   8029  C  C     . GLU B 2 80  ? 150.142 157.178 197.260 1.00 102.54 ? 80   GLU B C     1 
ATOM   8030  O  O     . GLU B 2 80  ? 149.468 157.577 198.215 1.00 102.12 ? 80   GLU B O     1 
ATOM   8031  C  CB    . GLU B 2 80  ? 150.818 158.985 195.678 1.00 101.95 ? 80   GLU B CB    1 
ATOM   8032  C  CG    . GLU B 2 80  ? 150.877 160.446 196.079 1.00 102.42 ? 80   GLU B CG    1 
ATOM   8033  C  CD    . GLU B 2 80  ? 152.296 160.944 196.264 1.00 103.23 ? 80   GLU B CD    1 
ATOM   8034  O  OE1   . GLU B 2 80  ? 153.221 160.355 195.667 1.00 103.03 ? 80   GLU B OE1   1 
ATOM   8035  O  OE2   . GLU B 2 80  ? 152.487 161.928 197.009 1.00 103.76 ? 80   GLU B OE2   1 
ATOM   8036  N  N     . HIS B 2 81  ? 149.881 156.022 196.650 1.00 100.07 ? 81   HIS B N     1 
ATOM   8037  C  CA    . HIS B 2 81  ? 148.675 155.280 196.979 1.00 100.07 ? 81   HIS B CA    1 
ATOM   8038  C  C     . HIS B 2 81  ? 148.932 154.094 197.900 1.00 100.23 ? 81   HIS B C     1 
ATOM   8039  O  O     . HIS B 2 81  ? 148.212 153.925 198.887 1.00 99.53  ? 81   HIS B O     1 
ATOM   8040  C  CB    . HIS B 2 81  ? 147.986 154.812 195.693 1.00 99.59  ? 81   HIS B CB    1 
ATOM   8041  C  CG    . HIS B 2 81  ? 146.511 154.607 195.840 1.00 98.77  ? 81   HIS B CG    1 
ATOM   8042  N  ND1   . HIS B 2 81  ? 145.636 154.710 194.780 1.00 98.45  ? 81   HIS B ND1   1 
ATOM   8043  C  CD2   . HIS B 2 81  ? 145.756 154.304 196.922 1.00 98.18  ? 81   HIS B CD2   1 
ATOM   8044  C  CE1   . HIS B 2 81  ? 144.407 154.479 195.203 1.00 97.89  ? 81   HIS B CE1   1 
ATOM   8045  N  NE2   . HIS B 2 81  ? 144.452 154.229 196.499 1.00 97.61  ? 81   HIS B NE2   1 
ATOM   8046  N  N     . VAL B 2 82  ? 149.936 153.263 197.615 1.00 105.75 ? 82   VAL B N     1 
ATOM   8047  C  CA    . VAL B 2 82  ? 150.106 152.063 198.424 1.00 107.14 ? 82   VAL B CA    1 
ATOM   8048  C  C     . VAL B 2 82  ? 151.034 152.278 199.614 1.00 107.63 ? 82   VAL B C     1 
ATOM   8049  O  O     . VAL B 2 82  ? 151.027 151.461 200.546 1.00 108.31 ? 82   VAL B O     1 
ATOM   8050  C  CB    . VAL B 2 82  ? 150.601 150.884 197.566 1.00 107.11 ? 82   VAL B CB    1 
ATOM   8051  C  CG1   . VAL B 2 82  ? 149.868 150.859 196.236 1.00 105.72 ? 82   VAL B CG1   1 
ATOM   8052  C  CG2   . VAL B 2 82  ? 152.102 150.946 197.364 1.00 106.98 ? 82   VAL B CG2   1 
ATOM   8053  N  N     . ILE B 2 83  ? 151.817 153.351 199.622 1.00 108.93 ? 83   ILE B N     1 
ATOM   8054  C  CA    . ILE B 2 83  ? 152.734 153.641 200.718 1.00 109.10 ? 83   ILE B CA    1 
ATOM   8055  C  C     . ILE B 2 83  ? 152.170 154.700 201.654 1.00 108.52 ? 83   ILE B C     1 
ATOM   8056  O  O     . ILE B 2 83  ? 152.138 154.511 202.870 1.00 107.79 ? 83   ILE B O     1 
ATOM   8057  C  CB    . ILE B 2 83  ? 154.115 154.058 200.166 1.00 108.91 ? 83   ILE B CB    1 
ATOM   8058  C  CG1   . ILE B 2 83  ? 154.746 152.905 199.387 1.00 107.91 ? 83   ILE B CG1   1 
ATOM   8059  C  CG2   . ILE B 2 83  ? 155.030 154.495 201.294 1.00 108.51 ? 83   ILE B CG2   1 
ATOM   8060  C  CD1   . ILE B 2 83  ? 154.971 151.663 200.218 1.00 107.10 ? 83   ILE B CD1   1 
ATOM   8061  N  N     . ASN B 2 84  ? 151.715 155.823 201.104 1.00 109.19 ? 84   ASN B N     1 
ATOM   8062  C  CA    . ASN B 2 84  ? 151.168 156.898 201.921 1.00 109.29 ? 84   ASN B CA    1 
ATOM   8063  C  C     . ASN B 2 84  ? 149.657 156.797 202.080 1.00 108.77 ? 84   ASN B C     1 
ATOM   8064  O  O     . ASN B 2 84  ? 149.133 157.050 203.170 1.00 108.11 ? 84   ASN B O     1 
ATOM   8065  C  CB    . ASN B 2 84  ? 151.537 158.254 201.318 1.00 108.54 ? 84   ASN B CB    1 
ATOM   8066  C  CG    . ASN B 2 84  ? 153.030 158.448 201.203 1.00 109.35 ? 84   ASN B CG    1 
ATOM   8067  O  OD1   . ASN B 2 84  ? 153.689 158.865 202.154 1.00 108.28 ? 84   ASN B OD1   1 
ATOM   8068  N  ND2   . ASN B 2 84  ? 153.576 158.148 200.032 1.00 109.92 ? 84   ASN B ND2   1 
ATOM   8069  N  N     . GLY B 2 85  ? 148.945 156.429 201.020 1.00 108.49 ? 85   GLY B N     1 
ATOM   8070  C  CA    . GLY B 2 85  ? 147.503 156.322 201.091 1.00 108.08 ? 85   GLY B CA    1 
ATOM   8071  C  C     . GLY B 2 85  ? 146.775 157.579 200.663 1.00 109.56 ? 85   GLY B C     1 
ATOM   8072  O  O     . GLY B 2 85  ? 145.934 158.098 201.402 1.00 109.09 ? 85   GLY B O     1 
ATOM   8073  N  N     . LYS B 2 86  ? 147.094 158.083 199.475 1.00 108.72 ? 86   LYS B N     1 
ATOM   8074  C  CA    . LYS B 2 86  ? 146.409 159.243 198.920 1.00 107.47 ? 86   LYS B CA    1 
ATOM   8075  C  C     . LYS B 2 86  ? 146.079 159.003 197.452 1.00 107.01 ? 86   LYS B C     1 
ATOM   8076  O  O     . LYS B 2 86  ? 146.986 158.766 196.645 1.00 106.56 ? 86   LYS B O     1 
ATOM   8077  C  CB    . LYS B 2 86  ? 147.265 160.504 199.061 1.00 107.39 ? 86   LYS B CB    1 
ATOM   8078  C  CG    . LYS B 2 86  ? 147.578 160.901 200.493 1.00 107.90 ? 86   LYS B CG    1 
ATOM   8079  C  CD    . LYS B 2 86  ? 148.513 162.099 200.537 1.00 107.59 ? 86   LYS B CD    1 
ATOM   8080  C  CE    . LYS B 2 86  ? 148.856 162.481 201.966 1.00 107.69 ? 86   LYS B CE    1 
ATOM   8081  N  NZ    . LYS B 2 86  ? 149.779 163.648 202.021 1.00 107.81 ? 86   LYS B NZ    1 
ATOM   8082  N  N     . PRO B 2 87  ? 144.805 159.032 197.070 1.00 105.22 ? 87   PRO B N     1 
ATOM   8083  C  CA    . PRO B 2 87  ? 144.469 158.976 195.644 1.00 104.76 ? 87   PRO B CA    1 
ATOM   8084  C  C     . PRO B 2 87  ? 144.959 160.217 194.913 1.00 103.93 ? 87   PRO B C     1 
ATOM   8085  O  O     . PRO B 2 87  ? 144.900 161.332 195.434 1.00 103.34 ? 87   PRO B O     1 
ATOM   8086  C  CB    . PRO B 2 87  ? 142.938 158.893 195.640 1.00 104.16 ? 87   PRO B CB    1 
ATOM   8087  C  CG    . PRO B 2 87  ? 142.574 158.412 197.004 1.00 104.63 ? 87   PRO B CG    1 
ATOM   8088  C  CD    . PRO B 2 87  ? 143.606 158.984 197.921 1.00 104.58 ? 87   PRO B CD    1 
ATOM   8089  N  N     . ILE B 2 88  ? 145.447 160.011 193.693 1.00 97.64  ? 88   ILE B N     1 
ATOM   8090  C  CA    . ILE B 2 88  ? 145.870 161.113 192.828 1.00 97.33  ? 88   ILE B CA    1 
ATOM   8091  C  C     . ILE B 2 88  ? 144.674 161.421 191.934 1.00 97.09  ? 88   ILE B C     1 
ATOM   8092  O  O     . ILE B 2 88  ? 144.489 160.823 190.876 1.00 97.23  ? 88   ILE B O     1 
ATOM   8093  C  CB    . ILE B 2 88  ? 147.123 160.766 192.029 1.00 95.72  ? 88   ILE B CB    1 
ATOM   8094  C  CG1   . ILE B 2 88  ? 148.247 160.328 192.966 1.00 96.67  ? 88   ILE B CG1   1 
ATOM   8095  C  CG2   . ILE B 2 88  ? 147.570 161.954 191.198 1.00 95.76  ? 88   ILE B CG2   1 
ATOM   8096  C  CD1   . ILE B 2 88  ? 149.521 159.963 192.249 1.00 96.60  ? 88   ILE B CD1   1 
ATOM   8097  N  N     . GLU B 2 89  ? 143.853 162.381 192.370 1.00 95.64  ? 89   GLU B N     1 
ATOM   8098  C  CA    . GLU B 2 89  ? 142.569 162.631 191.724 1.00 95.27  ? 89   GLU B CA    1 
ATOM   8099  C  C     . GLU B 2 89  ? 142.708 163.091 190.280 1.00 95.18  ? 89   GLU B C     1 
ATOM   8100  O  O     . GLU B 2 89  ? 141.747 162.976 189.513 1.00 95.14  ? 89   GLU B O     1 
ATOM   8101  C  CB    . GLU B 2 89  ? 141.777 163.666 192.521 1.00 96.19  ? 89   GLU B CB    1 
ATOM   8102  C  CG    . GLU B 2 89  ? 141.217 163.140 193.830 1.00 96.93  ? 89   GLU B CG    1 
ATOM   8103  C  CD    . GLU B 2 89  ? 140.102 162.135 193.622 1.00 95.91  ? 89   GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 2 89  ? 139.455 162.173 192.555 1.00 94.99  ? 89   GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 2 89  ? 139.873 161.305 194.526 1.00 96.09  ? 89   GLU B OE2   1 
ATOM   8106  N  N     . ASP B 2 90  ? 143.870 163.616 189.893 1.00 94.37  ? 90   ASP B N     1 
ATOM   8107  C  CA    . ASP B 2 90  ? 144.068 164.009 188.504 1.00 95.18  ? 90   ASP B CA    1 
ATOM   8108  C  C     . ASP B 2 90  ? 144.035 162.800 187.575 1.00 94.50  ? 90   ASP B C     1 
ATOM   8109  O  O     . ASP B 2 90  ? 143.411 162.848 186.508 1.00 93.57  ? 90   ASP B O     1 
ATOM   8110  C  CB    . ASP B 2 90  ? 145.390 164.764 188.361 1.00 95.25  ? 90   ASP B CB    1 
ATOM   8111  C  CG    . ASP B 2 90  ? 145.532 165.447 187.014 1.00 95.53  ? 90   ASP B CG    1 
ATOM   8112  O  OD1   . ASP B 2 90  ? 144.530 165.525 186.272 1.00 96.08  ? 90   ASP B OD1   1 
ATOM   8113  O  OD2   . ASP B 2 90  ? 146.648 165.908 186.697 1.00 95.20  ? 90   ASP B OD2   1 
ATOM   8114  N  N     . TRP B 2 91  ? 144.687 161.708 187.965 1.00 93.28  ? 91   TRP B N     1 
ATOM   8115  C  CA    . TRP B 2 91  ? 144.820 160.533 187.113 1.00 92.12  ? 91   TRP B CA    1 
ATOM   8116  C  C     . TRP B 2 91  ? 143.733 159.495 187.347 1.00 90.41  ? 91   TRP B C     1 
ATOM   8117  O  O     . TRP B 2 91  ? 143.690 158.497 186.622 1.00 90.32  ? 91   TRP B O     1 
ATOM   8118  C  CB    . TRP B 2 91  ? 146.187 159.875 187.320 1.00 92.28  ? 91   TRP B CB    1 
ATOM   8119  C  CG    . TRP B 2 91  ? 147.349 160.774 187.063 1.00 92.02  ? 91   TRP B CG    1 
ATOM   8120  C  CD1   . TRP B 2 91  ? 147.327 161.999 186.468 1.00 92.23  ? 91   TRP B CD1   1 
ATOM   8121  C  CD2   . TRP B 2 91  ? 148.714 160.517 187.401 1.00 91.16  ? 91   TRP B CD2   1 
ATOM   8122  N  NE1   . TRP B 2 91  ? 148.593 162.522 186.415 1.00 93.10  ? 91   TRP B NE1   1 
ATOM   8123  C  CE2   . TRP B 2 91  ? 149.464 161.631 186.982 1.00 92.69  ? 91   TRP B CE2   1 
ATOM   8124  C  CE3   . TRP B 2 91  ? 149.375 159.453 188.017 1.00 91.52  ? 91   TRP B CE3   1 
ATOM   8125  C  CZ2   . TRP B 2 91  ? 150.841 161.709 187.157 1.00 93.04  ? 91   TRP B CZ2   1 
ATOM   8126  C  CZ3   . TRP B 2 91  ? 150.739 159.535 188.191 1.00 92.74  ? 91   TRP B CZ3   1 
ATOM   8127  C  CH2   . TRP B 2 91  ? 151.458 160.653 187.762 1.00 92.96  ? 91   TRP B CH2   1 
ATOM   8128  N  N     . VAL B 2 92  ? 142.868 159.694 188.338 1.00 85.00  ? 92   VAL B N     1 
ATOM   8129  C  CA    . VAL B 2 92  ? 141.786 158.748 188.589 1.00 83.10  ? 92   VAL B CA    1 
ATOM   8130  C  C     . VAL B 2 92  ? 140.760 158.900 187.472 1.00 85.13  ? 92   VAL B C     1 
ATOM   8131  O  O     . VAL B 2 92  ? 140.015 159.882 187.426 1.00 90.28  ? 92   VAL B O     1 
ATOM   8132  C  CB    . VAL B 2 92  ? 141.149 158.967 189.965 1.00 84.60  ? 92   VAL B CB    1 
ATOM   8133  C  CG1   . VAL B 2 92  ? 139.934 158.075 190.132 1.00 82.98  ? 92   VAL B CG1   1 
ATOM   8134  C  CG2   . VAL B 2 92  ? 142.155 158.684 191.056 1.00 86.24  ? 92   VAL B CG2   1 
ATOM   8135  N  N     . VAL B 2 93  ? 140.727 157.930 186.560 1.00 81.85  ? 93   VAL B N     1 
ATOM   8136  C  CA    . VAL B 2 93  ? 139.770 157.951 185.462 1.00 82.81  ? 93   VAL B CA    1 
ATOM   8137  C  C     . VAL B 2 93  ? 138.541 157.105 185.748 1.00 81.46  ? 93   VAL B C     1 
ATOM   8138  O  O     . VAL B 2 93  ? 137.565 157.173 184.984 1.00 82.01  ? 93   VAL B O     1 
ATOM   8139  C  CB    . VAL B 2 93  ? 140.430 157.492 184.146 1.00 82.18  ? 93   VAL B CB    1 
ATOM   8140  C  CG1   . VAL B 2 93  ? 141.681 158.308 183.881 1.00 83.91  ? 93   VAL B CG1   1 
ATOM   8141  C  CG2   . VAL B 2 93  ? 140.761 156.016 184.210 1.00 81.42  ? 93   VAL B CG2   1 
ATOM   8142  N  N     . LYS B 2 94  ? 138.547 156.326 186.825 1.00 77.04  ? 94   LYS B N     1 
ATOM   8143  C  CA    . LYS B 2 94  ? 137.448 155.418 187.117 1.00 76.30  ? 94   LYS B CA    1 
ATOM   8144  C  C     . LYS B 2 94  ? 137.503 155.045 188.589 1.00 77.81  ? 94   LYS B C     1 
ATOM   8145  O  O     . LYS B 2 94  ? 138.578 154.737 189.111 1.00 79.19  ? 94   LYS B O     1 
ATOM   8146  C  CB    . LYS B 2 94  ? 137.534 154.172 186.231 1.00 77.52  ? 94   LYS B CB    1 
ATOM   8147  C  CG    . LYS B 2 94  ? 136.496 153.110 186.500 1.00 77.55  ? 94   LYS B CG    1 
ATOM   8148  C  CD    . LYS B 2 94  ? 136.541 152.057 185.411 1.00 75.91  ? 94   LYS B CD    1 
ATOM   8149  C  CE    . LYS B 2 94  ? 135.698 150.855 185.763 1.00 76.26  ? 94   LYS B CE    1 
ATOM   8150  N  NZ    . LYS B 2 94  ? 136.295 150.085 186.885 1.00 78.46  ? 94   LYS B NZ    1 
ATOM   8151  N  N     . LYS B 2 95  ? 136.353 155.094 189.253 1.00 81.06  ? 95   LYS B N     1 
ATOM   8152  C  CA    . LYS B 2 95  ? 136.231 154.690 190.646 1.00 80.27  ? 95   LYS B CA    1 
ATOM   8153  C  C     . LYS B 2 95  ? 135.099 153.684 190.758 1.00 80.41  ? 95   LYS B C     1 
ATOM   8154  O  O     . LYS B 2 95  ? 134.004 153.915 190.236 1.00 82.38  ? 95   LYS B O     1 
ATOM   8155  C  CB    . LYS B 2 95  ? 135.973 155.891 191.558 1.00 81.01  ? 95   LYS B CB    1 
ATOM   8156  C  CG    . LYS B 2 95  ? 135.925 155.540 193.030 1.00 81.70  ? 95   LYS B CG    1 
ATOM   8157  C  CD    . LYS B 2 95  ? 135.792 156.781 193.887 1.00 83.74  ? 95   LYS B CD    1 
ATOM   8158  C  CE    . LYS B 2 95  ? 135.792 156.426 195.362 1.00 84.74  ? 95   LYS B CE    1 
ATOM   8159  N  NZ    . LYS B 2 95  ? 135.674 157.634 196.223 1.00 83.00  ? 95   LYS B NZ    1 
ATOM   8160  N  N     . ASP B 2 96  ? 135.363 152.574 191.439 1.00 83.71  ? 96   ASP B N     1 
ATOM   8161  C  CA    . ASP B 2 96  ? 134.429 151.460 191.517 1.00 83.48  ? 96   ASP B CA    1 
ATOM   8162  C  C     . ASP B 2 96  ? 134.267 151.059 192.975 1.00 85.35  ? 96   ASP B C     1 
ATOM   8163  O  O     . ASP B 2 96  ? 135.246 150.696 193.631 1.00 85.69  ? 96   ASP B O     1 
ATOM   8164  C  CB    . ASP B 2 96  ? 134.935 150.286 190.673 1.00 82.67  ? 96   ASP B CB    1 
ATOM   8165  C  CG    . ASP B 2 96  ? 133.902 149.202 190.495 1.00 85.03  ? 96   ASP B CG    1 
ATOM   8166  O  OD1   . ASP B 2 96  ? 133.455 148.622 191.506 1.00 86.51  ? 96   ASP B OD1   1 
ATOM   8167  O  OD2   . ASP B 2 96  ? 133.537 148.927 189.333 1.00 85.55  ? 96   ASP B OD2   1 
ATOM   8168  N  N     . TRP B 2 97  ? 133.037 151.126 193.478 1.00 87.81  ? 97   TRP B N     1 
ATOM   8169  C  CA    . TRP B 2 97  ? 132.726 150.722 194.842 1.00 88.42  ? 97   TRP B CA    1 
ATOM   8170  C  C     . TRP B 2 97  ? 131.467 149.868 194.819 1.00 89.50  ? 97   TRP B C     1 
ATOM   8171  O  O     . TRP B 2 97  ? 130.809 149.724 193.787 1.00 88.32  ? 97   TRP B O     1 
ATOM   8172  C  CB    . TRP B 2 97  ? 132.551 151.931 195.772 1.00 88.71  ? 97   TRP B CB    1 
ATOM   8173  C  CG    . TRP B 2 97  ? 131.403 152.809 195.402 1.00 88.68  ? 97   TRP B CG    1 
ATOM   8174  C  CD1   . TRP B 2 97  ? 130.112 152.691 195.823 1.00 89.30  ? 97   TRP B CD1   1 
ATOM   8175  C  CD2   . TRP B 2 97  ? 131.438 153.940 194.528 1.00 87.38  ? 97   TRP B CD2   1 
ATOM   8176  N  NE1   . TRP B 2 97  ? 129.340 153.676 195.263 1.00 89.41  ? 97   TRP B NE1   1 
ATOM   8177  C  CE2   . TRP B 2 97  ? 130.131 154.457 194.463 1.00 88.18  ? 97   TRP B CE2   1 
ATOM   8178  C  CE3   . TRP B 2 97  ? 132.446 154.563 193.790 1.00 87.51  ? 97   TRP B CE3   1 
ATOM   8179  C  CZ2   . TRP B 2 97  ? 129.809 155.568 193.695 1.00 89.73  ? 97   TRP B CZ2   1 
ATOM   8180  C  CZ3   . TRP B 2 97  ? 132.124 155.664 193.028 1.00 86.50  ? 97   TRP B CZ3   1 
ATOM   8181  C  CH2   . TRP B 2 97  ? 130.817 156.156 192.985 1.00 88.32  ? 97   TRP B CH2   1 
ATOM   8182  N  N     . TRP B 2 98  ? 131.134 149.296 195.972 1.00 91.84  ? 98   TRP B N     1 
ATOM   8183  C  CA    . TRP B 2 98  ? 130.009 148.380 196.094 1.00 92.07  ? 98   TRP B CA    1 
ATOM   8184  C  C     . TRP B 2 98  ? 128.930 148.987 196.978 1.00 88.98  ? 98   TRP B C     1 
ATOM   8185  O  O     . TRP B 2 98  ? 129.227 149.539 198.041 1.00 89.33  ? 98   TRP B O     1 
ATOM   8186  C  CB    . TRP B 2 98  ? 130.457 147.031 196.656 1.00 92.10  ? 98   TRP B CB    1 
ATOM   8187  C  CG    . TRP B 2 98  ? 131.179 146.191 195.660 1.00 90.96  ? 98   TRP B CG    1 
ATOM   8188  C  CD1   . TRP B 2 98  ? 130.632 145.285 194.803 1.00 90.21  ? 98   TRP B CD1   1 
ATOM   8189  C  CD2   . TRP B 2 98  ? 132.588 146.179 195.410 1.00 91.87  ? 98   TRP B CD2   1 
ATOM   8190  N  NE1   . TRP B 2 98  ? 131.611 144.709 194.034 1.00 91.20  ? 98   TRP B NE1   1 
ATOM   8191  C  CE2   . TRP B 2 98  ? 132.822 145.241 194.389 1.00 91.76  ? 98   TRP B CE2   1 
ATOM   8192  C  CE3   . TRP B 2 98  ? 133.674 146.868 195.954 1.00 91.36  ? 98   TRP B CE3   1 
ATOM   8193  C  CZ2   . TRP B 2 98  ? 134.097 144.976 193.900 1.00 90.73  ? 98   TRP B CZ2   1 
ATOM   8194  C  CZ3   . TRP B 2 98  ? 134.937 146.604 195.466 1.00 92.41  ? 98   TRP B CZ3   1 
ATOM   8195  C  CH2   . TRP B 2 98  ? 135.139 145.667 194.451 1.00 92.12  ? 98   TRP B CH2   1 
ATOM   8196  N  N     . GLU B 2 99  ? 127.681 148.877 196.533 1.00 95.98  ? 99   GLU B N     1 
ATOM   8197  C  CA    . GLU B 2 99  ? 126.526 149.376 197.271 1.00 99.08  ? 99   GLU B CA    1 
ATOM   8198  C  C     . GLU B 2 99  ? 125.459 148.292 197.287 1.00 100.16 ? 99   GLU B C     1 
ATOM   8199  O  O     . GLU B 2 99  ? 124.816 148.037 196.264 1.00 98.09  ? 99   GLU B O     1 
ATOM   8200  C  CB    . GLU B 2 99  ? 125.986 150.661 196.646 1.00 100.10 ? 99   GLU B CB    1 
ATOM   8201  C  CG    . GLU B 2 99  ? 124.738 151.193 197.323 1.00 99.98  ? 99   GLU B CG    1 
ATOM   8202  C  CD    . GLU B 2 99  ? 124.226 152.461 196.680 1.00 99.80  ? 99   GLU B CD    1 
ATOM   8203  O  OE1   . GLU B 2 99  ? 124.894 152.971 195.758 1.00 99.79  ? 99   GLU B OE1   1 
ATOM   8204  O  OE2   . GLU B 2 99  ? 123.155 152.948 197.097 1.00 99.23  ? 99   GLU B OE2   1 
ATOM   8205  N  N     . ASN B 2 100 ? 125.276 147.663 198.450 1.00 111.15 ? 100  ASN B N     1 
ATOM   8206  C  CA    . ASN B 2 100 ? 124.242 146.648 198.664 1.00 111.21 ? 100  ASN B CA    1 
ATOM   8207  C  C     . ASN B 2 100 ? 124.371 145.486 197.682 1.00 110.12 ? 100  ASN B C     1 
ATOM   8208  O  O     . ASN B 2 100 ? 123.385 145.028 197.101 1.00 109.09 ? 100  ASN B O     1 
ATOM   8209  C  CB    . ASN B 2 100 ? 122.843 147.264 198.598 1.00 112.15 ? 100  ASN B CB    1 
ATOM   8210  C  CG    . ASN B 2 100 ? 122.652 148.378 199.606 1.00 111.75 ? 100  ASN B CG    1 
ATOM   8211  O  OD1   . ASN B 2 100 ? 122.296 149.501 199.248 1.00 112.19 ? 100  ASN B OD1   1 
ATOM   8212  N  ND2   . ASN B 2 100 ? 122.892 148.075 200.876 1.00 110.03 ? 100  ASN B ND2   1 
ATOM   8213  N  N     . GLY B 2 101 ? 125.597 145.007 197.492 1.00 112.02 ? 101  GLY B N     1 
ATOM   8214  C  CA    . GLY B 2 101 ? 125.843 143.844 196.668 1.00 112.47 ? 101  GLY B CA    1 
ATOM   8215  C  C     . GLY B 2 101 ? 125.991 144.109 195.187 1.00 113.16 ? 101  GLY B C     1 
ATOM   8216  O  O     . GLY B 2 101 ? 126.282 143.171 194.435 1.00 112.95 ? 101  GLY B O     1 
ATOM   8217  N  N     . GLN B 2 102 ? 125.798 145.345 194.739 1.00 100.59 ? 102  GLN B N     1 
ATOM   8218  C  CA    . GLN B 2 102 ? 125.972 145.701 193.343 1.00 98.52  ? 102  GLN B CA    1 
ATOM   8219  C  C     . GLN B 2 102 ? 127.294 146.438 193.159 1.00 96.86  ? 102  GLN B C     1 
ATOM   8220  O  O     . GLN B 2 102 ? 128.034 146.693 194.110 1.00 97.38  ? 102  GLN B O     1 
ATOM   8221  C  CB    . GLN B 2 102 ? 124.798 146.549 192.852 1.00 98.61  ? 102  GLN B CB    1 
ATOM   8222  C  CG    . GLN B 2 102 ? 123.472 145.818 192.828 1.00 99.34  ? 102  GLN B CG    1 
ATOM   8223  C  CD    . GLN B 2 102 ? 122.371 146.648 192.205 1.00 98.98  ? 102  GLN B CD    1 
ATOM   8224  O  OE1   . GLN B 2 102 ? 122.607 147.762 191.738 1.00 98.92  ? 102  GLN B OE1   1 
ATOM   8225  N  NE2   . GLN B 2 102 ? 121.157 146.110 192.193 1.00 99.15  ? 102  GLN B NE2   1 
ATOM   8226  N  N     . ARG B 2 103 ? 127.589 146.791 191.912 1.00 84.29  ? 103  ARG B N     1 
ATOM   8227  C  CA    . ARG B 2 103 ? 128.835 147.457 191.557 1.00 84.72  ? 103  ARG B CA    1 
ATOM   8228  C  C     . ARG B 2 103 ? 128.521 148.838 191.003 1.00 84.60  ? 103  ARG B C     1 
ATOM   8229  O  O     . ARG B 2 103 ? 127.812 148.963 190.000 1.00 83.99  ? 103  ARG B O     1 
ATOM   8230  C  CB    . ARG B 2 103 ? 129.614 146.627 190.539 1.00 84.46  ? 103  ARG B CB    1 
ATOM   8231  C  CG    . ARG B 2 103 ? 130.959 147.195 190.171 1.00 82.98  ? 103  ARG B CG    1 
ATOM   8232  C  CD    . ARG B 2 103 ? 131.692 146.226 189.279 1.00 83.82  ? 103  ARG B CD    1 
ATOM   8233  N  NE    . ARG B 2 103 ? 130.861 145.827 188.152 1.00 85.36  ? 103  ARG B NE    1 
ATOM   8234  C  CZ    . ARG B 2 103 ? 131.005 144.694 187.481 1.00 84.48  ? 103  ARG B CZ    1 
ATOM   8235  N  NH1   . ARG B 2 103 ? 131.933 143.811 187.808 1.00 83.68  ? 103  ARG B NH1   1 
ATOM   8236  N  NH2   . ARG B 2 103 ? 130.193 144.439 186.460 1.00 81.23  ? 103  ARG B NH2   1 
ATOM   8237  N  N     . LYS B 2 104 ? 129.056 149.868 191.650 1.00 85.58  ? 104  LYS B N     1 
ATOM   8238  C  CA    . LYS B 2 104 ? 128.804 151.254 191.282 1.00 82.34  ? 104  LYS B CA    1 
ATOM   8239  C  C     . LYS B 2 104 ? 130.071 151.856 190.697 1.00 82.62  ? 104  LYS B C     1 
ATOM   8240  O  O     . LYS B 2 104 ? 131.148 151.740 191.289 1.00 83.96  ? 104  LYS B O     1 
ATOM   8241  C  CB    . LYS B 2 104 ? 128.340 152.066 192.492 1.00 83.41  ? 104  LYS B CB    1 
ATOM   8242  C  CG    . LYS B 2 104 ? 127.120 151.488 193.182 1.00 84.57  ? 104  LYS B CG    1 
ATOM   8243  C  CD    . LYS B 2 104 ? 125.985 151.270 192.195 1.00 84.13  ? 104  LYS B CD    1 
ATOM   8244  C  CE    . LYS B 2 104 ? 124.805 150.577 192.853 1.00 84.80  ? 104  LYS B CE    1 
ATOM   8245  N  NZ    . LYS B 2 104 ? 123.708 150.317 191.882 1.00 84.07  ? 104  LYS B NZ    1 
ATOM   8246  N  N     . THR B 2 105 ? 129.939 152.497 189.541 1.00 79.30  ? 105  THR B N     1 
ATOM   8247  C  CA    . THR B 2 105 ? 131.073 153.050 188.818 1.00 81.36  ? 105  THR B CA    1 
ATOM   8248  C  C     . THR B 2 105 ? 130.887 154.548 188.630 1.00 78.66  ? 105  THR B C     1 
ATOM   8249  O  O     . THR B 2 105 ? 129.804 155.003 188.250 1.00 80.06  ? 105  THR B O     1 
ATOM   8250  C  CB    . THR B 2 105 ? 131.249 152.360 187.462 1.00 81.48  ? 105  THR B CB    1 
ATOM   8251  O  OG1   . THR B 2 105 ? 132.050 153.181 186.604 1.00 78.79  ? 105  THR B OG1   1 
ATOM   8252  C  CG2   . THR B 2 105 ? 129.902 152.103 186.810 1.00 81.38  ? 105  THR B CG2   1 
ATOM   8253  N  N     . TRP B 2 106 ? 131.941 155.306 188.911 1.00 75.61  ? 106  TRP B N     1 
ATOM   8254  C  CA    . TRP B 2 106 ? 132.002 156.727 188.608 1.00 76.86  ? 106  TRP B CA    1 
ATOM   8255  C  C     . TRP B 2 106 ? 133.092 156.946 187.574 1.00 76.82  ? 106  TRP B C     1 
ATOM   8256  O  O     . TRP B 2 106 ? 134.224 156.485 187.755 1.00 77.89  ? 106  TRP B O     1 
ATOM   8257  C  CB    . TRP B 2 106 ? 132.283 157.561 189.859 1.00 77.87  ? 106  TRP B CB    1 
ATOM   8258  C  CG    . TRP B 2 106 ? 132.608 158.983 189.544 1.00 77.03  ? 106  TRP B CG    1 
ATOM   8259  C  CD1   . TRP B 2 106 ? 131.726 160.011 189.401 1.00 76.07  ? 106  TRP B CD1   1 
ATOM   8260  C  CD2   . TRP B 2 106 ? 133.910 159.537 189.318 1.00 76.35  ? 106  TRP B CD2   1 
ATOM   8261  N  NE1   . TRP B 2 106 ? 132.397 161.171 189.103 1.00 78.29  ? 106  TRP B NE1   1 
ATOM   8262  C  CE2   . TRP B 2 106 ? 133.739 160.905 189.044 1.00 78.91  ? 106  TRP B CE2   1 
ATOM   8263  C  CE3   . TRP B 2 106 ? 135.203 159.006 189.317 1.00 75.44  ? 106  TRP B CE3   1 
ATOM   8264  C  CZ2   . TRP B 2 106 ? 134.811 161.750 188.777 1.00 78.20  ? 106  TRP B CZ2   1 
ATOM   8265  C  CZ3   . TRP B 2 106 ? 136.264 159.846 189.050 1.00 74.10  ? 106  TRP B CZ3   1 
ATOM   8266  C  CH2   . TRP B 2 106 ? 136.063 161.202 188.784 1.00 75.81  ? 106  TRP B CH2   1 
ATOM   8267  N  N     . ASP B 2 107 ? 132.756 157.647 186.497 1.00 73.39  ? 107  ASP B N     1 
ATOM   8268  C  CA    . ASP B 2 107 ? 133.677 157.870 185.395 1.00 69.93  ? 107  ASP B CA    1 
ATOM   8269  C  C     . ASP B 2 107 ? 133.945 159.358 185.231 1.00 73.37  ? 107  ASP B C     1 
ATOM   8270  O  O     . ASP B 2 107 ? 133.030 160.181 185.328 1.00 72.55  ? 107  ASP B O     1 
ATOM   8271  C  CB    . ASP B 2 107 ? 133.127 157.294 184.094 1.00 70.62  ? 107  ASP B CB    1 
ATOM   8272  C  CG    . ASP B 2 107 ? 134.132 157.349 182.969 1.00 71.72  ? 107  ASP B CG    1 
ATOM   8273  O  OD1   . ASP B 2 107 ? 135.117 156.584 183.016 1.00 73.87  ? 107  ASP B OD1   1 
ATOM   8274  O  OD2   . ASP B 2 107 ? 133.942 158.160 182.039 1.00 73.09  ? 107  ASP B OD2   1 
ATOM   8275  N  N     . PHE B 2 108 ? 135.213 159.692 184.985 1.00 76.51  ? 108  PHE B N     1 
ATOM   8276  C  CA    . PHE B 2 108 ? 135.597 161.086 184.792 1.00 75.58  ? 108  PHE B CA    1 
ATOM   8277  C  C     . PHE B 2 108 ? 134.960 161.665 183.536 1.00 74.76  ? 108  PHE B C     1 
ATOM   8278  O  O     . PHE B 2 108 ? 134.538 162.827 183.522 1.00 75.13  ? 108  PHE B O     1 
ATOM   8279  C  CB    . PHE B 2 108 ? 137.120 161.195 184.724 1.00 74.43  ? 108  PHE B CB    1 
ATOM   8280  C  CG    . PHE B 2 108 ? 137.634 162.602 184.772 1.00 77.16  ? 108  PHE B CG    1 
ATOM   8281  C  CD1   . PHE B 2 108 ? 137.825 163.240 185.984 1.00 77.41  ? 108  PHE B CD1   1 
ATOM   8282  C  CD2   . PHE B 2 108 ? 137.941 163.283 183.607 1.00 76.61  ? 108  PHE B CD2   1 
ATOM   8283  C  CE1   . PHE B 2 108 ? 138.302 164.535 186.034 1.00 76.30  ? 108  PHE B CE1   1 
ATOM   8284  C  CE2   . PHE B 2 108 ? 138.419 164.578 183.650 1.00 76.61  ? 108  PHE B CE2   1 
ATOM   8285  C  CZ    . PHE B 2 108 ? 138.600 165.204 184.865 1.00 77.31  ? 108  PHE B CZ    1 
ATOM   8286  N  N     . ASP B 2 109 ? 134.880 160.870 182.474 1.00 71.22  ? 109  ASP B N     1 
ATOM   8287  C  CA    . ASP B 2 109 ? 134.389 161.326 181.184 1.00 68.77  ? 109  ASP B CA    1 
ATOM   8288  C  C     . ASP B 2 109 ? 132.931 160.958 180.937 1.00 69.09  ? 109  ASP B C     1 
ATOM   8289  O  O     . ASP B 2 109 ? 132.429 161.178 179.832 1.00 72.33  ? 109  ASP B O     1 
ATOM   8290  C  CB    . ASP B 2 109 ? 135.267 160.756 180.071 1.00 69.39  ? 109  ASP B CB    1 
ATOM   8291  C  CG    . ASP B 2 109 ? 136.743 160.934 180.351 1.00 70.17  ? 109  ASP B CG    1 
ATOM   8292  O  OD1   . ASP B 2 109 ? 137.141 162.043 180.759 1.00 70.13  ? 109  ASP B OD1   1 
ATOM   8293  O  OD2   . ASP B 2 109 ? 137.506 159.962 180.174 1.00 71.28  ? 109  ASP B OD2   1 
ATOM   8294  N  N     . GLY B 2 110 ? 132.241 160.409 181.934 1.00 66.31  ? 110  GLY B N     1 
ATOM   8295  C  CA    . GLY B 2 110 ? 130.858 160.019 181.745 1.00 64.20  ? 110  GLY B CA    1 
ATOM   8296  C  C     . GLY B 2 110 ? 130.662 158.850 180.812 1.00 65.80  ? 110  GLY B C     1 
ATOM   8297  O  O     . GLY B 2 110 ? 129.599 158.724 180.202 1.00 67.43  ? 110  GLY B O     1 
ATOM   8298  N  N     . TYR B 2 111 ? 131.670 157.987 180.684 1.00 62.19  ? 111  TYR B N     1 
ATOM   8299  C  CA    . TYR B 2 111 ? 131.619 156.899 179.714 1.00 59.00  ? 111  TYR B CA    1 
ATOM   8300  C  C     . TYR B 2 111 ? 130.581 155.849 180.094 1.00 57.66  ? 111  TYR B C     1 
ATOM   8301  O  O     . TYR B 2 111 ? 129.904 155.295 179.222 1.00 57.71  ? 111  TYR B O     1 
ATOM   8302  C  CB    . TYR B 2 111 ? 133.004 156.264 179.596 1.00 58.41  ? 111  TYR B CB    1 
ATOM   8303  C  CG    . TYR B 2 111 ? 133.232 155.464 178.339 1.00 60.95  ? 111  TYR B CG    1 
ATOM   8304  C  CD1   . TYR B 2 111 ? 132.394 155.594 177.243 1.00 60.94  ? 111  TYR B CD1   1 
ATOM   8305  C  CD2   . TYR B 2 111 ? 134.290 154.573 178.251 1.00 60.62  ? 111  TYR B CD2   1 
ATOM   8306  C  CE1   . TYR B 2 111 ? 132.607 154.861 176.094 1.00 57.68  ? 111  TYR B CE1   1 
ATOM   8307  C  CE2   . TYR B 2 111 ? 134.509 153.836 177.111 1.00 59.88  ? 111  TYR B CE2   1 
ATOM   8308  C  CZ    . TYR B 2 111 ? 133.666 153.982 176.035 1.00 59.02  ? 111  TYR B CZ    1 
ATOM   8309  O  OH    . TYR B 2 111 ? 133.890 153.246 174.897 1.00 60.02  ? 111  TYR B OH    1 
ATOM   8310  N  N     . PHE B 2 112 ? 130.440 155.564 181.386 1.00 60.27  ? 112  PHE B N     1 
ATOM   8311  C  CA    . PHE B 2 112 ? 129.678 154.417 181.860 1.00 60.34  ? 112  PHE B CA    1 
ATOM   8312  C  C     . PHE B 2 112 ? 128.250 154.760 182.265 1.00 63.41  ? 112  PHE B C     1 
ATOM   8313  O  O     . PHE B 2 112 ? 127.550 153.893 182.795 1.00 66.04  ? 112  PHE B O     1 
ATOM   8314  C  CB    . PHE B 2 112 ? 130.396 153.765 183.041 1.00 59.88  ? 112  PHE B CB    1 
ATOM   8315  C  CG    . PHE B 2 112 ? 131.758 153.239 182.708 1.00 61.81  ? 112  PHE B CG    1 
ATOM   8316  C  CD1   . PHE B 2 112 ? 131.916 151.964 182.201 1.00 64.51  ? 112  PHE B CD1   1 
ATOM   8317  C  CD2   . PHE B 2 112 ? 132.883 154.017 182.910 1.00 58.53  ? 112  PHE B CD2   1 
ATOM   8318  C  CE1   . PHE B 2 112 ? 133.167 151.478 181.897 1.00 63.76  ? 112  PHE B CE1   1 
ATOM   8319  C  CE2   . PHE B 2 112 ? 134.136 153.535 182.606 1.00 59.84  ? 112  PHE B CE2   1 
ATOM   8320  C  CZ    . PHE B 2 112 ? 134.277 152.265 182.101 1.00 63.92  ? 112  PHE B CZ    1 
ATOM   8321  N  N     . VAL B 2 113 ? 127.805 155.997 182.040 1.00 63.40  ? 113  VAL B N     1 
ATOM   8322  C  CA    . VAL B 2 113 ? 126.510 156.428 182.560 1.00 63.58  ? 113  VAL B CA    1 
ATOM   8323  C  C     . VAL B 2 113 ? 125.371 155.649 181.911 1.00 59.30  ? 113  VAL B C     1 
ATOM   8324  O  O     . VAL B 2 113 ? 124.432 155.216 182.589 1.00 57.26  ? 113  VAL B O     1 
ATOM   8325  C  CB    . VAL B 2 113 ? 126.342 157.945 182.374 1.00 62.92  ? 113  VAL B CB    1 
ATOM   8326  C  CG1   . VAL B 2 113 ? 125.008 158.403 182.931 1.00 59.56  ? 113  VAL B CG1   1 
ATOM   8327  C  CG2   . VAL B 2 113 ? 127.482 158.681 183.050 1.00 63.92  ? 113  VAL B CG2   1 
ATOM   8328  N  N     . LYS B 2 114 ? 125.429 155.456 180.597 1.00 57.87  ? 114  LYS B N     1 
ATOM   8329  C  CA    . LYS B 2 114 ? 124.378 154.755 179.875 1.00 60.20  ? 114  LYS B CA    1 
ATOM   8330  C  C     . LYS B 2 114 ? 124.765 153.329 179.502 1.00 55.29  ? 114  LYS B C     1 
ATOM   8331  O  O     . LYS B 2 114 ? 124.033 152.677 178.753 1.00 50.72  ? 114  LYS B O     1 
ATOM   8332  C  CB    . LYS B 2 114 ? 123.991 155.539 178.620 1.00 58.47  ? 114  LYS B CB    1 
ATOM   8333  C  CG    . LYS B 2 114 ? 123.730 157.016 178.872 1.00 55.44  ? 114  LYS B CG    1 
ATOM   8334  C  CD    . LYS B 2 114 ? 122.479 157.481 178.157 1.00 56.79  ? 114  LYS B CD    1 
ATOM   8335  C  CE    . LYS B 2 114 ? 121.263 156.716 178.648 1.00 57.55  ? 114  LYS B CE    1 
ATOM   8336  N  NZ    . LYS B 2 114 ? 120.020 157.122 177.940 1.00 58.17  ? 114  LYS B NZ    1 
ATOM   8337  N  N     . GLN B 2 115 ? 125.890 152.832 180.007 1.00 54.47  ? 115  GLN B N     1 
ATOM   8338  C  CA    . GLN B 2 115 ? 126.351 151.489 179.688 1.00 52.84  ? 115  GLN B CA    1 
ATOM   8339  C  C     . GLN B 2 115 ? 125.746 150.469 180.643 1.00 55.39  ? 115  GLN B C     1 
ATOM   8340  O  O     . GLN B 2 115 ? 125.624 150.717 181.845 1.00 55.06  ? 115  GLN B O     1 
ATOM   8341  C  CB    . GLN B 2 115 ? 127.878 151.407 179.751 1.00 46.79  ? 115  GLN B CB    1 
ATOM   8342  C  CG    . GLN B 2 115 ? 128.606 152.256 178.729 1.00 49.17  ? 115  GLN B CG    1 
ATOM   8343  C  CD    . GLN B 2 115 ? 130.094 151.971 178.694 1.00 49.14  ? 115  GLN B CD    1 
ATOM   8344  O  OE1   . GLN B 2 115 ? 130.576 151.042 179.338 1.00 49.06  ? 115  GLN B OE1   1 
ATOM   8345  N  NE2   . GLN B 2 115 ? 130.831 152.771 177.936 1.00 48.86  ? 115  GLN B NE2   1 
ATOM   8346  N  N     . LYS B 2 116 ? 125.374 149.315 180.097 1.00 45.36  ? 116  LYS B N     1 
ATOM   8347  C  CA    . LYS B 2 116 ? 124.878 148.185 180.879 1.00 46.93  ? 116  LYS B CA    1 
ATOM   8348  C  C     . LYS B 2 116 ? 125.744 146.979 180.532 1.00 45.92  ? 116  LYS B C     1 
ATOM   8349  O  O     . LYS B 2 116 ? 125.552 146.356 179.485 1.00 46.67  ? 116  LYS B O     1 
ATOM   8350  C  CB    . LYS B 2 116 ? 123.407 147.914 180.590 1.00 49.38  ? 116  LYS B CB    1 
ATOM   8351  C  CG    . LYS B 2 116 ? 122.845 146.725 181.340 1.00 52.28  ? 116  LYS B CG    1 
ATOM   8352  C  CD    . LYS B 2 116 ? 122.959 146.919 182.842 1.00 49.92  ? 116  LYS B CD    1 
ATOM   8353  C  CE    . LYS B 2 116 ? 122.381 145.733 183.597 1.00 48.73  ? 116  LYS B CE    1 
ATOM   8354  N  NZ    . LYS B 2 116 ? 122.486 145.910 185.071 1.00 49.25  ? 116  LYS B NZ    1 
ATOM   8355  N  N     . LYS B 2 117 ? 126.688 146.648 181.407 1.00 41.26  ? 117  LYS B N     1 
ATOM   8356  C  CA    . LYS B 2 117 ? 127.658 145.591 181.139 1.00 45.48  ? 117  LYS B CA    1 
ATOM   8357  C  C     . LYS B 2 117 ? 127.063 144.240 181.519 1.00 45.35  ? 117  LYS B C     1 
ATOM   8358  O  O     . LYS B 2 117 ? 126.934 143.919 182.704 1.00 42.44  ? 117  LYS B O     1 
ATOM   8359  C  CB    . LYS B 2 117 ? 128.959 145.849 181.893 1.00 45.82  ? 117  LYS B CB    1 
ATOM   8360  C  CG    . LYS B 2 117 ? 129.839 146.904 181.254 1.00 40.04  ? 117  LYS B CG    1 
ATOM   8361  C  CD    . LYS B 2 117 ? 131.208 146.932 181.900 1.00 43.16  ? 117  LYS B CD    1 
ATOM   8362  C  CE    . LYS B 2 117 ? 132.128 147.904 181.195 1.00 43.56  ? 117  LYS B CE    1 
ATOM   8363  N  NZ    . LYS B 2 117 ? 133.478 147.915 181.813 1.00 48.29  ? 117  LYS B NZ    1 
ATOM   8364  N  N     . ILE B 2 118 ? 126.707 143.452 180.508 1.00 41.19  ? 118  ILE B N     1 
ATOM   8365  C  CA    . ILE B 2 118 ? 126.231 142.084 180.690 1.00 36.31  ? 118  ILE B CA    1 
ATOM   8366  C  C     . ILE B 2 118 ? 127.291 141.078 180.254 1.00 41.71  ? 118  ILE B C     1 
ATOM   8367  O  O     . ILE B 2 118 ? 127.675 140.194 181.020 1.00 46.07  ? 118  ILE B O     1 
ATOM   8368  C  CB    . ILE B 2 118 ? 124.901 141.856 179.938 1.00 39.89  ? 118  ILE B CB    1 
ATOM   8369  C  CG1   . ILE B 2 118 ? 123.783 142.685 180.566 1.00 44.25  ? 118  ILE B CG1   1 
ATOM   8370  C  CG2   . ILE B 2 118 ? 124.538 140.382 179.913 1.00 39.20  ? 118  ILE B CG2   1 
ATOM   8371  C  CD1   . ILE B 2 118 ? 122.436 142.441 179.945 1.00 44.69  ? 118  ILE B CD1   1 
ATOM   8372  N  N     . VAL B 2 119 ? 127.768 141.195 179.016 1.00 38.18  ? 119  VAL B N     1 
ATOM   8373  C  CA    . VAL B 2 119 ? 128.839 140.331 178.533 1.00 40.60  ? 119  VAL B CA    1 
ATOM   8374  C  C     . VAL B 2 119 ? 130.160 140.685 179.205 1.00 39.61  ? 119  VAL B C     1 
ATOM   8375  O  O     . VAL B 2 119 ? 130.958 139.803 179.541 1.00 39.28  ? 119  VAL B O     1 
ATOM   8376  C  CB    . VAL B 2 119 ? 128.931 140.431 176.999 1.00 39.21  ? 119  VAL B CB    1 
ATOM   8377  C  CG1   . VAL B 2 119 ? 130.140 139.693 176.474 1.00 37.18  ? 119  VAL B CG1   1 
ATOM   8378  C  CG2   . VAL B 2 119 ? 127.662 139.902 176.363 1.00 39.59  ? 119  VAL B CG2   1 
ATOM   8379  N  N     . LEU B 2 120 ? 130.406 141.974 179.426 1.00 46.71  ? 120  LEU B N     1 
ATOM   8380  C  CA    . LEU B 2 120 ? 131.706 142.464 179.866 1.00 45.38  ? 120  LEU B CA    1 
ATOM   8381  C  C     . LEU B 2 120 ? 131.709 142.890 181.331 1.00 49.29  ? 120  LEU B C     1 
ATOM   8382  O  O     . LEU B 2 120 ? 132.475 143.774 181.718 1.00 52.39  ? 120  LEU B O     1 
ATOM   8383  C  CB    . LEU B 2 120 ? 132.152 143.627 178.983 1.00 46.33  ? 120  LEU B CB    1 
ATOM   8384  C  CG    . LEU B 2 120 ? 132.134 143.401 177.473 1.00 45.62  ? 120  LEU B CG    1 
ATOM   8385  C  CD1   . LEU B 2 120 ? 132.484 144.685 176.748 1.00 45.19  ? 120  LEU B CD1   1 
ATOM   8386  C  CD2   . LEU B 2 120 ? 133.091 142.290 177.086 1.00 47.08  ? 120  LEU B CD2   1 
ATOM   8387  N  N     . GLU B 2 121 ? 130.866 142.272 182.160 1.00 48.04  ? 121  GLU B N     1 
ATOM   8388  C  CA    . GLU B 2 121 ? 130.774 142.697 183.554 1.00 47.79  ? 121  GLU B CA    1 
ATOM   8389  C  C     . GLU B 2 121 ? 132.024 142.322 184.343 1.00 51.67  ? 121  GLU B C     1 
ATOM   8390  O  O     . GLU B 2 121 ? 132.460 143.079 185.217 1.00 57.54  ? 121  GLU B O     1 
ATOM   8391  C  CB    . GLU B 2 121 ? 129.522 142.109 184.205 1.00 48.86  ? 121  GLU B CB    1 
ATOM   8392  C  CG    . GLU B 2 121 ? 129.391 140.610 184.078 1.00 52.33  ? 121  GLU B CG    1 
ATOM   8393  C  CD    . GLU B 2 121 ? 128.161 140.074 184.780 1.00 54.19  ? 121  GLU B CD    1 
ATOM   8394  O  OE1   . GLU B 2 121 ? 127.448 140.870 185.424 1.00 52.17  ? 121  GLU B OE1   1 
ATOM   8395  O  OE2   . GLU B 2 121 ? 127.907 138.855 184.688 1.00 50.35  ? 121  GLU B OE2   1 
ATOM   8396  N  N     . ASN B 2 122 ? 132.615 141.165 184.055 1.00 49.57  ? 122  ASN B N     1 
ATOM   8397  C  CA    . ASN B 2 122 ? 133.792 140.709 184.783 1.00 47.46  ? 122  ASN B CA    1 
ATOM   8398  C  C     . ASN B 2 122 ? 135.106 141.111 184.129 1.00 50.12  ? 122  ASN B C     1 
ATOM   8399  O  O     . ASN B 2 122 ? 136.165 140.878 184.720 1.00 49.97  ? 122  ASN B O     1 
ATOM   8400  C  CB    . ASN B 2 122 ? 133.763 139.186 184.941 1.00 50.69  ? 122  ASN B CB    1 
ATOM   8401  C  CG    . ASN B 2 122 ? 132.711 138.723 185.919 1.00 51.93  ? 122  ASN B CG    1 
ATOM   8402  O  OD1   . ASN B 2 122 ? 132.302 139.468 186.808 1.00 50.63  ? 122  ASN B OD1   1 
ATOM   8403  N  ND2   . ASN B 2 122 ? 132.270 137.481 185.766 1.00 52.22  ? 122  ASN B ND2   1 
ATOM   8404  N  N     . SER B 2 123 ? 135.070 141.695 182.935 1.00 54.87  ? 123  SER B N     1 
ATOM   8405  C  CA    . SER B 2 123 ? 136.298 142.094 182.261 1.00 54.46  ? 123  SER B CA    1 
ATOM   8406  C  C     . SER B 2 123 ? 136.938 143.267 182.988 1.00 57.91  ? 123  SER B C     1 
ATOM   8407  O  O     . SER B 2 123 ? 136.274 144.263 183.288 1.00 63.59  ? 123  SER B O     1 
ATOM   8408  C  CB    . SER B 2 123 ? 136.012 142.462 180.808 1.00 55.53  ? 123  SER B CB    1 
ATOM   8409  O  OG    . SER B 2 123 ? 135.570 141.335 180.075 1.00 59.56  ? 123  SER B OG    1 
ATOM   8410  N  N     . GLY B 2 124 ? 138.234 143.152 183.263 1.00 64.49  ? 124  GLY B N     1 
ATOM   8411  C  CA    . GLY B 2 124 ? 138.945 144.173 183.998 1.00 67.44  ? 124  GLY B CA    1 
ATOM   8412  C  C     . GLY B 2 124 ? 138.829 144.080 185.502 1.00 64.74  ? 124  GLY B C     1 
ATOM   8413  O  O     . GLY B 2 124 ? 139.401 144.926 186.201 1.00 66.36  ? 124  GLY B O     1 
ATOM   8414  N  N     . TYR B 2 125 ? 138.110 143.087 186.026 1.00 66.24  ? 125  TYR B N     1 
ATOM   8415  C  CA    . TYR B 2 125 ? 137.980 142.897 187.462 1.00 67.71  ? 125  TYR B CA    1 
ATOM   8416  C  C     . TYR B 2 125 ? 138.470 141.544 187.956 1.00 71.58  ? 125  TYR B C     1 
ATOM   8417  O  O     . TYR B 2 125 ? 138.747 141.413 189.153 1.00 72.12  ? 125  TYR B O     1 
ATOM   8418  C  CB    . TYR B 2 125 ? 136.518 143.070 187.901 1.00 69.75  ? 125  TYR B CB    1 
ATOM   8419  C  CG    . TYR B 2 125 ? 135.927 144.420 187.573 1.00 71.25  ? 125  TYR B CG    1 
ATOM   8420  C  CD1   . TYR B 2 125 ? 136.353 145.565 188.231 1.00 72.49  ? 125  TYR B CD1   1 
ATOM   8421  C  CD2   . TYR B 2 125 ? 134.931 144.547 186.617 1.00 69.74  ? 125  TYR B CD2   1 
ATOM   8422  C  CE1   . TYR B 2 125 ? 135.812 146.798 187.937 1.00 69.28  ? 125  TYR B CE1   1 
ATOM   8423  C  CE2   . TYR B 2 125 ? 134.383 145.775 186.318 1.00 68.17  ? 125  TYR B CE2   1 
ATOM   8424  C  CZ    . TYR B 2 125 ? 134.828 146.896 186.980 1.00 68.13  ? 125  TYR B CZ    1 
ATOM   8425  O  OH    . TYR B 2 125 ? 134.282 148.121 186.683 1.00 72.93  ? 125  TYR B OH    1 
ATOM   8426  N  N     . ILE B 2 126 ? 138.584 140.543 187.085 1.00 66.42  ? 126  ILE B N     1 
ATOM   8427  C  CA    . ILE B 2 126 ? 139.022 139.211 187.474 1.00 62.93  ? 126  ILE B CA    1 
ATOM   8428  C  C     . ILE B 2 126 ? 140.242 138.831 186.647 1.00 64.34  ? 126  ILE B C     1 
ATOM   8429  O  O     . ILE B 2 126 ? 140.482 139.366 185.562 1.00 68.42  ? 126  ILE B O     1 
ATOM   8430  C  CB    . ILE B 2 126 ? 137.910 138.158 187.305 1.00 60.50  ? 126  ILE B CB    1 
ATOM   8431  C  CG1   . ILE B 2 126 ? 137.528 138.027 185.833 1.00 60.98  ? 126  ILE B CG1   1 
ATOM   8432  C  CG2   . ILE B 2 126 ? 136.698 138.520 188.142 1.00 60.12  ? 126  ILE B CG2   1 
ATOM   8433  C  CD1   . ILE B 2 126 ? 136.580 136.898 185.555 1.00 62.93  ? 126  ILE B CD1   1 
ATOM   8434  N  N     . ASP B 2 127 ? 141.020 137.898 187.179 1.00 55.85  ? 127  ASP B N     1 
ATOM   8435  C  CA    . ASP B 2 127 ? 142.168 137.371 186.454 1.00 55.69  ? 127  ASP B CA    1 
ATOM   8436  C  C     . ASP B 2 127 ? 141.687 136.344 185.437 1.00 59.94  ? 127  ASP B C     1 
ATOM   8437  O  O     . ASP B 2 127 ? 141.077 135.343 185.826 1.00 68.24  ? 127  ASP B O     1 
ATOM   8438  C  CB    . ASP B 2 127 ? 143.164 136.737 187.419 1.00 56.71  ? 127  ASP B CB    1 
ATOM   8439  C  CG    . ASP B 2 127 ? 144.558 136.608 186.829 1.00 61.90  ? 127  ASP B CG    1 
ATOM   8440  O  OD1   . ASP B 2 127 ? 144.684 136.489 185.595 1.00 61.96  ? 127  ASP B OD1   1 
ATOM   8441  O  OD2   . ASP B 2 127 ? 145.537 136.621 187.604 1.00 63.49  ? 127  ASP B OD2   1 
ATOM   8442  N  N     . PRO B 2 128 ? 141.920 136.553 184.139 1.00 50.00  ? 128  PRO B N     1 
ATOM   8443  C  CA    . PRO B 2 128 ? 141.512 135.544 183.148 1.00 51.07  ? 128  PRO B CA    1 
ATOM   8444  C  C     . PRO B 2 128 ? 142.260 134.230 183.270 1.00 53.35  ? 128  PRO B C     1 
ATOM   8445  O  O     . PRO B 2 128 ? 141.765 133.206 182.785 1.00 53.62  ? 128  PRO B O     1 
ATOM   8446  C  CB    . PRO B 2 128 ? 141.809 136.229 181.809 1.00 49.24  ? 128  PRO B CB    1 
ATOM   8447  C  CG    . PRO B 2 128 ? 142.841 137.254 182.128 1.00 49.58  ? 128  PRO B CG    1 
ATOM   8448  C  CD    . PRO B 2 128 ? 142.528 137.735 183.507 1.00 49.24  ? 128  PRO B CD    1 
ATOM   8449  N  N     . GLU B 2 129 ? 143.428 134.225 183.899 1.00 54.98  ? 129  GLU B N     1 
ATOM   8450  C  CA    . GLU B 2 129 ? 144.257 133.037 184.012 1.00 54.22  ? 129  GLU B CA    1 
ATOM   8451  C  C     . GLU B 2 129 ? 144.021 132.271 185.305 1.00 56.63  ? 129  GLU B C     1 
ATOM   8452  O  O     . GLU B 2 129 ? 144.714 131.280 185.554 1.00 56.26  ? 129  GLU B O     1 
ATOM   8453  C  CB    . GLU B 2 129 ? 145.731 133.426 183.906 1.00 55.86  ? 129  GLU B CB    1 
ATOM   8454  C  CG    . GLU B 2 129 ? 146.028 134.364 182.755 1.00 53.25  ? 129  GLU B CG    1 
ATOM   8455  C  CD    . GLU B 2 129 ? 147.471 134.807 182.727 1.00 55.65  ? 129  GLU B CD    1 
ATOM   8456  O  OE1   . GLU B 2 129 ? 148.200 134.518 183.698 1.00 58.26  ? 129  GLU B OE1   1 
ATOM   8457  O  OE2   . GLU B 2 129 ? 147.880 135.444 181.735 1.00 56.06  ? 129  GLU B OE2   1 
ATOM   8458  N  N     . ASN B 2 130 ? 143.074 132.705 186.132 1.00 54.81  ? 130  ASN B N     1 
ATOM   8459  C  CA    . ASN B 2 130 ? 142.790 132.067 187.410 1.00 51.68  ? 130  ASN B CA    1 
ATOM   8460  C  C     . ASN B 2 130 ? 141.313 131.709 187.456 1.00 50.99  ? 130  ASN B C     1 
ATOM   8461  O  O     . ASN B 2 130 ? 140.455 132.581 187.291 1.00 52.51  ? 130  ASN B O     1 
ATOM   8462  C  CB    . ASN B 2 130 ? 143.165 132.986 188.576 1.00 54.82  ? 130  ASN B CB    1 
ATOM   8463  C  CG    . ASN B 2 130 ? 143.197 132.264 189.903 1.00 60.81  ? 130  ASN B CG    1 
ATOM   8464  O  OD1   . ASN B 2 130 ? 143.244 131.037 189.953 1.00 62.03  ? 130  ASN B OD1   1 
ATOM   8465  N  ND2   . ASN B 2 130 ? 143.179 133.022 190.989 1.00 59.24  ? 130  ASN B ND2   1 
ATOM   8466  N  N     . ILE B 2 131 ? 141.019 130.428 187.674 1.00 51.23  ? 131  ILE B N     1 
ATOM   8467  C  CA    . ILE B 2 131 ? 139.631 129.999 187.782 1.00 50.95  ? 131  ILE B CA    1 
ATOM   8468  C  C     . ILE B 2 131 ? 139.098 130.205 189.195 1.00 52.33  ? 131  ILE B C     1 
ATOM   8469  O  O     . ILE B 2 131 ? 137.879 130.268 189.391 1.00 54.37  ? 131  ILE B O     1 
ATOM   8470  C  CB    . ILE B 2 131 ? 139.503 128.536 187.321 1.00 46.78  ? 131  ILE B CB    1 
ATOM   8471  C  CG1   . ILE B 2 131 ? 138.037 128.141 187.128 1.00 46.69  ? 131  ILE B CG1   1 
ATOM   8472  C  CG2   . ILE B 2 131 ? 140.201 127.604 188.290 1.00 49.81  ? 131  ILE B CG2   1 
ATOM   8473  C  CD1   . ILE B 2 131 ? 137.851 126.769 186.538 1.00 50.10  ? 131  ILE B CD1   1 
ATOM   8474  N  N     . GLU B 2 132 ? 139.984 130.351 190.182 1.00 59.08  ? 132  GLU B N     1 
ATOM   8475  C  CA    . GLU B 2 132 ? 139.545 130.647 191.540 1.00 56.39  ? 132  GLU B CA    1 
ATOM   8476  C  C     . GLU B 2 132 ? 138.914 132.031 191.632 1.00 59.78  ? 132  GLU B C     1 
ATOM   8477  O  O     . GLU B 2 132 ? 137.921 132.218 192.341 1.00 58.55  ? 132  GLU B O     1 
ATOM   8478  C  CB    . GLU B 2 132 ? 140.721 130.529 192.506 1.00 53.89  ? 132  GLU B CB    1 
ATOM   8479  C  CG    . GLU B 2 132 ? 141.392 129.170 192.499 1.00 60.59  ? 132  GLU B CG    1 
ATOM   8480  C  CD    . GLU B 2 132 ? 140.528 128.092 193.114 1.00 62.77  ? 132  GLU B CD    1 
ATOM   8481  O  OE1   . GLU B 2 132 ? 139.622 128.430 193.903 1.00 60.91  ? 132  GLU B OE1   1 
ATOM   8482  O  OE2   . GLU B 2 132 ? 140.756 126.903 192.811 1.00 63.21  ? 132  GLU B OE2   1 
ATOM   8483  N  N     . GLU B 2 133 ? 139.478 133.016 190.929 1.00 62.39  ? 133  GLU B N     1 
ATOM   8484  C  CA    . GLU B 2 133 ? 138.909 134.359 190.965 1.00 59.84  ? 133  GLU B CA    1 
ATOM   8485  C  C     . GLU B 2 133 ? 137.575 134.420 190.233 1.00 59.09  ? 133  GLU B C     1 
ATOM   8486  O  O     . GLU B 2 133 ? 136.651 135.112 190.676 1.00 60.69  ? 133  GLU B O     1 
ATOM   8487  C  CB    . GLU B 2 133 ? 139.891 135.367 190.375 1.00 60.50  ? 133  GLU B CB    1 
ATOM   8488  C  CG    . GLU B 2 133 ? 141.074 135.655 191.270 1.00 61.99  ? 133  GLU B CG    1 
ATOM   8489  C  CD    . GLU B 2 133 ? 141.870 136.850 190.808 1.00 64.59  ? 133  GLU B CD    1 
ATOM   8490  O  OE1   . GLU B 2 133 ? 141.348 137.627 189.985 1.00 64.33  ? 133  GLU B OE1   1 
ATOM   8491  O  OE2   . GLU B 2 133 ? 143.018 137.012 191.267 1.00 63.23  ? 133  GLU B OE2   1 
ATOM   8492  N  N     . TYR B 2 134 ? 137.457 133.714 189.108 1.00 52.28  ? 134  TYR B N     1 
ATOM   8493  C  CA    . TYR B 2 134 ? 136.174 133.650 188.417 1.00 50.32  ? 134  TYR B CA    1 
ATOM   8494  C  C     . TYR B 2 134 ? 135.134 132.929 189.265 1.00 53.24  ? 134  TYR B C     1 
ATOM   8495  O  O     . TYR B 2 134 ? 133.959 133.308 189.267 1.00 55.28  ? 134  TYR B O     1 
ATOM   8496  C  CB    . TYR B 2 134 ? 136.339 132.972 187.058 1.00 49.80  ? 134  TYR B CB    1 
ATOM   8497  C  CG    . TYR B 2 134 ? 135.061 132.882 186.255 1.00 49.71  ? 134  TYR B CG    1 
ATOM   8498  C  CD1   . TYR B 2 134 ? 134.526 134.002 185.633 1.00 52.21  ? 134  TYR B CD1   1 
ATOM   8499  C  CD2   . TYR B 2 134 ? 134.392 131.678 186.115 1.00 52.27  ? 134  TYR B CD2   1 
ATOM   8500  C  CE1   . TYR B 2 134 ? 133.359 133.922 184.900 1.00 49.72  ? 134  TYR B CE1   1 
ATOM   8501  C  CE2   . TYR B 2 134 ? 133.227 131.589 185.380 1.00 52.10  ? 134  TYR B CE2   1 
ATOM   8502  C  CZ    . TYR B 2 134 ? 132.715 132.712 184.778 1.00 49.35  ? 134  TYR B CZ    1 
ATOM   8503  O  OH    . TYR B 2 134 ? 131.554 132.621 184.051 1.00 50.60  ? 134  TYR B OH    1 
ATOM   8504  N  N     . ILE B 2 135 ? 135.552 131.892 189.995 1.00 52.90  ? 135  ILE B N     1 
ATOM   8505  C  CA    . ILE B 2 135 ? 134.644 131.190 190.899 1.00 51.06  ? 135  ILE B CA    1 
ATOM   8506  C  C     . ILE B 2 135 ? 134.185 132.112 192.024 1.00 51.30  ? 135  ILE B C     1 
ATOM   8507  O  O     . ILE B 2 135 ? 132.995 132.170 192.355 1.00 54.94  ? 135  ILE B O     1 
ATOM   8508  C  CB    . ILE B 2 135 ? 135.320 129.919 191.444 1.00 55.15  ? 135  ILE B CB    1 
ATOM   8509  C  CG1   . ILE B 2 135 ? 135.137 128.761 190.467 1.00 56.74  ? 135  ILE B CG1   1 
ATOM   8510  C  CG2   . ILE B 2 135 ? 134.766 129.544 192.812 1.00 54.15  ? 135  ILE B CG2   1 
ATOM   8511  C  CD1   . ILE B 2 135 ? 133.729 128.231 190.437 1.00 54.99  ? 135  ILE B CD1   1 
ATOM   8512  N  N     . ALA B 2 136 ? 135.120 132.856 192.618 1.00 51.21  ? 136  ALA B N     1 
ATOM   8513  C  CA    . ALA B 2 136 ? 134.783 133.725 193.741 1.00 53.07  ? 136  ALA B CA    1 
ATOM   8514  C  C     . ALA B 2 136 ? 133.916 134.900 193.311 1.00 50.50  ? 136  ALA B C     1 
ATOM   8515  O  O     . ALA B 2 136 ? 133.159 135.437 194.125 1.00 51.94  ? 136  ALA B O     1 
ATOM   8516  C  CB    . ALA B 2 136 ? 136.056 134.227 194.418 1.00 54.09  ? 136  ALA B CB    1 
ATOM   8517  N  N     . ALA B 2 137 ? 134.007 135.308 192.047 1.00 49.11  ? 137  ALA B N     1 
ATOM   8518  C  CA    . ALA B 2 137 ? 133.201 136.397 191.516 1.00 49.76  ? 137  ALA B CA    1 
ATOM   8519  C  C     . ALA B 2 137 ? 131.831 135.932 191.035 1.00 51.36  ? 137  ALA B C     1 
ATOM   8520  O  O     . ALA B 2 137 ? 131.202 136.620 190.224 1.00 47.70  ? 137  ALA B O     1 
ATOM   8521  C  CB    . ALA B 2 137 ? 133.947 137.103 190.383 1.00 49.93  ? 137  ALA B CB    1 
ATOM   8522  N  N     . GLY B 2 138 ? 131.358 134.784 191.513 1.00 57.77  ? 138  GLY B N     1 
ATOM   8523  C  CA    . GLY B 2 138 ? 130.054 134.275 191.152 1.00 56.51  ? 138  GLY B CA    1 
ATOM   8524  C  C     . GLY B 2 138 ? 130.019 133.395 189.925 1.00 53.91  ? 138  GLY B C     1 
ATOM   8525  O  O     . GLY B 2 138 ? 128.933 132.940 189.543 1.00 55.24  ? 138  GLY B O     1 
ATOM   8526  N  N     . GLY B 2 139 ? 131.160 133.135 189.296 1.00 47.40  ? 139  GLY B N     1 
ATOM   8527  C  CA    . GLY B 2 139 ? 131.167 132.340 188.089 1.00 45.95  ? 139  GLY B CA    1 
ATOM   8528  C  C     . GLY B 2 139 ? 130.946 130.865 188.354 1.00 50.87  ? 139  GLY B C     1 
ATOM   8529  O  O     . GLY B 2 139 ? 131.120 130.362 189.464 1.00 53.96  ? 139  GLY B O     1 
ATOM   8530  N  N     . TYR B 2 140 ? 130.524 130.172 187.295 1.00 49.11  ? 140  TYR B N     1 
ATOM   8531  C  CA    . TYR B 2 140 ? 130.266 128.732 187.278 1.00 47.42  ? 140  TYR B CA    1 
ATOM   8532  C  C     . TYR B 2 140 ? 129.144 128.316 188.225 1.00 48.84  ? 140  TYR B C     1 
ATOM   8533  O  O     . TYR B 2 140 ? 128.856 127.123 188.355 1.00 53.99  ? 140  TYR B O     1 
ATOM   8534  C  CB    . TYR B 2 140 ? 131.541 127.944 187.589 1.00 48.54  ? 140  TYR B CB    1 
ATOM   8535  C  CG    . TYR B 2 140 ? 132.468 127.797 186.405 1.00 50.16  ? 140  TYR B CG    1 
ATOM   8536  C  CD1   . TYR B 2 140 ? 132.069 127.102 185.272 1.00 47.73  ? 140  TYR B CD1   1 
ATOM   8537  C  CD2   . TYR B 2 140 ? 133.743 128.340 186.424 1.00 49.40  ? 140  TYR B CD2   1 
ATOM   8538  C  CE1   . TYR B 2 140 ? 132.909 126.961 184.189 1.00 48.68  ? 140  TYR B CE1   1 
ATOM   8539  C  CE2   . TYR B 2 140 ? 134.590 128.205 185.345 1.00 47.70  ? 140  TYR B CE2   1 
ATOM   8540  C  CZ    . TYR B 2 140 ? 134.168 127.514 184.232 1.00 49.80  ? 140  TYR B CZ    1 
ATOM   8541  O  OH    . TYR B 2 140 ? 135.010 127.377 183.156 1.00 52.53  ? 140  TYR B OH    1 
ATOM   8542  N  N     . GLU B 2 141 ? 128.500 129.282 188.883 1.00 54.98  ? 141  GLU B N     1 
ATOM   8543  C  CA    . GLU B 2 141 ? 127.282 128.983 189.626 1.00 54.47  ? 141  GLU B CA    1 
ATOM   8544  C  C     . GLU B 2 141 ? 126.117 128.749 188.677 1.00 55.38  ? 141  GLU B C     1 
ATOM   8545  O  O     . GLU B 2 141 ? 125.243 127.912 188.940 1.00 57.11  ? 141  GLU B O     1 
ATOM   8546  C  CB    . GLU B 2 141 ? 126.963 130.119 190.595 1.00 54.78  ? 141  GLU B CB    1 
ATOM   8547  C  CG    . GLU B 2 141 ? 128.069 130.424 191.581 1.00 58.80  ? 141  GLU B CG    1 
ATOM   8548  C  CD    . GLU B 2 141 ? 127.713 131.564 192.513 1.00 58.87  ? 141  GLU B CD    1 
ATOM   8549  O  OE1   . GLU B 2 141 ? 126.597 132.109 192.386 1.00 58.88  ? 141  GLU B OE1   1 
ATOM   8550  O  OE2   . GLU B 2 141 ? 128.549 131.915 193.373 1.00 58.47  ? 141  GLU B OE2   1 
ATOM   8551  N  N     . ALA B 2 142 ? 126.091 129.488 187.566 1.00 49.25  ? 142  ALA B N     1 
ATOM   8552  C  CA    . ALA B 2 142 ? 125.088 129.245 186.539 1.00 47.15  ? 142  ALA B CA    1 
ATOM   8553  C  C     . ALA B 2 142 ? 125.251 127.863 185.930 1.00 49.31  ? 142  ALA B C     1 
ATOM   8554  O  O     . ALA B 2 142 ? 124.259 127.236 185.550 1.00 50.36  ? 142  ALA B O     1 
ATOM   8555  C  CB    . ALA B 2 142 ? 125.169 130.321 185.458 1.00 44.62  ? 142  ALA B CB    1 
ATOM   8556  N  N     . LEU B 2 143 ? 126.487 127.368 185.839 1.00 53.53  ? 143  LEU B N     1 
ATOM   8557  C  CA    . LEU B 2 143 ? 126.705 126.015 185.340 1.00 55.12  ? 143  LEU B CA    1 
ATOM   8558  C  C     . LEU B 2 143 ? 126.069 124.978 186.256 1.00 53.70  ? 143  LEU B C     1 
ATOM   8559  O  O     . LEU B 2 143 ? 125.416 124.042 185.784 1.00 52.25  ? 143  LEU B O     1 
ATOM   8560  C  CB    . LEU B 2 143 ? 128.201 125.747 185.189 1.00 54.38  ? 143  LEU B CB    1 
ATOM   8561  C  CG    . LEU B 2 143 ? 128.546 124.374 184.619 1.00 52.55  ? 143  LEU B CG    1 
ATOM   8562  C  CD1   . LEU B 2 143 ? 127.874 124.199 183.276 1.00 49.50  ? 143  LEU B CD1   1 
ATOM   8563  C  CD2   . LEU B 2 143 ? 130.044 124.198 184.494 1.00 52.91  ? 143  LEU B CD2   1 
ATOM   8564  N  N     . LYS B 2 144 ? 126.244 125.132 187.569 1.00 53.37  ? 144  LYS B N     1 
ATOM   8565  C  CA    . LYS B 2 144 ? 125.644 124.195 188.513 1.00 52.57  ? 144  LYS B CA    1 
ATOM   8566  C  C     . LYS B 2 144 ? 124.122 124.299 188.507 1.00 57.26  ? 144  LYS B C     1 
ATOM   8567  O  O     . LYS B 2 144 ? 123.422 123.277 188.558 1.00 60.98  ? 144  LYS B O     1 
ATOM   8568  C  CB    . LYS B 2 144 ? 126.213 124.443 189.908 1.00 54.83  ? 144  LYS B CB    1 
ATOM   8569  C  CG    . LYS B 2 144 ? 127.730 124.353 189.946 1.00 56.68  ? 144  LYS B CG    1 
ATOM   8570  C  CD    . LYS B 2 144 ? 128.298 124.742 191.294 1.00 58.25  ? 144  LYS B CD    1 
ATOM   8571  C  CE    . LYS B 2 144 ? 129.811 124.825 191.235 1.00 55.77  ? 144  LYS B CE    1 
ATOM   8572  N  NZ    . LYS B 2 144 ? 130.401 125.273 192.520 1.00 55.67  ? 144  LYS B NZ    1 
ATOM   8573  N  N     . LYS B 2 145 ? 123.592 125.522 188.424 1.00 55.40  ? 145  LYS B N     1 
ATOM   8574  C  CA    . LYS B 2 145 ? 122.144 125.684 188.338 1.00 52.92  ? 145  LYS B CA    1 
ATOM   8575  C  C     . LYS B 2 145 ? 121.589 125.038 187.073 1.00 56.35  ? 145  LYS B C     1 
ATOM   8576  O  O     . LYS B 2 145 ? 120.538 124.390 187.110 1.00 61.81  ? 145  LYS B O     1 
ATOM   8577  C  CB    . LYS B 2 145 ? 121.770 127.165 188.391 1.00 57.53  ? 145  LYS B CB    1 
ATOM   8578  C  CG    . LYS B 2 145 ? 120.275 127.412 188.319 1.00 58.45  ? 145  LYS B CG    1 
ATOM   8579  C  CD    . LYS B 2 145 ? 119.944 128.889 188.308 1.00 57.31  ? 145  LYS B CD    1 
ATOM   8580  C  CE    . LYS B 2 145 ? 118.452 129.100 188.122 1.00 58.75  ? 145  LYS B CE    1 
ATOM   8581  N  NZ    . LYS B 2 145 ? 118.093 130.541 188.075 1.00 58.80  ? 145  LYS B NZ    1 
ATOM   8582  N  N     . ALA B 2 146 ? 122.288 125.197 185.946 1.00 56.81  ? 146  ALA B N     1 
ATOM   8583  C  CA    . ALA B 2 146 ? 121.843 124.596 184.694 1.00 56.81  ? 146  ALA B CA    1 
ATOM   8584  C  C     . ALA B 2 146 ? 121.968 123.081 184.722 1.00 61.03  ? 146  ALA B C     1 
ATOM   8585  O  O     . ALA B 2 146 ? 121.167 122.383 184.092 1.00 59.15  ? 146  ALA B O     1 
ATOM   8586  C  CB    . ALA B 2 146 ? 122.639 125.173 183.526 1.00 53.77  ? 146  ALA B CB    1 
ATOM   8587  N  N     . PHE B 2 147 ? 122.972 122.557 185.426 1.00 62.42  ? 147  PHE B N     1 
ATOM   8588  C  CA    . PHE B 2 147 ? 123.070 121.115 185.612 1.00 58.79  ? 147  PHE B CA    1 
ATOM   8589  C  C     . PHE B 2 147 ? 121.928 120.589 186.466 1.00 59.06  ? 147  PHE B C     1 
ATOM   8590  O  O     . PHE B 2 147 ? 121.513 119.437 186.300 1.00 61.63  ? 147  PHE B O     1 
ATOM   8591  C  CB    . PHE B 2 147 ? 124.416 120.754 186.236 1.00 58.65  ? 147  PHE B CB    1 
ATOM   8592  C  CG    . PHE B 2 147 ? 125.525 120.619 185.238 1.00 57.29  ? 147  PHE B CG    1 
ATOM   8593  C  CD1   . PHE B 2 147 ? 125.266 120.170 183.955 1.00 61.91  ? 147  PHE B CD1   1 
ATOM   8594  C  CD2   . PHE B 2 147 ? 126.824 120.939 185.578 1.00 57.35  ? 147  PHE B CD2   1 
ATOM   8595  C  CE1   . PHE B 2 147 ? 126.281 120.046 183.032 1.00 61.16  ? 147  PHE B CE1   1 
ATOM   8596  C  CE2   . PHE B 2 147 ? 127.843 120.815 184.659 1.00 60.98  ? 147  PHE B CE2   1 
ATOM   8597  C  CZ    . PHE B 2 147 ? 127.570 120.368 183.385 1.00 62.25  ? 147  PHE B CZ    1 
ATOM   8598  N  N     . LYS B 2 148 ? 121.410 121.408 187.380 1.00 63.01  ? 148  LYS B N     1 
ATOM   8599  C  CA    . LYS B 2 148 ? 120.225 121.012 188.130 1.00 66.49  ? 148  LYS B CA    1 
ATOM   8600  C  C     . LYS B 2 148 ? 118.935 121.177 187.335 1.00 66.09  ? 148  LYS B C     1 
ATOM   8601  O  O     . LYS B 2 148 ? 117.872 120.780 187.823 1.00 69.28  ? 148  LYS B O     1 
ATOM   8602  C  CB    . LYS B 2 148 ? 120.137 121.809 189.431 1.00 66.06  ? 148  LYS B CB    1 
ATOM   8603  C  CG    . LYS B 2 148 ? 121.308 121.579 190.367 1.00 66.35  ? 148  LYS B CG    1 
ATOM   8604  C  CD    . LYS B 2 148 ? 121.284 122.545 191.534 1.00 66.61  ? 148  LYS B CD    1 
ATOM   8605  C  CE    . LYS B 2 148 ? 122.542 122.419 192.368 1.00 67.68  ? 148  LYS B CE    1 
ATOM   8606  N  NZ    . LYS B 2 148 ? 122.555 123.389 193.495 1.00 66.70  ? 148  LYS B NZ    1 
ATOM   8607  N  N     . MET B 2 149 ? 118.998 121.749 186.138 1.00 61.97  ? 149  MET B N     1 
ATOM   8608  C  CA    . MET B 2 149 ? 117.842 121.911 185.269 1.00 62.85  ? 149  MET B CA    1 
ATOM   8609  C  C     . MET B 2 149 ? 117.868 120.881 184.146 1.00 65.97  ? 149  MET B C     1 
ATOM   8610  O  O     . MET B 2 149 ? 118.908 120.309 183.816 1.00 68.98  ? 149  MET B O     1 
ATOM   8611  C  CB    . MET B 2 149 ? 117.801 123.319 184.667 1.00 63.31  ? 149  MET B CB    1 
ATOM   8612  C  CG    . MET B 2 149 ? 117.599 124.434 185.669 1.00 61.89  ? 149  MET B CG    1 
ATOM   8613  S  SD    . MET B 2 149 ? 117.845 126.059 184.932 1.00 67.43  ? 149  MET B SD    1 
ATOM   8614  C  CE    . MET B 2 149 ? 116.687 125.990 183.573 1.00 63.83  ? 149  MET B CE    1 
ATOM   8615  N  N     . LYS B 2 150 ? 116.705 120.648 183.568 1.00 64.41  ? 150  LYS B N     1 
ATOM   8616  C  CA    . LYS B 2 150 ? 116.652 119.806 182.387 1.00 65.83  ? 150  LYS B CA    1 
ATOM   8617  C  C     . LYS B 2 150 ? 117.127 120.587 181.164 1.00 64.21  ? 150  LYS B C     1 
ATOM   8618  O  O     . LYS B 2 150 ? 116.969 121.808 181.102 1.00 66.13  ? 150  LYS B O     1 
ATOM   8619  C  CB    . LYS B 2 150 ? 115.236 119.294 182.161 1.00 66.86  ? 150  LYS B CB    1 
ATOM   8620  C  CG    . LYS B 2 150 ? 114.707 118.443 183.296 1.00 66.77  ? 150  LYS B CG    1 
ATOM   8621  C  CD    . LYS B 2 150 ? 113.330 117.903 182.978 1.00 65.23  ? 150  LYS B CD    1 
ATOM   8622  C  CE    . LYS B 2 150 ? 112.359 119.023 182.669 1.00 65.43  ? 150  LYS B CE    1 
ATOM   8623  N  NZ    . LYS B 2 150 ? 111.005 118.505 182.334 1.00 65.02  ? 150  LYS B NZ    1 
ATOM   8624  N  N     . PRO B 2 151 ? 117.735 119.903 180.189 1.00 58.80  ? 151  PRO B N     1 
ATOM   8625  C  CA    . PRO B 2 151 ? 118.205 120.607 178.982 1.00 58.27  ? 151  PRO B CA    1 
ATOM   8626  C  C     . PRO B 2 151 ? 117.108 121.338 178.225 1.00 59.82  ? 151  PRO B C     1 
ATOM   8627  O  O     . PRO B 2 151 ? 117.339 122.445 177.715 1.00 57.68  ? 151  PRO B O     1 
ATOM   8628  C  CB    . PRO B 2 151 ? 118.811 119.471 178.148 1.00 54.93  ? 151  PRO B CB    1 
ATOM   8629  C  CG    . PRO B 2 151 ? 119.225 118.454 179.151 1.00 56.96  ? 151  PRO B CG    1 
ATOM   8630  C  CD    . PRO B 2 151 ? 118.172 118.497 180.213 1.00 57.03  ? 151  PRO B CD    1 
ATOM   8631  N  N     . GLU B 2 152 ? 115.913 120.748 178.143 1.00 63.32  ? 152  GLU B N     1 
ATOM   8632  C  CA    . GLU B 2 152 ? 114.796 121.421 177.487 1.00 62.33  ? 152  GLU B CA    1 
ATOM   8633  C  C     . GLU B 2 152 ? 114.424 122.700 178.221 1.00 62.11  ? 152  GLU B C     1 
ATOM   8634  O  O     . GLU B 2 152 ? 114.080 123.712 177.596 1.00 63.51  ? 152  GLU B O     1 
ATOM   8635  C  CB    . GLU B 2 152 ? 113.594 120.481 177.408 1.00 64.14  ? 152  GLU B CB    1 
ATOM   8636  C  CG    . GLU B 2 152 ? 113.863 119.184 176.671 1.00 64.52  ? 152  GLU B CG    1 
ATOM   8637  C  CD    . GLU B 2 152 ? 113.847 119.353 175.168 1.00 66.00  ? 152  GLU B CD    1 
ATOM   8638  O  OE1   . GLU B 2 152 ? 113.412 120.423 174.693 1.00 65.45  ? 152  GLU B OE1   1 
ATOM   8639  O  OE2   . GLU B 2 152 ? 114.265 118.415 174.459 1.00 66.29  ? 152  GLU B OE2   1 
ATOM   8640  N  N     . GLU B 2 153 ? 114.491 122.671 179.553 1.00 63.69  ? 153  GLU B N     1 
ATOM   8641  C  CA    . GLU B 2 153 ? 114.229 123.871 180.337 1.00 61.28  ? 153  GLU B CA    1 
ATOM   8642  C  C     . GLU B 2 153 ? 115.272 124.947 180.067 1.00 59.94  ? 153  GLU B C     1 
ATOM   8643  O  O     . GLU B 2 153 ? 114.945 126.136 180.038 1.00 61.77  ? 153  GLU B O     1 
ATOM   8644  C  CB    . GLU B 2 153 ? 114.180 123.524 181.823 1.00 65.62  ? 153  GLU B CB    1 
ATOM   8645  C  CG    . GLU B 2 153 ? 113.046 122.589 182.188 1.00 64.82  ? 153  GLU B CG    1 
ATOM   8646  C  CD    . GLU B 2 153 ? 112.932 122.372 183.680 1.00 67.19  ? 153  GLU B CD    1 
ATOM   8647  O  OE1   . GLU B 2 153 ? 113.899 122.686 184.402 1.00 64.97  ? 153  GLU B OE1   1 
ATOM   8648  O  OE2   . GLU B 2 153 ? 111.871 121.894 184.132 1.00 68.11  ? 153  GLU B OE2   1 
ATOM   8649  N  N     . ILE B 2 154 ? 116.529 124.553 179.852 1.00 50.15  ? 154  ILE B N     1 
ATOM   8650  C  CA    . ILE B 2 154 ? 117.562 125.528 179.507 1.00 50.44  ? 154  ILE B CA    1 
ATOM   8651  C  C     . ILE B 2 154 ? 117.285 126.138 178.138 1.00 55.36  ? 154  ILE B C     1 
ATOM   8652  O  O     . ILE B 2 154 ? 117.473 127.346 177.929 1.00 59.60  ? 154  ILE B O     1 
ATOM   8653  C  CB    . ILE B 2 154 ? 118.954 124.876 179.561 1.00 50.17  ? 154  ILE B CB    1 
ATOM   8654  C  CG1   . ILE B 2 154 ? 119.195 124.238 180.926 1.00 53.97  ? 154  ILE B CG1   1 
ATOM   8655  C  CG2   . ILE B 2 154 ? 120.036 125.901 179.273 1.00 49.30  ? 154  ILE B CG2   1 
ATOM   8656  C  CD1   . ILE B 2 154 ? 120.507 123.507 181.021 1.00 54.71  ? 154  ILE B CD1   1 
ATOM   8657  N  N     . ILE B 2 155 ? 116.844 125.316 177.183 1.00 55.22  ? 155  ILE B N     1 
ATOM   8658  C  CA    . ILE B 2 155 ? 116.529 125.826 175.849 1.00 52.71  ? 155  ILE B CA    1 
ATOM   8659  C  C     . ILE B 2 155 ? 115.382 126.827 175.919 1.00 53.59  ? 155  ILE B C     1 
ATOM   8660  O  O     . ILE B 2 155 ? 115.435 127.903 175.312 1.00 54.15  ? 155  ILE B O     1 
ATOM   8661  C  CB    . ILE B 2 155 ? 116.204 124.667 174.891 1.00 49.77  ? 155  ILE B CB    1 
ATOM   8662  C  CG1   . ILE B 2 155 ? 117.454 123.835 174.623 1.00 49.08  ? 155  ILE B CG1   1 
ATOM   8663  C  CG2   . ILE B 2 155 ? 115.631 125.194 173.589 1.00 48.47  ? 155  ILE B CG2   1 
ATOM   8664  C  CD1   . ILE B 2 155 ? 117.268 122.819 173.537 1.00 52.90  ? 155  ILE B CD1   1 
ATOM   8665  N  N     . ASP B 2 156 ? 114.330 126.488 176.666 1.00 53.58  ? 156  ASP B N     1 
ATOM   8666  C  CA    . ASP B 2 156 ? 113.213 127.415 176.828 1.00 50.72  ? 156  ASP B CA    1 
ATOM   8667  C  C     . ASP B 2 156 ? 113.645 128.679 177.561 1.00 55.10  ? 156  ASP B C     1 
ATOM   8668  O  O     . ASP B 2 156 ? 113.197 129.781 177.227 1.00 57.00  ? 156  ASP B O     1 
ATOM   8669  C  CB    . ASP B 2 156 ? 112.063 126.731 177.562 1.00 59.22  ? 156  ASP B CB    1 
ATOM   8670  C  CG    . ASP B 2 156 ? 111.250 125.835 176.655 1.00 62.32  ? 156  ASP B CG    1 
ATOM   8671  O  OD1   . ASP B 2 156 ? 111.491 125.857 175.430 1.00 58.54  ? 156  ASP B OD1   1 
ATOM   8672  O  OD2   . ASP B 2 156 ? 110.369 125.111 177.164 1.00 62.66  ? 156  ASP B OD2   1 
ATOM   8673  N  N     . PHE B 2 157 ? 114.513 128.533 178.566 1.00 47.81  ? 157  PHE B N     1 
ATOM   8674  C  CA    . PHE B 2 157 ? 115.091 129.670 179.273 1.00 43.85  ? 157  PHE B CA    1 
ATOM   8675  C  C     . PHE B 2 157 ? 115.747 130.643 178.303 1.00 43.32  ? 157  PHE B C     1 
ATOM   8676  O  O     . PHE B 2 157 ? 115.489 131.851 178.340 1.00 48.47  ? 157  PHE B O     1 
ATOM   8677  C  CB    . PHE B 2 157 ? 116.120 129.154 180.280 1.00 46.21  ? 157  PHE B CB    1 
ATOM   8678  C  CG    . PHE B 2 157 ? 116.029 129.776 181.638 1.00 49.10  ? 157  PHE B CG    1 
ATOM   8679  C  CD1   . PHE B 2 157 ? 116.742 130.920 181.939 1.00 51.73  ? 157  PHE B CD1   1 
ATOM   8680  C  CD2   . PHE B 2 157 ? 115.267 129.189 182.631 1.00 47.50  ? 157  PHE B CD2   1 
ATOM   8681  C  CE1   . PHE B 2 157 ? 116.673 131.483 183.195 1.00 53.96  ? 157  PHE B CE1   1 
ATOM   8682  C  CE2   . PHE B 2 157 ? 115.196 129.747 183.888 1.00 49.38  ? 157  PHE B CE2   1 
ATOM   8683  C  CZ    . PHE B 2 157 ? 115.900 130.895 184.170 1.00 51.68  ? 157  PHE B CZ    1 
ATOM   8684  N  N     . ILE B 2 158 ? 116.603 130.123 177.423 1.00 41.98  ? 158  ILE B N     1 
ATOM   8685  C  CA    . ILE B 2 158 ? 117.299 130.975 176.463 1.00 44.27  ? 158  ILE B CA    1 
ATOM   8686  C  C     . ILE B 2 158 ? 116.320 131.562 175.450 1.00 47.27  ? 158  ILE B C     1 
ATOM   8687  O  O     . ILE B 2 158 ? 116.477 132.705 175.006 1.00 51.59  ? 158  ILE B O     1 
ATOM   8688  C  CB    . ILE B 2 158 ? 118.433 130.187 175.783 1.00 43.06  ? 158  ILE B CB    1 
ATOM   8689  C  CG1   . ILE B 2 158 ? 119.446 129.731 176.828 1.00 45.70  ? 158  ILE B CG1   1 
ATOM   8690  C  CG2   . ILE B 2 158 ? 119.140 131.035 174.741 1.00 39.41  ? 158  ILE B CG2   1 
ATOM   8691  C  CD1   . ILE B 2 158 ? 120.090 130.871 177.574 1.00 40.43  ? 158  ILE B CD1   1 
ATOM   8692  N  N     . THR B 2 159 ? 115.298 130.792 175.068 1.00 47.60  ? 159  THR B N     1 
ATOM   8693  C  CA    . THR B 2 159 ? 114.312 131.281 174.109 1.00 44.80  ? 159  THR B CA    1 
ATOM   8694  C  C     . THR B 2 159 ? 113.527 132.463 174.669 1.00 45.74  ? 159  THR B C     1 
ATOM   8695  O  O     . THR B 2 159 ? 113.252 133.431 173.952 1.00 46.89  ? 159  THR B O     1 
ATOM   8696  C  CB    . THR B 2 159 ? 113.361 130.149 173.715 1.00 44.57  ? 159  THR B CB    1 
ATOM   8697  O  OG1   . THR B 2 159 ? 114.111 129.062 173.162 1.00 45.55  ? 159  THR B OG1   1 
ATOM   8698  C  CG2   . THR B 2 159 ? 112.353 130.626 172.688 1.00 47.55  ? 159  THR B CG2   1 
ATOM   8699  N  N     . LYS B 2 160 ? 113.164 132.404 175.950 1.00 44.28  ? 160  LYS B N     1 
ATOM   8700  C  CA    . LYS B 2 160 ? 112.337 133.449 176.542 1.00 45.48  ? 160  LYS B CA    1 
ATOM   8701  C  C     . LYS B 2 160 ? 113.083 134.764 176.728 1.00 46.21  ? 160  LYS B C     1 
ATOM   8702  O  O     . LYS B 2 160 ? 112.441 135.801 176.923 1.00 47.02  ? 160  LYS B O     1 
ATOM   8703  C  CB    . LYS B 2 160 ? 111.781 132.979 177.885 1.00 48.44  ? 160  LYS B CB    1 
ATOM   8704  C  CG    . LYS B 2 160 ? 110.859 131.783 177.787 1.00 50.04  ? 160  LYS B CG    1 
ATOM   8705  C  CD    . LYS B 2 160 ? 110.469 131.275 179.159 1.00 50.23  ? 160  LYS B CD    1 
ATOM   8706  C  CE    . LYS B 2 160 ? 109.776 129.931 179.062 1.00 48.80  ? 160  LYS B CE    1 
ATOM   8707  N  NZ    . LYS B 2 160 ? 108.624 129.976 178.125 1.00 49.97  ? 160  LYS B NZ    1 
ATOM   8708  N  N     . SER B 2 161 ? 114.413 134.754 176.677 1.00 44.41  ? 161  SER B N     1 
ATOM   8709  C  CA    . SER B 2 161 ? 115.169 135.976 176.916 1.00 45.03  ? 161  SER B CA    1 
ATOM   8710  C  C     . SER B 2 161 ? 115.186 136.911 175.719 1.00 48.54  ? 161  SER B C     1 
ATOM   8711  O  O     . SER B 2 161 ? 115.536 138.085 175.874 1.00 51.68  ? 161  SER B O     1 
ATOM   8712  C  CB    . SER B 2 161 ? 116.610 135.646 177.296 1.00 39.95  ? 161  SER B CB    1 
ATOM   8713  O  OG    . SER B 2 161 ? 116.647 134.755 178.388 1.00 49.36  ? 161  SER B OG    1 
ATOM   8714  N  N     . GLY B 2 162 ? 114.818 136.428 174.538 1.00 41.92  ? 162  GLY B N     1 
ATOM   8715  C  CA    . GLY B 2 162 ? 115.000 137.227 173.342 1.00 38.35  ? 162  GLY B CA    1 
ATOM   8716  C  C     . GLY B 2 162 ? 116.452 137.446 172.996 1.00 34.40  ? 162  GLY B C     1 
ATOM   8717  O  O     . GLY B 2 162 ? 116.792 138.461 172.381 1.00 35.82  ? 162  GLY B O     1 
ATOM   8718  N  N     . LEU B 2 163 ? 117.325 136.516 173.381 1.00 32.16  ? 163  LEU B N     1 
ATOM   8719  C  CA    . LEU B 2 163 ? 118.739 136.621 173.054 1.00 34.30  ? 163  LEU B CA    1 
ATOM   8720  C  C     . LEU B 2 163 ? 118.934 136.316 171.579 1.00 38.18  ? 163  LEU B C     1 
ATOM   8721  O  O     . LEU B 2 163 ? 119.083 135.156 171.186 1.00 44.93  ? 163  LEU B O     1 
ATOM   8722  C  CB    . LEU B 2 163 ? 119.578 135.675 173.916 1.00 37.53  ? 163  LEU B CB    1 
ATOM   8723  C  CG    . LEU B 2 163 ? 121.078 135.637 173.610 1.00 32.86  ? 163  LEU B CG    1 
ATOM   8724  C  CD1   . LEU B 2 163 ? 121.692 137.015 173.737 1.00 37.00  ? 163  LEU B CD1   1 
ATOM   8725  C  CD2   . LEU B 2 163 ? 121.792 134.645 174.507 1.00 32.42  ? 163  LEU B CD2   1 
ATOM   8726  N  N     . ARG B 2 164 ? 118.896 137.350 170.753 1.00 35.77  ? 164  ARG B N     1 
ATOM   8727  C  CA    . ARG B 2 164 ? 119.100 137.150 169.334 1.00 28.58  ? 164  ARG B CA    1 
ATOM   8728  C  C     . ARG B 2 164 ? 120.589 137.037 169.041 1.00 27.39  ? 164  ARG B C     1 
ATOM   8729  O  O     . ARG B 2 164 ? 121.438 137.431 169.843 1.00 28.08  ? 164  ARG B O     1 
ATOM   8730  C  CB    . ARG B 2 164 ? 118.467 138.288 168.539 1.00 26.93  ? 164  ARG B CB    1 
ATOM   8731  C  CG    . ARG B 2 164 ? 117.033 138.564 168.947 1.00 29.17  ? 164  ARG B CG    1 
ATOM   8732  C  CD    . ARG B 2 164 ? 116.370 139.540 168.008 1.00 31.58  ? 164  ARG B CD    1 
ATOM   8733  N  NE    . ARG B 2 164 ? 116.021 138.912 166.742 1.00 31.66  ? 164  ARG B NE    1 
ATOM   8734  C  CZ    . ARG B 2 164 ? 115.724 139.578 165.636 1.00 35.77  ? 164  ARG B CZ    1 
ATOM   8735  N  NH1   . ARG B 2 164 ? 115.752 140.899 165.598 1.00 37.64  ? 164  ARG B NH1   1 
ATOM   8736  N  NH2   . ARG B 2 164 ? 115.398 138.900 164.540 1.00 39.80  ? 164  ARG B NH2   1 
ATOM   8737  N  N     . GLY B 2 165 ? 120.896 136.469 167.881 1.00 36.66  ? 165  GLY B N     1 
ATOM   8738  C  CA    . GLY B 2 165 ? 122.268 136.196 167.516 1.00 35.99  ? 165  GLY B CA    1 
ATOM   8739  C  C     . GLY B 2 165 ? 123.152 137.422 167.496 1.00 32.52  ? 165  GLY B C     1 
ATOM   8740  O  O     . GLY B 2 165 ? 123.022 138.282 166.622 1.00 37.04  ? 165  GLY B O     1 
ATOM   8741  N  N     . ARG B 2 166 ? 124.063 137.507 168.464 1.00 21.11  ? 166  ARG B N     1 
ATOM   8742  C  CA    . ARG B 2 166 ? 125.028 138.595 168.503 1.00 28.11  ? 166  ARG B CA    1 
ATOM   8743  C  C     . ARG B 2 166 ? 126.101 138.463 167.435 1.00 26.76  ? 166  ARG B C     1 
ATOM   8744  O  O     . ARG B 2 166 ? 127.011 139.296 167.387 1.00 31.76  ? 166  ARG B O     1 
ATOM   8745  C  CB    . ARG B 2 166 ? 125.677 138.668 169.884 1.00 38.30  ? 166  ARG B CB    1 
ATOM   8746  C  CG    . ARG B 2 166 ? 124.712 138.973 171.015 1.00 26.64  ? 166  ARG B CG    1 
ATOM   8747  C  CD    . ARG B 2 166 ? 124.200 140.396 170.939 1.00 24.81  ? 166  ARG B CD    1 
ATOM   8748  N  NE    . ARG B 2 166 ? 123.423 140.761 172.116 1.00 28.81  ? 166  ARG B NE    1 
ATOM   8749  C  CZ    . ARG B 2 166 ? 122.107 140.632 172.216 1.00 33.75  ? 166  ARG B CZ    1 
ATOM   8750  N  NH1   . ARG B 2 166 ? 121.383 140.148 171.222 1.00 34.35  ? 166  ARG B NH1   1 
ATOM   8751  N  NH2   . ARG B 2 166 ? 121.504 140.997 173.342 1.00 34.70  ? 166  ARG B NH2   1 
ATOM   8752  N  N     . GLY B 2 167 ? 126.022 137.439 166.589 1.00 21.72  ? 167  GLY B N     1 
ATOM   8753  C  CA    . GLY B 2 167 ? 126.941 137.296 165.482 1.00 26.57  ? 167  GLY B CA    1 
ATOM   8754  C  C     . GLY B 2 167 ? 126.684 138.222 164.322 1.00 23.33  ? 167  GLY B C     1 
ATOM   8755  O  O     . GLY B 2 167 ? 127.508 138.281 163.410 1.00 23.18  ? 167  GLY B O     1 
ATOM   8756  N  N     . GLY B 2 168 ? 125.561 138.934 164.325 1.00 26.73  ? 168  GLY B N     1 
ATOM   8757  C  CA    . GLY B 2 168 ? 125.303 139.943 163.319 1.00 29.48  ? 168  GLY B CA    1 
ATOM   8758  C  C     . GLY B 2 168 ? 123.952 139.834 162.646 1.00 29.80  ? 168  GLY B C     1 
ATOM   8759  O  O     . GLY B 2 168 ? 123.312 140.851 162.367 1.00 38.55  ? 168  GLY B O     1 
ATOM   8760  N  N     . ALA B 2 169 ? 123.503 138.610 162.382 1.00 26.33  ? 169  ALA B N     1 
ATOM   8761  C  CA    . ALA B 2 169 ? 122.240 138.414 161.686 1.00 31.14  ? 169  ALA B CA    1 
ATOM   8762  C  C     . ALA B 2 169 ? 121.034 138.473 162.610 1.00 34.06  ? 169  ALA B C     1 
ATOM   8763  O  O     . ALA B 2 169 ? 119.905 138.561 162.118 1.00 35.19  ? 169  ALA B O     1 
ATOM   8764  C  CB    . ALA B 2 169 ? 122.250 137.080 160.942 1.00 28.74  ? 169  ALA B CB    1 
ATOM   8765  N  N     . GLY B 2 170 ? 121.242 138.430 163.921 1.00 27.62  ? 170  GLY B N     1 
ATOM   8766  C  CA    . GLY B 2 170 ? 120.144 138.532 164.864 1.00 21.95  ? 170  GLY B CA    1 
ATOM   8767  C  C     . GLY B 2 170 ? 119.171 137.374 164.835 1.00 26.12  ? 170  GLY B C     1 
ATOM   8768  O  O     . GLY B 2 170 ? 117.966 137.580 165.016 1.00 38.11  ? 170  GLY B O     1 
ATOM   8769  N  N     . PHE B 2 171 ? 119.657 136.169 164.607 1.00 18.93  ? 171  PHE B N     1 
ATOM   8770  C  CA    . PHE B 2 171 ? 118.770 135.018 164.671 1.00 20.02  ? 171  PHE B CA    1 
ATOM   8771  C  C     . PHE B 2 171 ? 118.490 134.659 166.130 1.00 29.62  ? 171  PHE B C     1 
ATOM   8772  O  O     . PHE B 2 171 ? 119.376 134.783 166.978 1.00 39.81  ? 171  PHE B O     1 
ATOM   8773  C  CB    . PHE B 2 171 ? 119.388 133.826 163.945 1.00 24.82  ? 171  PHE B CB    1 
ATOM   8774  C  CG    . PHE B 2 171 ? 118.435 132.691 163.718 1.00 23.32  ? 171  PHE B CG    1 
ATOM   8775  C  CD1   . PHE B 2 171 ? 117.571 132.702 162.638 1.00 26.97  ? 171  PHE B CD1   1 
ATOM   8776  C  CD2   . PHE B 2 171 ? 118.409 131.609 164.578 1.00 22.04  ? 171  PHE B CD2   1 
ATOM   8777  C  CE1   . PHE B 2 171 ? 116.693 131.662 162.428 1.00 25.69  ? 171  PHE B CE1   1 
ATOM   8778  C  CE2   . PHE B 2 171 ? 117.534 130.565 164.370 1.00 26.37  ? 171  PHE B CE2   1 
ATOM   8779  C  CZ    . PHE B 2 171 ? 116.675 130.592 163.294 1.00 26.93  ? 171  PHE B CZ    1 
ATOM   8780  N  N     . PRO B 2 172 ? 117.268 134.236 166.454 1.00 26.90  ? 172  PRO B N     1 
ATOM   8781  C  CA    . PRO B 2 172 ? 116.973 133.816 167.833 1.00 27.59  ? 172  PRO B CA    1 
ATOM   8782  C  C     . PRO B 2 172 ? 117.792 132.595 168.223 1.00 28.10  ? 172  PRO B C     1 
ATOM   8783  O  O     . PRO B 2 172 ? 117.647 131.516 167.646 1.00 41.69  ? 172  PRO B O     1 
ATOM   8784  C  CB    . PRO B 2 172 ? 115.472 133.511 167.793 1.00 28.54  ? 172  PRO B CB    1 
ATOM   8785  C  CG    . PRO B 2 172 ? 114.957 134.320 166.661 1.00 27.17  ? 172  PRO B CG    1 
ATOM   8786  C  CD    . PRO B 2 172 ? 116.049 134.325 165.635 1.00 24.12  ? 172  PRO B CD    1 
ATOM   8787  N  N     . THR B 2 173 ? 118.660 132.780 169.220 1.00 12.91  ? 173  THR B N     1 
ATOM   8788  C  CA    . THR B 2 173 ? 119.615 131.742 169.603 1.00 19.63  ? 173  THR B CA    1 
ATOM   8789  C  C     . THR B 2 173 ? 118.915 130.508 170.160 1.00 25.74  ? 173  THR B C     1 
ATOM   8790  O  O     . THR B 2 173 ? 119.331 129.374 169.885 1.00 24.58  ? 173  THR B O     1 
ATOM   8791  C  CB    . THR B 2 173 ? 120.610 132.313 170.614 1.00 27.40  ? 173  THR B CB    1 
ATOM   8792  O  OG1   . THR B 2 173 ? 121.494 133.218 169.943 1.00 36.33  ? 173  THR B OG1   1 
ATOM   8793  C  CG2   . THR B 2 173 ? 121.421 131.215 171.276 1.00 29.72  ? 173  THR B CG2   1 
ATOM   8794  N  N     . GLY B 2 174 ? 117.854 130.706 170.944 1.00 38.36  ? 174  GLY B N     1 
ATOM   8795  C  CA    . GLY B 2 174 ? 117.114 129.571 171.468 1.00 36.09  ? 174  GLY B CA    1 
ATOM   8796  C  C     . GLY B 2 174 ? 116.540 128.694 170.373 1.00 36.46  ? 174  GLY B C     1 
ATOM   8797  O  O     . GLY B 2 174 ? 116.535 127.468 170.488 1.00 35.70  ? 174  GLY B O     1 
ATOM   8798  N  N     . LEU B 2 175 ? 116.061 129.311 169.290 1.00 27.53  ? 175  LEU B N     1 
ATOM   8799  C  CA    . LEU B 2 175 ? 115.595 128.544 168.139 1.00 27.40  ? 175  LEU B CA    1 
ATOM   8800  C  C     . LEU B 2 175 ? 116.731 127.748 167.513 1.00 29.60  ? 175  LEU B C     1 
ATOM   8801  O  O     . LEU B 2 175 ? 116.536 126.607 167.082 1.00 36.78  ? 175  LEU B O     1 
ATOM   8802  C  CB    . LEU B 2 175 ? 114.967 129.475 167.104 1.00 25.93  ? 175  LEU B CB    1 
ATOM   8803  C  CG    . LEU B 2 175 ? 113.443 129.480 167.028 1.00 33.74  ? 175  LEU B CG    1 
ATOM   8804  C  CD1   . LEU B 2 175 ? 112.844 130.004 168.319 1.00 32.64  ? 175  LEU B CD1   1 
ATOM   8805  C  CD2   . LEU B 2 175 ? 112.979 130.302 165.840 1.00 29.59  ? 175  LEU B CD2   1 
ATOM   8806  N  N     . LYS B 2 176 ? 117.923 128.338 167.452 1.00 23.68  ? 176  LYS B N     1 
ATOM   8807  C  CA    . LYS B 2 176 ? 119.078 127.637 166.905 1.00 20.17  ? 176  LYS B CA    1 
ATOM   8808  C  C     . LYS B 2 176 ? 119.429 126.411 167.741 1.00 27.54  ? 176  LYS B C     1 
ATOM   8809  O  O     . LYS B 2 176 ? 119.672 125.323 167.204 1.00 33.97  ? 176  LYS B O     1 
ATOM   8810  C  CB    . LYS B 2 176 ? 120.258 128.598 166.829 1.00 21.32  ? 176  LYS B CB    1 
ATOM   8811  C  CG    . LYS B 2 176 ? 121.314 128.202 165.850 1.00 24.34  ? 176  LYS B CG    1 
ATOM   8812  C  CD    . LYS B 2 176 ? 122.268 129.343 165.648 1.00 13.70  ? 176  LYS B CD    1 
ATOM   8813  C  CE    . LYS B 2 176 ? 123.262 129.000 164.584 1.00 21.31  ? 176  LYS B CE    1 
ATOM   8814  N  NZ    . LYS B 2 176 ? 124.222 130.119 164.405 1.00 18.49  ? 176  LYS B NZ    1 
ATOM   8815  N  N     . TRP B 2 177 ? 119.455 126.571 169.066 1.00 28.87  ? 177  TRP B N     1 
ATOM   8816  C  CA    . TRP B 2 177 ? 119.738 125.434 169.938 1.00 26.41  ? 177  TRP B CA    1 
ATOM   8817  C  C     . TRP B 2 177 ? 118.646 124.381 169.838 1.00 24.93  ? 177  TRP B C     1 
ATOM   8818  O  O     . TRP B 2 177 ? 118.932 123.180 169.878 1.00 30.85  ? 177  TRP B O     1 
ATOM   8819  C  CB    . TRP B 2 177 ? 119.878 125.883 171.389 1.00 35.15  ? 177  TRP B CB    1 
ATOM   8820  C  CG    . TRP B 2 177 ? 121.033 126.767 171.681 1.00 32.57  ? 177  TRP B CG    1 
ATOM   8821  C  CD1   . TRP B 2 177 ? 121.858 127.376 170.785 1.00 28.60  ? 177  TRP B CD1   1 
ATOM   8822  C  CD2   . TRP B 2 177 ? 121.493 127.148 172.976 1.00 27.17  ? 177  TRP B CD2   1 
ATOM   8823  N  NE1   . TRP B 2 177 ? 122.806 128.117 171.445 1.00 23.18  ? 177  TRP B NE1   1 
ATOM   8824  C  CE2   . TRP B 2 177 ? 122.601 127.994 172.793 1.00 23.73  ? 177  TRP B CE2   1 
ATOM   8825  C  CE3   . TRP B 2 177 ? 121.074 126.857 174.276 1.00 28.45  ? 177  TRP B CE3   1 
ATOM   8826  C  CZ2   . TRP B 2 177 ? 123.294 128.549 173.859 1.00 30.50  ? 177  TRP B CZ2   1 
ATOM   8827  C  CZ3   . TRP B 2 177 ? 121.762 127.408 175.330 1.00 33.62  ? 177  TRP B CZ3   1 
ATOM   8828  C  CH2   . TRP B 2 177 ? 122.861 128.243 175.118 1.00 32.79  ? 177  TRP B CH2   1 
ATOM   8829  N  N     . LYS B 2 178 ? 117.388 124.816 169.740 1.00 19.40  ? 178  LYS B N     1 
ATOM   8830  C  CA    . LYS B 2 178 ? 116.280 123.879 169.607 1.00 25.47  ? 178  LYS B CA    1 
ATOM   8831  C  C     . LYS B 2 178 ? 116.391 123.079 168.317 1.00 34.15  ? 178  LYS B C     1 
ATOM   8832  O  O     . LYS B 2 178 ? 116.123 121.873 168.300 1.00 35.88  ? 178  LYS B O     1 
ATOM   8833  C  CB    . LYS B 2 178 ? 114.956 124.641 169.662 1.00 26.78  ? 178  LYS B CB    1 
ATOM   8834  C  CG    . LYS B 2 178 ? 113.724 123.758 169.694 1.00 32.91  ? 178  LYS B CG    1 
ATOM   8835  C  CD    . LYS B 2 178 ? 112.457 124.582 169.582 1.00 36.83  ? 178  LYS B CD    1 
ATOM   8836  C  CE    . LYS B 2 178 ? 112.418 125.679 170.630 1.00 37.05  ? 178  LYS B CE    1 
ATOM   8837  N  NZ    . LYS B 2 178 ? 112.520 125.134 172.011 1.00 38.45  ? 178  LYS B NZ    1 
ATOM   8838  N  N     . PHE B 2 179 ? 116.783 123.737 167.225 1.00 31.33  ? 179  PHE B N     1 
ATOM   8839  C  CA    . PHE B 2 179 ? 117.001 123.033 165.966 1.00 26.02  ? 179  PHE B CA    1 
ATOM   8840  C  C     . PHE B 2 179 ? 118.149 122.040 166.077 1.00 27.94  ? 179  PHE B C     1 
ATOM   8841  O  O     . PHE B 2 179 ? 118.044 120.905 165.600 1.00 36.83  ? 179  PHE B O     1 
ATOM   8842  C  CB    . PHE B 2 179 ? 117.279 124.034 164.847 1.00 26.33  ? 179  PHE B CB    1 
ATOM   8843  C  CG    . PHE B 2 179 ? 116.054 124.716 164.323 1.00 28.80  ? 179  PHE B CG    1 
ATOM   8844  C  CD1   . PHE B 2 179 ? 114.854 124.040 164.234 1.00 30.73  ? 179  PHE B CD1   1 
ATOM   8845  C  CD2   . PHE B 2 179 ? 116.105 126.037 163.917 1.00 24.40  ? 179  PHE B CD2   1 
ATOM   8846  C  CE1   . PHE B 2 179 ? 113.729 124.666 163.750 1.00 31.66  ? 179  PHE B CE1   1 
ATOM   8847  C  CE2   . PHE B 2 179 ? 114.984 126.668 163.432 1.00 29.77  ? 179  PHE B CE2   1 
ATOM   8848  C  CZ    . PHE B 2 179 ? 113.795 125.982 163.349 1.00 32.06  ? 179  PHE B CZ    1 
ATOM   8849  N  N     . THR B 2 180 ? 119.256 122.453 166.698 1.00 28.87  ? 180  THR B N     1 
ATOM   8850  C  CA    . THR B 2 180 ? 120.417 121.571 166.793 1.00 26.66  ? 180  THR B CA    1 
ATOM   8851  C  C     . THR B 2 180 ? 120.128 120.359 167.674 1.00 31.15  ? 180  THR B C     1 
ATOM   8852  O  O     . THR B 2 180 ? 120.563 119.244 167.365 1.00 31.41  ? 180  THR B O     1 
ATOM   8853  C  CB    . THR B 2 180 ? 121.625 122.344 167.317 1.00 28.20  ? 180  THR B CB    1 
ATOM   8854  O  OG1   . THR B 2 180 ? 121.801 123.533 166.540 1.00 32.87  ? 180  THR B OG1   1 
ATOM   8855  C  CG2   . THR B 2 180 ? 122.880 121.500 167.211 1.00 27.77  ? 180  THR B CG2   1 
ATOM   8856  N  N     . ARG B 2 181 ? 119.405 120.557 168.779 1.00 35.45  ? 181  ARG B N     1 
ATOM   8857  C  CA    . ARG B 2 181 ? 119.024 119.429 169.623 1.00 34.09  ? 181  ARG B CA    1 
ATOM   8858  C  C     . ARG B 2 181 ? 118.037 118.512 168.912 1.00 33.00  ? 181  ARG B C     1 
ATOM   8859  O  O     . ARG B 2 181 ? 118.166 117.284 168.975 1.00 31.49  ? 181  ARG B O     1 
ATOM   8860  C  CB    . ARG B 2 181 ? 118.436 119.931 170.942 1.00 26.47  ? 181  ARG B CB    1 
ATOM   8861  C  CG    . ARG B 2 181 ? 117.567 118.904 171.651 1.00 33.21  ? 181  ARG B CG    1 
ATOM   8862  C  CD    . ARG B 2 181 ? 117.263 119.298 173.080 1.00 30.17  ? 181  ARG B CD    1 
ATOM   8863  N  NE    . ARG B 2 181 ? 118.279 118.818 174.006 1.00 38.35  ? 181  ARG B NE    1 
ATOM   8864  C  CZ    . ARG B 2 181 ? 118.162 117.717 174.734 1.00 37.72  ? 181  ARG B CZ    1 
ATOM   8865  N  NH1   . ARG B 2 181 ? 117.077 116.965 174.680 1.00 35.23  ? 181  ARG B NH1   1 
ATOM   8866  N  NH2   . ARG B 2 181 ? 119.160 117.362 175.537 1.00 35.99  ? 181  ARG B NH2   1 
ATOM   8867  N  N     . ASP B 2 182 ? 117.050 119.087 168.224 1.00 31.24  ? 182  ASP B N     1 
ATOM   8868  C  CA    . ASP B 2 182 ? 116.055 118.289 167.519 1.00 34.39  ? 182  ASP B CA    1 
ATOM   8869  C  C     . ASP B 2 182 ? 116.598 117.635 166.258 1.00 37.43  ? 182  ASP B C     1 
ATOM   8870  O  O     . ASP B 2 182 ? 115.895 116.813 165.663 1.00 40.71  ? 182  ASP B O     1 
ATOM   8871  C  CB    . ASP B 2 182 ? 114.844 119.149 167.155 1.00 33.83  ? 182  ASP B CB    1 
ATOM   8872  C  CG    . ASP B 2 182 ? 114.043 119.572 168.364 1.00 38.16  ? 182  ASP B CG    1 
ATOM   8873  O  OD1   . ASP B 2 182 ? 114.531 119.388 169.497 1.00 34.56  ? 182  ASP B OD1   1 
ATOM   8874  O  OD2   . ASP B 2 182 ? 112.919 120.082 168.181 1.00 38.13  ? 182  ASP B OD2   1 
ATOM   8875  N  N     . ALA B 2 183 ? 117.805 117.986 165.831 1.00 32.60  ? 183  ALA B N     1 
ATOM   8876  C  CA    . ALA B 2 183 ? 118.354 117.433 164.599 1.00 35.32  ? 183  ALA B CA    1 
ATOM   8877  C  C     . ALA B 2 183 ? 118.578 115.933 164.754 1.00 42.29  ? 183  ALA B C     1 
ATOM   8878  O  O     . ALA B 2 183 ? 119.116 115.493 165.776 1.00 42.78  ? 183  ALA B O     1 
ATOM   8879  C  CB    . ALA B 2 183 ? 119.659 118.132 164.232 1.00 31.82  ? 183  ALA B CB    1 
ATOM   8880  N  N     . PRO B 2 184 ? 118.184 115.121 163.772 1.00 41.22  ? 184  PRO B N     1 
ATOM   8881  C  CA    . PRO B 2 184 ? 118.298 113.661 163.913 1.00 44.08  ? 184  PRO B CA    1 
ATOM   8882  C  C     . PRO B 2 184 ? 119.754 113.223 163.915 1.00 47.44  ? 184  PRO B C     1 
ATOM   8883  O  O     . PRO B 2 184 ? 120.483 113.434 162.944 1.00 48.84  ? 184  PRO B O     1 
ATOM   8884  C  CB    . PRO B 2 184 ? 117.546 113.129 162.688 1.00 43.26  ? 184  PRO B CB    1 
ATOM   8885  C  CG    . PRO B 2 184 ? 117.623 114.235 161.694 1.00 41.42  ? 184  PRO B CG    1 
ATOM   8886  C  CD    . PRO B 2 184 ? 117.580 115.507 162.486 1.00 40.42  ? 184  PRO B CD    1 
ATOM   8887  N  N     . GLY B 2 185 ? 120.170 112.608 165.012 1.00 59.96  ? 185  GLY B N     1 
ATOM   8888  C  CA    . GLY B 2 185 ? 121.537 112.152 165.141 1.00 58.26  ? 185  GLY B CA    1 
ATOM   8889  C  C     . GLY B 2 185 ? 121.833 111.777 166.575 1.00 60.49  ? 185  GLY B C     1 
ATOM   8890  O  O     . GLY B 2 185 ? 120.970 111.842 167.454 1.00 60.50  ? 185  GLY B O     1 
ATOM   8891  N  N     . ASP B 2 186 ? 123.070 111.377 166.790 1.00 64.81  ? 186  ASP B N     1 
ATOM   8892  C  CA    . ASP B 2 186 ? 123.510 110.983 168.122 1.00 63.81  ? 186  ASP B CA    1 
ATOM   8893  C  C     . ASP B 2 186 ? 124.765 111.711 168.575 1.00 65.64  ? 186  ASP B C     1 
ATOM   8894  O  O     . ASP B 2 186 ? 124.883 112.037 169.758 1.00 64.92  ? 186  ASP B O     1 
ATOM   8895  C  CB    . ASP B 2 186 ? 123.744 109.464 168.168 1.00 65.00  ? 186  ASP B CB    1 
ATOM   8896  C  CG    . ASP B 2 186 ? 124.652 108.978 167.054 1.00 66.28  ? 186  ASP B CG    1 
ATOM   8897  O  OD1   . ASP B 2 186 ? 125.009 109.791 166.176 1.00 67.92  ? 186  ASP B OD1   1 
ATOM   8898  O  OD2   . ASP B 2 186 ? 125.009 107.781 167.057 1.00 64.54  ? 186  ASP B OD2   1 
ATOM   8899  N  N     . GLU B 2 187 ? 125.701 111.973 167.671 1.00 52.98  ? 187  GLU B N     1 
ATOM   8900  C  CA    . GLU B 2 187 ? 126.935 112.675 167.995 1.00 50.78  ? 187  GLU B CA    1 
ATOM   8901  C  C     . GLU B 2 187 ? 126.852 114.079 167.417 1.00 47.83  ? 187  GLU B C     1 
ATOM   8902  O  O     . GLU B 2 187 ? 126.702 114.245 166.202 1.00 46.40  ? 187  GLU B O     1 
ATOM   8903  C  CB    . GLU B 2 187 ? 128.150 111.930 167.445 1.00 49.26  ? 187  GLU B CB    1 
ATOM   8904  C  CG    . GLU B 2 187 ? 129.473 112.589 167.769 1.00 49.22  ? 187  GLU B CG    1 
ATOM   8905  C  CD    . GLU B 2 187 ? 130.655 111.812 167.228 1.00 53.24  ? 187  GLU B CD    1 
ATOM   8906  O  OE1   . GLU B 2 187 ? 130.437 110.735 166.635 1.00 50.87  ? 187  GLU B OE1   1 
ATOM   8907  O  OE2   . GLU B 2 187 ? 131.801 112.278 167.395 1.00 49.73  ? 187  GLU B OE2   1 
ATOM   8908  N  N     . LYS B 2 188 ? 126.946 115.082 168.283 1.00 36.89  ? 188  LYS B N     1 
ATOM   8909  C  CA    . LYS B 2 188 ? 126.766 116.468 167.886 1.00 29.59  ? 188  LYS B CA    1 
ATOM   8910  C  C     . LYS B 2 188 ? 127.953 117.297 168.349 1.00 31.47  ? 188  LYS B C     1 
ATOM   8911  O  O     . LYS B 2 188 ? 128.664 116.941 169.291 1.00 41.22  ? 188  LYS B O     1 
ATOM   8912  C  CB    . LYS B 2 188 ? 125.466 117.052 168.454 1.00 23.71  ? 188  LYS B CB    1 
ATOM   8913  C  CG    . LYS B 2 188 ? 124.213 116.343 167.981 1.00 29.47  ? 188  LYS B CG    1 
ATOM   8914  C  CD    . LYS B 2 188 ? 122.967 116.945 168.598 1.00 30.86  ? 188  LYS B CD    1 
ATOM   8915  C  CE    . LYS B 2 188 ? 121.717 116.258 168.085 1.00 34.20  ? 188  LYS B CE    1 
ATOM   8916  N  NZ    . LYS B 2 188 ? 121.710 114.811 168.419 1.00 38.14  ? 188  LYS B NZ    1 
ATOM   8917  N  N     . TYR B 2 189 ? 128.160 118.415 167.665 1.00 20.44  ? 189  TYR B N     1 
ATOM   8918  C  CA    . TYR B 2 189 ? 129.235 119.336 167.986 1.00 18.21  ? 189  TYR B CA    1 
ATOM   8919  C  C     . TYR B 2 189 ? 128.660 120.733 168.152 1.00 27.84  ? 189  TYR B C     1 
ATOM   8920  O  O     . TYR B 2 189 ? 127.607 121.057 167.602 1.00 39.43  ? 189  TYR B O     1 
ATOM   8921  C  CB    . TYR B 2 189 ? 130.316 119.336 166.898 1.00 15.34  ? 189  TYR B CB    1 
ATOM   8922  C  CG    . TYR B 2 189 ? 130.792 117.955 166.509 1.00 27.32  ? 189  TYR B CG    1 
ATOM   8923  C  CD1   . TYR B 2 189 ? 131.618 117.222 167.348 1.00 32.94  ? 189  TYR B CD1   1 
ATOM   8924  C  CD2   . TYR B 2 189 ? 130.414 117.385 165.303 1.00 28.21  ? 189  TYR B CD2   1 
ATOM   8925  C  CE1   . TYR B 2 189 ? 132.054 115.963 166.997 1.00 33.08  ? 189  TYR B CE1   1 
ATOM   8926  C  CE2   . TYR B 2 189 ? 130.845 116.127 164.944 1.00 27.62  ? 189  TYR B CE2   1 
ATOM   8927  C  CZ    . TYR B 2 189 ? 131.663 115.421 165.796 1.00 32.29  ? 189  TYR B CZ    1 
ATOM   8928  O  OH    . TYR B 2 189 ? 132.097 114.166 165.446 1.00 31.35  ? 189  TYR B OH    1 
ATOM   8929  N  N     . ILE B 2 190 ? 129.345 121.549 168.945 1.00 26.32  ? 190  ILE B N     1 
ATOM   8930  C  CA    . ILE B 2 190 ? 129.027 122.963 169.071 1.00 25.30  ? 190  ILE B CA    1 
ATOM   8931  C  C     . ILE B 2 190 ? 130.295 123.756 168.803 1.00 21.63  ? 190  ILE B C     1 
ATOM   8932  O  O     . ILE B 2 190 ? 131.387 123.370 169.232 1.00 34.71  ? 190  ILE B O     1 
ATOM   8933  C  CB    . ILE B 2 190 ? 128.431 123.325 170.449 1.00 25.87  ? 190  ILE B CB    1 
ATOM   8934  C  CG1   . ILE B 2 190 ? 129.385 122.948 171.577 1.00 29.19  ? 190  ILE B CG1   1 
ATOM   8935  C  CG2   . ILE B 2 190 ? 127.082 122.658 170.638 1.00 26.34  ? 190  ILE B CG2   1 
ATOM   8936  C  CD1   . ILE B 2 190 ? 129.064 123.629 172.870 1.00 31.85  ? 190  ILE B CD1   1 
ATOM   8937  N  N     . VAL B 2 191 ? 130.152 124.851 168.070 1.00 15.81  ? 191  VAL B N     1 
ATOM   8938  C  CA    . VAL B 2 191 ? 131.280 125.658 167.636 1.00 17.21  ? 191  VAL B CA    1 
ATOM   8939  C  C     . VAL B 2 191 ? 131.104 127.065 168.178 1.00 23.02  ? 191  VAL B C     1 
ATOM   8940  O  O     . VAL B 2 191 ? 130.025 127.654 168.054 1.00 34.80  ? 191  VAL B O     1 
ATOM   8941  C  CB    . VAL B 2 191 ? 131.412 125.671 166.102 1.00 18.19  ? 191  VAL B CB    1 
ATOM   8942  C  CG1   . VAL B 2 191 ? 132.485 126.649 165.669 1.00 21.90  ? 191  VAL B CG1   1 
ATOM   8943  C  CG2   . VAL B 2 191 ? 131.731 124.280 165.597 1.00 18.06  ? 191  VAL B CG2   1 
ATOM   8944  N  N     . CYS B 2 192 ? 132.154 127.588 168.800 1.00 16.77  ? 192  CYS B N     1 
ATOM   8945  C  CA    . CYS B 2 192 ? 132.226 128.999 169.142 1.00 18.19  ? 192  CYS B CA    1 
ATOM   8946  C  C     . CYS B 2 192 ? 132.847 129.731 167.960 1.00 18.80  ? 192  CYS B C     1 
ATOM   8947  O  O     . CYS B 2 192 ? 133.951 129.388 167.524 1.00 31.88  ? 192  CYS B O     1 
ATOM   8948  C  CB    . CYS B 2 192 ? 133.043 129.210 170.414 1.00 15.59  ? 192  CYS B CB    1 
ATOM   8949  S  SG    . CYS B 2 192 ? 133.072 130.907 171.009 1.00 17.23  ? 192  CYS B SG    1 
ATOM   8950  N  N     . ASN B 2 193 ? 132.132 130.717 167.432 1.00 20.64  ? 193  ASN B N     1 
ATOM   8951  C  CA    . ASN B 2 193 ? 132.563 131.438 166.237 1.00 20.43  ? 193  ASN B CA    1 
ATOM   8952  C  C     . ASN B 2 193 ? 133.359 132.657 166.683 1.00 20.17  ? 193  ASN B C     1 
ATOM   8953  O  O     . ASN B 2 193 ? 132.793 133.709 166.987 1.00 23.36  ? 193  ASN B O     1 
ATOM   8954  C  CB    . ASN B 2 193 ? 131.362 131.825 165.383 1.00 15.96  ? 193  ASN B CB    1 
ATOM   8955  C  CG    . ASN B 2 193 ? 131.727 132.053 163.935 1.00 20.27  ? 193  ASN B CG    1 
ATOM   8956  O  OD1   . ASN B 2 193 ? 132.836 132.481 163.621 1.00 31.53  ? 193  ASN B OD1   1 
ATOM   8957  N  ND2   . ASN B 2 193 ? 130.793 131.766 163.041 1.00 22.90  ? 193  ASN B ND2   1 
ATOM   8958  N  N     . ALA B 2 194 ? 134.682 132.512 166.729 1.00 26.69  ? 194  ALA B N     1 
ATOM   8959  C  CA    . ALA B 2 194 ? 135.572 133.587 167.143 1.00 25.44  ? 194  ALA B CA    1 
ATOM   8960  C  C     . ALA B 2 194 ? 136.438 134.094 165.998 1.00 31.69  ? 194  ALA B C     1 
ATOM   8961  O  O     . ALA B 2 194 ? 137.505 134.667 166.237 1.00 35.24  ? 194  ALA B O     1 
ATOM   8962  C  CB    . ALA B 2 194 ? 136.448 133.129 168.306 1.00 25.29  ? 194  ALA B CB    1 
ATOM   8963  N  N     . ASP B 2 195 ? 136.005 133.890 164.757 1.00 29.14  ? 195  ASP B N     1 
ATOM   8964  C  CA    . ASP B 2 195 ? 136.758 134.348 163.591 1.00 24.20  ? 195  ASP B CA    1 
ATOM   8965  C  C     . ASP B 2 195 ? 136.354 135.777 163.229 1.00 30.59  ? 195  ASP B C     1 
ATOM   8966  O  O     . ASP B 2 195 ? 135.856 136.065 162.143 1.00 39.61  ? 195  ASP B O     1 
ATOM   8967  C  CB    . ASP B 2 195 ? 136.546 133.398 162.420 1.00 33.21  ? 195  ASP B CB    1 
ATOM   8968  C  CG    . ASP B 2 195 ? 137.399 133.751 161.218 1.00 41.99  ? 195  ASP B CG    1 
ATOM   8969  O  OD1   . ASP B 2 195 ? 138.329 134.569 161.356 1.00 43.08  ? 195  ASP B OD1   1 
ATOM   8970  O  OD2   . ASP B 2 195 ? 137.127 133.218 160.128 1.00 42.52  ? 195  ASP B OD2   1 
ATOM   8971  N  N     . GLU B 2 196 ? 136.627 136.688 164.158 1.00 35.01  ? 196  GLU B N     1 
ATOM   8972  C  CA    . GLU B 2 196 ? 136.192 138.069 164.016 1.00 37.37  ? 196  GLU B CA    1 
ATOM   8973  C  C     . GLU B 2 196 ? 136.980 138.750 162.905 1.00 41.63  ? 196  GLU B C     1 
ATOM   8974  O  O     . GLU B 2 196 ? 138.081 139.260 163.132 1.00 50.63  ? 196  GLU B O     1 
ATOM   8975  C  CB    . GLU B 2 196 ? 136.362 138.808 165.342 1.00 36.58  ? 196  GLU B CB    1 
ATOM   8976  C  CG    . GLU B 2 196 ? 135.569 140.086 165.454 1.00 42.16  ? 196  GLU B CG    1 
ATOM   8977  C  CD    . GLU B 2 196 ? 135.616 140.658 166.849 1.00 49.22  ? 196  GLU B CD    1 
ATOM   8978  O  OE1   . GLU B 2 196 ? 136.372 140.119 167.682 1.00 49.30  ? 196  GLU B OE1   1 
ATOM   8979  O  OE2   . GLU B 2 196 ? 134.897 141.642 167.115 1.00 51.02  ? 196  GLU B OE2   1 
ATOM   8980  N  N     . GLY B 2 197 ? 136.420 138.752 161.696 1.00 39.16  ? 197  GLY B N     1 
ATOM   8981  C  CA    . GLY B 2 197 ? 137.131 139.225 160.526 1.00 41.92  ? 197  GLY B CA    1 
ATOM   8982  C  C     . GLY B 2 197 ? 137.116 140.717 160.312 1.00 47.31  ? 197  GLY B C     1 
ATOM   8983  O  O     . GLY B 2 197 ? 137.803 141.205 159.411 1.00 54.47  ? 197  GLY B O     1 
ATOM   8984  N  N     . ASP B 2 198 ? 136.358 141.451 161.107 1.00 56.19  ? 198  ASP B N     1 
ATOM   8985  C  CA    . ASP B 2 198 ? 136.317 142.898 160.975 1.00 51.21  ? 198  ASP B CA    1 
ATOM   8986  C  C     . ASP B 2 198 ? 137.608 143.485 161.529 1.00 53.20  ? 198  ASP B C     1 
ATOM   8987  O  O     . ASP B 2 198 ? 137.919 143.266 162.707 1.00 55.02  ? 198  ASP B O     1 
ATOM   8988  C  CB    . ASP B 2 198 ? 135.101 143.448 161.716 1.00 49.92  ? 198  ASP B CB    1 
ATOM   8989  C  CG    . ASP B 2 198 ? 134.816 144.901 161.392 1.00 57.57  ? 198  ASP B CG    1 
ATOM   8990  O  OD1   . ASP B 2 198 ? 135.625 145.540 160.694 1.00 62.29  ? 198  ASP B OD1   1 
ATOM   8991  O  OD2   . ASP B 2 198 ? 133.768 145.407 161.840 1.00 61.10  ? 198  ASP B OD2   1 
ATOM   8992  N  N     . PRO B 2 199 ? 138.394 144.211 160.729 1.00 61.98  ? 199  PRO B N     1 
ATOM   8993  C  CA    . PRO B 2 199 ? 139.624 144.816 161.265 1.00 64.67  ? 199  PRO B CA    1 
ATOM   8994  C  C     . PRO B 2 199 ? 139.376 145.886 162.313 1.00 68.50  ? 199  PRO B C     1 
ATOM   8995  O  O     . PRO B 2 199 ? 140.300 146.211 163.068 1.00 67.56  ? 199  PRO B O     1 
ATOM   8996  C  CB    . PRO B 2 199 ? 140.301 145.400 160.018 1.00 66.97  ? 199  PRO B CB    1 
ATOM   8997  C  CG    . PRO B 2 199 ? 139.194 145.577 159.033 1.00 65.32  ? 199  PRO B CG    1 
ATOM   8998  C  CD    . PRO B 2 199 ? 138.246 144.449 159.284 1.00 61.66  ? 199  PRO B CD    1 
ATOM   8999  N  N     . GLY B 2 200 ? 138.173 146.449 162.380 1.00 74.98  ? 200  GLY B N     1 
ATOM   9000  C  CA    . GLY B 2 200 ? 137.839 147.466 163.351 1.00 74.81  ? 200  GLY B CA    1 
ATOM   9001  C  C     . GLY B 2 200 ? 137.049 146.998 164.550 1.00 72.46  ? 200  GLY B C     1 
ATOM   9002  O  O     . GLY B 2 200 ? 136.782 147.803 165.447 1.00 75.98  ? 200  GLY B O     1 
ATOM   9003  N  N     . ALA B 2 201 ? 136.662 145.727 164.600 1.00 55.19  ? 201  ALA B N     1 
ATOM   9004  C  CA    . ALA B 2 201 ? 135.899 145.176 165.710 1.00 53.87  ? 201  ALA B CA    1 
ATOM   9005  C  C     . ALA B 2 201 ? 136.717 144.092 166.394 1.00 56.81  ? 201  ALA B C     1 
ATOM   9006  O  O     . ALA B 2 201 ? 137.224 143.181 165.732 1.00 62.45  ? 201  ALA B O     1 
ATOM   9007  C  CB    . ALA B 2 201 ? 134.562 144.607 165.233 1.00 54.13  ? 201  ALA B CB    1 
ATOM   9008  N  N     . PHE B 2 202 ? 136.841 144.190 167.719 1.00 47.64  ? 202  PHE B N     1 
ATOM   9009  C  CA    . PHE B 2 202 ? 137.580 143.201 168.494 1.00 43.89  ? 202  PHE B CA    1 
ATOM   9010  C  C     . PHE B 2 202 ? 136.828 142.809 169.759 1.00 42.98  ? 202  PHE B C     1 
ATOM   9011  O  O     . PHE B 2 202 ? 137.448 142.501 170.782 1.00 49.31  ? 202  PHE B O     1 
ATOM   9012  C  CB    . PHE B 2 202 ? 138.973 143.713 168.855 1.00 45.36  ? 202  PHE B CB    1 
ATOM   9013  C  CG    . PHE B 2 202 ? 139.836 144.006 167.665 1.00 48.85  ? 202  PHE B CG    1 
ATOM   9014  C  CD1   . PHE B 2 202 ? 140.294 142.980 166.858 1.00 50.45  ? 202  PHE B CD1   1 
ATOM   9015  C  CD2   . PHE B 2 202 ? 140.196 145.305 167.358 1.00 52.97  ? 202  PHE B CD2   1 
ATOM   9016  C  CE1   . PHE B 2 202 ? 141.090 143.244 165.763 1.00 50.87  ? 202  PHE B CE1   1 
ATOM   9017  C  CE2   . PHE B 2 202 ? 140.993 145.576 166.263 1.00 55.72  ? 202  PHE B CE2   1 
ATOM   9018  C  CZ    . PHE B 2 202 ? 141.441 144.543 165.466 1.00 53.40  ? 202  PHE B CZ    1 
ATOM   9019  N  N     . MET B 2 203 ? 135.495 142.812 169.704 1.00 36.52  ? 203  MET B N     1 
ATOM   9020  C  CA    . MET B 2 203 ? 134.691 142.523 170.887 1.00 42.31  ? 203  MET B CA    1 
ATOM   9021  C  C     . MET B 2 203 ? 134.778 141.051 171.276 1.00 46.83  ? 203  MET B C     1 
ATOM   9022  O  O     . MET B 2 203 ? 134.963 140.720 172.453 1.00 44.95  ? 203  MET B O     1 
ATOM   9023  C  CB    . MET B 2 203 ? 133.240 142.920 170.629 1.00 42.30  ? 203  MET B CB    1 
ATOM   9024  C  CG    . MET B 2 203 ? 133.082 144.007 169.588 1.00 45.34  ? 203  MET B CG    1 
ATOM   9025  S  SD    . MET B 2 203 ? 131.566 143.808 168.645 1.00 49.04  ? 203  MET B SD    1 
ATOM   9026  C  CE    . MET B 2 203 ? 131.738 142.102 168.134 1.00 41.77  ? 203  MET B CE    1 
ATOM   9027  N  N     . ASP B 2 204 ? 134.635 140.153 170.297 1.00 41.46  ? 204  ASP B N     1 
ATOM   9028  C  CA    . ASP B 2 204 ? 134.652 138.721 170.585 1.00 33.39  ? 204  ASP B CA    1 
ATOM   9029  C  C     . ASP B 2 204 ? 136.011 138.276 171.109 1.00 40.89  ? 204  ASP B C     1 
ATOM   9030  O  O     . ASP B 2 204 ? 136.093 137.463 172.039 1.00 49.93  ? 204  ASP B O     1 
ATOM   9031  C  CB    . ASP B 2 204 ? 134.276 137.933 169.332 1.00 38.33  ? 204  ASP B CB    1 
ATOM   9032  C  CG    . ASP B 2 204 ? 132.929 138.337 168.777 1.00 44.30  ? 204  ASP B CG    1 
ATOM   9033  O  OD1   . ASP B 2 204 ? 132.141 138.952 169.523 1.00 41.85  ? 204  ASP B OD1   1 
ATOM   9034  O  OD2   . ASP B 2 204 ? 132.656 138.038 167.597 1.00 41.19  ? 204  ASP B OD2   1 
ATOM   9035  N  N     . ARG B 2 205 ? 137.088 138.797 170.520 1.00 43.02  ? 205  ARG B N     1 
ATOM   9036  C  CA    . ARG B 2 205 ? 138.422 138.511 171.030 1.00 35.96  ? 205  ARG B CA    1 
ATOM   9037  C  C     . ARG B 2 205 ? 138.592 139.055 172.440 1.00 38.92  ? 205  ARG B C     1 
ATOM   9038  O  O     . ARG B 2 205 ? 139.249 138.432 173.281 1.00 44.63  ? 205  ARG B O     1 
ATOM   9039  C  CB    . ARG B 2 205 ? 139.474 139.104 170.094 1.00 38.29  ? 205  ARG B CB    1 
ATOM   9040  C  CG    . ARG B 2 205 ? 140.896 138.737 170.450 1.00 40.98  ? 205  ARG B CG    1 
ATOM   9041  C  CD    . ARG B 2 205 ? 141.880 139.454 169.554 1.00 42.38  ? 205  ARG B CD    1 
ATOM   9042  N  NE    . ARG B 2 205 ? 141.824 140.898 169.740 1.00 47.59  ? 205  ARG B NE    1 
ATOM   9043  C  CZ    . ARG B 2 205 ? 142.572 141.765 169.074 1.00 50.59  ? 205  ARG B CZ    1 
ATOM   9044  N  NH1   . ARG B 2 205 ? 143.443 141.369 168.163 1.00 49.25  ? 205  ARG B NH1   1 
ATOM   9045  N  NH2   . ARG B 2 205 ? 142.441 143.064 169.330 1.00 46.44  ? 205  ARG B NH2   1 
ATOM   9046  N  N     . ASN B 2 206 ? 138.003 140.220 172.715 1.00 42.32  ? 206  ASN B N     1 
ATOM   9047  C  CA    . ASN B 2 206 ? 138.068 140.792 174.055 1.00 38.40  ? 206  ASN B CA    1 
ATOM   9048  C  C     . ASN B 2 206 ? 137.369 139.898 175.069 1.00 38.34  ? 206  ASN B C     1 
ATOM   9049  O  O     . ASN B 2 206 ? 137.841 139.744 176.201 1.00 46.90  ? 206  ASN B O     1 
ATOM   9050  C  CB    . ASN B 2 206 ? 137.450 142.188 174.050 1.00 37.56  ? 206  ASN B CB    1 
ATOM   9051  C  CG    . ASN B 2 206 ? 138.277 143.189 174.817 1.00 44.42  ? 206  ASN B CG    1 
ATOM   9052  O  OD1   . ASN B 2 206 ? 137.921 143.585 175.926 1.00 49.38  ? 206  ASN B OD1   1 
ATOM   9053  N  ND2   . ASN B 2 206 ? 139.395 143.600 174.235 1.00 45.34  ? 206  ASN B ND2   1 
ATOM   9054  N  N     . VAL B 2 207 ? 136.237 139.307 174.687 1.00 36.11  ? 207  VAL B N     1 
ATOM   9055  C  CA    . VAL B 2 207 ? 135.559 138.372 175.581 1.00 37.95  ? 207  VAL B CA    1 
ATOM   9056  C  C     . VAL B 2 207 ? 136.395 137.111 175.771 1.00 39.45  ? 207  VAL B C     1 
ATOM   9057  O  O     . VAL B 2 207 ? 136.506 136.587 176.885 1.00 44.78  ? 207  VAL B O     1 
ATOM   9058  C  CB    . VAL B 2 207 ? 134.150 138.047 175.054 1.00 44.03  ? 207  VAL B CB    1 
ATOM   9059  C  CG1   . VAL B 2 207 ? 133.414 137.155 176.031 1.00 37.23  ? 207  VAL B CG1   1 
ATOM   9060  C  CG2   . VAL B 2 207 ? 133.369 139.319 174.820 1.00 43.16  ? 207  VAL B CG2   1 
ATOM   9061  N  N     . LEU B 2 208 ? 136.996 136.605 174.692 1.00 41.94  ? 208  LEU B N     1 
ATOM   9062  C  CA    . LEU B 2 208 ? 137.805 135.393 174.801 1.00 43.17  ? 208  LEU B CA    1 
ATOM   9063  C  C     . LEU B 2 208 ? 139.064 135.612 175.630 1.00 41.46  ? 208  LEU B C     1 
ATOM   9064  O  O     . LEU B 2 208 ? 139.583 134.662 176.227 1.00 40.83  ? 208  LEU B O     1 
ATOM   9065  C  CB    . LEU B 2 208 ? 138.185 134.877 173.415 1.00 34.93  ? 208  LEU B CB    1 
ATOM   9066  C  CG    . LEU B 2 208 ? 137.194 133.952 172.715 1.00 35.42  ? 208  LEU B CG    1 
ATOM   9067  C  CD1   . LEU B 2 208 ? 137.884 133.270 171.564 1.00 36.89  ? 208  LEU B CD1   1 
ATOM   9068  C  CD2   . LEU B 2 208 ? 136.632 132.928 173.678 1.00 40.20  ? 208  LEU B CD2   1 
ATOM   9069  N  N     . GLU B 2 209 ? 139.578 136.837 175.671 1.00 38.64  ? 209  GLU B N     1 
ATOM   9070  C  CA    . GLU B 2 209 ? 140.785 137.116 176.441 1.00 32.10  ? 209  GLU B CA    1 
ATOM   9071  C  C     . GLU B 2 209 ? 140.463 137.481 177.888 1.00 38.85  ? 209  GLU B C     1 
ATOM   9072  O  O     . GLU B 2 209 ? 140.961 136.844 178.820 1.00 41.53  ? 209  GLU B O     1 
ATOM   9073  C  CB    . GLU B 2 209 ? 141.588 138.237 175.771 1.00 37.32  ? 209  GLU B CB    1 
ATOM   9074  C  CG    . GLU B 2 209 ? 142.211 137.848 174.449 1.00 35.96  ? 209  GLU B CG    1 
ATOM   9075  C  CD    . GLU B 2 209 ? 142.881 139.014 173.759 1.00 40.50  ? 209  GLU B CD    1 
ATOM   9076  O  OE1   . GLU B 2 209 ? 142.913 140.115 174.342 1.00 45.85  ? 209  GLU B OE1   1 
ATOM   9077  O  OE2   . GLU B 2 209 ? 143.375 138.832 172.629 1.00 42.87  ? 209  GLU B OE2   1 
ATOM   9078  N  N     . GLY B 2 210 ? 139.643 138.513 178.087 1.00 42.99  ? 210  GLY B N     1 
ATOM   9079  C  CA    . GLY B 2 210 ? 139.386 139.000 179.432 1.00 41.44  ? 210  GLY B CA    1 
ATOM   9080  C  C     . GLY B 2 210 ? 138.617 138.021 180.298 1.00 43.75  ? 210  GLY B C     1 
ATOM   9081  O  O     . GLY B 2 210 ? 138.958 137.813 181.465 1.00 50.48  ? 210  GLY B O     1 
ATOM   9082  N  N     . ASP B 2 211 ? 137.569 137.412 179.750 1.00 43.87  ? 211  ASP B N     1 
ATOM   9083  C  CA    . ASP B 2 211 ? 136.702 136.508 180.504 1.00 45.08  ? 211  ASP B CA    1 
ATOM   9084  C  C     . ASP B 2 211 ? 136.472 135.227 179.709 1.00 45.31  ? 211  ASP B C     1 
ATOM   9085  O  O     . ASP B 2 211 ? 135.369 134.980 179.210 1.00 45.89  ? 211  ASP B O     1 
ATOM   9086  C  CB    . ASP B 2 211 ? 135.378 137.194 180.842 1.00 42.47  ? 211  ASP B CB    1 
ATOM   9087  C  CG    . ASP B 2 211 ? 134.685 136.570 182.031 1.00 48.31  ? 211  ASP B CG    1 
ATOM   9088  O  OD1   . ASP B 2 211 ? 135.199 135.566 182.561 1.00 51.26  ? 211  ASP B OD1   1 
ATOM   9089  O  OD2   . ASP B 2 211 ? 133.626 137.087 182.438 1.00 45.82  ? 211  ASP B OD2   1 
ATOM   9090  N  N     . PRO B 2 212 ? 137.500 134.381 179.580 1.00 37.71  ? 212  PRO B N     1 
ATOM   9091  C  CA    . PRO B 2 212 ? 137.325 133.150 178.795 1.00 34.27  ? 212  PRO B CA    1 
ATOM   9092  C  C     . PRO B 2 212 ? 136.434 132.127 179.472 1.00 36.39  ? 212  PRO B C     1 
ATOM   9093  O  O     . PRO B 2 212 ? 135.756 131.355 178.780 1.00 40.72  ? 212  PRO B O     1 
ATOM   9094  C  CB    . PRO B 2 212 ? 138.760 132.631 178.639 1.00 38.37  ? 212  PRO B CB    1 
ATOM   9095  C  CG    . PRO B 2 212 ? 139.462 133.140 179.840 1.00 36.27  ? 212  PRO B CG    1 
ATOM   9096  C  CD    . PRO B 2 212 ? 138.851 134.476 180.160 1.00 39.85  ? 212  PRO B CD    1 
ATOM   9097  N  N     . HIS B 2 213 ? 136.414 132.097 180.805 1.00 37.18  ? 213  HIS B N     1 
ATOM   9098  C  CA    . HIS B 2 213 ? 135.584 131.126 181.506 1.00 39.02  ? 213  HIS B CA    1 
ATOM   9099  C  C     . HIS B 2 213 ? 134.103 131.400 181.297 1.00 36.98  ? 213  HIS B C     1 
ATOM   9100  O  O     . HIS B 2 213 ? 133.293 130.476 181.372 1.00 34.91  ? 213  HIS B O     1 
ATOM   9101  C  CB    . HIS B 2 213 ? 135.920 131.119 182.994 1.00 40.81  ? 213  HIS B CB    1 
ATOM   9102  C  CG    . HIS B 2 213 ? 137.266 130.546 183.305 1.00 38.41  ? 213  HIS B CG    1 
ATOM   9103  N  ND1   . HIS B 2 213 ? 137.512 129.190 183.316 1.00 36.99  ? 213  HIS B ND1   1 
ATOM   9104  C  CD2   . HIS B 2 213 ? 138.438 131.144 183.624 1.00 39.16  ? 213  HIS B CD2   1 
ATOM   9105  C  CE1   . HIS B 2 213 ? 138.778 128.978 183.625 1.00 39.69  ? 213  HIS B CE1   1 
ATOM   9106  N  NE2   . HIS B 2 213 ? 139.363 130.147 183.816 1.00 42.67  ? 213  HIS B NE2   1 
ATOM   9107  N  N     . ARG B 2 214 ? 133.732 132.650 181.021 1.00 40.44  ? 214  ARG B N     1 
ATOM   9108  C  CA    . ARG B 2 214 ? 132.350 132.952 180.667 1.00 36.84  ? 214  ARG B CA    1 
ATOM   9109  C  C     . ARG B 2 214 ? 131.953 132.254 179.372 1.00 34.59  ? 214  ARG B C     1 
ATOM   9110  O  O     . ARG B 2 214 ? 130.880 131.643 179.286 1.00 41.05  ? 214  ARG B O     1 
ATOM   9111  C  CB    . ARG B 2 214 ? 132.174 134.466 180.552 1.00 40.55  ? 214  ARG B CB    1 
ATOM   9112  C  CG    . ARG B 2 214 ? 130.821 134.922 180.067 1.00 38.83  ? 214  ARG B CG    1 
ATOM   9113  C  CD    . ARG B 2 214 ? 130.709 136.436 180.145 1.00 36.10  ? 214  ARG B CD    1 
ATOM   9114  N  NE    . ARG B 2 214 ? 130.568 136.898 181.518 1.00 35.48  ? 214  ARG B NE    1 
ATOM   9115  C  CZ    . ARG B 2 214 ? 129.408 137.019 182.148 1.00 41.63  ? 214  ARG B CZ    1 
ATOM   9116  N  NH1   . ARG B 2 214 ? 128.263 136.741 181.548 1.00 43.63  ? 214  ARG B NH1   1 
ATOM   9117  N  NH2   . ARG B 2 214 ? 129.397 137.422 183.414 1.00 39.39  ? 214  ARG B NH2   1 
ATOM   9118  N  N     . VAL B 2 215 ? 132.826 132.306 178.365 1.00 35.38  ? 215  VAL B N     1 
ATOM   9119  C  CA    . VAL B 2 215 ? 132.568 131.609 177.110 1.00 33.73  ? 215  VAL B CA    1 
ATOM   9120  C  C     . VAL B 2 215 ? 132.547 130.102 177.327 1.00 37.16  ? 215  VAL B C     1 
ATOM   9121  O  O     . VAL B 2 215 ? 131.692 129.396 176.782 1.00 41.78  ? 215  VAL B O     1 
ATOM   9122  C  CB    . VAL B 2 215 ? 133.613 132.014 176.057 1.00 33.18  ? 215  VAL B CB    1 
ATOM   9123  C  CG1   . VAL B 2 215 ? 133.219 131.491 174.691 1.00 31.91  ? 215  VAL B CG1   1 
ATOM   9124  C  CG2   . VAL B 2 215 ? 133.773 133.517 176.034 1.00 37.79  ? 215  VAL B CG2   1 
ATOM   9125  N  N     . ILE B 2 216 ? 133.485 129.586 178.125 1.00 44.09  ? 216  ILE B N     1 
ATOM   9126  C  CA    . ILE B 2 216 ? 133.545 128.147 178.379 1.00 35.87  ? 216  ILE B CA    1 
ATOM   9127  C  C     . ILE B 2 216 ? 132.282 127.670 179.090 1.00 30.17  ? 216  ILE B C     1 
ATOM   9128  O  O     . ILE B 2 216 ? 131.712 126.628 178.746 1.00 35.73  ? 216  ILE B O     1 
ATOM   9129  C  CB    . ILE B 2 216 ? 134.816 127.805 179.177 1.00 31.80  ? 216  ILE B CB    1 
ATOM   9130  C  CG1   . ILE B 2 216 ? 136.060 128.158 178.362 1.00 30.78  ? 216  ILE B CG1   1 
ATOM   9131  C  CG2   . ILE B 2 216 ? 134.836 126.339 179.562 1.00 35.64  ? 216  ILE B CG2   1 
ATOM   9132  C  CD1   . ILE B 2 216 ? 137.347 127.984 179.116 1.00 39.09  ? 216  ILE B CD1   1 
ATOM   9133  N  N     . GLU B 2 217 ? 131.820 128.430 180.083 1.00 40.78  ? 217  GLU B N     1 
ATOM   9134  C  CA    . GLU B 2 217 ? 130.609 128.074 180.811 1.00 43.67  ? 217  GLU B CA    1 
ATOM   9135  C  C     . GLU B 2 217 ? 129.379 128.151 179.916 1.00 42.54  ? 217  GLU B C     1 
ATOM   9136  O  O     . GLU B 2 217 ? 128.497 127.288 179.993 1.00 49.58  ? 217  GLU B O     1 
ATOM   9137  C  CB    . GLU B 2 217 ? 130.454 128.986 182.024 1.00 42.10  ? 217  GLU B CB    1 
ATOM   9138  C  CG    . GLU B 2 217 ? 129.246 128.690 182.874 1.00 41.94  ? 217  GLU B CG    1 
ATOM   9139  C  CD    . GLU B 2 217 ? 129.142 129.624 184.049 1.00 52.95  ? 217  GLU B CD    1 
ATOM   9140  O  OE1   . GLU B 2 217 ? 130.006 130.516 184.172 1.00 56.55  ? 217  GLU B OE1   1 
ATOM   9141  O  OE2   . GLU B 2 217 ? 128.201 129.469 184.851 1.00 53.49  ? 217  GLU B OE2   1 
ATOM   9142  N  N     . GLY B 2 218 ? 129.301 129.177 179.066 1.00 31.26  ? 218  GLY B N     1 
ATOM   9143  C  CA    . GLY B 2 218 ? 128.211 129.241 178.110 1.00 20.84  ? 218  GLY B CA    1 
ATOM   9144  C  C     . GLY B 2 218 ? 128.204 128.054 177.168 1.00 34.82  ? 218  GLY B C     1 
ATOM   9145  O  O     . GLY B 2 218 ? 127.147 127.503 176.856 1.00 44.01  ? 218  GLY B O     1 
ATOM   9146  N  N     . MET B 2 219 ? 129.388 127.634 176.719 1.00 34.36  ? 219  MET B N     1 
ATOM   9147  C  CA    . MET B 2 219 ? 129.478 126.485 175.826 1.00 24.26  ? 219  MET B CA    1 
ATOM   9148  C  C     . MET B 2 219 ? 129.084 125.193 176.533 1.00 29.55  ? 219  MET B C     1 
ATOM   9149  O  O     . MET B 2 219 ? 128.445 124.328 175.931 1.00 32.36  ? 219  MET B O     1 
ATOM   9150  C  CB    . MET B 2 219 ? 130.886 126.378 175.246 1.00 25.30  ? 219  MET B CB    1 
ATOM   9151  C  CG    . MET B 2 219 ? 131.244 127.515 174.310 1.00 20.32  ? 219  MET B CG    1 
ATOM   9152  S  SD    . MET B 2 219 ? 132.873 127.346 173.571 1.00 28.46  ? 219  MET B SD    1 
ATOM   9153  C  CE    . MET B 2 219 ? 132.603 125.919 172.529 1.00 35.96  ? 219  MET B CE    1 
ATOM   9154  N  N     . ILE B 2 220 ? 129.445 125.042 177.808 1.00 35.28  ? 220  ILE B N     1 
ATOM   9155  C  CA    . ILE B 2 220 ? 129.063 123.831 178.532 1.00 32.03  ? 220  ILE B CA    1 
ATOM   9156  C  C     . ILE B 2 220 ? 127.556 123.804 178.781 1.00 30.40  ? 220  ILE B C     1 
ATOM   9157  O  O     . ILE B 2 220 ? 126.914 122.750 178.677 1.00 38.19  ? 220  ILE B O     1 
ATOM   9158  C  CB    . ILE B 2 220 ? 129.867 123.700 179.838 1.00 33.52  ? 220  ILE B CB    1 
ATOM   9159  C  CG1   . ILE B 2 220 ? 131.361 123.626 179.534 1.00 35.09  ? 220  ILE B CG1   1 
ATOM   9160  C  CG2   . ILE B 2 220 ? 129.478 122.439 180.575 1.00 38.21  ? 220  ILE B CG2   1 
ATOM   9161  C  CD1   . ILE B 2 220 ? 132.234 123.681 180.758 1.00 39.37  ? 220  ILE B CD1   1 
ATOM   9162  N  N     . ILE B 2 221 ? 126.962 124.959 179.095 1.00 35.10  ? 221  ILE B N     1 
ATOM   9163  C  CA    . ILE B 2 221 ? 125.511 125.030 179.257 1.00 37.02  ? 221  ILE B CA    1 
ATOM   9164  C  C     . ILE B 2 221 ? 124.808 124.703 177.945 1.00 37.93  ? 221  ILE B C     1 
ATOM   9165  O  O     . ILE B 2 221 ? 123.835 123.938 177.915 1.00 44.58  ? 221  ILE B O     1 
ATOM   9166  C  CB    . ILE B 2 221 ? 125.100 126.417 179.786 1.00 37.97  ? 221  ILE B CB    1 
ATOM   9167  C  CG1   . ILE B 2 221 ? 125.631 126.633 181.201 1.00 38.51  ? 221  ILE B CG1   1 
ATOM   9168  C  CG2   . ILE B 2 221 ? 123.595 126.575 179.763 1.00 39.57  ? 221  ILE B CG2   1 
ATOM   9169  C  CD1   . ILE B 2 221 ? 125.507 128.057 181.676 1.00 37.36  ? 221  ILE B CD1   1 
ATOM   9170  N  N     . GLY B 2 222 ? 125.297 125.268 176.839 1.00 29.11  ? 222  GLY B N     1 
ATOM   9171  C  CA    . GLY B 2 222 ? 124.705 124.978 175.546 1.00 31.43  ? 222  GLY B CA    1 
ATOM   9172  C  C     . GLY B 2 222 ? 124.877 123.530 175.131 1.00 38.84  ? 222  GLY B C     1 
ATOM   9173  O  O     . GLY B 2 222 ? 123.986 122.946 174.516 1.00 37.11  ? 222  GLY B O     1 
ATOM   9174  N  N     . ALA B 2 223 ? 126.023 122.933 175.460 1.00 40.15  ? 223  ALA B N     1 
ATOM   9175  C  CA    . ALA B 2 223 ? 126.263 121.535 175.126 1.00 30.58  ? 223  ALA B CA    1 
ATOM   9176  C  C     . ALA B 2 223 ? 125.367 120.612 175.936 1.00 30.54  ? 223  ALA B C     1 
ATOM   9177  O  O     . ALA B 2 223 ? 124.881 119.601 175.419 1.00 39.42  ? 223  ALA B O     1 
ATOM   9178  C  CB    . ALA B 2 223 ? 127.732 121.189 175.355 1.00 30.23  ? 223  ALA B CB    1 
ATOM   9179  N  N     . TYR B 2 224 ? 125.151 120.932 177.213 1.00 41.14  ? 224  TYR B N     1 
ATOM   9180  C  CA    . TYR B 2 224 ? 124.228 120.143 178.020 1.00 44.51  ? 224  TYR B CA    1 
ATOM   9181  C  C     . TYR B 2 224 ? 122.797 120.299 177.522 1.00 46.14  ? 224  TYR B C     1 
ATOM   9182  O  O     . TYR B 2 224 ? 122.022 119.336 177.540 1.00 53.86  ? 224  TYR B O     1 
ATOM   9183  C  CB    . TYR B 2 224 ? 124.345 120.540 179.491 1.00 49.33  ? 224  TYR B CB    1 
ATOM   9184  C  CG    . TYR B 2 224 ? 123.452 119.747 180.415 1.00 50.29  ? 224  TYR B CG    1 
ATOM   9185  C  CD1   . TYR B 2 224 ? 123.432 118.361 180.374 1.00 49.95  ? 224  TYR B CD1   1 
ATOM   9186  C  CD2   . TYR B 2 224 ? 122.634 120.384 181.336 1.00 50.88  ? 224  TYR B CD2   1 
ATOM   9187  C  CE1   . TYR B 2 224 ? 122.617 117.633 181.215 1.00 49.14  ? 224  TYR B CE1   1 
ATOM   9188  C  CE2   . TYR B 2 224 ? 121.817 119.664 182.181 1.00 52.25  ? 224  TYR B CE2   1 
ATOM   9189  C  CZ    . TYR B 2 224 ? 121.813 118.290 182.116 1.00 54.10  ? 224  TYR B CZ    1 
ATOM   9190  O  OH    . TYR B 2 224 ? 121.001 117.567 182.958 1.00 57.11  ? 224  TYR B OH    1 
ATOM   9191  N  N     . ALA B 2 225 ? 122.428 121.501 177.070 1.00 35.19  ? 225  ALA B N     1 
ATOM   9192  C  CA    . ALA B 2 225 ? 121.085 121.707 176.533 1.00 33.83  ? 225  ALA B CA    1 
ATOM   9193  C  C     . ALA B 2 225 ? 120.887 120.976 175.209 1.00 39.30  ? 225  ALA B C     1 
ATOM   9194  O  O     . ALA B 2 225 ? 119.826 120.389 174.971 1.00 47.30  ? 225  ALA B O     1 
ATOM   9195  C  CB    . ALA B 2 225 ? 120.812 123.200 176.365 1.00 40.67  ? 225  ALA B CB    1 
ATOM   9196  N  N     . ILE B 2 226 ? 121.892 121.001 174.338 1.00 33.45  ? 226  ILE B N     1 
ATOM   9197  C  CA    . ILE B 2 226 ? 121.758 120.426 173.005 1.00 30.65  ? 226  ILE B CA    1 
ATOM   9198  C  C     . ILE B 2 226 ? 122.004 118.923 173.030 1.00 26.55  ? 226  ILE B C     1 
ATOM   9199  O  O     . ILE B 2 226 ? 121.302 118.155 172.363 1.00 32.57  ? 226  ILE B O     1 
ATOM   9200  C  CB    . ILE B 2 226 ? 122.719 121.139 172.037 1.00 26.75  ? 226  ILE B CB    1 
ATOM   9201  C  CG1   . ILE B 2 226 ? 122.312 122.598 171.854 1.00 30.79  ? 226  ILE B CG1   1 
ATOM   9202  C  CG2   . ILE B 2 226 ? 122.765 120.431 170.698 1.00 31.55  ? 226  ILE B CG2   1 
ATOM   9203  C  CD1   . ILE B 2 226 ? 123.368 123.431 171.183 1.00 31.40  ? 226  ILE B CD1   1 
ATOM   9204  N  N     . GLY B 2 227 ? 122.990 118.481 173.795 1.00 31.77  ? 227  GLY B N     1 
ATOM   9205  C  CA    . GLY B 2 227 ? 123.440 117.113 173.753 1.00 32.76  ? 227  GLY B CA    1 
ATOM   9206  C  C     . GLY B 2 227 ? 124.735 116.908 173.006 1.00 35.05  ? 227  GLY B C     1 
ATOM   9207  O  O     . GLY B 2 227 ? 124.919 115.845 172.403 1.00 44.31  ? 227  GLY B O     1 
ATOM   9208  N  N     . ALA B 2 228 ? 125.628 117.889 173.012 1.00 26.46  ? 228  ALA B N     1 
ATOM   9209  C  CA    . ALA B 2 228 ? 126.888 117.779 172.301 1.00 27.63  ? 228  ALA B CA    1 
ATOM   9210  C  C     . ALA B 2 228 ? 127.909 117.010 173.132 1.00 33.58  ? 228  ALA B C     1 
ATOM   9211  O  O     . ALA B 2 228 ? 127.835 116.951 174.361 1.00 43.34  ? 228  ALA B O     1 
ATOM   9212  C  CB    . ALA B 2 228 ? 127.433 119.163 171.950 1.00 25.96  ? 228  ALA B CB    1 
ATOM   9213  N  N     . THR B 2 229 ? 128.870 116.410 172.436 1.00 34.15  ? 229  THR B N     1 
ATOM   9214  C  CA    . THR B 2 229 ? 129.950 115.676 173.078 1.00 35.75  ? 229  THR B CA    1 
ATOM   9215  C  C     . THR B 2 229 ? 131.311 116.323 172.896 1.00 36.46  ? 229  THR B C     1 
ATOM   9216  O  O     . THR B 2 229 ? 132.161 116.197 173.778 1.00 40.25  ? 229  THR B O     1 
ATOM   9217  C  CB    . THR B 2 229 ? 130.007 114.239 172.546 1.00 42.91  ? 229  THR B CB    1 
ATOM   9218  O  OG1   . THR B 2 229 ? 130.031 114.258 171.115 1.00 43.78  ? 229  THR B OG1   1 
ATOM   9219  C  CG2   . THR B 2 229 ? 128.799 113.453 173.015 1.00 42.43  ? 229  THR B CG2   1 
ATOM   9220  N  N     . LYS B 2 230 ? 131.533 117.010 171.780 1.00 28.24  ? 230  LYS B N     1 
ATOM   9221  C  CA    . LYS B 2 230 ? 132.768 117.736 171.533 1.00 23.18  ? 230  LYS B CA    1 
ATOM   9222  C  C     . LYS B 2 230 ? 132.446 119.183 171.198 1.00 30.97  ? 230  LYS B C     1 
ATOM   9223  O  O     . LYS B 2 230 ? 131.429 119.481 170.568 1.00 43.81  ? 230  LYS B O     1 
ATOM   9224  C  CB    . LYS B 2 230 ? 133.577 117.112 170.392 1.00 29.79  ? 230  LYS B CB    1 
ATOM   9225  C  CG    . LYS B 2 230 ? 134.104 115.725 170.687 1.00 39.57  ? 230  LYS B CG    1 
ATOM   9226  C  CD    . LYS B 2 230 ? 134.852 115.160 169.492 1.00 35.31  ? 230  LYS B CD    1 
ATOM   9227  C  CE    . LYS B 2 230 ? 135.987 116.075 169.077 1.00 33.47  ? 230  LYS B CE    1 
ATOM   9228  N  NZ    . LYS B 2 230 ? 136.918 116.323 170.203 1.00 34.17  ? 230  LYS B NZ    1 
ATOM   9229  N  N     . GLY B 2 231 ? 133.322 120.077 171.629 1.00 27.40  ? 231  GLY B N     1 
ATOM   9230  C  CA    . GLY B 2 231 ? 133.169 121.502 171.376 1.00 22.32  ? 231  GLY B CA    1 
ATOM   9231  C  C     . GLY B 2 231 ? 134.397 122.061 170.688 1.00 19.90  ? 231  GLY B C     1 
ATOM   9232  O  O     . GLY B 2 231 ? 135.525 121.716 171.040 1.00 30.66  ? 231  GLY B O     1 
ATOM   9233  N  N     . PHE B 2 232 ? 134.169 122.928 169.708 1.00 10.46  ? 232  PHE B N     1 
ATOM   9234  C  CA    . PHE B 2 232 ? 135.239 123.539 168.936 1.00 14.19  ? 232  PHE B CA    1 
ATOM   9235  C  C     . PHE B 2 232 ? 135.193 125.047 169.119 1.00 22.18  ? 232  PHE B C     1 
ATOM   9236  O  O     . PHE B 2 232 ? 134.131 125.660 168.986 1.00 35.84  ? 232  PHE B O     1 
ATOM   9237  C  CB    . PHE B 2 232 ? 135.122 123.185 167.453 1.00 21.49  ? 232  PHE B CB    1 
ATOM   9238  C  CG    . PHE B 2 232 ? 135.120 121.712 167.180 1.00 23.83  ? 232  PHE B CG    1 
ATOM   9239  C  CD1   . PHE B 2 232 ? 136.307 121.022 167.018 1.00 26.10  ? 232  PHE B CD1   1 
ATOM   9240  C  CD2   . PHE B 2 232 ? 133.931 121.015 167.083 1.00 20.36  ? 232  PHE B CD2   1 
ATOM   9241  C  CE1   . PHE B 2 232 ? 136.307 119.669 166.764 1.00 21.13  ? 232  PHE B CE1   1 
ATOM   9242  C  CE2   . PHE B 2 232 ? 133.927 119.661 166.829 1.00 20.33  ? 232  PHE B CE2   1 
ATOM   9243  C  CZ    . PHE B 2 232 ? 135.116 118.988 166.669 1.00 22.52  ? 232  PHE B CZ    1 
ATOM   9244  N  N     . ILE B 2 233 ? 136.336 125.640 169.428 1.00 15.64  ? 233  ILE B N     1 
ATOM   9245  C  CA    . ILE B 2 233 ? 136.464 127.088 169.498 1.00 18.02  ? 233  ILE B CA    1 
ATOM   9246  C  C     . ILE B 2 233 ? 137.257 127.511 168.271 1.00 25.29  ? 233  ILE B C     1 
ATOM   9247  O  O     . ILE B 2 233 ? 138.485 127.383 168.235 1.00 33.26  ? 233  ILE B O     1 
ATOM   9248  C  CB    . ILE B 2 233 ? 137.136 127.554 170.793 1.00 14.99  ? 233  ILE B CB    1 
ATOM   9249  C  CG1   . ILE B 2 233 ? 136.332 127.086 172.004 1.00 18.32  ? 233  ILE B CG1   1 
ATOM   9250  C  CG2   . ILE B 2 233 ? 137.263 129.065 170.801 1.00 16.37  ? 233  ILE B CG2   1 
ATOM   9251  C  CD1   . ILE B 2 233 ? 136.860 127.599 173.314 1.00 23.88  ? 233  ILE B CD1   1 
ATOM   9252  N  N     . TYR B 2 234 ? 136.554 128.007 167.259 1.00 24.70  ? 234  TYR B N     1 
ATOM   9253  C  CA    . TYR B 2 234 ? 137.187 128.434 166.016 1.00 23.52  ? 234  TYR B CA    1 
ATOM   9254  C  C     . TYR B 2 234 ? 137.709 129.849 166.213 1.00 21.05  ? 234  TYR B C     1 
ATOM   9255  O  O     . TYR B 2 234 ? 136.965 130.823 166.091 1.00 19.87  ? 234  TYR B O     1 
ATOM   9256  C  CB    . TYR B 2 234 ? 136.202 128.356 164.856 1.00 20.01  ? 234  TYR B CB    1 
ATOM   9257  C  CG    . TYR B 2 234 ? 136.833 128.583 163.503 1.00 22.24  ? 234  TYR B CG    1 
ATOM   9258  C  CD1   . TYR B 2 234 ? 137.376 127.529 162.786 1.00 29.06  ? 234  TYR B CD1   1 
ATOM   9259  C  CD2   . TYR B 2 234 ? 136.886 129.850 162.943 1.00 17.43  ? 234  TYR B CD2   1 
ATOM   9260  C  CE1   . TYR B 2 234 ? 137.950 127.729 161.550 1.00 24.92  ? 234  TYR B CE1   1 
ATOM   9261  C  CE2   . TYR B 2 234 ? 137.460 130.059 161.708 1.00 20.52  ? 234  TYR B CE2   1 
ATOM   9262  C  CZ    . TYR B 2 234 ? 137.989 128.997 161.016 1.00 24.92  ? 234  TYR B CZ    1 
ATOM   9263  O  OH    . TYR B 2 234 ? 138.561 129.204 159.785 1.00 37.21  ? 234  TYR B OH    1 
ATOM   9264  N  N     . VAL B 2 235 ? 138.995 129.961 166.519 1.00 22.67  ? 235  VAL B N     1 
ATOM   9265  C  CA    . VAL B 2 235 ? 139.658 131.239 166.727 1.00 21.58  ? 235  VAL B CA    1 
ATOM   9266  C  C     . VAL B 2 235 ? 140.880 131.281 165.822 1.00 18.83  ? 235  VAL B C     1 
ATOM   9267  O  O     . VAL B 2 235 ? 141.530 130.256 165.599 1.00 29.38  ? 235  VAL B O     1 
ATOM   9268  C  CB    . VAL B 2 235 ? 140.037 131.443 168.213 1.00 24.12  ? 235  VAL B CB    1 
ATOM   9269  C  CG1   . VAL B 2 235 ? 140.892 130.294 168.718 1.00 26.84  ? 235  VAL B CG1   1 
ATOM   9270  C  CG2   . VAL B 2 235 ? 140.734 132.773 168.430 1.00 23.47  ? 235  VAL B CG2   1 
ATOM   9271  N  N     . ARG B 2 236 ? 141.167 132.454 165.268 1.00 19.89  ? 236  ARG B N     1 
ATOM   9272  C  CA    . ARG B 2 236 ? 142.306 132.593 164.373 1.00 22.59  ? 236  ARG B CA    1 
ATOM   9273  C  C     . ARG B 2 236 ? 143.617 132.359 165.110 1.00 28.30  ? 236  ARG B C     1 
ATOM   9274  O  O     . ARG B 2 236 ? 143.769 132.726 166.277 1.00 33.48  ? 236  ARG B O     1 
ATOM   9275  C  CB    . ARG B 2 236 ? 142.320 133.978 163.737 1.00 23.71  ? 236  ARG B CB    1 
ATOM   9276  C  CG    . ARG B 2 236 ? 141.204 134.221 162.760 1.00 23.64  ? 236  ARG B CG    1 
ATOM   9277  C  CD    . ARG B 2 236 ? 141.436 135.508 162.002 1.00 31.59  ? 236  ARG B CD    1 
ATOM   9278  N  NE    . ARG B 2 236 ? 140.369 135.770 161.047 1.00 32.73  ? 236  ARG B NE    1 
ATOM   9279  C  CZ    . ARG B 2 236 ? 140.350 136.801 160.215 1.00 32.37  ? 236  ARG B CZ    1 
ATOM   9280  N  NH1   . ARG B 2 236 ? 141.331 137.686 160.190 1.00 34.00  ? 236  ARG B NH1   1 
ATOM   9281  N  NH2   . ARG B 2 236 ? 139.321 136.946 159.388 1.00 37.72  ? 236  ARG B NH2   1 
ATOM   9282  N  N     . ALA B 2 237 ? 144.571 131.743 164.412 1.00 27.42  ? 237  ALA B N     1 
ATOM   9283  C  CA    . ALA B 2 237 ? 145.932 131.646 164.921 1.00 26.11  ? 237  ALA B CA    1 
ATOM   9284  C  C     . ALA B 2 237 ? 146.633 132.996 164.953 1.00 35.98  ? 237  ALA B C     1 
ATOM   9285  O  O     . ALA B 2 237 ? 147.709 133.103 165.551 1.00 45.09  ? 237  ALA B O     1 
ATOM   9286  C  CB    . ALA B 2 237 ? 146.736 130.657 164.080 1.00 31.37  ? 237  ALA B CB    1 
ATOM   9287  N  N     . GLU B 2 238 ? 146.055 134.018 164.321 1.00 38.71  ? 238  GLU B N     1 
ATOM   9288  C  CA    . GLU B 2 238 ? 146.521 135.392 164.444 1.00 36.00  ? 238  GLU B CA    1 
ATOM   9289  C  C     . GLU B 2 238 ? 146.220 135.987 165.815 1.00 38.98  ? 238  GLU B C     1 
ATOM   9290  O  O     . GLU B 2 238 ? 146.703 137.082 166.119 1.00 44.40  ? 238  GLU B O     1 
ATOM   9291  C  CB    . GLU B 2 238 ? 145.879 136.247 163.349 1.00 34.08  ? 238  GLU B CB    1 
ATOM   9292  C  CG    . GLU B 2 238 ? 146.584 137.557 163.058 1.00 36.43  ? 238  GLU B CG    1 
ATOM   9293  C  CD    . GLU B 2 238 ? 145.737 138.493 162.224 1.00 46.20  ? 238  GLU B CD    1 
ATOM   9294  O  OE1   . GLU B 2 238 ? 144.580 138.136 161.923 1.00 50.46  ? 238  GLU B OE1   1 
ATOM   9295  O  OE2   . GLU B 2 238 ? 146.227 139.586 161.872 1.00 46.90  ? 238  GLU B OE2   1 
ATOM   9296  N  N     . TYR B 2 239 ? 145.427 135.304 166.638 1.00 32.42  ? 239  TYR B N     1 
ATOM   9297  C  CA    . TYR B 2 239 ? 145.143 135.734 168.001 1.00 29.02  ? 239  TYR B CA    1 
ATOM   9298  C  C     . TYR B 2 239 ? 145.871 134.811 168.970 1.00 31.68  ? 239  TYR B C     1 
ATOM   9299  O  O     . TYR B 2 239 ? 145.268 133.862 169.485 1.00 35.88  ? 239  TYR B O     1 
ATOM   9300  C  CB    . TYR B 2 239 ? 143.639 135.709 168.292 1.00 27.88  ? 239  TYR B CB    1 
ATOM   9301  C  CG    . TYR B 2 239 ? 142.760 136.417 167.283 1.00 32.86  ? 239  TYR B CG    1 
ATOM   9302  C  CD1   . TYR B 2 239 ? 143.214 137.522 166.577 1.00 35.97  ? 239  TYR B CD1   1 
ATOM   9303  C  CD2   . TYR B 2 239 ? 141.465 135.979 167.046 1.00 31.79  ? 239  TYR B CD2   1 
ATOM   9304  C  CE1   . TYR B 2 239 ? 142.407 138.162 165.660 1.00 39.21  ? 239  TYR B CE1   1 
ATOM   9305  C  CE2   . TYR B 2 239 ? 140.652 136.613 166.132 1.00 31.08  ? 239  TYR B CE2   1 
ATOM   9306  C  CZ    . TYR B 2 239 ? 141.127 137.703 165.442 1.00 34.57  ? 239  TYR B CZ    1 
ATOM   9307  O  OH    . TYR B 2 239 ? 140.320 138.337 164.531 1.00 34.59  ? 239  TYR B OH    1 
ATOM   9308  N  N     . PRO B 2 240 ? 147.156 135.048 169.248 1.00 38.29  ? 240  PRO B N     1 
ATOM   9309  C  CA    . PRO B 2 240 ? 147.918 134.100 170.070 1.00 35.09  ? 240  PRO B CA    1 
ATOM   9310  C  C     . PRO B 2 240 ? 147.581 134.186 171.549 1.00 37.03  ? 240  PRO B C     1 
ATOM   9311  O  O     . PRO B 2 240 ? 147.523 133.163 172.238 1.00 42.03  ? 240  PRO B O     1 
ATOM   9312  C  CB    . PRO B 2 240 ? 149.378 134.506 169.815 1.00 36.82  ? 240  PRO B CB    1 
ATOM   9313  C  CG    . PRO B 2 240 ? 149.334 135.557 168.736 1.00 41.71  ? 240  PRO B CG    1 
ATOM   9314  C  CD    . PRO B 2 240 ? 147.990 136.180 168.828 1.00 42.20  ? 240  PRO B CD    1 
ATOM   9315  N  N     . LEU B 2 241 ? 147.378 135.408 172.047 1.00 37.18  ? 241  LEU B N     1 
ATOM   9316  C  CA    . LEU B 2 241 ? 147.074 135.597 173.462 1.00 40.15  ? 241  LEU B CA    1 
ATOM   9317  C  C     . LEU B 2 241 ? 145.746 134.952 173.828 1.00 35.36  ? 241  LEU B C     1 
ATOM   9318  O  O     . LEU B 2 241 ? 145.619 134.323 174.887 1.00 38.93  ? 241  LEU B O     1 
ATOM   9319  C  CB    . LEU B 2 241 ? 147.057 137.087 173.796 1.00 36.68  ? 241  LEU B CB    1 
ATOM   9320  C  CG    . LEU B 2 241 ? 146.631 137.454 175.216 1.00 32.89  ? 241  LEU B CG    1 
ATOM   9321  C  CD1   . LEU B 2 241 ? 147.685 137.017 176.215 1.00 40.12  ? 241  LEU B CD1   1 
ATOM   9322  C  CD2   . LEU B 2 241 ? 146.368 138.942 175.324 1.00 36.38  ? 241  LEU B CD2   1 
ATOM   9323  N  N     . ALA B 2 242 ? 144.747 135.097 172.956 1.00 33.82  ? 242  ALA B N     1 
ATOM   9324  C  CA    . ALA B 2 242 ? 143.457 134.464 173.191 1.00 35.04  ? 242  ALA B CA    1 
ATOM   9325  C  C     . ALA B 2 242 ? 143.588 132.950 173.214 1.00 39.76  ? 242  ALA B C     1 
ATOM   9326  O  O     . ALA B 2 242 ? 142.964 132.282 174.043 1.00 44.56  ? 242  ALA B O     1 
ATOM   9327  C  CB    . ALA B 2 242 ? 142.456 134.902 172.124 1.00 36.62  ? 242  ALA B CB    1 
ATOM   9328  N  N     . ILE B 2 243 ? 144.407 132.391 172.321 1.00 34.39  ? 243  ILE B N     1 
ATOM   9329  C  CA    . ILE B 2 243 ? 144.596 130.945 172.291 1.00 34.68  ? 243  ILE B CA    1 
ATOM   9330  C  C     . ILE B 2 243 ? 145.295 130.466 173.559 1.00 34.81  ? 243  ILE B C     1 
ATOM   9331  O  O     . ILE B 2 243 ? 144.910 129.451 174.146 1.00 39.61  ? 243  ILE B O     1 
ATOM   9332  C  CB    . ILE B 2 243 ? 145.358 130.535 171.019 1.00 31.94  ? 243  ILE B CB    1 
ATOM   9333  C  CG1   . ILE B 2 243 ? 144.457 130.700 169.794 1.00 28.36  ? 243  ILE B CG1   1 
ATOM   9334  C  CG2   . ILE B 2 243 ? 145.848 129.104 171.117 1.00 35.35  ? 243  ILE B CG2   1 
ATOM   9335  C  CD1   . ILE B 2 243 ? 145.123 130.340 168.497 1.00 31.19  ? 243  ILE B CD1   1 
ATOM   9336  N  N     . LYS B 2 244 ? 146.319 131.195 174.008 1.00 35.21  ? 244  LYS B N     1 
ATOM   9337  C  CA    . LYS B 2 244 ? 147.024 130.824 175.233 1.00 35.95  ? 244  LYS B CA    1 
ATOM   9338  C  C     . LYS B 2 244 ? 146.094 130.852 176.442 1.00 38.93  ? 244  LYS B C     1 
ATOM   9339  O  O     . LYS B 2 244 ? 146.077 129.916 177.257 1.00 45.09  ? 244  LYS B O     1 
ATOM   9340  C  CB    . LYS B 2 244 ? 148.211 131.762 175.443 1.00 40.76  ? 244  LYS B CB    1 
ATOM   9341  C  CG    . LYS B 2 244 ? 148.714 131.836 176.868 1.00 39.53  ? 244  LYS B CG    1 
ATOM   9342  C  CD    . LYS B 2 244 ? 149.715 132.963 177.029 1.00 37.46  ? 244  LYS B CD    1 
ATOM   9343  C  CE    . LYS B 2 244 ? 150.084 133.162 178.486 1.00 41.48  ? 244  LYS B CE    1 
ATOM   9344  N  NZ    . LYS B 2 244 ? 150.654 131.924 179.085 1.00 42.75  ? 244  LYS B NZ    1 
ATOM   9345  N  N     . ARG B 2 245 ? 145.304 131.921 176.574 1.00 32.70  ? 245  ARG B N     1 
ATOM   9346  C  CA    . ARG B 2 245 ? 144.401 132.013 177.714 1.00 32.81  ? 245  ARG B CA    1 
ATOM   9347  C  C     . ARG B 2 245 ? 143.281 130.988 177.628 1.00 35.96  ? 245  ARG B C     1 
ATOM   9348  O  O     . ARG B 2 245 ? 142.868 130.442 178.656 1.00 44.84  ? 245  ARG B O     1 
ATOM   9349  C  CB    . ARG B 2 245 ? 143.845 133.428 177.834 1.00 30.27  ? 245  ARG B CB    1 
ATOM   9350  C  CG    . ARG B 2 245 ? 144.883 134.401 178.334 1.00 33.27  ? 245  ARG B CG    1 
ATOM   9351  C  CD    . ARG B 2 245 ? 144.330 135.783 178.544 1.00 36.59  ? 245  ARG B CD    1 
ATOM   9352  N  NE    . ARG B 2 245 ? 145.395 136.699 178.927 1.00 32.16  ? 245  ARG B NE    1 
ATOM   9353  C  CZ    . ARG B 2 245 ? 145.246 138.007 179.058 1.00 33.26  ? 245  ARG B CZ    1 
ATOM   9354  N  NH1   . ARG B 2 245 ? 144.081 138.594 178.848 1.00 41.35  ? 245  ARG B NH1   1 
ATOM   9355  N  NH2   . ARG B 2 245 ? 146.294 138.745 179.409 1.00 37.16  ? 245  ARG B NH2   1 
ATOM   9356  N  N     . LEU B 2 246 ? 142.802 130.689 176.419 1.00 36.81  ? 246  LEU B N     1 
ATOM   9357  C  CA    . LEU B 2 246 ? 141.817 129.630 176.256 1.00 38.77  ? 246  LEU B CA    1 
ATOM   9358  C  C     . LEU B 2 246 ? 142.387 128.279 176.657 1.00 38.79  ? 246  LEU B C     1 
ATOM   9359  O  O     . LEU B 2 246 ? 141.700 127.481 177.295 1.00 38.91  ? 246  LEU B O     1 
ATOM   9360  C  CB    . LEU B 2 246 ? 141.318 129.594 174.816 1.00 34.89  ? 246  LEU B CB    1 
ATOM   9361  C  CG    . LEU B 2 246 ? 140.103 130.457 174.499 1.00 37.34  ? 246  LEU B CG    1 
ATOM   9362  C  CD1   . LEU B 2 246 ? 139.814 130.397 173.018 1.00 40.61  ? 246  LEU B CD1   1 
ATOM   9363  C  CD2   . LEU B 2 246 ? 138.902 129.996 175.305 1.00 31.78  ? 246  LEU B CD2   1 
ATOM   9364  N  N     . ARG B 2 247 ? 143.643 128.005 176.296 1.00 38.48  ? 247  ARG B N     1 
ATOM   9365  C  CA    . ARG B 2 247 ? 144.254 126.728 176.655 1.00 34.75  ? 247  ARG B CA    1 
ATOM   9366  C  C     . ARG B 2 247 ? 144.409 126.593 178.165 1.00 39.19  ? 247  ARG B C     1 
ATOM   9367  O  O     . ARG B 2 247 ? 144.076 125.549 178.743 1.00 46.09  ? 247  ARG B O     1 
ATOM   9368  C  CB    . ARG B 2 247 ? 145.609 126.578 175.962 1.00 34.09  ? 247  ARG B CB    1 
ATOM   9369  C  CG    . ARG B 2 247 ? 145.518 126.405 174.459 1.00 37.29  ? 247  ARG B CG    1 
ATOM   9370  C  CD    . ARG B 2 247 ? 146.013 125.049 174.008 1.00 38.17  ? 247  ARG B CD    1 
ATOM   9371  N  NE    . ARG B 2 247 ? 145.414 124.653 172.740 1.00 41.79  ? 247  ARG B NE    1 
ATOM   9372  C  CZ    . ARG B 2 247 ? 145.843 125.048 171.550 1.00 39.05  ? 247  ARG B CZ    1 
ATOM   9373  N  NH1   . ARG B 2 247 ? 146.874 125.866 171.424 1.00 35.18  ? 247  ARG B NH1   1 
ATOM   9374  N  NH2   . ARG B 2 247 ? 145.221 124.612 170.459 1.00 39.73  ? 247  ARG B NH2   1 
ATOM   9375  N  N     . ILE B 2 248 ? 144.904 127.642 178.825 1.00 36.19  ? 248  ILE B N     1 
ATOM   9376  C  CA    . ILE B 2 248 ? 145.105 127.538 180.268 1.00 38.70  ? 248  ILE B CA    1 
ATOM   9377  C  C     . ILE B 2 248 ? 143.764 127.465 180.993 1.00 34.66  ? 248  ILE B C     1 
ATOM   9378  O  O     . ILE B 2 248 ? 143.614 126.720 181.970 1.00 41.44  ? 248  ILE B O     1 
ATOM   9379  C  CB    . ILE B 2 248 ? 145.997 128.682 180.792 1.00 37.08  ? 248  ILE B CB    1 
ATOM   9380  C  CG1   . ILE B 2 248 ? 145.344 130.046 180.606 1.00 35.79  ? 248  ILE B CG1   1 
ATOM   9381  C  CG2   . ILE B 2 248 ? 147.350 128.658 180.100 1.00 40.09  ? 248  ILE B CG2   1 
ATOM   9382  C  CD1   . ILE B 2 248 ? 146.238 131.193 180.993 1.00 39.92  ? 248  ILE B CD1   1 
ATOM   9383  N  N     . ALA B 2 249 ? 142.755 128.195 180.504 1.00 35.42  ? 249  ALA B N     1 
ATOM   9384  C  CA    . ALA B 2 249 ? 141.427 128.117 181.100 1.00 36.53  ? 249  ALA B CA    1 
ATOM   9385  C  C     . ALA B 2 249 ? 140.797 126.745 180.888 1.00 42.42  ? 249  ALA B C     1 
ATOM   9386  O  O     . ALA B 2 249 ? 140.131 126.221 181.787 1.00 51.55  ? 249  ALA B O     1 
ATOM   9387  C  CB    . ALA B 2 249 ? 140.534 129.214 180.525 1.00 40.06  ? 249  ALA B CB    1 
ATOM   9388  N  N     . LEU B 2 250 ? 140.991 126.149 179.708 1.00 39.03  ? 250  LEU B N     1 
ATOM   9389  C  CA    . LEU B 2 250 ? 140.474 124.808 179.458 1.00 40.93  ? 250  LEU B CA    1 
ATOM   9390  C  C     . LEU B 2 250 ? 141.125 123.785 180.377 1.00 46.90  ? 250  LEU B C     1 
ATOM   9391  O  O     . LEU B 2 250 ? 140.441 122.915 180.923 1.00 46.16  ? 250  LEU B O     1 
ATOM   9392  C  CB    . LEU B 2 250 ? 140.687 124.414 177.995 1.00 40.74  ? 250  LEU B CB    1 
ATOM   9393  C  CG    . LEU B 2 250 ? 139.794 125.028 176.915 1.00 42.04  ? 250  LEU B CG    1 
ATOM   9394  C  CD1   . LEU B 2 250 ? 140.045 124.369 175.573 1.00 42.76  ? 250  LEU B CD1   1 
ATOM   9395  C  CD2   . LEU B 2 250 ? 138.336 124.934 177.287 1.00 42.54  ? 250  LEU B CD2   1 
ATOM   9396  N  N     . LYS B 2 251 ? 142.444 123.873 180.567 1.00 47.97  ? 251  LYS B N     1 
ATOM   9397  C  CA    . LYS B 2 251 ? 143.100 122.905 181.443 1.00 41.30  ? 251  LYS B CA    1 
ATOM   9398  C  C     . LYS B 2 251 ? 142.690 123.112 182.900 1.00 43.62  ? 251  LYS B C     1 
ATOM   9399  O  O     . LYS B 2 251 ? 142.527 122.139 183.649 1.00 50.03  ? 251  LYS B O     1 
ATOM   9400  C  CB    . LYS B 2 251 ? 144.622 122.962 181.269 1.00 40.26  ? 251  LYS B CB    1 
ATOM   9401  C  CG    . LYS B 2 251 ? 145.364 123.945 182.154 1.00 45.60  ? 251  LYS B CG    1 
ATOM   9402  C  CD    . LYS B 2 251 ? 146.867 123.814 181.982 1.00 47.17  ? 251  LYS B CD    1 
ATOM   9403  C  CE    . LYS B 2 251 ? 147.346 122.420 182.339 1.00 45.28  ? 251  LYS B CE    1 
ATOM   9404  N  NZ    . LYS B 2 251 ? 147.043 122.078 183.752 1.00 46.63  ? 251  LYS B NZ    1 
ATOM   9405  N  N     . GLN B 2 252 ? 142.478 124.368 183.310 1.00 45.87  ? 252  GLN B N     1 
ATOM   9406  C  CA    . GLN B 2 252 ? 142.040 124.632 184.677 1.00 43.46  ? 252  GLN B CA    1 
ATOM   9407  C  C     . GLN B 2 252 ? 140.613 124.152 184.908 1.00 43.00  ? 252  GLN B C     1 
ATOM   9408  O  O     . GLN B 2 252 ? 140.285 123.666 185.996 1.00 47.86  ? 252  GLN B O     1 
ATOM   9409  C  CB    . GLN B 2 252 ? 142.160 126.121 184.990 1.00 43.65  ? 252  GLN B CB    1 
ATOM   9410  C  CG    . GLN B 2 252 ? 143.569 126.579 185.282 1.00 43.89  ? 252  GLN B CG    1 
ATOM   9411  C  CD    . GLN B 2 252 ? 143.629 128.042 185.649 1.00 45.84  ? 252  GLN B CD    1 
ATOM   9412  O  OE1   . GLN B 2 252 ? 142.759 128.822 185.271 1.00 46.72  ? 252  GLN B OE1   1 
ATOM   9413  N  NE2   . GLN B 2 252 ? 144.655 128.422 186.396 1.00 49.33  ? 252  GLN B NE2   1 
ATOM   9414  N  N     . ALA B 2 253 ? 139.745 124.295 183.905 1.00 46.44  ? 253  ALA B N     1 
ATOM   9415  C  CA    . ALA B 2 253 ? 138.389 123.774 184.029 1.00 50.31  ? 253  ALA B CA    1 
ATOM   9416  C  C     . ALA B 2 253 ? 138.373 122.255 183.986 1.00 56.62  ? 253  ALA B C     1 
ATOM   9417  O  O     . ALA B 2 253 ? 137.514 121.625 184.611 1.00 59.80  ? 253  ALA B O     1 
ATOM   9418  C  CB    . ALA B 2 253 ? 137.502 124.347 182.926 1.00 50.08  ? 253  ALA B CB    1 
ATOM   9419  N  N     . ARG B 2 254 ? 139.309 121.654 183.252 1.00 53.30  ? 254  ARG B N     1 
ATOM   9420  C  CA    . ARG B 2 254 ? 139.381 120.201 183.182 1.00 47.14  ? 254  ARG B CA    1 
ATOM   9421  C  C     . ARG B 2 254 ? 139.875 119.610 184.495 1.00 47.11  ? 254  ARG B C     1 
ATOM   9422  O  O     . ARG B 2 254 ? 139.430 118.532 184.902 1.00 50.02  ? 254  ARG B O     1 
ATOM   9423  C  CB    . ARG B 2 254 ? 140.280 119.789 182.019 1.00 49.85  ? 254  ARG B CB    1 
ATOM   9424  C  CG    . ARG B 2 254 ? 140.328 118.304 181.746 1.00 51.81  ? 254  ARG B CG    1 
ATOM   9425  C  CD    . ARG B 2 254 ? 140.505 118.021 180.261 1.00 51.03  ? 254  ARG B CD    1 
ATOM   9426  N  NE    . ARG B 2 254 ? 141.480 118.902 179.629 1.00 46.56  ? 254  ARG B NE    1 
ATOM   9427  C  CZ    . ARG B 2 254 ? 141.183 119.828 178.729 1.00 53.86  ? 254  ARG B CZ    1 
ATOM   9428  N  NH1   . ARG B 2 254 ? 139.940 120.024 178.322 1.00 55.33  ? 254  ARG B NH1   1 
ATOM   9429  N  NH2   . ARG B 2 254 ? 142.158 120.574 178.220 1.00 55.46  ? 254  ARG B NH2   1 
ATOM   9430  N  N     . GLU B 2 255 ? 140.787 120.302 185.178 1.00 56.83  ? 255  GLU B N     1 
ATOM   9431  C  CA    . GLU B 2 255 ? 141.271 119.794 186.455 1.00 58.55  ? 255  GLU B CA    1 
ATOM   9432  C  C     . GLU B 2 255 ? 140.317 120.071 187.612 1.00 56.63  ? 255  GLU B C     1 
ATOM   9433  O  O     . GLU B 2 255 ? 140.522 119.525 188.701 1.00 61.10  ? 255  GLU B O     1 
ATOM   9434  C  CB    . GLU B 2 255 ? 142.653 120.373 186.769 1.00 58.93  ? 255  GLU B CB    1 
ATOM   9435  C  CG    . GLU B 2 255 ? 142.666 121.840 187.128 1.00 59.65  ? 255  GLU B CG    1 
ATOM   9436  C  CD    . GLU B 2 255 ? 144.066 122.414 187.147 1.00 61.14  ? 255  GLU B CD    1 
ATOM   9437  O  OE1   . GLU B 2 255 ? 144.985 121.752 186.624 1.00 57.33  ? 255  GLU B OE1   1 
ATOM   9438  O  OE2   . GLU B 2 255 ? 144.249 123.524 187.685 1.00 62.90  ? 255  GLU B OE2   1 
ATOM   9439  N  N     . LYS B 2 256 ? 139.283 120.889 187.412 1.00 48.96  ? 256  LYS B N     1 
ATOM   9440  C  CA    . LYS B 2 256 ? 138.309 121.174 188.459 1.00 49.01  ? 256  LYS B CA    1 
ATOM   9441  C  C     . LYS B 2 256 ? 136.955 120.529 188.185 1.00 50.00  ? 256  LYS B C     1 
ATOM   9442  O  O     . LYS B 2 256 ? 135.952 120.923 188.787 1.00 56.13  ? 256  LYS B O     1 
ATOM   9443  C  CB    . LYS B 2 256 ? 138.150 122.681 188.653 1.00 53.24  ? 256  LYS B CB    1 
ATOM   9444  C  CG    . LYS B 2 256 ? 139.396 123.360 189.186 1.00 51.90  ? 256  LYS B CG    1 
ATOM   9445  C  CD    . LYS B 2 256 ? 139.056 124.621 189.953 1.00 51.04  ? 256  LYS B CD    1 
ATOM   9446  C  CE    . LYS B 2 256 ? 138.175 124.315 191.146 1.00 50.99  ? 256  LYS B CE    1 
ATOM   9447  N  NZ    . LYS B 2 256 ? 137.916 125.527 191.962 1.00 49.24  ? 256  LYS B NZ    1 
ATOM   9448  N  N     . GLY B 2 257 ? 136.905 119.546 187.292 1.00 56.45  ? 257  GLY B N     1 
ATOM   9449  C  CA    . GLY B 2 257 ? 135.690 118.787 187.093 1.00 60.48  ? 257  GLY B CA    1 
ATOM   9450  C  C     . GLY B 2 257 ? 134.607 119.477 186.302 1.00 62.06  ? 257  GLY B C     1 
ATOM   9451  O  O     . GLY B 2 257 ? 133.433 119.127 186.450 1.00 65.93  ? 257  GLY B O     1 
ATOM   9452  N  N     . PHE B 2 258 ? 134.955 120.458 185.471 1.00 58.63  ? 258  PHE B N     1 
ATOM   9453  C  CA    . PHE B 2 258 ? 133.982 121.079 184.585 1.00 57.17  ? 258  PHE B CA    1 
ATOM   9454  C  C     . PHE B 2 258 ? 134.123 120.643 183.136 1.00 57.69  ? 258  PHE B C     1 
ATOM   9455  O  O     . PHE B 2 258 ? 133.183 120.830 182.359 1.00 59.33  ? 258  PHE B O     1 
ATOM   9456  C  CB    . PHE B 2 258 ? 134.081 122.610 184.666 1.00 55.08  ? 258  PHE B CB    1 
ATOM   9457  C  CG    . PHE B 2 258 ? 133.812 123.159 186.039 1.00 60.75  ? 258  PHE B CG    1 
ATOM   9458  C  CD1   . PHE B 2 258 ? 132.615 122.896 186.681 1.00 60.10  ? 258  PHE B CD1   1 
ATOM   9459  C  CD2   . PHE B 2 258 ? 134.754 123.939 186.687 1.00 59.64  ? 258  PHE B CD2   1 
ATOM   9460  C  CE1   . PHE B 2 258 ? 132.364 123.395 187.943 1.00 56.86  ? 258  PHE B CE1   1 
ATOM   9461  C  CE2   . PHE B 2 258 ? 134.507 124.441 187.949 1.00 57.86  ? 258  PHE B CE2   1 
ATOM   9462  C  CZ    . PHE B 2 258 ? 133.310 124.169 188.577 1.00 56.08  ? 258  PHE B CZ    1 
ATOM   9463  N  N     . LEU B 2 259 ? 135.261 120.069 182.759 1.00 51.43  ? 259  LEU B N     1 
ATOM   9464  C  CA    . LEU B 2 259 ? 135.471 119.500 181.437 1.00 49.58  ? 259  LEU B CA    1 
ATOM   9465  C  C     . LEU B 2 259 ? 136.112 118.131 181.585 1.00 50.93  ? 259  LEU B C     1 
ATOM   9466  O  O     . LEU B 2 259 ? 136.934 117.916 182.480 1.00 55.82  ? 259  LEU B O     1 
ATOM   9467  C  CB    . LEU B 2 259 ? 136.353 120.394 180.571 1.00 48.89  ? 259  LEU B CB    1 
ATOM   9468  C  CG    . LEU B 2 259 ? 135.719 121.681 180.059 1.00 50.06  ? 259  LEU B CG    1 
ATOM   9469  C  CD1   . LEU B 2 259 ? 136.785 122.558 179.464 1.00 49.60  ? 259  LEU B CD1   1 
ATOM   9470  C  CD2   . LEU B 2 259 ? 134.652 121.370 179.030 1.00 51.16  ? 259  LEU B CD2   1 
ATOM   9471  N  N     . GLY B 2 260 ? 135.739 117.209 180.699 1.00 56.84  ? 260  GLY B N     1 
ATOM   9472  C  CA    . GLY B 2 260 ? 136.206 115.842 180.765 1.00 60.26  ? 260  GLY B CA    1 
ATOM   9473  C  C     . GLY B 2 260 ? 135.060 114.877 181.008 1.00 63.06  ? 260  GLY B C     1 
ATOM   9474  O  O     . GLY B 2 260 ? 133.911 115.147 180.640 1.00 63.73  ? 260  GLY B O     1 
ATOM   9475  N  N     . GLU B 2 261 ? 135.386 113.752 181.635 1.00 69.29  ? 261  GLU B N     1 
ATOM   9476  C  CA    . GLU B 2 261 ? 134.416 112.696 181.880 1.00 68.69  ? 261  GLU B CA    1 
ATOM   9477  C  C     . GLU B 2 261 ? 133.693 112.934 183.197 1.00 72.72  ? 261  GLU B C     1 
ATOM   9478  O  O     . GLU B 2 261 ? 134.315 113.281 184.204 1.00 74.94  ? 261  GLU B O     1 
ATOM   9479  C  CB    . GLU B 2 261 ? 135.104 111.331 181.904 1.00 71.78  ? 261  GLU B CB    1 
ATOM   9480  C  CG    . GLU B 2 261 ? 135.750 110.937 180.590 1.00 72.94  ? 261  GLU B CG    1 
ATOM   9481  C  CD    . GLU B 2 261 ? 134.737 110.502 179.553 1.00 73.55  ? 261  GLU B CD    1 
ATOM   9482  O  OE1   . GLU B 2 261 ? 133.599 110.162 179.938 1.00 74.71  ? 261  GLU B OE1   1 
ATOM   9483  O  OE2   . GLU B 2 261 ? 135.078 110.499 178.352 1.00 72.24  ? 261  GLU B OE2   1 
ATOM   9484  N  N     . ASN B 2 262 ? 132.372 112.742 183.176 1.00 77.87  ? 262  ASN B N     1 
ATOM   9485  C  CA    . ASN B 2 262 ? 131.511 112.886 184.350 1.00 77.83  ? 262  ASN B CA    1 
ATOM   9486  C  C     . ASN B 2 262 ? 131.652 114.286 184.958 1.00 77.45  ? 262  ASN B C     1 
ATOM   9487  O  O     . ASN B 2 262 ? 132.144 114.476 186.071 1.00 77.74  ? 262  ASN B O     1 
ATOM   9488  C  CB    . ASN B 2 262 ? 131.810 111.796 185.386 1.00 79.33  ? 262  ASN B CB    1 
ATOM   9489  C  CG    . ASN B 2 262 ? 130.712 111.659 186.416 1.00 80.87  ? 262  ASN B CG    1 
ATOM   9490  O  OD1   . ASN B 2 262 ? 129.533 111.830 186.109 1.00 82.08  ? 262  ASN B OD1   1 
ATOM   9491  N  ND2   . ASN B 2 262 ? 131.093 111.352 187.650 1.00 81.17  ? 262  ASN B ND2   1 
ATOM   9492  N  N     . ILE B 2 263 ? 131.223 115.269 184.172 1.00 74.04  ? 263  ILE B N     1 
ATOM   9493  C  CA    . ILE B 2 263 ? 131.277 116.666 184.589 1.00 74.22  ? 263  ILE B CA    1 
ATOM   9494  C  C     . ILE B 2 263 ? 130.269 116.870 185.716 1.00 70.93  ? 263  ILE B C     1 
ATOM   9495  O  O     . ILE B 2 263 ? 129.057 116.805 185.493 1.00 71.90  ? 263  ILE B O     1 
ATOM   9496  C  CB    . ILE B 2 263 ? 130.999 117.613 183.418 1.00 75.13  ? 263  ILE B CB    1 
ATOM   9497  C  CG1   . ILE B 2 263 ? 132.074 117.467 182.344 1.00 70.66  ? 263  ILE B CG1   1 
ATOM   9498  C  CG2   . ILE B 2 263 ? 130.924 119.046 183.904 1.00 71.52  ? 263  ILE B CG2   1 
ATOM   9499  C  CD1   . ILE B 2 263 ? 131.756 118.204 181.072 1.00 69.74  ? 263  ILE B CD1   1 
ATOM   9500  N  N     . LEU B 2 264 ? 130.775 117.115 186.925 1.00 72.77  ? 264  LEU B N     1 
ATOM   9501  C  CA    . LEU B 2 264 ? 129.955 117.381 188.110 1.00 76.46  ? 264  LEU B CA    1 
ATOM   9502  C  C     . LEU B 2 264 ? 128.949 116.261 188.370 1.00 77.04  ? 264  LEU B C     1 
ATOM   9503  O  O     . LEU B 2 264 ? 127.814 116.501 188.785 1.00 75.00  ? 264  LEU B O     1 
ATOM   9504  C  CB    . LEU B 2 264 ? 129.250 118.733 188.002 1.00 75.21  ? 264  LEU B CB    1 
ATOM   9505  C  CG    . LEU B 2 264 ? 130.149 119.965 188.106 1.00 74.63  ? 264  LEU B CG    1 
ATOM   9506  C  CD1   . LEU B 2 264 ? 129.312 121.223 188.232 1.00 73.86  ? 264  LEU B CD1   1 
ATOM   9507  C  CD2   . LEU B 2 264 ? 131.104 119.839 189.277 1.00 75.20  ? 264  LEU B CD2   1 
ATOM   9508  N  N     . GLY B 2 265 ? 129.373 115.025 188.120 1.00 85.07  ? 265  GLY B N     1 
ATOM   9509  C  CA    . GLY B 2 265 ? 128.583 113.860 188.484 1.00 83.18  ? 265  GLY B CA    1 
ATOM   9510  C  C     . GLY B 2 265 ? 127.239 113.757 187.801 1.00 85.11  ? 265  GLY B C     1 
ATOM   9511  O  O     . GLY B 2 265 ? 126.325 113.124 188.341 1.00 85.79  ? 265  GLY B O     1 
ATOM   9512  N  N     . SER B 2 266 ? 127.087 114.359 186.625 1.00 78.81  ? 266  SER B N     1 
ATOM   9513  C  CA    . SER B 2 266 ? 125.815 114.364 185.918 1.00 75.80  ? 266  SER B CA    1 
ATOM   9514  C  C     . SER B 2 266 ? 125.772 113.365 184.771 1.00 76.37  ? 266  SER B C     1 
ATOM   9515  O  O     . SER B 2 266 ? 124.806 113.363 184.002 1.00 75.08  ? 266  SER B O     1 
ATOM   9516  C  CB    . SER B 2 266 ? 125.508 115.767 185.394 1.00 74.28  ? 266  SER B CB    1 
ATOM   9517  O  OG    . SER B 2 266 ? 124.258 115.795 184.731 1.00 75.92  ? 266  SER B OG    1 
ATOM   9518  N  N     . GLY B 2 267 ? 126.787 112.517 184.638 1.00 76.05  ? 267  GLY B N     1 
ATOM   9519  C  CA    . GLY B 2 267 ? 126.831 111.611 183.510 1.00 75.02  ? 267  GLY B CA    1 
ATOM   9520  C  C     . GLY B 2 267 ? 127.061 112.293 182.185 1.00 74.30  ? 267  GLY B C     1 
ATOM   9521  O  O     . GLY B 2 267 ? 126.700 111.744 181.142 1.00 73.98  ? 267  GLY B O     1 
ATOM   9522  N  N     . PHE B 2 268 ? 127.652 113.483 182.199 1.00 60.97  ? 268  PHE B N     1 
ATOM   9523  C  CA    . PHE B 2 268 ? 127.848 114.297 181.010 1.00 56.56  ? 268  PHE B CA    1 
ATOM   9524  C  C     . PHE B 2 268 ? 129.339 114.469 180.768 1.00 56.07  ? 268  PHE B C     1 
ATOM   9525  O  O     . PHE B 2 268 ? 130.068 114.920 181.656 1.00 57.79  ? 268  PHE B O     1 
ATOM   9526  C  CB    . PHE B 2 268 ? 127.162 115.656 181.178 1.00 57.78  ? 268  PHE B CB    1 
ATOM   9527  C  CG    . PHE B 2 268 ? 127.382 116.601 180.037 1.00 59.61  ? 268  PHE B CG    1 
ATOM   9528  C  CD1   . PHE B 2 268 ? 126.818 116.359 178.799 1.00 58.16  ? 268  PHE B CD1   1 
ATOM   9529  C  CD2   . PHE B 2 268 ? 128.130 117.751 180.212 1.00 58.82  ? 268  PHE B CD2   1 
ATOM   9530  C  CE1   . PHE B 2 268 ? 127.015 117.236 177.754 1.00 54.27  ? 268  PHE B CE1   1 
ATOM   9531  C  CE2   . PHE B 2 268 ? 128.327 118.629 179.172 1.00 54.46  ? 268  PHE B CE2   1 
ATOM   9532  C  CZ    . PHE B 2 268 ? 127.770 118.372 177.942 1.00 50.83  ? 268  PHE B CZ    1 
ATOM   9533  N  N     . SER B 2 269 ? 129.788 114.105 179.571 1.00 55.51  ? 269  SER B N     1 
ATOM   9534  C  CA    . SER B 2 269 ? 131.186 114.217 179.181 1.00 56.28  ? 269  SER B CA    1 
ATOM   9535  C  C     . SER B 2 269 ? 131.299 115.190 178.020 1.00 55.68  ? 269  SER B C     1 
ATOM   9536  O  O     . SER B 2 269 ? 130.554 115.081 177.041 1.00 58.32  ? 269  SER B O     1 
ATOM   9537  C  CB    . SER B 2 269 ? 131.762 112.856 178.791 1.00 58.22  ? 269  SER B CB    1 
ATOM   9538  O  OG    . SER B 2 269 ? 133.111 112.976 178.378 1.00 57.97  ? 269  SER B OG    1 
ATOM   9539  N  N     . PHE B 2 270 ? 132.228 116.135 178.127 1.00 42.23  ? 270  PHE B N     1 
ATOM   9540  C  CA    . PHE B 2 270 ? 132.350 117.179 177.114 1.00 39.66  ? 270  PHE B CA    1 
ATOM   9541  C  C     . PHE B 2 270 ? 133.762 117.738 177.149 1.00 44.01  ? 270  PHE B C     1 
ATOM   9542  O  O     . PHE B 2 270 ? 134.211 118.220 178.192 1.00 50.97  ? 270  PHE B O     1 
ATOM   9543  C  CB    . PHE B 2 270 ? 131.319 118.277 177.358 1.00 41.35  ? 270  PHE B CB    1 
ATOM   9544  C  CG    . PHE B 2 270 ? 131.348 119.377 176.345 1.00 42.56  ? 270  PHE B CG    1 
ATOM   9545  C  CD1   . PHE B 2 270 ? 130.886 119.166 175.062 1.00 40.62  ? 270  PHE B CD1   1 
ATOM   9546  C  CD2   . PHE B 2 270 ? 131.820 120.632 176.682 1.00 46.27  ? 270  PHE B CD2   1 
ATOM   9547  C  CE1   . PHE B 2 270 ? 130.910 120.180 174.132 1.00 42.42  ? 270  PHE B CE1   1 
ATOM   9548  C  CE2   . PHE B 2 270 ? 131.842 121.648 175.755 1.00 41.35  ? 270  PHE B CE2   1 
ATOM   9549  C  CZ    . PHE B 2 270 ? 131.388 121.422 174.481 1.00 40.87  ? 270  PHE B CZ    1 
ATOM   9550  N  N     . GLU B 2 271 ? 134.455 117.677 176.018 1.00 39.42  ? 271  GLU B N     1 
ATOM   9551  C  CA    . GLU B 2 271 ? 135.781 118.255 175.876 1.00 34.65  ? 271  GLU B CA    1 
ATOM   9552  C  C     . GLU B 2 271 ? 135.745 119.357 174.827 1.00 34.89  ? 271  GLU B C     1 
ATOM   9553  O  O     . GLU B 2 271 ? 134.964 119.304 173.873 1.00 43.51  ? 271  GLU B O     1 
ATOM   9554  C  CB    . GLU B 2 271 ? 136.816 117.196 175.486 1.00 32.15  ? 271  GLU B CB    1 
ATOM   9555  C  CG    . GLU B 2 271 ? 136.478 116.445 174.217 1.00 37.83  ? 271  GLU B CG    1 
ATOM   9556  C  CD    . GLU B 2 271 ? 137.672 115.720 173.635 1.00 44.72  ? 271  GLU B CD    1 
ATOM   9557  O  OE1   . GLU B 2 271 ? 138.802 115.955 174.112 1.00 47.35  ? 271  GLU B OE1   1 
ATOM   9558  O  OE2   . GLU B 2 271 ? 137.483 114.915 172.700 1.00 37.78  ? 271  GLU B OE2   1 
ATOM   9559  N  N     . ILE B 2 272 ? 136.594 120.361 175.015 1.00 31.15  ? 272  ILE B N     1 
ATOM   9560  C  CA    . ILE B 2 272 ? 136.659 121.516 174.129 1.00 29.21  ? 272  ILE B CA    1 
ATOM   9561  C  C     . ILE B 2 272 ? 137.999 121.489 173.410 1.00 34.49  ? 272  ILE B C     1 
ATOM   9562  O  O     . ILE B 2 272 ? 139.057 121.460 174.050 1.00 39.16  ? 272  ILE B O     1 
ATOM   9563  C  CB    . ILE B 2 272 ? 136.475 122.834 174.895 1.00 33.50  ? 272  ILE B CB    1 
ATOM   9564  C  CG1   . ILE B 2 272 ? 135.086 122.904 175.524 1.00 33.16  ? 272  ILE B CG1   1 
ATOM   9565  C  CG2   . ILE B 2 272 ? 136.687 124.011 173.971 1.00 34.72  ? 272  ILE B CG2   1 
ATOM   9566  C  CD1   . ILE B 2 272 ? 134.811 124.200 176.246 1.00 29.76  ? 272  ILE B CD1   1 
ATOM   9567  N  N     . VAL B 2 273 ? 137.953 121.510 172.083 1.00 28.90  ? 273  VAL B N     1 
ATOM   9568  C  CA    . VAL B 2 273 ? 139.142 121.512 171.242 1.00 28.30  ? 273  VAL B CA    1 
ATOM   9569  C  C     . VAL B 2 273 ? 139.238 122.871 170.568 1.00 26.75  ? 273  VAL B C     1 
ATOM   9570  O  O     . VAL B 2 273 ? 138.250 123.371 170.021 1.00 38.02  ? 273  VAL B O     1 
ATOM   9571  C  CB    . VAL B 2 273 ? 139.099 120.381 170.200 1.00 26.69  ? 273  VAL B CB    1 
ATOM   9572  C  CG1   . VAL B 2 273 ? 140.440 120.251 169.505 1.00 29.89  ? 273  VAL B CG1   1 
ATOM   9573  C  CG2   . VAL B 2 273 ? 138.708 119.076 170.857 1.00 30.77  ? 273  VAL B CG2   1 
ATOM   9574  N  N     . ILE B 2 274 ? 140.418 123.474 170.618 1.00 24.12  ? 274  ILE B N     1 
ATOM   9575  C  CA    . ILE B 2 274 ? 140.638 124.782 170.016 1.00 27.21  ? 274  ILE B CA    1 
ATOM   9576  C  C     . ILE B 2 274 ? 141.057 124.565 168.569 1.00 30.36  ? 274  ILE B C     1 
ATOM   9577  O  O     . ILE B 2 274 ? 142.175 124.125 168.293 1.00 33.09  ? 274  ILE B O     1 
ATOM   9578  C  CB    . ILE B 2 274 ? 141.684 125.589 170.790 1.00 26.59  ? 274  ILE B CB    1 
ATOM   9579  C  CG1   . ILE B 2 274 ? 141.208 125.820 172.221 1.00 26.12  ? 274  ILE B CG1   1 
ATOM   9580  C  CG2   . ILE B 2 274 ? 141.948 126.913 170.103 1.00 28.83  ? 274  ILE B CG2   1 
ATOM   9581  C  CD1   . ILE B 2 274 ? 142.195 126.557 173.066 1.00 29.15  ? 274  ILE B CD1   1 
ATOM   9582  N  N     . LYS B 2 275 ? 140.153 124.866 167.643 1.00 26.46  ? 275  LYS B N     1 
ATOM   9583  C  CA    . LYS B 2 275 ? 140.451 124.789 166.222 1.00 25.09  ? 275  LYS B CA    1 
ATOM   9584  C  C     . LYS B 2 275 ? 140.877 126.162 165.727 1.00 22.68  ? 275  LYS B C     1 
ATOM   9585  O  O     . LYS B 2 275 ? 140.196 127.161 165.976 1.00 21.76  ? 275  LYS B O     1 
ATOM   9586  C  CB    . LYS B 2 275 ? 139.242 124.288 165.435 1.00 17.43  ? 275  LYS B CB    1 
ATOM   9587  C  CG    . LYS B 2 275 ? 138.979 122.808 165.601 1.00 23.04  ? 275  LYS B CG    1 
ATOM   9588  C  CD    . LYS B 2 275 ? 140.165 121.986 165.138 1.00 26.74  ? 275  LYS B CD    1 
ATOM   9589  C  CE    . LYS B 2 275 ? 139.902 120.503 165.299 1.00 29.26  ? 275  LYS B CE    1 
ATOM   9590  N  NZ    . LYS B 2 275 ? 141.041 119.684 164.816 1.00 30.76  ? 275  LYS B NZ    1 
ATOM   9591  N  N     . GLU B 2 276 ? 142.007 126.207 165.039 1.00 29.10  ? 276  GLU B N     1 
ATOM   9592  C  CA    . GLU B 2 276 ? 142.603 127.456 164.598 1.00 24.88  ? 276  GLU B CA    1 
ATOM   9593  C  C     . GLU B 2 276 ? 142.417 127.604 163.097 1.00 23.05  ? 276  GLU B C     1 
ATOM   9594  O  O     . GLU B 2 276 ? 142.715 126.679 162.334 1.00 23.82  ? 276  GLU B O     1 
ATOM   9595  C  CB    . GLU B 2 276 ? 144.084 127.502 164.973 1.00 25.19  ? 276  GLU B CB    1 
ATOM   9596  C  CG    . GLU B 2 276 ? 144.325 127.336 166.461 1.00 26.49  ? 276  GLU B CG    1 
ATOM   9597  C  CD    . GLU B 2 276 ? 145.748 126.942 166.785 1.00 33.36  ? 276  GLU B CD    1 
ATOM   9598  O  OE1   . GLU B 2 276 ? 146.516 126.654 165.846 1.00 32.03  ? 276  GLU B OE1   1 
ATOM   9599  O  OE2   . GLU B 2 276 ? 146.098 126.917 167.981 1.00 37.14  ? 276  GLU B OE2   1 
ATOM   9600  N  N     . GLY B 2 277 ? 141.907 128.756 162.683 1.00 25.01  ? 277  GLY B N     1 
ATOM   9601  C  CA    . GLY B 2 277 ? 141.776 129.086 161.280 1.00 25.93  ? 277  GLY B CA    1 
ATOM   9602  C  C     . GLY B 2 277 ? 142.968 129.899 160.813 1.00 34.56  ? 277  GLY B C     1 
ATOM   9603  O  O     . GLY B 2 277 ? 143.563 130.650 161.579 1.00 39.72  ? 277  GLY B O     1 
ATOM   9604  N  N     . ALA B 2 278 ? 143.312 129.736 159.535 1.00 27.75  ? 278  ALA B N     1 
ATOM   9605  C  CA    . ALA B 2 278 ? 144.476 130.424 158.992 1.00 25.79  ? 278  ALA B CA    1 
ATOM   9606  C  C     . ALA B 2 278 ? 144.237 131.916 158.816 1.00 29.12  ? 278  ALA B C     1 
ATOM   9607  O  O     . ALA B 2 278 ? 145.204 132.675 158.701 1.00 31.91  ? 278  ALA B O     1 
ATOM   9608  C  CB    . ALA B 2 278 ? 144.885 129.799 157.661 1.00 24.65  ? 278  ALA B CB    1 
ATOM   9609  N  N     . GLY B 2 279 ? 142.983 132.351 158.790 1.00 23.97  ? 279  GLY B N     1 
ATOM   9610  C  CA    . GLY B 2 279 ? 142.686 133.764 158.695 1.00 26.28  ? 279  GLY B CA    1 
ATOM   9611  C  C     . GLY B 2 279 ? 142.062 134.175 157.381 1.00 24.92  ? 279  GLY B C     1 
ATOM   9612  O  O     . GLY B 2 279 ? 142.757 134.336 156.374 1.00 33.40  ? 279  GLY B O     1 
ATOM   9613  N  N     . ALA B 2 280 ? 140.744 134.350 157.384 1.00 25.91  ? 280  ALA B N     1 
ATOM   9614  C  CA    . ALA B 2 280 ? 140.026 134.843 156.221 1.00 22.39  ? 280  ALA B CA    1 
ATOM   9615  C  C     . ALA B 2 280 ? 138.688 135.400 156.679 1.00 25.23  ? 280  ALA B C     1 
ATOM   9616  O  O     . ALA B 2 280 ? 138.053 134.843 157.576 1.00 25.73  ? 280  ALA B O     1 
ATOM   9617  C  CB    . ALA B 2 280 ? 139.820 133.743 155.174 1.00 25.48  ? 280  ALA B CB    1 
ATOM   9618  N  N     . PHE B 2 281 ? 138.278 136.508 156.067 1.00 25.89  ? 281  PHE B N     1 
ATOM   9619  C  CA    . PHE B 2 281 ? 136.994 137.118 156.384 1.00 22.35  ? 281  PHE B CA    1 
ATOM   9620  C  C     . PHE B 2 281 ? 135.821 136.237 155.981 1.00 15.76  ? 281  PHE B C     1 
ATOM   9621  O  O     . PHE B 2 281 ? 134.739 136.362 156.564 1.00 16.66  ? 281  PHE B O     1 
ATOM   9622  C  CB    . PHE B 2 281 ? 136.901 138.474 155.687 1.00 22.85  ? 281  PHE B CB    1 
ATOM   9623  C  CG    . PHE B 2 281 ? 135.726 139.304 156.102 1.00 29.84  ? 281  PHE B CG    1 
ATOM   9624  C  CD1   . PHE B 2 281 ? 135.809 140.139 157.196 1.00 28.06  ? 281  PHE B CD1   1 
ATOM   9625  C  CD2   . PHE B 2 281 ? 134.552 139.280 155.374 1.00 26.15  ? 281  PHE B CD2   1 
ATOM   9626  C  CE1   . PHE B 2 281 ? 134.740 140.915 157.566 1.00 25.45  ? 281  PHE B CE1   1 
ATOM   9627  C  CE2   . PHE B 2 281 ? 133.478 140.055 155.742 1.00 18.41  ? 281  PHE B CE2   1 
ATOM   9628  C  CZ    . PHE B 2 281 ? 133.571 140.871 156.838 1.00 21.13  ? 281  PHE B CZ    1 
ATOM   9629  N  N     . VAL B 2 282 ? 136.008 135.354 155.001 1.00 16.15  ? 282  VAL B N     1 
ATOM   9630  C  CA    . VAL B 2 282 ? 134.899 134.536 154.530 1.00 12.82  ? 282  VAL B CA    1 
ATOM   9631  C  C     . VAL B 2 282 ? 134.738 133.280 155.381 1.00 20.76  ? 282  VAL B C     1 
ATOM   9632  O  O     . VAL B 2 282 ? 133.623 132.772 155.535 1.00 23.53  ? 282  VAL B O     1 
ATOM   9633  C  CB    . VAL B 2 282 ? 135.085 134.203 153.038 1.00 14.07  ? 282  VAL B CB    1 
ATOM   9634  C  CG1   . VAL B 2 282 ? 136.299 133.316 152.820 1.00 16.84  ? 282  VAL B CG1   1 
ATOM   9635  C  CG2   . VAL B 2 282 ? 133.834 133.563 152.466 1.00 18.14  ? 282  VAL B CG2   1 
ATOM   9636  N  N     . CYS B 2 283 ? 135.819 132.769 155.968 1.00 29.92  ? 283  CYS B N     1 
ATOM   9637  C  CA    . CYS B 2 283 ? 135.703 131.554 156.762 1.00 22.13  ? 283  CYS B CA    1 
ATOM   9638  C  C     . CYS B 2 283 ? 135.106 131.810 158.137 1.00 21.26  ? 283  CYS B C     1 
ATOM   9639  O  O     . CYS B 2 283 ? 134.900 130.857 158.893 1.00 30.57  ? 283  CYS B O     1 
ATOM   9640  C  CB    . CYS B 2 283 ? 137.061 130.850 156.880 1.00 22.66  ? 283  CYS B CB    1 
ATOM   9641  S  SG    . CYS B 2 283 ? 138.358 131.742 157.738 1.00 45.75  ? 283  CYS B SG    1 
ATOM   9642  N  N     . GLY B 2 284 ? 134.828 133.070 158.479 1.00 24.60  ? 284  GLY B N     1 
ATOM   9643  C  CA    . GLY B 2 284 ? 133.982 133.359 159.620 1.00 15.05  ? 284  GLY B CA    1 
ATOM   9644  C  C     . GLY B 2 284 ? 132.523 133.049 159.376 1.00 14.41  ? 284  GLY B C     1 
ATOM   9645  O  O     . GLY B 2 284 ? 131.768 132.869 160.337 1.00 14.61  ? 284  GLY B O     1 
ATOM   9646  N  N     . GLU B 2 285 ? 132.107 132.993 158.114 1.00 15.31  ? 285  GLU B N     1 
ATOM   9647  C  CA    . GLU B 2 285 ? 130.781 132.493 157.789 1.00 13.75  ? 285  GLU B CA    1 
ATOM   9648  C  C     . GLU B 2 285 ? 130.703 131.017 158.149 1.00 26.60  ? 285  GLU B C     1 
ATOM   9649  O  O     . GLU B 2 285 ? 131.684 130.280 158.019 1.00 32.45  ? 285  GLU B O     1 
ATOM   9650  C  CB    . GLU B 2 285 ? 130.473 132.704 156.308 1.00 19.49  ? 285  GLU B CB    1 
ATOM   9651  C  CG    . GLU B 2 285 ? 128.993 132.799 155.994 1.00 19.00  ? 285  GLU B CG    1 
ATOM   9652  C  CD    . GLU B 2 285 ? 128.490 131.630 155.185 1.00 23.03  ? 285  GLU B CD    1 
ATOM   9653  O  OE1   . GLU B 2 285 ? 129.279 130.700 154.932 1.00 30.80  ? 285  GLU B OE1   1 
ATOM   9654  O  OE2   . GLU B 2 285 ? 127.304 131.641 154.802 1.00 22.19  ? 285  GLU B OE2   1 
ATOM   9655  N  N     . GLU B 2 286 ? 129.531 130.591 158.615 1.00 22.57  ? 286  GLU B N     1 
ATOM   9656  C  CA    . GLU B 2 286 ? 129.425 129.292 159.271 1.00 12.86  ? 286  GLU B CA    1 
ATOM   9657  C  C     . GLU B 2 286 ? 129.718 128.138 158.317 1.00 23.23  ? 286  GLU B C     1 
ATOM   9658  O  O     . GLU B 2 286 ? 130.378 127.169 158.703 1.00 31.78  ? 286  GLU B O     1 
ATOM   9659  C  CB    . GLU B 2 286 ? 128.044 129.143 159.895 1.00 9.66   ? 286  GLU B CB    1 
ATOM   9660  C  CG    . GLU B 2 286 ? 126.919 129.533 158.981 1.00 22.64  ? 286  GLU B CG    1 
ATOM   9661  C  CD    . GLU B 2 286 ? 125.584 129.298 159.617 1.00 32.74  ? 286  GLU B CD    1 
ATOM   9662  O  OE1   . GLU B 2 286 ? 125.525 129.253 160.863 1.00 35.52  ? 286  GLU B OE1   1 
ATOM   9663  O  OE2   . GLU B 2 286 ? 124.597 129.140 158.876 1.00 27.99  ? 286  GLU B OE2   1 
ATOM   9664  N  N     . THR B 2 287 ? 129.234 128.214 157.076 1.00 11.82  ? 287  THR B N     1 
ATOM   9665  C  CA    . THR B 2 287 ? 129.492 127.135 156.125 1.00 13.05  ? 287  THR B CA    1 
ATOM   9666  C  C     . THR B 2 287 ? 130.966 127.073 155.741 1.00 12.95  ? 287  THR B C     1 
ATOM   9667  O  O     . THR B 2 287 ? 131.553 125.985 155.663 1.00 17.83  ? 287  THR B O     1 
ATOM   9668  C  CB    . THR B 2 287 ? 128.614 127.306 154.888 1.00 19.18  ? 287  THR B CB    1 
ATOM   9669  O  OG1   . THR B 2 287 ? 128.842 128.596 154.313 1.00 33.93  ? 287  THR B OG1   1 
ATOM   9670  C  CG2   . THR B 2 287 ? 127.153 127.188 155.264 1.00 13.77  ? 287  THR B CG2   1 
ATOM   9671  N  N     . ALA B 2 288 ? 131.591 128.231 155.521 1.00 13.92  ? 288  ALA B N     1 
ATOM   9672  C  CA    . ALA B 2 288 ? 133.024 128.249 155.258 1.00 16.22  ? 288  ALA B CA    1 
ATOM   9673  C  C     . ALA B 2 288 ? 133.823 127.862 156.495 1.00 24.06  ? 288  ALA B C     1 
ATOM   9674  O  O     . ALA B 2 288 ? 134.901 127.274 156.376 1.00 19.30  ? 288  ALA B O     1 
ATOM   9675  C  CB    . ALA B 2 288 ? 133.444 129.624 154.750 1.00 14.04  ? 288  ALA B CB    1 
ATOM   9676  N  N     . LEU B 2 289 ? 133.308 128.175 157.686 1.00 26.13  ? 289  LEU B N     1 
ATOM   9677  C  CA    . LEU B 2 289 ? 133.941 127.715 158.918 1.00 9.85   ? 289  LEU B CA    1 
ATOM   9678  C  C     . LEU B 2 289 ? 133.929 126.194 159.007 1.00 9.70   ? 289  LEU B C     1 
ATOM   9679  O  O     . LEU B 2 289 ? 134.934 125.573 159.376 1.00 27.87  ? 289  LEU B O     1 
ATOM   9680  C  CB    . LEU B 2 289 ? 133.227 128.344 160.117 1.00 13.11  ? 289  LEU B CB    1 
ATOM   9681  C  CG    . LEU B 2 289 ? 133.549 127.954 161.557 1.00 20.57  ? 289  LEU B CG    1 
ATOM   9682  C  CD1   . LEU B 2 289 ? 133.412 129.168 162.444 1.00 17.83  ? 289  LEU B CD1   1 
ATOM   9683  C  CD2   . LEU B 2 289 ? 132.612 126.864 162.036 1.00 28.94  ? 289  LEU B CD2   1 
ATOM   9684  N  N     . ILE B 2 290 ? 132.796 125.579 158.666 1.00 15.92  ? 290  ILE B N     1 
ATOM   9685  C  CA    . ILE B 2 290 ? 132.702 124.123 158.651 1.00 17.46  ? 290  ILE B CA    1 
ATOM   9686  C  C     . ILE B 2 290 ? 133.663 123.538 157.629 1.00 20.88  ? 290  ILE B C     1 
ATOM   9687  O  O     . ILE B 2 290 ? 134.349 122.545 157.896 1.00 21.55  ? 290  ILE B O     1 
ATOM   9688  C  CB    . ILE B 2 290 ? 131.252 123.692 158.370 1.00 14.95  ? 290  ILE B CB    1 
ATOM   9689  C  CG1   . ILE B 2 290 ? 130.356 124.067 159.544 1.00 11.54  ? 290  ILE B CG1   1 
ATOM   9690  C  CG2   . ILE B 2 290 ? 131.177 122.207 158.088 1.00 24.98  ? 290  ILE B CG2   1 
ATOM   9691  C  CD1   . ILE B 2 290 ? 128.911 123.994 159.208 1.00 13.96  ? 290  ILE B CD1   1 
ATOM   9692  N  N     . ALA B 2 291 ? 133.731 124.148 156.444 1.00 19.98  ? 291  ALA B N     1 
ATOM   9693  C  CA    . ALA B 2 291 ? 134.632 123.648 155.410 1.00 9.47   ? 291  ALA B CA    1 
ATOM   9694  C  C     . ALA B 2 291 ? 136.094 123.769 155.831 1.00 20.29  ? 291  ALA B C     1 
ATOM   9695  O  O     . ALA B 2 291 ? 136.906 122.889 155.528 1.00 32.66  ? 291  ALA B O     1 
ATOM   9696  C  CB    . ALA B 2 291 ? 134.381 124.384 154.096 1.00 20.14  ? 291  ALA B CB    1 
ATOM   9697  N  N     . SER B 2 292 ? 136.451 124.848 156.532 1.00 19.89  ? 292  SER B N     1 
ATOM   9698  C  CA    . SER B 2 292 ? 137.832 125.028 156.967 1.00 16.68  ? 292  SER B CA    1 
ATOM   9699  C  C     . SER B 2 292 ? 138.198 124.121 158.137 1.00 21.19  ? 292  SER B C     1 
ATOM   9700  O  O     . SER B 2 292 ? 139.353 123.697 158.242 1.00 28.73  ? 292  SER B O     1 
ATOM   9701  C  CB    . SER B 2 292 ? 138.085 126.490 157.337 1.00 18.33  ? 292  SER B CB    1 
ATOM   9702  O  OG    . SER B 2 292 ? 137.306 126.879 158.451 1.00 28.22  ? 292  SER B OG    1 
ATOM   9703  N  N     . ILE B 2 293 ? 137.250 123.822 159.028 1.00 20.44  ? 293  ILE B N     1 
ATOM   9704  C  CA    . ILE B 2 293 ? 137.532 122.862 160.093 1.00 21.25  ? 293  ILE B CA    1 
ATOM   9705  C  C     . ILE B 2 293 ? 137.703 121.461 159.518 1.00 24.59  ? 293  ILE B C     1 
ATOM   9706  O  O     . ILE B 2 293 ? 138.539 120.683 159.992 1.00 33.30  ? 293  ILE B O     1 
ATOM   9707  C  CB    . ILE B 2 293 ? 136.436 122.911 161.175 1.00 17.06  ? 293  ILE B CB    1 
ATOM   9708  C  CG1   . ILE B 2 293 ? 136.477 124.246 161.914 1.00 20.56  ? 293  ILE B CG1   1 
ATOM   9709  C  CG2   . ILE B 2 293 ? 136.605 121.783 162.179 1.00 15.33  ? 293  ILE B CG2   1 
ATOM   9710  C  CD1   . ILE B 2 293 ? 135.526 124.326 163.087 1.00 18.94  ? 293  ILE B CD1   1 
ATOM   9711  N  N     . GLU B 2 294 ? 136.940 121.122 158.479 1.00 20.47  ? 294  GLU B N     1 
ATOM   9712  C  CA    . GLU B 2 294 ? 137.068 119.822 157.834 1.00 18.97  ? 294  GLU B CA    1 
ATOM   9713  C  C     . GLU B 2 294 ? 138.335 119.689 156.998 1.00 27.07  ? 294  GLU B C     1 
ATOM   9714  O  O     . GLU B 2 294 ? 138.630 118.585 156.530 1.00 31.49  ? 294  GLU B O     1 
ATOM   9715  C  CB    . GLU B 2 294 ? 135.848 119.553 156.954 1.00 17.65  ? 294  GLU B CB    1 
ATOM   9716  C  CG    . GLU B 2 294 ? 134.563 119.338 157.722 1.00 21.25  ? 294  GLU B CG    1 
ATOM   9717  C  CD    . GLU B 2 294 ? 133.356 119.294 156.816 1.00 26.56  ? 294  GLU B CD    1 
ATOM   9718  O  OE1   . GLU B 2 294 ? 133.528 119.459 155.592 1.00 25.74  ? 294  GLU B OE1   1 
ATOM   9719  O  OE2   . GLU B 2 294 ? 132.235 119.097 157.324 1.00 24.80  ? 294  GLU B OE2   1 
ATOM   9720  N  N     . GLY B 2 295 ? 139.077 120.770 156.789 1.00 24.03  ? 295  GLY B N     1 
ATOM   9721  C  CA    . GLY B 2 295 ? 140.311 120.717 156.037 1.00 25.23  ? 295  GLY B CA    1 
ATOM   9722  C  C     . GLY B 2 295 ? 140.209 121.098 154.578 1.00 23.59  ? 295  GLY B C     1 
ATOM   9723  O  O     . GLY B 2 295 ? 141.174 120.888 153.837 1.00 29.19  ? 295  GLY B O     1 
ATOM   9724  N  N     . LYS B 2 296 ? 139.082 121.644 154.144 1.00 20.99  ? 296  LYS B N     1 
ATOM   9725  C  CA    . LYS B 2 296 ? 138.892 122.091 152.777 1.00 22.12  ? 296  LYS B CA    1 
ATOM   9726  C  C     . LYS B 2 296 ? 139.198 123.585 152.691 1.00 24.58  ? 296  LYS B C     1 
ATOM   9727  O  O     . LYS B 2 296 ? 139.679 124.200 153.647 1.00 27.64  ? 296  LYS B O     1 
ATOM   9728  C  CB    . LYS B 2 296 ? 137.469 121.767 152.322 1.00 18.20  ? 296  LYS B CB    1 
ATOM   9729  C  CG    . LYS B 2 296 ? 137.005 120.365 152.680 1.00 27.42  ? 296  LYS B CG    1 
ATOM   9730  C  CD    . LYS B 2 296 ? 135.535 120.171 152.352 1.00 29.03  ? 296  LYS B CD    1 
ATOM   9731  C  CE    . LYS B 2 296 ? 135.053 118.782 152.734 1.00 30.55  ? 296  LYS B CE    1 
ATOM   9732  N  NZ    . LYS B 2 296 ? 135.778 117.711 152.004 1.00 28.48  ? 296  LYS B NZ    1 
ATOM   9733  N  N     . ARG B 2 297 ? 138.931 124.184 151.537 1.00 23.89  ? 297  ARG B N     1 
ATOM   9734  C  CA    . ARG B 2 297 ? 139.017 125.630 151.410 1.00 23.41  ? 297  ARG B CA    1 
ATOM   9735  C  C     . ARG B 2 297 ? 137.661 126.243 151.731 1.00 25.60  ? 297  ARG B C     1 
ATOM   9736  O  O     . ARG B 2 297 ? 136.617 125.715 151.341 1.00 25.10  ? 297  ARG B O     1 
ATOM   9737  C  CB    . ARG B 2 297 ? 139.482 126.046 150.013 1.00 17.73  ? 297  ARG B CB    1 
ATOM   9738  C  CG    . ARG B 2 297 ? 138.911 125.235 148.874 1.00 24.25  ? 297  ARG B CG    1 
ATOM   9739  C  CD    . ARG B 2 297 ? 138.866 126.059 147.600 1.00 20.52  ? 297  ARG B CD    1 
ATOM   9740  N  NE    . ARG B 2 297 ? 140.086 126.827 147.390 1.00 28.53  ? 297  ARG B NE    1 
ATOM   9741  C  CZ    . ARG B 2 297 ? 140.160 127.924 146.649 1.00 24.74  ? 297  ARG B CZ    1 
ATOM   9742  N  NH1   . ARG B 2 297 ? 139.096 128.424 146.045 1.00 25.17  ? 297  ARG B NH1   1 
ATOM   9743  N  NH2   . ARG B 2 297 ? 141.330 128.542 146.520 1.00 17.76  ? 297  ARG B NH2   1 
ATOM   9744  N  N     . GLY B 2 298 ? 137.687 127.360 152.452 1.00 23.84  ? 298  GLY B N     1 
ATOM   9745  C  CA    . GLY B 2 298 ? 136.475 127.938 152.994 1.00 22.37  ? 298  GLY B CA    1 
ATOM   9746  C  C     . GLY B 2 298 ? 135.586 128.623 151.980 1.00 23.28  ? 298  GLY B C     1 
ATOM   9747  O  O     . GLY B 2 298 ? 135.447 129.848 151.995 1.00 30.71  ? 298  GLY B O     1 
ATOM   9748  N  N     . MET B 2 299 ? 134.977 127.842 151.089 1.00 15.63  ? 299  MET B N     1 
ATOM   9749  C  CA    . MET B 2 299 ? 134.008 128.376 150.147 1.00 21.43  ? 299  MET B CA    1 
ATOM   9750  C  C     . MET B 2 299 ? 132.612 128.149 150.696 1.00 25.95  ? 299  MET B C     1 
ATOM   9751  O  O     . MET B 2 299 ? 132.214 126.989 150.880 1.00 23.91  ? 299  MET B O     1 
ATOM   9752  C  CB    . MET B 2 299 ? 134.152 127.715 148.783 1.00 20.01  ? 299  MET B CB    1 
ATOM   9753  C  CG    . MET B 2 299 ? 135.583 127.564 148.318 1.00 27.15  ? 299  MET B CG    1 
ATOM   9754  S  SD    . MET B 2 299 ? 135.723 127.293 146.546 1.00 20.66  ? 299  MET B SD    1 
ATOM   9755  C  CE    . MET B 2 299 ? 135.706 128.978 145.950 1.00 13.33  ? 299  MET B CE    1 
ATOM   9756  N  N     . PRO B 2 300 ? 131.854 129.202 150.995 1.00 14.94  ? 300  PRO B N     1 
ATOM   9757  C  CA    . PRO B 2 300 ? 130.507 129.008 151.541 1.00 10.17  ? 300  PRO B CA    1 
ATOM   9758  C  C     . PRO B 2 300 ? 129.601 128.259 150.577 1.00 13.60  ? 300  PRO B C     1 
ATOM   9759  O  O     . PRO B 2 300 ? 129.688 128.416 149.358 1.00 30.37  ? 300  PRO B O     1 
ATOM   9760  C  CB    . PRO B 2 300 ? 130.011 130.438 151.785 1.00 16.40  ? 300  PRO B CB    1 
ATOM   9761  C  CG    . PRO B 2 300 ? 130.936 131.317 151.014 1.00 27.91  ? 300  PRO B CG    1 
ATOM   9762  C  CD    . PRO B 2 300 ? 132.247 130.618 150.985 1.00 11.79  ? 300  PRO B CD    1 
ATOM   9763  N  N     . ARG B 2 301 ? 128.733 127.438 151.142 1.00 10.31  ? 301  ARG B N     1 
ATOM   9764  C  CA    . ARG B 2 301 ? 127.774 126.637 150.408 1.00 12.20  ? 301  ARG B CA    1 
ATOM   9765  C  C     . ARG B 2 301 ? 126.367 127.193 150.592 1.00 16.43  ? 301  ARG B C     1 
ATOM   9766  O  O     . ARG B 2 301 ? 126.112 127.964 151.523 1.00 17.90  ? 301  ARG B O     1 
ATOM   9767  C  CB    . ARG B 2 301 ? 127.826 125.177 150.880 1.00 18.87  ? 301  ARG B CB    1 
ATOM   9768  C  CG    . ARG B 2 301 ? 127.331 124.971 152.292 1.00 17.10  ? 301  ARG B CG    1 
ATOM   9769  C  CD    . ARG B 2 301 ? 127.169 123.501 152.613 1.00 20.47  ? 301  ARG B CD    1 
ATOM   9770  N  NE    . ARG B 2 301 ? 126.115 123.285 153.595 1.00 24.61  ? 301  ARG B NE    1 
ATOM   9771  C  CZ    . ARG B 2 301 ? 126.305 123.241 154.905 1.00 22.26  ? 301  ARG B CZ    1 
ATOM   9772  N  NH1   . ARG B 2 301 ? 127.509 123.383 155.434 1.00 14.19  ? 301  ARG B NH1   1 
ATOM   9773  N  NH2   . ARG B 2 301 ? 125.263 123.048 155.706 1.00 23.99  ? 301  ARG B NH2   1 
ATOM   9774  N  N     . PRO B 2 302 ? 125.438 126.857 149.697 1.00 19.06  ? 302  PRO B N     1 
ATOM   9775  C  CA    . PRO B 2 302 ? 124.037 127.265 149.887 1.00 19.15  ? 302  PRO B CA    1 
ATOM   9776  C  C     . PRO B 2 302 ? 123.466 126.739 151.197 1.00 22.83  ? 302  PRO B C     1 
ATOM   9777  O  O     . PRO B 2 302 ? 123.383 125.532 151.425 1.00 23.05  ? 302  PRO B O     1 
ATOM   9778  C  CB    . PRO B 2 302 ? 123.332 126.658 148.672 1.00 17.23  ? 302  PRO B CB    1 
ATOM   9779  C  CG    . PRO B 2 302 ? 124.387 126.621 147.631 1.00 18.69  ? 302  PRO B CG    1 
ATOM   9780  C  CD    . PRO B 2 302 ? 125.669 126.316 148.345 1.00 18.01  ? 302  PRO B CD    1 
ATOM   9781  N  N     . ARG B 2 303 ? 123.074 127.669 152.056 1.00 20.43  ? 303  ARG B N     1 
ATOM   9782  C  CA    . ARG B 2 303 ? 122.688 127.444 153.446 1.00 21.85  ? 303  ARG B CA    1 
ATOM   9783  C  C     . ARG B 2 303 ? 121.389 126.689 153.759 1.00 19.54  ? 303  ARG B C     1 
ATOM   9784  O  O     . ARG B 2 303 ? 121.276 126.205 154.889 1.00 17.04  ? 303  ARG B O     1 
ATOM   9785  C  CB    . ARG B 2 303 ? 122.657 128.786 154.177 1.00 25.73  ? 303  ARG B CB    1 
ATOM   9786  C  CG    . ARG B 2 303 ? 123.308 128.721 155.552 1.00 11.94  ? 303  ARG B CG    1 
ATOM   9787  C  CD    . ARG B 2 303 ? 124.170 129.936 155.838 1.00 15.52  ? 303  ARG B CD    1 
ATOM   9788  N  NE    . ARG B 2 303 ? 123.384 131.154 155.975 1.00 29.94  ? 303  ARG B NE    1 
ATOM   9789  C  CZ    . ARG B 2 303 ? 123.230 132.057 155.016 1.00 29.64  ? 303  ARG B CZ    1 
ATOM   9790  N  NH1   . ARG B 2 303 ? 123.808 131.914 153.834 1.00 21.21  ? 303  ARG B NH1   1 
ATOM   9791  N  NH2   . ARG B 2 303 ? 122.480 133.129 155.249 1.00 29.42  ? 303  ARG B NH2   1 
ATOM   9792  N  N     . PRO B 2 304 ? 120.370 126.618 152.892 1.00 33.53  ? 304  PRO B N     1 
ATOM   9793  C  CA    . PRO B 2 304 ? 119.113 125.925 153.280 1.00 31.99  ? 304  PRO B CA    1 
ATOM   9794  C  C     . PRO B 2 304 ? 119.332 124.514 153.809 1.00 22.95  ? 304  PRO B C     1 
ATOM   9795  O  O     . PRO B 2 304 ? 118.531 124.041 154.629 1.00 29.53  ? 304  PRO B O     1 
ATOM   9796  C  CB    . PRO B 2 304 ? 118.302 125.926 151.979 1.00 37.38  ? 304  PRO B CB    1 
ATOM   9797  C  CG    . PRO B 2 304 ? 118.669 127.212 151.367 1.00 30.81  ? 304  PRO B CG    1 
ATOM   9798  C  CD    . PRO B 2 304 ? 120.130 127.454 151.699 1.00 34.03  ? 304  PRO B CD    1 
ATOM   9799  N  N     . PRO B 2 305 ? 120.382 123.789 153.379 1.00 24.51  ? 305  PRO B N     1 
ATOM   9800  C  CA    . PRO B 2 305 ? 120.892 122.710 154.240 1.00 30.39  ? 305  PRO B CA    1 
ATOM   9801  C  C     . PRO B 2 305 ? 121.718 123.274 155.388 1.00 26.24  ? 305  PRO B C     1 
ATOM   9802  O  O     . PRO B 2 305 ? 122.944 123.372 155.289 1.00 25.42  ? 305  PRO B O     1 
ATOM   9803  C  CB    . PRO B 2 305 ? 121.741 121.861 153.287 1.00 26.86  ? 305  PRO B CB    1 
ATOM   9804  C  CG    . PRO B 2 305 ? 121.199 122.161 151.941 1.00 30.63  ? 305  PRO B CG    1 
ATOM   9805  C  CD    . PRO B 2 305 ? 120.843 123.611 151.990 1.00 22.12  ? 305  PRO B CD    1 
ATOM   9806  N  N     . TYR B 2 306 ? 121.052 123.660 156.474 1.00 21.59  ? 306  TYR B N     1 
ATOM   9807  C  CA    . TYR B 2 306 ? 121.667 124.527 157.467 1.00 18.52  ? 306  TYR B CA    1 
ATOM   9808  C  C     . TYR B 2 306 ? 122.698 123.785 158.316 1.00 28.06  ? 306  TYR B C     1 
ATOM   9809  O  O     . TYR B 2 306 ? 122.615 122.566 158.488 1.00 35.36  ? 306  TYR B O     1 
ATOM   9810  C  CB    . TYR B 2 306 ? 120.599 125.151 158.358 1.00 14.55  ? 306  TYR B CB    1 
ATOM   9811  C  CG    . TYR B 2 306 ? 119.964 126.364 157.726 1.00 25.32  ? 306  TYR B CG    1 
ATOM   9812  C  CD1   . TYR B 2 306 ? 120.625 127.583 157.709 1.00 25.18  ? 306  TYR B CD1   1 
ATOM   9813  C  CD2   . TYR B 2 306 ? 118.716 126.288 157.127 1.00 25.31  ? 306  TYR B CD2   1 
ATOM   9814  C  CE1   . TYR B 2 306 ? 120.059 128.694 157.123 1.00 18.98  ? 306  TYR B CE1   1 
ATOM   9815  C  CE2   . TYR B 2 306 ? 118.141 127.396 156.539 1.00 25.15  ? 306  TYR B CE2   1 
ATOM   9816  C  CZ    . TYR B 2 306 ? 118.818 128.595 156.540 1.00 23.13  ? 306  TYR B CZ    1 
ATOM   9817  O  OH    . TYR B 2 306 ? 118.251 129.702 155.957 1.00 26.43  ? 306  TYR B OH    1 
ATOM   9818  N  N     . PRO B 2 307 ? 123.690 124.508 158.846 1.00 25.88  ? 307  PRO B N     1 
ATOM   9819  C  CA    . PRO B 2 307 ? 124.721 123.863 159.675 1.00 25.73  ? 307  PRO B CA    1 
ATOM   9820  C  C     . PRO B 2 307 ? 124.189 123.190 160.922 1.00 19.53  ? 307  PRO B C     1 
ATOM   9821  O  O     . PRO B 2 307 ? 124.867 122.307 161.460 1.00 21.46  ? 307  PRO B O     1 
ATOM   9822  C  CB    . PRO B 2 307 ? 125.652 125.027 160.029 1.00 19.69  ? 307  PRO B CB    1 
ATOM   9823  C  CG    . PRO B 2 307 ? 125.522 125.945 158.882 1.00 16.35  ? 307  PRO B CG    1 
ATOM   9824  C  CD    . PRO B 2 307 ? 124.076 125.879 158.476 1.00 19.60  ? 307  PRO B CD    1 
ATOM   9825  N  N     . ALA B 2 308 ? 123.015 123.584 161.414 1.00 23.23  ? 308  ALA B N     1 
ATOM   9826  C  CA    . ALA B 2 308 ? 122.412 122.862 162.527 1.00 20.03  ? 308  ALA B CA    1 
ATOM   9827  C  C     . ALA B 2 308 ? 121.978 121.463 162.112 1.00 25.68  ? 308  ALA B C     1 
ATOM   9828  O  O     . ALA B 2 308 ? 121.940 120.556 162.948 1.00 29.07  ? 308  ALA B O     1 
ATOM   9829  C  CB    . ALA B 2 308 ? 121.227 123.645 163.090 1.00 26.38  ? 308  ALA B CB    1 
ATOM   9830  N  N     . GLN B 2 309 ? 121.648 121.271 160.835 1.00 23.95  ? 309  GLN B N     1 
ATOM   9831  C  CA    . GLN B 2 309 ? 121.243 119.964 160.337 1.00 21.45  ? 309  GLN B CA    1 
ATOM   9832  C  C     . GLN B 2 309 ? 122.426 119.161 159.812 1.00 29.45  ? 309  GLN B C     1 
ATOM   9833  O  O     . GLN B 2 309 ? 122.544 117.968 160.108 1.00 33.81  ? 309  GLN B O     1 
ATOM   9834  C  CB    . GLN B 2 309 ? 120.194 120.118 159.231 1.00 20.91  ? 309  GLN B CB    1 
ATOM   9835  C  CG    . GLN B 2 309 ? 119.215 121.263 159.438 1.00 27.95  ? 309  GLN B CG    1 
ATOM   9836  C  CD    . GLN B 2 309 ? 118.194 120.983 160.518 1.00 31.92  ? 309  GLN B CD    1 
ATOM   9837  O  OE1   . GLN B 2 309 ? 118.012 119.842 160.936 1.00 34.42  ? 309  GLN B OE1   1 
ATOM   9838  N  NE2   . GLN B 2 309 ? 117.517 122.029 160.976 1.00 29.14  ? 309  GLN B NE2   1 
ATOM   9839  N  N     . LYS B 2 310 ? 123.307 119.791 159.038 1.00 18.32  ? 310  LYS B N     1 
ATOM   9840  C  CA    . LYS B 2 310 ? 124.500 119.126 158.515 1.00 26.79  ? 310  LYS B CA    1 
ATOM   9841  C  C     . LYS B 2 310 ? 125.680 120.072 158.708 1.00 16.69  ? 310  LYS B C     1 
ATOM   9842  O  O     . LYS B 2 310 ? 125.903 120.970 157.893 1.00 24.24  ? 310  LYS B O     1 
ATOM   9843  C  CB    . LYS B 2 310 ? 124.333 118.738 157.052 1.00 27.47  ? 310  LYS B CB    1 
ATOM   9844  C  CG    . LYS B 2 310 ? 123.464 117.514 156.837 1.00 28.88  ? 310  LYS B CG    1 
ATOM   9845  C  CD    . LYS B 2 310 ? 123.624 116.972 155.431 1.00 26.26  ? 310  LYS B CD    1 
ATOM   9846  C  CE    . LYS B 2 310 ? 125.062 116.576 155.162 1.00 28.16  ? 310  LYS B CE    1 
ATOM   9847  N  NZ    . LYS B 2 310 ? 125.243 116.046 153.784 1.00 31.18  ? 310  LYS B NZ    1 
ATOM   9848  N  N     . GLY B 2 311 ? 126.430 119.863 159.784 1.00 15.84  ? 311  GLY B N     1 
ATOM   9849  C  CA    . GLY B 2 311 ? 127.565 120.708 160.082 1.00 22.08  ? 311  GLY B CA    1 
ATOM   9850  C  C     . GLY B 2 311 ? 128.899 120.030 159.868 1.00 22.74  ? 311  GLY B C     1 
ATOM   9851  O  O     . GLY B 2 311 ? 129.257 119.691 158.737 1.00 16.31  ? 311  GLY B O     1 
ATOM   9852  N  N     . LEU B 2 312 ? 129.641 119.817 160.951 1.00 19.95  ? 312  LEU B N     1 
ATOM   9853  C  CA    . LEU B 2 312 ? 130.991 119.269 160.870 1.00 23.42  ? 312  LEU B CA    1 
ATOM   9854  C  C     . LEU B 2 312 ? 130.920 117.775 160.587 1.00 30.95  ? 312  LEU B C     1 
ATOM   9855  O  O     . LEU B 2 312 ? 130.446 116.999 161.424 1.00 32.24  ? 312  LEU B O     1 
ATOM   9856  C  CB    . LEU B 2 312 ? 131.755 119.543 162.161 1.00 19.38  ? 312  LEU B CB    1 
ATOM   9857  C  CG    . LEU B 2 312 ? 132.175 120.993 162.372 1.00 24.65  ? 312  LEU B CG    1 
ATOM   9858  C  CD1   . LEU B 2 312 ? 132.889 121.148 163.692 1.00 20.63  ? 312  LEU B CD1   1 
ATOM   9859  C  CD2   . LEU B 2 312 ? 133.059 121.439 161.232 1.00 26.08  ? 312  LEU B CD2   1 
ATOM   9860  N  N     . TRP B 2 313 ? 131.417 117.378 159.415 1.00 28.97  ? 313  TRP B N     1 
ATOM   9861  C  CA    . TRP B 2 313 ? 131.431 115.983 158.972 1.00 25.17  ? 313  TRP B CA    1 
ATOM   9862  C  C     . TRP B 2 313 ? 130.026 115.388 158.970 1.00 26.31  ? 313  TRP B C     1 
ATOM   9863  O  O     . TRP B 2 313 ? 129.815 114.238 159.355 1.00 30.89  ? 313  TRP B O     1 
ATOM   9864  C  CB    . TRP B 2 313 ? 132.393 115.144 159.817 1.00 22.70  ? 313  TRP B CB    1 
ATOM   9865  C  CG    . TRP B 2 313 ? 133.763 115.745 159.884 1.00 25.88  ? 313  TRP B CG    1 
ATOM   9866  C  CD1   . TRP B 2 313 ? 134.640 115.890 158.853 1.00 26.74  ? 313  TRP B CD1   1 
ATOM   9867  C  CD2   . TRP B 2 313 ? 134.409 116.290 161.040 1.00 26.77  ? 313  TRP B CD2   1 
ATOM   9868  N  NE1   . TRP B 2 313 ? 135.793 116.491 159.292 1.00 31.83  ? 313  TRP B NE1   1 
ATOM   9869  C  CE2   . TRP B 2 313 ? 135.676 116.748 160.631 1.00 25.08  ? 313  TRP B CE2   1 
ATOM   9870  C  CE3   . TRP B 2 313 ? 134.040 116.437 162.378 1.00 31.80  ? 313  TRP B CE3   1 
ATOM   9871  C  CZ2   . TRP B 2 313 ? 136.575 117.339 161.512 1.00 26.62  ? 313  TRP B CZ2   1 
ATOM   9872  C  CZ3   . TRP B 2 313 ? 134.934 117.024 163.250 1.00 31.08  ? 313  TRP B CZ3   1 
ATOM   9873  C  CH2   . TRP B 2 313 ? 136.186 117.468 162.815 1.00 29.97  ? 313  TRP B CH2   1 
ATOM   9874  N  N     . GLY B 2 314 ? 129.056 116.186 158.529 1.00 19.80  ? 314  GLY B N     1 
ATOM   9875  C  CA    . GLY B 2 314 ? 127.689 115.728 158.389 1.00 20.67  ? 314  GLY B CA    1 
ATOM   9876  C  C     . GLY B 2 314 ? 126.864 115.812 159.655 1.00 24.89  ? 314  GLY B C     1 
ATOM   9877  O  O     . GLY B 2 314 ? 125.661 116.080 159.599 1.00 28.76  ? 314  GLY B O     1 
ATOM   9878  N  N     . ARG B 2 315 ? 127.496 115.580 160.801 1.00 28.26  ? 315  ARG B N     1 
ATOM   9879  C  CA    . ARG B 2 315 ? 126.773 115.550 162.060 1.00 26.86  ? 315  ARG B CA    1 
ATOM   9880  C  C     . ARG B 2 315 ? 126.343 116.959 162.472 1.00 28.09  ? 315  ARG B C     1 
ATOM   9881  O  O     . ARG B 2 315 ? 126.995 117.943 162.114 1.00 26.62  ? 315  ARG B O     1 
ATOM   9882  C  CB    . ARG B 2 315 ? 127.632 114.912 163.147 1.00 26.19  ? 315  ARG B CB    1 
ATOM   9883  C  CG    . ARG B 2 315 ? 127.611 113.389 163.122 1.00 32.32  ? 315  ARG B CG    1 
ATOM   9884  C  CD    . ARG B 2 315 ? 128.823 112.812 162.416 1.00 25.70  ? 315  ARG B CD    1 
ATOM   9885  N  NE    . ARG B 2 315 ? 130.018 112.875 163.249 1.00 30.40  ? 315  ARG B NE    1 
ATOM   9886  C  CZ    . ARG B 2 315 ? 131.230 112.517 162.849 1.00 36.21  ? 315  ARG B CZ    1 
ATOM   9887  N  NH1   . ARG B 2 315 ? 131.451 112.072 161.623 1.00 36.29  ? 315  ARG B NH1   1 
ATOM   9888  N  NH2   . ARG B 2 315 ? 132.247 112.608 163.700 1.00 31.20  ? 315  ARG B NH2   1 
ATOM   9889  N  N     . PRO B 2 316 ? 125.238 117.079 163.213 1.00 30.55  ? 316  PRO B N     1 
ATOM   9890  C  CA    . PRO B 2 316 ? 124.693 118.406 163.531 1.00 21.27  ? 316  PRO B CA    1 
ATOM   9891  C  C     . PRO B 2 316 ? 125.665 119.273 164.320 1.00 16.11  ? 316  PRO B C     1 
ATOM   9892  O  O     . PRO B 2 316 ? 126.386 118.797 165.198 1.00 29.66  ? 316  PRO B O     1 
ATOM   9893  C  CB    . PRO B 2 316 ? 123.442 118.082 164.353 1.00 23.89  ? 316  PRO B CB    1 
ATOM   9894  C  CG    . PRO B 2 316 ? 123.051 116.726 163.911 1.00 25.33  ? 316  PRO B CG    1 
ATOM   9895  C  CD    . PRO B 2 316 ? 124.329 116.001 163.640 1.00 28.91  ? 316  PRO B CD    1 
ATOM   9896  N  N     . THR B 2 317 ? 125.657 120.566 164.005 1.00 15.48  ? 317  THR B N     1 
ATOM   9897  C  CA    . THR B 2 317 ? 126.587 121.524 164.586 1.00 9.61   ? 317  THR B CA    1 
ATOM   9898  C  C     . THR B 2 317 ? 125.850 122.804 164.945 1.00 21.99  ? 317  THR B C     1 
ATOM   9899  O  O     . THR B 2 317 ? 125.113 123.350 164.121 1.00 30.77  ? 317  THR B O     1 
ATOM   9900  C  CB    . THR B 2 317 ? 127.726 121.836 163.611 1.00 8.36   ? 317  THR B CB    1 
ATOM   9901  O  OG1   . THR B 2 317 ? 128.378 120.620 163.230 1.00 16.14  ? 317  THR B OG1   1 
ATOM   9902  C  CG2   . THR B 2 317 ? 128.735 122.762 164.251 1.00 16.45  ? 317  THR B CG2   1 
ATOM   9903  N  N     . ASN B 2 318 ? 126.058 123.289 166.164 1.00 22.79  ? 318  ASN B N     1 
ATOM   9904  C  CA    . ASN B 2 318 ? 125.537 124.581 166.587 1.00 20.39  ? 318  ASN B CA    1 
ATOM   9905  C  C     . ASN B 2 318 ? 126.684 125.581 166.614 1.00 16.25  ? 318  ASN B C     1 
ATOM   9906  O  O     . ASN B 2 318 ? 127.701 125.347 167.273 1.00 24.07  ? 318  ASN B O     1 
ATOM   9907  C  CB    . ASN B 2 318 ? 124.874 124.488 167.959 1.00 15.08  ? 318  ASN B CB    1 
ATOM   9908  C  CG    . ASN B 2 318 ? 124.183 125.771 168.356 1.00 17.90  ? 318  ASN B CG    1 
ATOM   9909  O  OD1   . ASN B 2 318 ? 123.000 125.960 168.083 1.00 25.89  ? 318  ASN B OD1   1 
ATOM   9910  N  ND2   . ASN B 2 318 ? 124.918 126.663 169.004 1.00 21.79  ? 318  ASN B ND2   1 
ATOM   9911  N  N     . ILE B 2 319 ? 126.521 126.689 165.900 1.00 20.09  ? 319  ILE B N     1 
ATOM   9912  C  CA    . ILE B 2 319 ? 127.558 127.704 165.770 1.00 17.93  ? 319  ILE B CA    1 
ATOM   9913  C  C     . ILE B 2 319 ? 127.005 129.017 166.302 1.00 26.51  ? 319  ILE B C     1 
ATOM   9914  O  O     . ILE B 2 319 ? 126.055 129.569 165.738 1.00 39.16  ? 319  ILE B O     1 
ATOM   9915  C  CB    . ILE B 2 319 ? 128.023 127.857 164.314 1.00 15.30  ? 319  ILE B CB    1 
ATOM   9916  C  CG1   . ILE B 2 319 ? 128.411 126.495 163.738 1.00 18.99  ? 319  ILE B CG1   1 
ATOM   9917  C  CG2   . ILE B 2 319 ? 129.185 128.829 164.226 1.00 19.79  ? 319  ILE B CG2   1 
ATOM   9918  C  CD1   . ILE B 2 319 ? 128.874 126.542 162.309 1.00 23.59  ? 319  ILE B CD1   1 
ATOM   9919  N  N     . ASN B 2 320 ? 127.608 129.524 167.372 1.00 15.17  ? 320  ASN B N     1 
ATOM   9920  C  CA    . ASN B 2 320 ? 127.209 130.793 167.959 1.00 12.81  ? 320  ASN B CA    1 
ATOM   9921  C  C     . ASN B 2 320 ? 128.422 131.701 168.091 1.00 13.82  ? 320  ASN B C     1 
ATOM   9922  O  O     . ASN B 2 320 ? 129.568 131.246 168.115 1.00 24.43  ? 320  ASN B O     1 
ATOM   9923  C  CB    . ASN B 2 320 ? 126.546 130.606 169.331 1.00 22.41  ? 320  ASN B CB    1 
ATOM   9924  C  CG    . ASN B 2 320 ? 125.125 130.092 169.230 1.00 17.77  ? 320  ASN B CG    1 
ATOM   9925  O  OD1   . ASN B 2 320 ? 124.835 128.961 169.612 1.00 28.54  ? 320  ASN B OD1   1 
ATOM   9926  N  ND2   . ASN B 2 320 ? 124.229 130.927 168.726 1.00 20.00  ? 320  ASN B ND2   1 
ATOM   9927  N  N     . ASN B 2 321 ? 128.150 132.999 168.163 1.00 16.35  ? 321  ASN B N     1 
ATOM   9928  C  CA    . ASN B 2 321 ? 129.185 133.993 168.393 1.00 19.36  ? 321  ASN B CA    1 
ATOM   9929  C  C     . ASN B 2 321 ? 129.684 133.910 169.835 1.00 27.61  ? 321  ASN B C     1 
ATOM   9930  O  O     . ASN B 2 321 ? 129.044 133.320 170.709 1.00 33.17  ? 321  ASN B O     1 
ATOM   9931  C  CB    . ASN B 2 321 ? 128.645 135.392 168.085 1.00 25.70  ? 321  ASN B CB    1 
ATOM   9932  C  CG    . ASN B 2 321 ? 129.726 136.453 168.069 1.00 26.08  ? 321  ASN B CG    1 
ATOM   9933  O  OD1   . ASN B 2 321 ? 129.839 137.252 168.996 1.00 24.58  ? 321  ASN B OD1   1 
ATOM   9934  N  ND2   . ASN B 2 321 ? 130.529 136.464 167.016 1.00 26.43  ? 321  ASN B ND2   1 
ATOM   9935  N  N     . VAL B 2 322 ? 130.857 134.500 170.072 1.00 27.85  ? 322  VAL B N     1 
ATOM   9936  C  CA    . VAL B 2 322 ? 131.414 134.548 171.421 1.00 24.23  ? 322  VAL B CA    1 
ATOM   9937  C  C     . VAL B 2 322 ? 130.488 135.320 172.353 1.00 29.28  ? 322  VAL B C     1 
ATOM   9938  O  O     . VAL B 2 322 ? 130.267 134.925 173.504 1.00 39.61  ? 322  VAL B O     1 
ATOM   9939  C  CB    . VAL B 2 322 ? 132.825 135.164 171.389 1.00 23.45  ? 322  VAL B CB    1 
ATOM   9940  C  CG1   . VAL B 2 322 ? 133.435 135.175 172.772 1.00 21.86  ? 322  VAL B CG1   1 
ATOM   9941  C  CG2   . VAL B 2 322 ? 133.707 134.407 170.423 1.00 32.70  ? 322  VAL B CG2   1 
ATOM   9942  N  N     . GLU B 2 323 ? 129.930 136.429 171.867 1.00 31.62  ? 323  GLU B N     1 
ATOM   9943  C  CA    . GLU B 2 323 ? 129.034 137.242 172.682 1.00 24.41  ? 323  GLU B CA    1 
ATOM   9944  C  C     . GLU B 2 323 ? 127.742 136.497 173.004 1.00 24.77  ? 323  GLU B C     1 
ATOM   9945  O  O     . GLU B 2 323 ? 127.197 136.631 174.108 1.00 38.92  ? 323  GLU B O     1 
ATOM   9946  C  CB    . GLU B 2 323 ? 128.748 138.556 171.959 1.00 27.99  ? 323  GLU B CB    1 
ATOM   9947  C  CG    . GLU B 2 323 ? 127.936 139.554 172.751 1.00 35.27  ? 323  GLU B CG    1 
ATOM   9948  C  CD    . GLU B 2 323 ? 127.810 140.881 172.038 1.00 35.72  ? 323  GLU B CD    1 
ATOM   9949  O  OE1   . GLU B 2 323 ? 128.603 141.133 171.110 1.00 32.68  ? 323  GLU B OE1   1 
ATOM   9950  O  OE2   . GLU B 2 323 ? 126.915 141.670 172.403 1.00 38.18  ? 323  GLU B OE2   1 
ATOM   9951  N  N     . THR B 2 324 ? 127.237 135.708 172.052 1.00 14.32  ? 324  THR B N     1 
ATOM   9952  C  CA    . THR B 2 324 ? 126.045 134.906 172.306 1.00 21.77  ? 324  THR B CA    1 
ATOM   9953  C  C     . THR B 2 324 ? 126.295 133.876 173.403 1.00 25.00  ? 324  THR B C     1 
ATOM   9954  O  O     . THR B 2 324 ? 125.443 133.664 174.273 1.00 26.09  ? 324  THR B O     1 
ATOM   9955  C  CB    . THR B 2 324 ? 125.590 134.221 171.016 1.00 27.87  ? 324  THR B CB    1 
ATOM   9956  O  OG1   . THR B 2 324 ? 125.185 135.209 170.063 1.00 31.29  ? 324  THR B OG1   1 
ATOM   9957  C  CG2   . THR B 2 324 ? 124.427 133.295 171.283 1.00 26.37  ? 324  THR B CG2   1 
ATOM   9958  N  N     . TRP B 2 325 ? 127.464 133.232 173.382 1.00 33.01  ? 325  TRP B N     1 
ATOM   9959  C  CA    . TRP B 2 325 ? 127.813 132.303 174.451 1.00 21.46  ? 325  TRP B CA    1 
ATOM   9960  C  C     . TRP B 2 325 ? 128.016 133.023 175.776 1.00 26.41  ? 325  TRP B C     1 
ATOM   9961  O  O     . TRP B 2 325 ? 127.714 132.465 176.835 1.00 40.58  ? 325  TRP B O     1 
ATOM   9962  C  CB    . TRP B 2 325 ? 129.077 131.522 174.090 1.00 16.40  ? 325  TRP B CB    1 
ATOM   9963  C  CG    . TRP B 2 325 ? 128.920 130.522 172.982 1.00 18.11  ? 325  TRP B CG    1 
ATOM   9964  C  CD1   . TRP B 2 325 ? 129.562 130.527 171.780 1.00 18.59  ? 325  TRP B CD1   1 
ATOM   9965  C  CD2   . TRP B 2 325 ? 128.084 129.359 172.982 1.00 20.42  ? 325  TRP B CD2   1 
ATOM   9966  N  NE1   . TRP B 2 325 ? 129.176 129.447 171.029 1.00 20.87  ? 325  TRP B NE1   1 
ATOM   9967  C  CE2   . TRP B 2 325 ? 128.270 128.712 171.745 1.00 18.61  ? 325  TRP B CE2   1 
ATOM   9968  C  CE3   . TRP B 2 325 ? 127.196 128.803 173.905 1.00 24.20  ? 325  TRP B CE3   1 
ATOM   9969  C  CZ2   . TRP B 2 325 ? 127.599 127.542 171.408 1.00 19.21  ? 325  TRP B CZ2   1 
ATOM   9970  C  CZ3   . TRP B 2 325 ? 126.536 127.641 173.570 1.00 22.50  ? 325  TRP B CZ3   1 
ATOM   9971  C  CH2   . TRP B 2 325 ? 126.738 127.024 172.332 1.00 23.92  ? 325  TRP B CH2   1 
ATOM   9972  N  N     . ALA B 2 326 ? 128.532 134.250 175.740 1.00 28.02  ? 326  ALA B N     1 
ATOM   9973  C  CA    . ALA B 2 326 ? 128.789 134.996 176.963 1.00 23.31  ? 326  ALA B CA    1 
ATOM   9974  C  C     . ALA B 2 326 ? 127.519 135.543 177.606 1.00 25.24  ? 326  ALA B C     1 
ATOM   9975  O  O     . ALA B 2 326 ? 127.512 135.790 178.816 1.00 39.22  ? 326  ALA B O     1 
ATOM   9976  C  CB    . ALA B 2 326 ? 129.763 136.137 176.675 1.00 20.41  ? 326  ALA B CB    1 
ATOM   9977  N  N     . ASN B 2 327 ? 126.458 135.754 176.825 1.00 33.23  ? 327  ASN B N     1 
ATOM   9978  C  CA    . ASN B 2 327 ? 125.180 136.150 177.412 1.00 30.15  ? 327  ASN B CA    1 
ATOM   9979  C  C     . ASN B 2 327 ? 124.482 135.003 178.137 1.00 25.18  ? 327  ASN B C     1 
ATOM   9980  O  O     . ASN B 2 327 ? 123.638 135.259 179.001 1.00 27.39  ? 327  ASN B O     1 
ATOM   9981  C  CB    . ASN B 2 327 ? 124.244 136.706 176.338 1.00 31.12  ? 327  ASN B CB    1 
ATOM   9982  C  CG    . ASN B 2 327 ? 124.670 138.066 175.833 1.00 32.02  ? 327  ASN B CG    1 
ATOM   9983  O  OD1   . ASN B 2 327 ? 124.328 139.092 176.416 1.00 35.78  ? 327  ASN B OD1   1 
ATOM   9984  N  ND2   . ASN B 2 327 ? 125.407 138.082 174.732 1.00 33.16  ? 327  ASN B ND2   1 
ATOM   9985  N  N     . VAL B 2 328 ? 124.805 133.753 177.796 1.00 23.88  ? 328  VAL B N     1 
ATOM   9986  C  CA    . VAL B 2 328 ? 124.075 132.610 178.357 1.00 31.00  ? 328  VAL B CA    1 
ATOM   9987  C  C     . VAL B 2 328 ? 124.249 132.466 179.868 1.00 34.98  ? 328  VAL B C     1 
ATOM   9988  O  O     . VAL B 2 328 ? 123.240 132.250 180.563 1.00 37.06  ? 328  VAL B O     1 
ATOM   9989  C  CB    . VAL B 2 328 ? 124.438 131.327 177.588 1.00 26.75  ? 328  VAL B CB    1 
ATOM   9990  C  CG1   . VAL B 2 328 ? 123.853 130.101 178.265 1.00 27.95  ? 328  VAL B CG1   1 
ATOM   9991  C  CG2   . VAL B 2 328 ? 123.942 131.426 176.161 1.00 25.78  ? 328  VAL B CG2   1 
ATOM   9992  N  N     . PRO B 2 329 ? 125.466 132.537 180.440 1.00 32.59  ? 329  PRO B N     1 
ATOM   9993  C  CA    . PRO B 2 329 ? 125.567 132.436 181.908 1.00 31.46  ? 329  PRO B CA    1 
ATOM   9994  C  C     . PRO B 2 329 ? 124.784 133.505 182.644 1.00 34.96  ? 329  PRO B C     1 
ATOM   9995  O  O     . PRO B 2 329 ? 124.185 133.222 183.687 1.00 35.09  ? 329  PRO B O     1 
ATOM   9996  C  CB    . PRO B 2 329 ? 127.075 132.569 182.166 1.00 35.42  ? 329  PRO B CB    1 
ATOM   9997  C  CG    . PRO B 2 329 ? 127.712 132.160 180.913 1.00 30.12  ? 329  PRO B CG    1 
ATOM   9998  C  CD    . PRO B 2 329 ? 126.805 132.634 179.831 1.00 30.06  ? 329  PRO B CD    1 
ATOM   9999  N  N     . TRP B 2 330 ? 124.764 134.729 182.112 1.00 41.98  ? 330  TRP B N     1 
ATOM   10000 C  CA    . TRP B 2 330 ? 123.991 135.805 182.724 1.00 40.81  ? 330  TRP B CA    1 
ATOM   10001 C  C     . TRP B 2 330 ? 122.503 135.481 182.711 1.00 41.20  ? 330  TRP B C     1 
ATOM   10002 O  O     . TRP B 2 330 ? 121.782 135.789 183.666 1.00 46.24  ? 330  TRP B O     1 
ATOM   10003 C  CB    . TRP B 2 330 ? 124.264 137.115 181.983 1.00 38.16  ? 330  TRP B CB    1 
ATOM   10004 C  CG    . TRP B 2 330 ? 123.947 138.364 182.748 1.00 44.08  ? 330  TRP B CG    1 
ATOM   10005 C  CD1   . TRP B 2 330 ? 124.811 139.104 183.496 1.00 44.35  ? 330  TRP B CD1   1 
ATOM   10006 C  CD2   . TRP B 2 330 ? 122.682 139.036 182.815 1.00 43.12  ? 330  TRP B CD2   1 
ATOM   10007 N  NE1   . TRP B 2 330 ? 124.164 140.187 184.034 1.00 43.54  ? 330  TRP B NE1   1 
ATOM   10008 C  CE2   . TRP B 2 330 ? 122.856 140.169 183.631 1.00 42.06  ? 330  TRP B CE2   1 
ATOM   10009 C  CE3   . TRP B 2 330 ? 121.421 138.787 182.268 1.00 42.07  ? 330  TRP B CE3   1 
ATOM   10010 C  CZ2   . TRP B 2 330 ? 121.817 141.050 183.914 1.00 41.74  ? 330  TRP B CZ2   1 
ATOM   10011 C  CZ3   . TRP B 2 330 ? 120.391 139.663 182.551 1.00 40.29  ? 330  TRP B CZ3   1 
ATOM   10012 C  CH2   . TRP B 2 330 ? 120.595 140.780 183.365 1.00 43.38  ? 330  TRP B CH2   1 
ATOM   10013 N  N     . ILE B 2 331 ? 122.030 134.858 181.632 1.00 39.03  ? 331  ILE B N     1 
ATOM   10014 C  CA    . ILE B 2 331 ? 120.622 134.494 181.528 1.00 37.96  ? 331  ILE B CA    1 
ATOM   10015 C  C     . ILE B 2 331 ? 120.271 133.394 182.521 1.00 40.35  ? 331  ILE B C     1 
ATOM   10016 O  O     . ILE B 2 331 ? 119.229 133.449 183.183 1.00 47.85  ? 331  ILE B O     1 
ATOM   10017 C  CB    . ILE B 2 331 ? 120.294 134.081 180.083 1.00 34.66  ? 331  ILE B CB    1 
ATOM   10018 C  CG1   . ILE B 2 331 ? 120.312 135.303 179.169 1.00 34.47  ? 331  ILE B CG1   1 
ATOM   10019 C  CG2   . ILE B 2 331 ? 118.960 133.371 180.020 1.00 41.97  ? 331  ILE B CG2   1 
ATOM   10020 C  CD1   . ILE B 2 331 ? 120.126 134.967 177.721 1.00 35.35  ? 331  ILE B CD1   1 
ATOM   10021 N  N     . ILE B 2 332 ? 121.125 132.377 182.641 1.00 40.11  ? 332  ILE B N     1 
ATOM   10022 C  CA    . ILE B 2 332 ? 120.826 131.301 183.584 1.00 37.19  ? 332  ILE B CA    1 
ATOM   10023 C  C     . ILE B 2 332 ? 120.944 131.791 185.026 1.00 41.48  ? 332  ILE B C     1 
ATOM   10024 O  O     . ILE B 2 332 ? 120.246 131.295 185.918 1.00 43.86  ? 332  ILE B O     1 
ATOM   10025 C  CB    . ILE B 2 332 ? 121.730 130.084 183.312 1.00 37.53  ? 332  ILE B CB    1 
ATOM   10026 C  CG1   . ILE B 2 332 ? 121.648 129.684 181.841 1.00 43.16  ? 332  ILE B CG1   1 
ATOM   10027 C  CG2   . ILE B 2 332 ? 121.315 128.900 184.168 1.00 39.51  ? 332  ILE B CG2   1 
ATOM   10028 C  CD1   . ILE B 2 332 ? 120.274 129.229 181.409 1.00 41.00  ? 332  ILE B CD1   1 
ATOM   10029 N  N     . LYS B 2 333 ? 121.803 132.780 185.278 1.00 45.25  ? 333  LYS B N     1 
ATOM   10030 C  CA    . LYS B 2 333 ? 122.030 133.258 186.638 1.00 44.18  ? 333  LYS B CA    1 
ATOM   10031 C  C     . LYS B 2 333 ? 120.945 134.232 187.085 1.00 45.27  ? 333  LYS B C     1 
ATOM   10032 O  O     . LYS B 2 333 ? 120.333 134.048 188.142 1.00 47.10  ? 333  LYS B O     1 
ATOM   10033 C  CB    . LYS B 2 333 ? 123.412 133.908 186.720 1.00 41.71  ? 333  LYS B CB    1 
ATOM   10034 C  CG    . LYS B 2 333 ? 123.969 134.088 188.116 1.00 43.73  ? 333  LYS B CG    1 
ATOM   10035 C  CD    . LYS B 2 333 ? 125.427 134.518 188.042 1.00 45.05  ? 333  LYS B CD    1 
ATOM   10036 C  CE    . LYS B 2 333 ? 126.039 134.700 189.420 1.00 51.04  ? 333  LYS B CE    1 
ATOM   10037 N  NZ    . LYS B 2 333 ? 125.381 135.793 190.184 1.00 49.27  ? 333  LYS B NZ    1 
ATOM   10038 N  N     . HIS B 2 334 ? 120.693 135.276 186.300 1.00 43.09  ? 334  HIS B N     1 
ATOM   10039 C  CA    . HIS B 2 334 ? 119.737 136.307 186.677 1.00 43.27  ? 334  HIS B CA    1 
ATOM   10040 C  C     . HIS B 2 334 ? 118.336 136.058 186.133 1.00 46.50  ? 334  HIS B C     1 
ATOM   10041 O  O     . HIS B 2 334 ? 117.442 136.875 186.375 1.00 51.01  ? 334  HIS B O     1 
ATOM   10042 C  CB    . HIS B 2 334 ? 120.228 137.681 186.208 1.00 43.25  ? 334  HIS B CB    1 
ATOM   10043 C  CG    . HIS B 2 334 ? 121.538 138.094 186.805 1.00 45.18  ? 334  HIS B CG    1 
ATOM   10044 N  ND1   . HIS B 2 334 ? 122.752 137.741 186.255 1.00 46.25  ? 334  HIS B ND1   1 
ATOM   10045 C  CD2   . HIS B 2 334 ? 121.825 138.832 187.902 1.00 49.26  ? 334  HIS B CD2   1 
ATOM   10046 C  CE1   . HIS B 2 334 ? 123.729 138.244 186.987 1.00 47.29  ? 334  HIS B CE1   1 
ATOM   10047 N  NE2   . HIS B 2 334 ? 123.194 138.910 187.993 1.00 51.10  ? 334  HIS B NE2   1 
ATOM   10048 N  N     . GLY B 2 335 ? 118.119 134.970 185.410 1.00 42.43  ? 335  GLY B N     1 
ATOM   10049 C  CA    . GLY B 2 335 ? 116.815 134.680 184.857 1.00 44.49  ? 335  GLY B CA    1 
ATOM   10050 C  C     . GLY B 2 335 ? 116.559 135.420 183.555 1.00 46.79  ? 335  GLY B C     1 
ATOM   10051 O  O     . GLY B 2 335 ? 117.211 136.406 183.219 1.00 49.48  ? 335  GLY B O     1 
ATOM   10052 N  N     . TRP B 2 336 ? 115.578 134.919 182.807 1.00 50.53  ? 336  TRP B N     1 
ATOM   10053 C  CA    . TRP B 2 336 ? 115.201 135.559 181.555 1.00 48.00  ? 336  TRP B CA    1 
ATOM   10054 C  C     . TRP B 2 336 ? 114.373 136.818 181.769 1.00 50.66  ? 336  TRP B C     1 
ATOM   10055 O  O     . TRP B 2 336 ? 114.263 137.638 180.850 1.00 49.88  ? 336  TRP B O     1 
ATOM   10056 C  CB    . TRP B 2 336 ? 114.433 134.576 180.674 1.00 46.93  ? 336  TRP B CB    1 
ATOM   10057 C  CG    . TRP B 2 336 ? 113.170 134.066 181.277 1.00 52.35  ? 336  TRP B CG    1 
ATOM   10058 C  CD1   . TRP B 2 336 ? 113.020 132.949 182.045 1.00 53.67  ? 336  TRP B CD1   1 
ATOM   10059 C  CD2   . TRP B 2 336 ? 111.867 134.641 181.147 1.00 53.41  ? 336  TRP B CD2   1 
ATOM   10060 N  NE1   . TRP B 2 336 ? 111.704 132.796 182.406 1.00 55.86  ? 336  TRP B NE1   1 
ATOM   10061 C  CE2   . TRP B 2 336 ? 110.976 133.823 181.866 1.00 54.37  ? 336  TRP B CE2   1 
ATOM   10062 C  CE3   . TRP B 2 336 ? 111.367 135.770 180.492 1.00 53.84  ? 336  TRP B CE3   1 
ATOM   10063 C  CZ2   . TRP B 2 336 ? 109.616 134.099 181.951 1.00 51.50  ? 336  TRP B CZ2   1 
ATOM   10064 C  CZ3   . TRP B 2 336 ? 110.017 136.040 180.577 1.00 53.26  ? 336  TRP B CZ3   1 
ATOM   10065 C  CH2   . TRP B 2 336 ? 109.156 135.209 181.301 1.00 50.84  ? 336  TRP B CH2   1 
ATOM   10066 N  N     . GLU B 2 337 ? 113.800 136.989 182.962 1.00 47.90  ? 337  GLU B N     1 
ATOM   10067 C  CA    . GLU B 2 337 ? 113.037 138.196 183.261 1.00 50.18  ? 337  GLU B CA    1 
ATOM   10068 C  C     . GLU B 2 337 ? 113.925 139.434 183.226 1.00 47.70  ? 337  GLU B C     1 
ATOM   10069 O  O     . GLU B 2 337 ? 113.504 140.497 182.755 1.00 46.35  ? 337  GLU B O     1 
ATOM   10070 C  CB    . GLU B 2 337 ? 112.366 138.054 184.626 1.00 48.45  ? 337  GLU B CB    1 
ATOM   10071 C  CG    . GLU B 2 337 ? 111.139 138.922 184.814 1.00 49.31  ? 337  GLU B CG    1 
ATOM   10072 C  CD    . GLU B 2 337 ? 109.904 138.325 184.173 1.00 52.23  ? 337  GLU B CD    1 
ATOM   10073 O  OE1   . GLU B 2 337 ? 109.960 137.151 183.754 1.00 52.45  ? 337  GLU B OE1   1 
ATOM   10074 O  OE2   . GLU B 2 337 ? 108.877 139.029 184.091 1.00 50.59  ? 337  GLU B OE2   1 
ATOM   10075 N  N     . ALA B 2 338 ? 115.156 139.318 183.729 1.00 45.51  ? 338  ALA B N     1 
ATOM   10076 C  CA    . ALA B 2 338 ? 116.068 140.457 183.736 1.00 44.11  ? 338  ALA B CA    1 
ATOM   10077 C  C     . ALA B 2 338 ? 116.553 140.809 182.334 1.00 47.83  ? 338  ALA B C     1 
ATOM   10078 O  O     . ALA B 2 338 ? 116.762 141.989 182.033 1.00 54.36  ? 338  ALA B O     1 
ATOM   10079 C  CB    . ALA B 2 338 ? 117.257 140.170 184.651 1.00 47.31  ? 338  ALA B CB    1 
ATOM   10080 N  N     . TYR B 2 339 ? 116.748 139.811 181.471 1.00 47.69  ? 339  TYR B N     1 
ATOM   10081 C  CA    . TYR B 2 339 ? 117.162 140.087 180.101 1.00 42.36  ? 339  TYR B CA    1 
ATOM   10082 C  C     . TYR B 2 339 ? 116.015 140.636 179.262 1.00 42.36  ? 339  TYR B C     1 
ATOM   10083 O  O     . TYR B 2 339 ? 116.242 141.471 178.380 1.00 42.81  ? 339  TYR B O     1 
ATOM   10084 C  CB    . TYR B 2 339 ? 117.731 138.822 179.460 1.00 44.77  ? 339  TYR B CB    1 
ATOM   10085 C  CG    . TYR B 2 339 ? 118.804 139.082 178.428 1.00 45.42  ? 339  TYR B CG    1 
ATOM   10086 C  CD1   . TYR B 2 339 ? 120.032 139.610 178.796 1.00 41.64  ? 339  TYR B CD1   1 
ATOM   10087 C  CD2   . TYR B 2 339 ? 118.596 138.780 177.089 1.00 42.30  ? 339  TYR B CD2   1 
ATOM   10088 C  CE1   . TYR B 2 339 ? 121.016 139.842 177.860 1.00 38.94  ? 339  TYR B CE1   1 
ATOM   10089 C  CE2   . TYR B 2 339 ? 119.576 139.008 176.148 1.00 37.11  ? 339  TYR B CE2   1 
ATOM   10090 C  CZ    . TYR B 2 339 ? 120.784 139.538 176.539 1.00 39.87  ? 339  TYR B CZ    1 
ATOM   10091 O  OH    . TYR B 2 339 ? 121.763 139.770 175.605 1.00 46.33  ? 339  TYR B OH    1 
ATOM   10092 N  N     . ALA B 2 340 ? 114.786 140.186 179.517 1.00 50.91  ? 340  ALA B N     1 
ATOM   10093 C  CA    . ALA B 2 340 ? 113.628 140.764 178.848 1.00 47.02  ? 340  ALA B CA    1 
ATOM   10094 C  C     . ALA B 2 340 ? 113.262 142.137 179.393 1.00 44.78  ? 340  ALA B C     1 
ATOM   10095 O  O     . ALA B 2 340 ? 112.458 142.836 178.769 1.00 52.29  ? 340  ALA B O     1 
ATOM   10096 C  CB    . ALA B 2 340 ? 112.428 139.826 178.965 1.00 48.81  ? 340  ALA B CB    1 
ATOM   10097 N  N     . ALA B 2 341 ? 113.823 142.535 180.533 1.00 45.40  ? 341  ALA B N     1 
ATOM   10098 C  CA    . ALA B 2 341 ? 113.601 143.868 181.074 1.00 49.81  ? 341  ALA B CA    1 
ATOM   10099 C  C     . ALA B 2 341 ? 114.447 144.931 180.391 1.00 51.60  ? 341  ALA B C     1 
ATOM   10100 O  O     . ALA B 2 341 ? 114.242 146.121 180.649 1.00 51.05  ? 341  ALA B O     1 
ATOM   10101 C  CB    . ALA B 2 341 ? 113.882 143.881 182.578 1.00 48.91  ? 341  ALA B CB    1 
ATOM   10102 N  N     . LEU B 2 342 ? 115.384 144.537 179.535 1.00 51.88  ? 342  LEU B N     1 
ATOM   10103 C  CA    . LEU B 2 342 ? 116.239 145.464 178.810 1.00 52.69  ? 342  LEU B CA    1 
ATOM   10104 C  C     . LEU B 2 342 ? 115.929 145.410 177.321 1.00 53.58  ? 342  LEU B C     1 
ATOM   10105 O  O     . LEU B 2 342 ? 115.601 144.348 176.783 1.00 52.38  ? 342  LEU B O     1 
ATOM   10106 C  CB    . LEU B 2 342 ? 117.717 145.140 179.035 1.00 51.43  ? 342  LEU B CB    1 
ATOM   10107 C  CG    . LEU B 2 342 ? 118.227 145.157 180.473 1.00 51.49  ? 342  LEU B CG    1 
ATOM   10108 C  CD1   . LEU B 2 342 ? 119.713 144.863 180.501 1.00 51.52  ? 342  LEU B CD1   1 
ATOM   10109 C  CD2   . LEU B 2 342 ? 117.930 146.494 181.129 1.00 51.97  ? 342  LEU B CD2   1 
ATOM   10110 N  N     . GLY B 2 343 ? 116.030 146.559 176.662 1.00 56.43  ? 343  GLY B N     1 
ATOM   10111 C  CA    . GLY B 2 343 ? 115.968 146.629 175.216 1.00 58.37  ? 343  GLY B CA    1 
ATOM   10112 C  C     . GLY B 2 343 ? 114.602 147.032 174.700 1.00 60.76  ? 343  GLY B C     1 
ATOM   10113 O  O     . GLY B 2 343 ? 113.676 147.357 175.449 1.00 59.07  ? 343  GLY B O     1 
ATOM   10114 N  N     . THR B 2 344 ? 114.495 147.015 173.374 1.00 63.24  ? 344  THR B N     1 
ATOM   10115 C  CA    . THR B 2 344 ? 113.237 147.273 172.695 1.00 63.15  ? 344  THR B CA    1 
ATOM   10116 C  C     . THR B 2 344 ? 112.402 145.998 172.636 1.00 63.88  ? 344  THR B C     1 
ATOM   10117 O  O     . THR B 2 344 ? 112.794 144.941 173.134 1.00 64.75  ? 344  THR B O     1 
ATOM   10118 C  CB    . THR B 2 344 ? 113.484 147.816 171.291 1.00 66.19  ? 344  THR B CB    1 
ATOM   10119 O  OG1   . THR B 2 344 ? 114.848 147.587 170.920 1.00 65.46  ? 344  THR B OG1   1 
ATOM   10120 C  CG2   . THR B 2 344 ? 113.175 149.305 171.233 1.00 67.48  ? 344  THR B CG2   1 
ATOM   10121 N  N     . GLU B 2 345 ? 111.231 146.101 172.009 1.00 72.25  ? 345  GLU B N     1 
ATOM   10122 C  CA    . GLU B 2 345 ? 110.316 144.967 171.954 1.00 72.77  ? 345  GLU B CA    1 
ATOM   10123 C  C     . GLU B 2 345 ? 110.891 143.829 171.119 1.00 73.72  ? 345  GLU B C     1 
ATOM   10124 O  O     . GLU B 2 345 ? 110.887 142.670 171.547 1.00 75.12  ? 345  GLU B O     1 
ATOM   10125 C  CB    . GLU B 2 345 ? 108.963 145.407 171.396 1.00 72.89  ? 345  GLU B CB    1 
ATOM   10126 C  CG    . GLU B 2 345 ? 108.267 146.486 172.204 1.00 73.44  ? 345  GLU B CG    1 
ATOM   10127 C  CD    . GLU B 2 345 ? 108.695 147.881 171.805 1.00 72.86  ? 345  GLU B CD    1 
ATOM   10128 O  OE1   . GLU B 2 345 ? 109.439 148.011 170.811 1.00 71.67  ? 345  GLU B OE1   1 
ATOM   10129 O  OE2   . GLU B 2 345 ? 108.289 148.847 172.483 1.00 73.62  ? 345  GLU B OE2   1 
ATOM   10130 N  N     . LYS B 2 346 ? 111.389 144.139 169.926 1.00 71.47  ? 346  LYS B N     1 
ATOM   10131 C  CA    . LYS B 2 346 ? 111.871 143.120 169.005 1.00 70.69  ? 346  LYS B CA    1 
ATOM   10132 C  C     . LYS B 2 346 ? 113.373 142.886 169.098 1.00 70.58  ? 346  LYS B C     1 
ATOM   10133 O  O     . LYS B 2 346 ? 113.895 142.027 168.382 1.00 73.42  ? 346  LYS B O     1 
ATOM   10134 C  CB    . LYS B 2 346 ? 111.491 143.489 167.570 1.00 69.08  ? 346  LYS B CB    1 
ATOM   10135 C  CG    . LYS B 2 346 ? 110.000 143.666 167.364 1.00 72.19  ? 346  LYS B CG    1 
ATOM   10136 C  CD    . LYS B 2 346 ? 109.660 143.800 165.893 1.00 72.41  ? 346  LYS B CD    1 
ATOM   10137 C  CE    . LYS B 2 346 ? 110.114 142.577 165.116 1.00 71.86  ? 346  LYS B CE    1 
ATOM   10138 N  NZ    . LYS B 2 346 ? 109.539 141.324 165.678 1.00 69.39  ? 346  LYS B NZ    1 
ATOM   10139 N  N     . SER B 2 347 ? 114.076 143.616 169.959 1.00 58.31  ? 347  SER B N     1 
ATOM   10140 C  CA    . SER B 2 347 ? 115.511 143.420 170.159 1.00 57.43  ? 347  SER B CA    1 
ATOM   10141 C  C     . SER B 2 347 ? 115.789 143.583 171.649 1.00 58.88  ? 347  SER B C     1 
ATOM   10142 O  O     . SER B 2 347 ? 115.934 144.705 172.140 1.00 60.78  ? 347  SER B O     1 
ATOM   10143 C  CB    . SER B 2 347 ? 116.326 144.402 169.328 1.00 56.09  ? 347  SER B CB    1 
ATOM   10144 O  OG    . SER B 2 347 ? 116.009 144.289 167.954 1.00 59.40  ? 347  SER B OG    1 
ATOM   10145 N  N     . LYS B 2 348 ? 115.855 142.464 172.363 1.00 52.08  ? 348  LYS B N     1 
ATOM   10146 C  CA    . LYS B 2 348 ? 116.067 142.486 173.799 1.00 48.38  ? 348  LYS B CA    1 
ATOM   10147 C  C     . LYS B 2 348 ? 117.559 142.479 174.118 1.00 49.30  ? 348  LYS B C     1 
ATOM   10148 O  O     . LYS B 2 348 ? 118.416 142.370 173.238 1.00 48.60  ? 348  LYS B O     1 
ATOM   10149 C  CB    . LYS B 2 348 ? 115.364 141.302 174.459 1.00 50.60  ? 348  LYS B CB    1 
ATOM   10150 C  CG    . LYS B 2 348 ? 113.853 141.355 174.382 1.00 54.55  ? 348  LYS B CG    1 
ATOM   10151 C  CD    . LYS B 2 348 ? 113.311 142.533 175.162 1.00 50.17  ? 348  LYS B CD    1 
ATOM   10152 C  CE    . LYS B 2 348 ? 111.798 142.582 175.105 1.00 53.07  ? 348  LYS B CE    1 
ATOM   10153 N  NZ    . LYS B 2 348 ? 111.264 143.755 175.843 1.00 53.26  ? 348  LYS B NZ    1 
ATOM   10154 N  N     . GLY B 2 349 ? 117.871 142.603 175.401 1.00 50.83  ? 349  GLY B N     1 
ATOM   10155 C  CA    . GLY B 2 349 ? 119.238 142.499 175.856 1.00 47.32  ? 349  GLY B CA    1 
ATOM   10156 C  C     . GLY B 2 349 ? 120.062 143.742 175.578 1.00 46.04  ? 349  GLY B C     1 
ATOM   10157 O  O     . GLY B 2 349 ? 119.553 144.855 175.423 1.00 48.04  ? 349  GLY B O     1 
ATOM   10158 N  N     . THR B 2 350 ? 121.373 143.533 175.535 1.00 42.06  ? 350  THR B N     1 
ATOM   10159 C  CA    . THR B 2 350 ? 122.333 144.594 175.287 1.00 38.58  ? 350  THR B CA    1 
ATOM   10160 C  C     . THR B 2 350 ? 123.270 144.171 174.166 1.00 34.84  ? 350  THR B C     1 
ATOM   10161 O  O     . THR B 2 350 ? 123.437 142.984 173.880 1.00 39.59  ? 350  THR B O     1 
ATOM   10162 C  CB    . THR B 2 350 ? 123.144 144.939 176.544 1.00 44.88  ? 350  THR B CB    1 
ATOM   10163 O  OG1   . THR B 2 350 ? 123.916 143.803 176.948 1.00 47.55  ? 350  THR B OG1   1 
ATOM   10164 C  CG2   . THR B 2 350 ? 122.233 145.356 177.684 1.00 45.25  ? 350  THR B CG2   1 
ATOM   10165 N  N     . LYS B 2 351 ? 123.875 145.165 173.524 1.00 38.72  ? 351  LYS B N     1 
ATOM   10166 C  CA    . LYS B 2 351 ? 124.757 144.955 172.387 1.00 42.26  ? 351  LYS B CA    1 
ATOM   10167 C  C     . LYS B 2 351 ? 126.120 145.561 172.688 1.00 41.85  ? 351  LYS B C     1 
ATOM   10168 O  O     . LYS B 2 351 ? 126.213 146.607 173.337 1.00 52.87  ? 351  LYS B O     1 
ATOM   10169 C  CB    . LYS B 2 351 ? 124.170 145.581 171.116 1.00 38.76  ? 351  LYS B CB    1 
ATOM   10170 C  CG    . LYS B 2 351 ? 124.835 145.146 169.821 1.00 40.85  ? 351  LYS B CG    1 
ATOM   10171 C  CD    . LYS B 2 351 ? 124.405 143.750 169.419 1.00 42.28  ? 351  LYS B CD    1 
ATOM   10172 C  CE    . LYS B 2 351 ? 125.028 143.337 168.099 1.00 43.60  ? 351  LYS B CE    1 
ATOM   10173 N  NZ    . LYS B 2 351 ? 126.510 143.305 168.178 1.00 43.53  ? 351  LYS B NZ    1 
ATOM   10174 N  N     . VAL B 2 352 ? 127.174 144.900 172.224 1.00 30.24  ? 352  VAL B N     1 
ATOM   10175 C  CA    . VAL B 2 352 ? 128.534 145.405 172.361 1.00 28.53  ? 352  VAL B CA    1 
ATOM   10176 C  C     . VAL B 2 352 ? 128.918 146.077 171.052 1.00 35.73  ? 352  VAL B C     1 
ATOM   10177 O  O     . VAL B 2 352 ? 128.924 145.437 169.994 1.00 41.58  ? 352  VAL B O     1 
ATOM   10178 C  CB    . VAL B 2 352 ? 129.525 144.287 172.716 1.00 31.62  ? 352  VAL B CB    1 
ATOM   10179 C  CG1   . VAL B 2 352 ? 130.917 144.862 172.896 1.00 32.32  ? 352  VAL B CG1   1 
ATOM   10180 C  CG2   . VAL B 2 352 ? 129.085 143.571 173.969 1.00 33.94  ? 352  VAL B CG2   1 
ATOM   10181 N  N     . PHE B 2 353 ? 129.237 147.364 171.119 1.00 42.22  ? 353  PHE B N     1 
ATOM   10182 C  CA    . PHE B 2 353 ? 129.617 148.133 169.946 1.00 38.63  ? 353  PHE B CA    1 
ATOM   10183 C  C     . PHE B 2 353 ? 131.056 148.604 170.067 1.00 39.32  ? 353  PHE B C     1 
ATOM   10184 O  O     . PHE B 2 353 ? 131.493 149.040 171.136 1.00 50.26  ? 353  PHE B O     1 
ATOM   10185 C  CB    . PHE B 2 353 ? 128.695 149.335 169.740 1.00 34.02  ? 353  PHE B CB    1 
ATOM   10186 C  CG    . PHE B 2 353 ? 127.383 148.981 169.121 1.00 33.08  ? 353  PHE B CG    1 
ATOM   10187 C  CD1   . PHE B 2 353 ? 127.316 148.582 167.800 1.00 38.49  ? 353  PHE B CD1   1 
ATOM   10188 C  CD2   . PHE B 2 353 ? 126.217 149.041 169.857 1.00 41.35  ? 353  PHE B CD2   1 
ATOM   10189 C  CE1   . PHE B 2 353 ? 126.113 148.250 167.225 1.00 42.45  ? 353  PHE B CE1   1 
ATOM   10190 C  CE2   . PHE B 2 353 ? 125.011 148.712 169.286 1.00 44.50  ? 353  PHE B CE2   1 
ATOM   10191 C  CZ    . PHE B 2 353 ? 124.960 148.314 167.968 1.00 44.70  ? 353  PHE B CZ    1 
ATOM   10192 N  N     . ALA B 2 354 ? 131.789 148.500 168.966 1.00 35.88  ? 354  ALA B N     1 
ATOM   10193 C  CA    . ALA B 2 354 ? 133.140 149.035 168.877 1.00 39.04  ? 354  ALA B CA    1 
ATOM   10194 C  C     . ALA B 2 354 ? 133.054 150.435 168.286 1.00 48.92  ? 354  ALA B C     1 
ATOM   10195 O  O     . ALA B 2 354 ? 132.786 150.597 167.092 1.00 51.80  ? 354  ALA B O     1 
ATOM   10196 C  CB    . ALA B 2 354 ? 134.027 148.127 168.032 1.00 43.40  ? 354  ALA B CB    1 
ATOM   10197 N  N     . LEU B 2 355 ? 133.268 151.446 169.120 1.00 48.42  ? 355  LEU B N     1 
ATOM   10198 C  CA    . LEU B 2 355 ? 133.256 152.830 168.670 1.00 46.97  ? 355  LEU B CA    1 
ATOM   10199 C  C     . LEU B 2 355 ? 134.648 153.194 168.170 1.00 46.71  ? 355  LEU B C     1 
ATOM   10200 O  O     . LEU B 2 355 ? 135.615 153.180 168.939 1.00 46.03  ? 355  LEU B O     1 
ATOM   10201 C  CB    . LEU B 2 355 ? 132.821 153.768 169.794 1.00 49.40  ? 355  LEU B CB    1 
ATOM   10202 C  CG    . LEU B 2 355 ? 131.455 153.490 170.423 1.00 44.61  ? 355  LEU B CG    1 
ATOM   10203 C  CD1   . LEU B 2 355 ? 131.074 154.604 171.381 1.00 44.33  ? 355  LEU B CD1   1 
ATOM   10204 C  CD2   . LEU B 2 355 ? 130.395 153.312 169.355 1.00 45.60  ? 355  LEU B CD2   1 
ATOM   10205 N  N     . SER B 2 356 ? 134.747 153.513 166.884 1.00 46.35  ? 356  SER B N     1 
ATOM   10206 C  CA    . SER B 2 356 ? 136.016 153.859 166.265 1.00 50.04  ? 356  SER B CA    1 
ATOM   10207 C  C     . SER B 2 356 ? 135.771 155.016 165.305 1.00 49.83  ? 356  SER B C     1 
ATOM   10208 O  O     . SER B 2 356 ? 134.712 155.651 165.322 1.00 49.84  ? 356  SER B O     1 
ATOM   10209 C  CB    . SER B 2 356 ? 136.631 152.634 165.575 1.00 51.61  ? 356  SER B CB    1 
ATOM   10210 O  OG    . SER B 2 356 ? 135.707 152.027 164.692 1.00 49.62  ? 356  SER B OG    1 
ATOM   10211 N  N     . GLY B 2 357 ? 136.759 155.298 164.468 1.00 53.37  ? 357  GLY B N     1 
ATOM   10212 C  CA    . GLY B 2 357 ? 136.651 156.387 163.513 1.00 52.24  ? 357  GLY B CA    1 
ATOM   10213 C  C     . GLY B 2 357 ? 137.115 157.692 164.122 1.00 54.85  ? 357  GLY B C     1 
ATOM   10214 O  O     . GLY B 2 357 ? 138.155 157.741 164.777 1.00 56.66  ? 357  GLY B O     1 
ATOM   10215 N  N     . LYS B 2 358 ? 136.335 158.753 163.909 1.00 61.12  ? 358  LYS B N     1 
ATOM   10216 C  CA    . LYS B 2 358 ? 136.644 160.075 164.438 1.00 60.56  ? 358  LYS B CA    1 
ATOM   10217 C  C     . LYS B 2 358 ? 135.941 160.356 165.758 1.00 61.49  ? 358  LYS B C     1 
ATOM   10218 O  O     . LYS B 2 358 ? 135.598 161.510 166.038 1.00 66.13  ? 358  LYS B O     1 
ATOM   10219 C  CB    . LYS B 2 358 ? 136.287 161.149 163.410 1.00 62.57  ? 358  LYS B CB    1 
ATOM   10220 C  CG    . LYS B 2 358 ? 137.202 161.184 162.197 1.00 63.30  ? 358  LYS B CG    1 
ATOM   10221 C  CD    . LYS B 2 358 ? 138.601 161.645 162.572 1.00 65.62  ? 358  LYS B CD    1 
ATOM   10222 C  CE    . LYS B 2 358 ? 139.484 161.777 161.343 1.00 62.87  ? 358  LYS B CE    1 
ATOM   10223 N  NZ    . LYS B 2 358 ? 138.921 162.742 160.358 1.00 62.11  ? 358  LYS B NZ    1 
ATOM   10224 N  N     . ILE B 2 359 ? 135.716 159.334 166.573 1.00 60.62  ? 359  ILE B N     1 
ATOM   10225 C  CA    . ILE B 2 359 ? 134.959 159.491 167.804 1.00 60.57  ? 359  ILE B CA    1 
ATOM   10226 C  C     . ILE B 2 359 ? 135.915 159.789 168.954 1.00 61.72  ? 359  ILE B C     1 
ATOM   10227 O  O     . ILE B 2 359 ? 137.110 159.488 168.903 1.00 60.62  ? 359  ILE B O     1 
ATOM   10228 C  CB    . ILE B 2 359 ? 134.096 158.243 168.087 1.00 58.25  ? 359  ILE B CB    1 
ATOM   10229 C  CG1   . ILE B 2 359 ? 132.871 158.612 168.923 1.00 60.72  ? 359  ILE B CG1   1 
ATOM   10230 C  CG2   . ILE B 2 359 ? 134.912 157.168 168.771 1.00 58.20  ? 359  ILE B CG2   1 
ATOM   10231 C  CD1   . ILE B 2 359 ? 131.892 157.478 169.090 1.00 60.46  ? 359  ILE B CD1   1 
ATOM   10232 N  N     . LYS B 2 360 ? 135.376 160.404 170.006 1.00 66.26  ? 360  LYS B N     1 
ATOM   10233 C  CA    . LYS B 2 360 ? 136.171 160.871 171.137 1.00 64.88  ? 360  LYS B CA    1 
ATOM   10234 C  C     . LYS B 2 360 ? 136.372 159.775 172.180 1.00 64.21  ? 360  LYS B C     1 
ATOM   10235 O  O     . LYS B 2 360 ? 137.509 159.413 172.499 1.00 64.64  ? 360  LYS B O     1 
ATOM   10236 C  CB    . LYS B 2 360 ? 135.498 162.098 171.762 1.00 63.16  ? 360  LYS B CB    1 
ATOM   10237 C  CG    . LYS B 2 360 ? 136.280 162.761 172.870 1.00 63.87  ? 360  LYS B CG    1 
ATOM   10238 C  CD    . LYS B 2 360 ? 135.550 163.995 173.365 1.00 65.71  ? 360  LYS B CD    1 
ATOM   10239 C  CE    . LYS B 2 360 ? 136.351 164.723 174.426 1.00 66.63  ? 360  LYS B CE    1 
ATOM   10240 N  NZ    . LYS B 2 360 ? 135.635 165.929 174.923 1.00 65.17  ? 360  LYS B NZ    1 
ATOM   10241 N  N     . HIS B 2 361 ? 135.280 159.245 172.722 1.00 61.91  ? 361  HIS B N     1 
ATOM   10242 C  CA    . HIS B 2 361 ? 135.351 158.181 173.722 1.00 62.02  ? 361  HIS B CA    1 
ATOM   10243 C  C     . HIS B 2 361 ? 135.139 156.824 173.053 1.00 65.22  ? 361  HIS B C     1 
ATOM   10244 O  O     . HIS B 2 361 ? 134.146 156.130 173.265 1.00 65.57  ? 361  HIS B O     1 
ATOM   10245 C  CB    . HIS B 2 361 ? 134.334 158.430 174.829 1.00 61.63  ? 361  HIS B CB    1 
ATOM   10246 C  CG    . HIS B 2 361 ? 134.600 159.668 175.623 1.00 65.73  ? 361  HIS B CG    1 
ATOM   10247 N  ND1   . HIS B 2 361 ? 135.851 160.240 175.709 1.00 68.27  ? 361  HIS B ND1   1 
ATOM   10248 C  CD2   . HIS B 2 361 ? 133.778 160.448 176.364 1.00 64.00  ? 361  HIS B CD2   1 
ATOM   10249 C  CE1   . HIS B 2 361 ? 135.789 161.316 176.471 1.00 66.27  ? 361  HIS B CE1   1 
ATOM   10250 N  NE2   . HIS B 2 361 ? 134.542 161.466 176.880 1.00 64.56  ? 361  HIS B NE2   1 
ATOM   10251 N  N     . GLY B 2 362 ? 136.112 156.454 172.226 1.00 61.19  ? 362  GLY B N     1 
ATOM   10252 C  CA    . GLY B 2 362 ? 136.048 155.182 171.542 1.00 58.16  ? 362  GLY B CA    1 
ATOM   10253 C  C     . GLY B 2 362 ? 136.350 154.013 172.457 1.00 62.32  ? 362  GLY B C     1 
ATOM   10254 O  O     . GLY B 2 362 ? 136.960 154.149 173.518 1.00 67.22  ? 362  GLY B O     1 
ATOM   10255 N  N     . GLY B 2 363 ? 135.912 152.843 172.031 1.00 55.79  ? 363  GLY B N     1 
ATOM   10256 C  CA    . GLY B 2 363 ? 136.126 151.629 172.786 1.00 55.44  ? 363  GLY B CA    1 
ATOM   10257 C  C     . GLY B 2 363 ? 134.977 150.668 172.569 1.00 51.37  ? 363  GLY B C     1 
ATOM   10258 O  O     . GLY B 2 363 ? 134.185 150.815 171.643 1.00 58.14  ? 363  GLY B O     1 
ATOM   10259 N  N     . ASN B 2 364 ? 134.906 149.673 173.448 1.00 45.28  ? 364  ASN B N     1 
ATOM   10260 C  CA    . ASN B 2 364 ? 133.845 148.675 173.421 1.00 46.01  ? 364  ASN B CA    1 
ATOM   10261 C  C     . ASN B 2 364 ? 132.788 149.070 174.444 1.00 49.16  ? 364  ASN B C     1 
ATOM   10262 O  O     . ASN B 2 364 ? 133.041 149.040 175.652 1.00 54.07  ? 364  ASN B O     1 
ATOM   10263 C  CB    . ASN B 2 364 ? 134.398 147.281 173.705 1.00 51.23  ? 364  ASN B CB    1 
ATOM   10264 C  CG    . ASN B 2 364 ? 135.167 146.709 172.533 1.00 54.81  ? 364  ASN B CG    1 
ATOM   10265 O  OD1   . ASN B 2 364 ? 134.613 145.987 171.707 1.00 51.27  ? 364  ASN B OD1   1 
ATOM   10266 N  ND2   . ASN B 2 364 ? 136.451 147.032 172.453 1.00 55.83  ? 364  ASN B ND2   1 
ATOM   10267 N  N     . VAL B 2 365 ? 131.605 149.436 173.960 1.00 43.82  ? 365  VAL B N     1 
ATOM   10268 C  CA    . VAL B 2 365 ? 130.510 149.879 174.813 1.00 41.39  ? 365  VAL B CA    1 
ATOM   10269 C  C     . VAL B 2 365 ? 129.481 148.765 174.911 1.00 38.75  ? 365  VAL B C     1 
ATOM   10270 O  O     . VAL B 2 365 ? 129.138 148.128 173.908 1.00 44.36  ? 365  VAL B O     1 
ATOM   10271 C  CB    . VAL B 2 365 ? 129.877 151.182 174.290 1.00 40.57  ? 365  VAL B CB    1 
ATOM   10272 C  CG1   . VAL B 2 365 ? 130.884 152.305 174.341 1.00 45.39  ? 365  VAL B CG1   1 
ATOM   10273 C  CG2   . VAL B 2 365 ? 129.359 151.021 172.875 1.00 41.69  ? 365  VAL B CG2   1 
ATOM   10274 N  N     . GLU B 2 366 ? 129.017 148.506 176.125 1.00 39.00  ? 366  GLU B N     1 
ATOM   10275 C  CA    . GLU B 2 366 ? 127.917 147.582 176.373 1.00 40.65  ? 366  GLU B CA    1 
ATOM   10276 C  C     . GLU B 2 366 ? 126.675 148.431 176.606 1.00 47.03  ? 366  GLU B C     1 
ATOM   10277 O  O     . GLU B 2 366 ? 126.494 148.998 177.685 1.00 52.70  ? 366  GLU B O     1 
ATOM   10278 C  CB    . GLU B 2 366 ? 128.225 146.684 177.565 1.00 45.95  ? 366  GLU B CB    1 
ATOM   10279 C  CG    . GLU B 2 366 ? 128.543 145.247 177.206 1.00 46.10  ? 366  GLU B CG    1 
ATOM   10280 C  CD    . GLU B 2 366 ? 127.296 144.419 176.997 1.00 48.01  ? 366  GLU B CD    1 
ATOM   10281 O  OE1   . GLU B 2 366 ? 126.193 144.967 177.156 1.00 46.38  ? 366  GLU B OE1   1 
ATOM   10282 O  OE2   . GLU B 2 366 ? 127.413 143.221 176.683 1.00 48.24  ? 366  GLU B OE2   1 
ATOM   10283 N  N     . VAL B 2 367 ? 125.820 148.522 175.594 1.00 39.15  ? 367  VAL B N     1 
ATOM   10284 C  CA    . VAL B 2 367 ? 124.674 149.427 175.646 1.00 37.60  ? 367  VAL B CA    1 
ATOM   10285 C  C     . VAL B 2 367 ? 123.383 148.645 175.439 1.00 41.25  ? 367  VAL B C     1 
ATOM   10286 O  O     . VAL B 2 367 ? 123.372 147.649 174.702 1.00 44.88  ? 367  VAL B O     1 
ATOM   10287 C  CB    . VAL B 2 367 ? 124.812 150.548 174.604 1.00 45.67  ? 367  VAL B CB    1 
ATOM   10288 C  CG1   . VAL B 2 367 ? 125.996 151.428 174.939 1.00 45.60  ? 367  VAL B CG1   1 
ATOM   10289 C  CG2   . VAL B 2 367 ? 124.966 149.960 173.213 1.00 44.63  ? 367  VAL B CG2   1 
ATOM   10290 N  N     . PRO B 2 368 ? 122.285 149.043 176.076 1.00 45.19  ? 368  PRO B N     1 
ATOM   10291 C  CA    . PRO B 2 368 ? 121.009 148.359 175.844 1.00 46.29  ? 368  PRO B CA    1 
ATOM   10292 C  C     . PRO B 2 368 ? 120.514 148.577 174.425 1.00 47.76  ? 368  PRO B C     1 
ATOM   10293 O  O     . PRO B 2 368 ? 120.771 149.609 173.802 1.00 52.21  ? 368  PRO B O     1 
ATOM   10294 C  CB    . PRO B 2 368 ? 120.065 149.007 176.864 1.00 47.09  ? 368  PRO B CB    1 
ATOM   10295 C  CG    . PRO B 2 368 ? 120.961 149.636 177.878 1.00 48.32  ? 368  PRO B CG    1 
ATOM   10296 C  CD    . PRO B 2 368 ? 122.180 150.062 177.132 1.00 48.50  ? 368  PRO B CD    1 
ATOM   10297 N  N     . MET B 2 369 ? 119.799 147.583 173.911 1.00 49.63  ? 369  MET B N     1 
ATOM   10298 C  CA    . MET B 2 369 ? 119.205 147.729 172.595 1.00 51.05  ? 369  MET B CA    1 
ATOM   10299 C  C     . MET B 2 369 ? 118.028 148.696 172.661 1.00 52.24  ? 369  MET B C     1 
ATOM   10300 O  O     . MET B 2 369 ? 117.485 148.985 173.729 1.00 56.26  ? 369  MET B O     1 
ATOM   10301 C  CB    . MET B 2 369 ? 118.762 146.375 172.044 1.00 49.05  ? 369  MET B CB    1 
ATOM   10302 C  CG    . MET B 2 369 ? 119.864 145.334 172.040 1.00 48.54  ? 369  MET B CG    1 
ATOM   10303 S  SD    . MET B 2 369 ? 119.674 144.089 170.755 1.00 64.32  ? 369  MET B SD    1 
ATOM   10304 C  CE    . MET B 2 369 ? 120.059 145.058 169.304 1.00 54.64  ? 369  MET B CE    1 
ATOM   10305 N  N     . GLY B 2 370 ? 117.641 149.208 171.499 1.00 54.62  ? 370  GLY B N     1 
ATOM   10306 C  CA    . GLY B 2 370 ? 116.638 150.256 171.482 1.00 57.23  ? 370  GLY B CA    1 
ATOM   10307 C  C     . GLY B 2 370 ? 117.107 151.529 172.150 1.00 59.33  ? 370  GLY B C     1 
ATOM   10308 O  O     . GLY B 2 370 ? 116.356 152.141 172.919 1.00 60.32  ? 370  GLY B O     1 
ATOM   10309 N  N     . ILE B 2 371 ? 118.345 151.930 171.889 1.00 54.81  ? 371  ILE B N     1 
ATOM   10310 C  CA    . ILE B 2 371 ? 118.903 153.178 172.389 1.00 52.77  ? 371  ILE B CA    1 
ATOM   10311 C  C     . ILE B 2 371 ? 119.002 154.143 171.219 1.00 56.76  ? 371  ILE B C     1 
ATOM   10312 O  O     . ILE B 2 371 ? 119.252 153.728 170.082 1.00 56.72  ? 371  ILE B O     1 
ATOM   10313 C  CB    . ILE B 2 371 ? 120.275 152.952 173.059 1.00 51.92  ? 371  ILE B CB    1 
ATOM   10314 C  CG1   . ILE B 2 371 ? 120.841 154.256 173.624 1.00 53.68  ? 371  ILE B CG1   1 
ATOM   10315 C  CG2   . ILE B 2 371 ? 121.258 152.323 172.089 1.00 53.67  ? 371  ILE B CG2   1 
ATOM   10316 C  CD1   . ILE B 2 371 ? 122.167 154.086 174.320 1.00 54.81  ? 371  ILE B CD1   1 
ATOM   10317 N  N     . THR B 2 372 ? 118.759 155.423 171.486 1.00 68.99  ? 372  THR B N     1 
ATOM   10318 C  CA    . THR B 2 372 ? 118.919 156.436 170.454 1.00 65.29  ? 372  THR B CA    1 
ATOM   10319 C  C     . THR B 2 372 ? 120.372 156.483 169.999 1.00 62.48  ? 372  THR B C     1 
ATOM   10320 O  O     . THR B 2 372 ? 121.292 156.447 170.821 1.00 62.57  ? 372  THR B O     1 
ATOM   10321 C  CB    . THR B 2 372 ? 118.477 157.800 170.981 1.00 61.66  ? 372  THR B CB    1 
ATOM   10322 O  OG1   . THR B 2 372 ? 117.194 157.678 171.604 1.00 64.42  ? 372  THR B OG1   1 
ATOM   10323 C  CG2   . THR B 2 372 ? 118.377 158.799 169.849 1.00 64.13  ? 372  THR B CG2   1 
ATOM   10324 N  N     . LEU B 2 373 ? 120.573 156.542 168.680 1.00 54.41  ? 373  LEU B N     1 
ATOM   10325 C  CA    . LEU B 2 373 ? 121.926 156.549 168.132 1.00 53.15  ? 373  LEU B CA    1 
ATOM   10326 C  C     . LEU B 2 373 ? 122.723 157.740 168.644 1.00 57.78  ? 373  LEU B C     1 
ATOM   10327 O  O     . LEU B 2 373 ? 123.912 157.611 168.964 1.00 63.77  ? 373  LEU B O     1 
ATOM   10328 C  CB    . LEU B 2 373 ? 121.876 156.567 166.603 1.00 55.11  ? 373  LEU B CB    1 
ATOM   10329 C  CG    . LEU B 2 373 ? 122.488 155.402 165.822 1.00 58.43  ? 373  LEU B CG    1 
ATOM   10330 C  CD1   . LEU B 2 373 ? 122.516 155.701 164.333 1.00 58.10  ? 373  LEU B CD1   1 
ATOM   10331 C  CD2   . LEU B 2 373 ? 123.876 155.075 166.323 1.00 59.98  ? 373  LEU B CD2   1 
ATOM   10332 N  N     . ARG B 2 374 ? 122.086 158.911 168.729 1.00 61.37  ? 374  ARG B N     1 
ATOM   10333 C  CA    . ARG B 2 374 ? 122.809 160.109 169.130 1.00 60.25  ? 374  ARG B CA    1 
ATOM   10334 C  C     . ARG B 2 374 ? 123.279 160.043 170.574 1.00 61.80  ? 374  ARG B C     1 
ATOM   10335 O  O     . ARG B 2 374 ? 124.268 160.697 170.910 1.00 61.54  ? 374  ARG B O     1 
ATOM   10336 C  CB    . ARG B 2 374 ? 121.953 161.357 168.911 1.00 60.07  ? 374  ARG B CB    1 
ATOM   10337 C  CG    . ARG B 2 374 ? 120.839 161.561 169.911 1.00 59.72  ? 374  ARG B CG    1 
ATOM   10338 C  CD    . ARG B 2 374 ? 120.163 162.907 169.711 1.00 60.19  ? 374  ARG B CD    1 
ATOM   10339 N  NE    . ARG B 2 374 ? 119.538 163.025 168.399 1.00 62.53  ? 374  ARG B NE    1 
ATOM   10340 C  CZ    . ARG B 2 374 ? 120.055 163.692 167.377 1.00 63.05  ? 374  ARG B CZ    1 
ATOM   10341 N  NH1   . ARG B 2 374 ? 121.213 164.322 167.478 1.00 61.90  ? 374  ARG B NH1   1 
ATOM   10342 N  NH2   . ARG B 2 374 ? 119.393 163.728 166.224 1.00 62.68  ? 374  ARG B NH2   1 
ATOM   10343 N  N     . GLU B 2 375 ? 122.618 159.258 171.426 1.00 68.40  ? 375  GLU B N     1 
ATOM   10344 C  CA    . GLU B 2 375 ? 123.142 159.039 172.770 1.00 68.12  ? 375  GLU B CA    1 
ATOM   10345 C  C     . GLU B 2 375 ? 124.507 158.368 172.711 1.00 65.62  ? 375  GLU B C     1 
ATOM   10346 O  O     . GLU B 2 375 ? 125.483 158.879 173.270 1.00 61.24  ? 375  GLU B O     1 
ATOM   10347 C  CB    . GLU B 2 375 ? 122.161 158.205 173.591 1.00 65.53  ? 375  GLU B CB    1 
ATOM   10348 C  CG    . GLU B 2 375 ? 120.854 158.915 173.880 1.00 69.89  ? 375  GLU B CG    1 
ATOM   10349 C  CD    . GLU B 2 375 ? 119.959 158.127 174.807 1.00 70.15  ? 375  GLU B CD    1 
ATOM   10350 O  OE1   . GLU B 2 375 ? 120.393 157.059 175.287 1.00 68.78  ? 375  GLU B OE1   1 
ATOM   10351 O  OE2   . GLU B 2 375 ? 118.821 158.573 175.058 1.00 71.44  ? 375  GLU B OE2   1 
ATOM   10352 N  N     . ILE B 2 376 ? 124.601 157.252 171.982 1.00 60.21  ? 376  ILE B N     1 
ATOM   10353 C  CA    . ILE B 2 376 ? 125.875 156.557 171.815 1.00 56.72  ? 376  ILE B CA    1 
ATOM   10354 C  C     . ILE B 2 376 ? 126.905 157.482 171.185 1.00 59.16  ? 376  ILE B C     1 
ATOM   10355 O  O     . ILE B 2 376 ? 128.080 157.486 171.572 1.00 62.15  ? 376  ILE B O     1 
ATOM   10356 C  CB    . ILE B 2 376 ? 125.679 155.280 170.975 1.00 51.25  ? 376  ILE B CB    1 
ATOM   10357 C  CG1   . ILE B 2 376 ? 124.851 154.249 171.738 1.00 55.17  ? 376  ILE B CG1   1 
ATOM   10358 C  CG2   . ILE B 2 376 ? 127.016 154.683 170.568 1.00 53.55  ? 376  ILE B CG2   1 
ATOM   10359 C  CD1   . ILE B 2 376 ? 124.727 152.933 171.017 1.00 55.10  ? 376  ILE B CD1   1 
ATOM   10360 N  N     . LEU B 2 377 ? 126.478 158.295 170.221 1.00 62.44  ? 377  LEU B N     1 
ATOM   10361 C  CA    . LEU B 2 377 ? 127.428 159.111 169.477 1.00 61.79  ? 377  LEU B CA    1 
ATOM   10362 C  C     . LEU B 2 377 ? 127.938 160.311 170.268 1.00 65.14  ? 377  LEU B C     1 
ATOM   10363 O  O     . LEU B 2 377 ? 129.106 160.685 170.116 1.00 63.98  ? 377  LEU B O     1 
ATOM   10364 C  CB    . LEU B 2 377 ? 126.800 159.571 168.163 1.00 62.97  ? 377  LEU B CB    1 
ATOM   10365 C  CG    . LEU B 2 377 ? 127.180 158.701 166.966 1.00 63.28  ? 377  LEU B CG    1 
ATOM   10366 C  CD1   . LEU B 2 377 ? 128.683 158.582 166.895 1.00 61.44  ? 377  LEU B CD1   1 
ATOM   10367 C  CD2   . LEU B 2 377 ? 126.557 157.331 167.059 1.00 61.49  ? 377  LEU B CD2   1 
ATOM   10368 N  N     . TYR B 2 378 ? 127.109 160.923 171.111 1.00 68.23  ? 378  TYR B N     1 
ATOM   10369 C  CA    . TYR B 2 378 ? 127.465 162.185 171.749 1.00 68.84  ? 378  TYR B CA    1 
ATOM   10370 C  C     . TYR B 2 378 ? 127.718 162.089 173.245 1.00 69.16  ? 378  TYR B C     1 
ATOM   10371 O  O     . TYR B 2 378 ? 128.588 162.797 173.753 1.00 68.56  ? 378  TYR B O     1 
ATOM   10372 C  CB    . TYR B 2 378 ? 126.374 163.229 171.495 1.00 65.50  ? 378  TYR B CB    1 
ATOM   10373 C  CG    . TYR B 2 378 ? 126.310 163.709 170.066 1.00 66.49  ? 378  TYR B CG    1 
ATOM   10374 C  CD1   . TYR B 2 378 ? 127.359 164.425 169.507 1.00 66.41  ? 378  TYR B CD1   1 
ATOM   10375 C  CD2   . TYR B 2 378 ? 125.196 163.460 169.281 1.00 67.29  ? 378  TYR B CD2   1 
ATOM   10376 C  CE1   . TYR B 2 378 ? 127.304 164.868 168.202 1.00 66.95  ? 378  TYR B CE1   1 
ATOM   10377 C  CE2   . TYR B 2 378 ? 125.131 163.901 167.978 1.00 66.05  ? 378  TYR B CE2   1 
ATOM   10378 C  CZ    . TYR B 2 378 ? 126.186 164.604 167.444 1.00 67.69  ? 378  TYR B CZ    1 
ATOM   10379 O  OH    . TYR B 2 378 ? 126.119 165.046 166.145 1.00 70.87  ? 378  TYR B OH    1 
ATOM   10380 N  N     . GLU B 2 379 ? 126.981 161.260 173.984 1.00 63.91  ? 379  GLU B N     1 
ATOM   10381 C  CA    . GLU B 2 379 ? 127.219 161.166 175.417 1.00 62.51  ? 379  GLU B CA    1 
ATOM   10382 C  C     . GLU B 2 379 ? 128.186 160.037 175.752 1.00 65.49  ? 379  GLU B C     1 
ATOM   10383 O  O     . GLU B 2 379 ? 129.201 160.264 176.417 1.00 63.17  ? 379  GLU B O     1 
ATOM   10384 C  CB    . GLU B 2 379 ? 125.892 160.973 176.153 1.00 62.28  ? 379  GLU B CB    1 
ATOM   10385 C  CG    . GLU B 2 379 ? 124.881 162.070 175.882 1.00 63.68  ? 379  GLU B CG    1 
ATOM   10386 C  CD    . GLU B 2 379 ? 123.559 161.828 176.580 1.00 66.30  ? 379  GLU B CD    1 
ATOM   10387 O  OE1   . GLU B 2 379 ? 123.437 160.808 177.289 1.00 66.45  ? 379  GLU B OE1   1 
ATOM   10388 O  OE2   . GLU B 2 379 ? 122.640 162.659 176.419 1.00 66.37  ? 379  GLU B OE2   1 
ATOM   10389 N  N     . ILE B 2 380 ? 127.884 158.819 175.301 1.00 63.31  ? 380  ILE B N     1 
ATOM   10390 C  CA    . ILE B 2 380 ? 128.792 157.698 175.521 1.00 59.14  ? 380  ILE B CA    1 
ATOM   10391 C  C     . ILE B 2 380 ? 130.066 157.882 174.708 1.00 60.75  ? 380  ILE B C     1 
ATOM   10392 O  O     . ILE B 2 380 ? 131.179 157.725 175.221 1.00 62.15  ? 380  ILE B O     1 
ATOM   10393 C  CB    . ILE B 2 380 ? 128.099 156.368 175.179 1.00 57.79  ? 380  ILE B CB    1 
ATOM   10394 C  CG1   . ILE B 2 380 ? 126.769 156.248 175.917 1.00 58.01  ? 380  ILE B CG1   1 
ATOM   10395 C  CG2   . ILE B 2 380 ? 128.991 155.202 175.537 1.00 56.42  ? 380  ILE B CG2   1 
ATOM   10396 C  CD1   . ILE B 2 380 ? 125.989 155.015 175.541 1.00 55.56  ? 380  ILE B CD1   1 
ATOM   10397 N  N     . GLY B 2 381 ? 129.921 158.220 173.425 1.00 65.87  ? 381  GLY B N     1 
ATOM   10398 C  CA    . GLY B 2 381 ? 131.078 158.429 172.576 1.00 66.66  ? 381  GLY B CA    1 
ATOM   10399 C  C     . GLY B 2 381 ? 131.741 159.777 172.738 1.00 71.22  ? 381  GLY B C     1 
ATOM   10400 O  O     . GLY B 2 381 ? 132.872 159.957 172.276 1.00 74.32  ? 381  GLY B O     1 
ATOM   10401 N  N     . GLY B 2 382 ? 131.067 160.728 173.380 1.00 69.77  ? 382  GLY B N     1 
ATOM   10402 C  CA    . GLY B 2 382 ? 131.646 162.040 173.578 1.00 69.98  ? 382  GLY B CA    1 
ATOM   10403 C  C     . GLY B 2 382 ? 131.705 162.907 172.345 1.00 71.11  ? 382  GLY B C     1 
ATOM   10404 O  O     . GLY B 2 382 ? 132.396 163.930 172.359 1.00 75.70  ? 382  GLY B O     1 
ATOM   10405 N  N     . GLY B 2 383 ? 131.004 162.538 171.277 1.00 68.85  ? 383  GLY B N     1 
ATOM   10406 C  CA    . GLY B 2 383 ? 131.110 163.311 170.060 1.00 71.19  ? 383  GLY B CA    1 
ATOM   10407 C  C     . GLY B 2 383 ? 132.429 163.043 169.353 1.00 71.42  ? 383  GLY B C     1 
ATOM   10408 O  O     . GLY B 2 383 ? 133.121 162.056 169.607 1.00 72.73  ? 383  GLY B O     1 
ATOM   10409 N  N     . THR B 2 384 ? 132.770 163.946 168.441 1.00 72.58  ? 384  THR B N     1 
ATOM   10410 C  CA    . THR B 2 384 ? 134.009 163.804 167.699 1.00 74.44  ? 384  THR B CA    1 
ATOM   10411 C  C     . THR B 2 384 ? 135.189 164.312 168.520 1.00 75.29  ? 384  THR B C     1 
ATOM   10412 O  O     . THR B 2 384 ? 135.029 165.013 169.522 1.00 77.77  ? 384  THR B O     1 
ATOM   10413 C  CB    . THR B 2 384 ? 133.935 164.544 166.366 1.00 74.61  ? 384  THR B CB    1 
ATOM   10414 O  OG1   . THR B 2 384 ? 133.456 165.877 166.582 1.00 77.19  ? 384  THR B OG1   1 
ATOM   10415 C  CG2   . THR B 2 384 ? 133.005 163.817 165.412 1.00 73.81  ? 384  THR B CG2   1 
ATOM   10416 N  N     . LYS B 2 385 ? 136.391 163.938 168.077 1.00 75.87  ? 385  LYS B N     1 
ATOM   10417 C  CA    . LYS B 2 385 ? 137.596 164.242 168.840 1.00 78.28  ? 385  LYS B CA    1 
ATOM   10418 C  C     . LYS B 2 385 ? 137.866 165.741 168.895 1.00 81.43  ? 385  LYS B C     1 
ATOM   10419 O  O     . LYS B 2 385 ? 138.245 166.268 169.947 1.00 81.23  ? 385  LYS B O     1 
ATOM   10420 C  CB    . LYS B 2 385 ? 138.792 163.507 168.239 1.00 78.72  ? 385  LYS B CB    1 
ATOM   10421 C  CG    . LYS B 2 385 ? 140.077 163.687 169.022 1.00 79.64  ? 385  LYS B CG    1 
ATOM   10422 C  CD    . LYS B 2 385 ? 141.208 162.877 168.419 1.00 80.67  ? 385  LYS B CD    1 
ATOM   10423 C  CE    . LYS B 2 385 ? 142.486 163.032 169.225 1.00 81.80  ? 385  LYS B CE    1 
ATOM   10424 N  NZ    . LYS B 2 385 ? 142.928 164.452 169.295 1.00 81.60  ? 385  LYS B NZ    1 
ATOM   10425 N  N     . THR B 2 386 ? 137.675 166.444 167.780 1.00 87.60  ? 386  THR B N     1 
ATOM   10426 C  CA    . THR B 2 386 ? 137.998 167.862 167.689 1.00 86.83  ? 386  THR B CA    1 
ATOM   10427 C  C     . THR B 2 386 ? 136.755 168.744 167.624 1.00 86.90  ? 386  THR B C     1 
ATOM   10428 O  O     . THR B 2 386 ? 136.837 169.893 167.181 1.00 87.13  ? 386  THR B O     1 
ATOM   10429 C  CB    . THR B 2 386 ? 138.898 168.121 166.482 1.00 86.36  ? 386  THR B CB    1 
ATOM   10430 O  OG1   . THR B 2 386 ? 139.014 169.531 166.261 1.00 87.39  ? 386  THR B OG1   1 
ATOM   10431 C  CG2   . THR B 2 386 ? 138.326 167.459 165.241 1.00 87.09  ? 386  THR B CG2   1 
ATOM   10432 N  N     . GLY B 2 387 ? 135.605 168.227 168.048 1.00 88.76  ? 387  GLY B N     1 
ATOM   10433 C  CA    . GLY B 2 387 ? 134.396 169.015 168.129 1.00 88.67  ? 387  GLY B CA    1 
ATOM   10434 C  C     . GLY B 2 387 ? 133.654 169.207 166.827 1.00 88.69  ? 387  GLY B C     1 
ATOM   10435 O  O     . GLY B 2 387 ? 132.596 169.847 166.828 1.00 87.55  ? 387  GLY B O     1 
ATOM   10436 N  N     . LYS B 2 388 ? 134.167 168.678 165.720 1.00 86.32  ? 388  LYS B N     1 
ATOM   10437 C  CA    . LYS B 2 388 ? 133.499 168.834 164.438 1.00 86.20  ? 388  LYS B CA    1 
ATOM   10438 C  C     . LYS B 2 388 ? 132.228 167.996 164.392 1.00 85.22  ? 388  LYS B C     1 
ATOM   10439 O  O     . LYS B 2 388 ? 132.140 166.925 164.995 1.00 86.76  ? 388  LYS B O     1 
ATOM   10440 C  CB    . LYS B 2 388 ? 134.437 168.437 163.301 1.00 85.78  ? 388  LYS B CB    1 
ATOM   10441 C  CG    . LYS B 2 388 ? 135.758 169.185 163.317 1.00 84.55  ? 388  LYS B CG    1 
ATOM   10442 C  CD    . LYS B 2 388 ? 136.645 168.774 162.155 1.00 86.20  ? 388  LYS B CD    1 
ATOM   10443 C  CE    . LYS B 2 388 ? 136.023 169.159 160.825 1.00 86.32  ? 388  LYS B CE    1 
ATOM   10444 N  NZ    . LYS B 2 388 ? 135.822 170.629 160.714 1.00 84.75  ? 388  LYS B NZ    1 
ATOM   10445 N  N     . LYS B 2 389 ? 131.229 168.505 163.677 1.00 79.38  ? 389  LYS B N     1 
ATOM   10446 C  CA    . LYS B 2 389 ? 129.962 167.799 163.560 1.00 78.91  ? 389  LYS B CA    1 
ATOM   10447 C  C     . LYS B 2 389 ? 130.145 166.511 162.769 1.00 81.61  ? 389  LYS B C     1 
ATOM   10448 O  O     . LYS B 2 389 ? 130.825 166.484 161.741 1.00 82.57  ? 389  LYS B O     1 
ATOM   10449 C  CB    . LYS B 2 389 ? 128.921 168.693 162.890 1.00 80.09  ? 389  LYS B CB    1 
ATOM   10450 C  CG    . LYS B 2 389 ? 127.536 168.090 162.821 1.00 80.49  ? 389  LYS B CG    1 
ATOM   10451 C  CD    . LYS B 2 389 ? 126.576 169.022 162.108 1.00 81.15  ? 389  LYS B CD    1 
ATOM   10452 C  CE    . LYS B 2 389 ? 127.058 169.330 160.702 1.00 81.96  ? 389  LYS B CE    1 
ATOM   10453 N  NZ    . LYS B 2 389 ? 127.207 168.094 159.885 1.00 81.21  ? 389  LYS B NZ    1 
ATOM   10454 N  N     . ILE B 2 390 ? 129.536 165.435 163.256 1.00 73.86  ? 390  ILE B N     1 
ATOM   10455 C  CA    . ILE B 2 390 ? 129.688 164.127 162.630 1.00 71.86  ? 390  ILE B CA    1 
ATOM   10456 C  C     . ILE B 2 390 ? 128.740 164.036 161.441 1.00 70.20  ? 390  ILE B C     1 
ATOM   10457 O  O     . ILE B 2 390 ? 127.528 164.226 161.581 1.00 71.01  ? 390  ILE B O     1 
ATOM   10458 C  CB    . ILE B 2 390 ? 129.436 162.996 163.638 1.00 70.92  ? 390  ILE B CB    1 
ATOM   10459 C  CG1   . ILE B 2 390 ? 129.166 161.681 162.912 1.00 71.23  ? 390  ILE B CG1   1 
ATOM   10460 C  CG2   . ILE B 2 390 ? 128.294 163.345 164.566 1.00 71.06  ? 390  ILE B CG2   1 
ATOM   10461 C  CD1   . ILE B 2 390 ? 128.881 160.534 163.838 1.00 66.89  ? 390  ILE B CD1   1 
ATOM   10462 N  N     . LYS B 2 391 ? 129.297 163.766 160.261 1.00 65.37  ? 391  LYS B N     1 
ATOM   10463 C  CA    . LYS B 2 391 ? 128.484 163.705 159.052 1.00 64.24  ? 391  LYS B CA    1 
ATOM   10464 C  C     . LYS B 2 391 ? 127.629 162.444 159.024 1.00 63.86  ? 391  LYS B C     1 
ATOM   10465 O  O     . LYS B 2 391 ? 126.433 162.499 158.721 1.00 65.90  ? 391  LYS B O     1 
ATOM   10466 C  CB    . LYS B 2 391 ? 129.381 163.776 157.817 1.00 64.87  ? 391  LYS B CB    1 
ATOM   10467 C  CG    . LYS B 2 391 ? 128.620 163.791 156.504 1.00 66.93  ? 391  LYS B CG    1 
ATOM   10468 C  CD    . LYS B 2 391 ? 129.554 163.687 155.311 1.00 65.60  ? 391  LYS B CD    1 
ATOM   10469 C  CE    . LYS B 2 391 ? 130.478 164.886 155.224 1.00 67.35  ? 391  LYS B CE    1 
ATOM   10470 N  NZ    . LYS B 2 391 ? 131.388 164.796 154.050 1.00 67.23  ? 391  LYS B NZ    1 
ATOM   10471 N  N     . ALA B 2 392 ? 128.224 161.300 159.346 1.00 64.98  ? 392  ALA B N     1 
ATOM   10472 C  CA    . ALA B 2 392 ? 127.519 160.029 159.279 1.00 60.93  ? 392  ALA B CA    1 
ATOM   10473 C  C     . ALA B 2 392 ? 128.239 159.018 160.156 1.00 62.49  ? 392  ALA B C     1 
ATOM   10474 O  O     . ALA B 2 392 ? 129.341 159.263 160.651 1.00 63.54  ? 392  ALA B O     1 
ATOM   10475 C  CB    . ALA B 2 392 ? 127.425 159.514 157.843 1.00 60.15  ? 392  ALA B CB    1 
ATOM   10476 N  N     . VAL B 2 393 ? 127.595 157.873 160.339 1.00 57.43  ? 393  VAL B N     1 
ATOM   10477 C  CA    . VAL B 2 393 ? 128.189 156.735 161.022 1.00 53.14  ? 393  VAL B CA    1 
ATOM   10478 C  C     . VAL B 2 393 ? 127.883 155.494 160.199 1.00 51.24  ? 393  VAL B C     1 
ATOM   10479 O  O     . VAL B 2 393 ? 126.781 155.353 159.658 1.00 56.57  ? 393  VAL B O     1 
ATOM   10480 C  CB    . VAL B 2 393 ? 127.672 156.598 162.472 1.00 54.42  ? 393  VAL B CB    1 
ATOM   10481 C  CG1   . VAL B 2 393 ? 126.155 156.491 162.505 1.00 52.91  ? 393  VAL B CG1   1 
ATOM   10482 C  CG2   . VAL B 2 393 ? 128.316 155.413 163.170 1.00 52.43  ? 393  VAL B CG2   1 
ATOM   10483 N  N     . GLN B 2 394 ? 128.867 154.614 160.065 1.00 51.87  ? 394  GLN B N     1 
ATOM   10484 C  CA    . GLN B 2 394 ? 128.677 153.358 159.361 1.00 51.73  ? 394  GLN B CA    1 
ATOM   10485 C  C     . GLN B 2 394 ? 128.687 152.218 160.374 1.00 45.30  ? 394  GLN B C     1 
ATOM   10486 O  O     . GLN B 2 394 ? 129.555 152.160 161.251 1.00 48.99  ? 394  GLN B O     1 
ATOM   10487 C  CB    . GLN B 2 394 ? 129.730 153.175 158.262 1.00 51.20  ? 394  GLN B CB    1 
ATOM   10488 C  CG    . GLN B 2 394 ? 131.078 152.651 158.684 1.00 47.97  ? 394  GLN B CG    1 
ATOM   10489 C  CD    . GLN B 2 394 ? 131.306 151.243 158.192 1.00 53.99  ? 394  GLN B CD    1 
ATOM   10490 O  OE1   . GLN B 2 394 ? 130.649 150.794 157.252 1.00 60.92  ? 394  GLN B OE1   1 
ATOM   10491 N  NE2   . GLN B 2 394 ? 132.237 150.535 158.819 1.00 48.44  ? 394  GLN B NE2   1 
ATOM   10492 N  N     . LEU B 2 395 ? 127.683 151.352 160.285 1.00 39.19  ? 395  LEU B N     1 
ATOM   10493 C  CA    . LEU B 2 395 ? 127.481 150.270 161.237 1.00 47.25  ? 395  LEU B CA    1 
ATOM   10494 C  C     . LEU B 2 395 ? 127.567 148.944 160.505 1.00 41.73  ? 395  LEU B C     1 
ATOM   10495 O  O     . LEU B 2 395 ? 126.958 148.778 159.445 1.00 45.27  ? 395  LEU B O     1 
ATOM   10496 C  CB    . LEU B 2 395 ? 126.128 150.386 161.944 1.00 48.25  ? 395  LEU B CB    1 
ATOM   10497 C  CG    . LEU B 2 395 ? 125.933 151.463 163.009 1.00 48.35  ? 395  LEU B CG    1 
ATOM   10498 C  CD1   . LEU B 2 395 ? 125.709 152.829 162.385 1.00 46.10  ? 395  LEU B CD1   1 
ATOM   10499 C  CD2   . LEU B 2 395 ? 124.772 151.089 163.912 1.00 46.81  ? 395  LEU B CD2   1 
ATOM   10500 N  N     . GLY B 2 396 ? 128.309 148.002 161.076 1.00 33.79  ? 396  GLY B N     1 
ATOM   10501 C  CA    . GLY B 2 396 ? 128.480 146.695 160.485 1.00 38.43  ? 396  GLY B CA    1 
ATOM   10502 C  C     . GLY B 2 396 ? 129.838 146.428 159.882 1.00 42.66  ? 396  GLY B C     1 
ATOM   10503 O  O     . GLY B 2 396 ? 130.005 145.403 159.210 1.00 47.69  ? 396  GLY B O     1 
ATOM   10504 N  N     . GLY B 2 397 ? 130.812 147.305 160.095 1.00 40.39  ? 397  GLY B N     1 
ATOM   10505 C  CA    . GLY B 2 397 ? 132.127 147.124 159.535 1.00 38.19  ? 397  GLY B CA    1 
ATOM   10506 C  C     . GLY B 2 397 ? 132.150 147.385 158.045 1.00 42.91  ? 397  GLY B C     1 
ATOM   10507 O  O     . GLY B 2 397 ? 131.291 148.084 157.500 1.00 39.10  ? 397  GLY B O     1 
ATOM   10508 N  N     . PRO B 2 398 ? 133.135 146.810 157.350 1.00 34.79  ? 398  PRO B N     1 
ATOM   10509 C  CA    . PRO B 2 398 ? 133.296 147.092 155.915 1.00 29.87  ? 398  PRO B CA    1 
ATOM   10510 C  C     . PRO B 2 398 ? 132.170 146.562 155.043 1.00 30.88  ? 398  PRO B C     1 
ATOM   10511 O  O     . PRO B 2 398 ? 132.167 146.840 153.838 1.00 31.28  ? 398  PRO B O     1 
ATOM   10512 C  CB    . PRO B 2 398 ? 134.626 146.412 155.573 1.00 33.45  ? 398  PRO B CB    1 
ATOM   10513 C  CG    . PRO B 2 398 ? 134.782 145.356 156.613 1.00 33.49  ? 398  PRO B CG    1 
ATOM   10514 C  CD    . PRO B 2 398 ? 134.182 145.910 157.860 1.00 30.98  ? 398  PRO B CD    1 
ATOM   10515 N  N     . SER B 2 399 ? 131.228 145.806 155.599 1.00 36.18  ? 399  SER B N     1 
ATOM   10516 C  CA    . SER B 2 399 ? 130.065 145.336 154.862 1.00 33.30  ? 399  SER B CA    1 
ATOM   10517 C  C     . SER B 2 399 ? 128.785 146.063 155.259 1.00 35.95  ? 399  SER B C     1 
ATOM   10518 O  O     . SER B 2 399 ? 127.698 145.653 154.842 1.00 30.12  ? 399  SER B O     1 
ATOM   10519 C  CB    . SER B 2 399 ? 129.895 143.830 155.061 1.00 34.81  ? 399  SER B CB    1 
ATOM   10520 O  OG    . SER B 2 399 ? 131.025 143.122 154.583 1.00 32.96  ? 399  SER B OG    1 
ATOM   10521 N  N     . GLY B 2 400 ? 128.886 147.126 156.054 1.00 36.13  ? 400  GLY B N     1 
ATOM   10522 C  CA    . GLY B 2 400 ? 127.725 147.823 156.560 1.00 37.51  ? 400  GLY B CA    1 
ATOM   10523 C  C     . GLY B 2 400 ? 127.357 149.038 155.732 1.00 38.53  ? 400  GLY B C     1 
ATOM   10524 O  O     . GLY B 2 400 ? 127.879 149.273 154.642 1.00 44.96  ? 400  GLY B O     1 
ATOM   10525 N  N     . GLY B 2 401 ? 126.433 149.826 156.273 1.00 32.59  ? 401  GLY B N     1 
ATOM   10526 C  CA    . GLY B 2 401 ? 125.984 151.025 155.596 1.00 39.44  ? 401  GLY B CA    1 
ATOM   10527 C  C     . GLY B 2 401 ? 126.174 152.284 156.414 1.00 46.37  ? 401  GLY B C     1 
ATOM   10528 O  O     . GLY B 2 401 ? 126.255 152.222 157.642 1.00 51.81  ? 401  GLY B O     1 
ATOM   10529 N  N     . CYS B 2 402 ? 126.241 153.434 155.748 1.00 51.22  ? 402  CYS B N     1 
ATOM   10530 C  CA    . CYS B 2 402 ? 126.445 154.710 156.421 1.00 46.57  ? 402  CYS B CA    1 
ATOM   10531 C  C     . CYS B 2 402 ? 125.095 155.350 156.718 1.00 49.68  ? 402  CYS B C     1 
ATOM   10532 O  O     . CYS B 2 402 ? 124.333 155.659 155.797 1.00 52.92  ? 402  CYS B O     1 
ATOM   10533 C  CB    . CYS B 2 402 ? 127.301 155.644 155.567 1.00 51.57  ? 402  CYS B CB    1 
ATOM   10534 S  SG    . CYS B 2 402 ? 128.921 154.986 155.117 1.00 57.35  ? 402  CYS B SG    1 
ATOM   10535 N  N     . ILE B 2 403 ? 124.807 155.548 157.995 1.00 54.60  ? 403  ILE B N     1 
ATOM   10536 C  CA    . ILE B 2 403 ? 123.585 156.212 158.446 1.00 54.42  ? 403  ILE B CA    1 
ATOM   10537 C  C     . ILE B 2 403 ? 123.909 157.682 158.687 1.00 55.68  ? 403  ILE B C     1 
ATOM   10538 O  O     . ILE B 2 403 ? 124.847 157.978 159.439 1.00 57.94  ? 403  ILE B O     1 
ATOM   10539 C  CB    . ILE B 2 403 ? 123.026 155.555 159.720 1.00 54.05  ? 403  ILE B CB    1 
ATOM   10540 C  CG1   . ILE B 2 403 ? 122.640 154.102 159.437 1.00 53.15  ? 403  ILE B CG1   1 
ATOM   10541 C  CG2   . ILE B 2 403 ? 121.835 156.331 160.250 1.00 57.26  ? 403  ILE B CG2   1 
ATOM   10542 C  CD1   . ILE B 2 403 ? 122.104 153.371 160.641 1.00 56.97  ? 403  ILE B CD1   1 
ATOM   10543 N  N     . PRO B 2 404 ? 123.183 158.614 158.078 1.00 59.47  ? 404  PRO B N     1 
ATOM   10544 C  CA    . PRO B 2 404 ? 123.574 160.024 158.138 1.00 58.68  ? 404  PRO B CA    1 
ATOM   10545 C  C     . PRO B 2 404 ? 123.242 160.651 159.487 1.00 63.01  ? 404  PRO B C     1 
ATOM   10546 O  O     . PRO B 2 404 ? 122.601 160.051 160.350 1.00 64.99  ? 404  PRO B O     1 
ATOM   10547 C  CB    . PRO B 2 404 ? 122.749 160.656 157.018 1.00 60.59  ? 404  PRO B CB    1 
ATOM   10548 C  CG    . PRO B 2 404 ? 121.513 159.831 156.990 1.00 63.31  ? 404  PRO B CG    1 
ATOM   10549 C  CD    . PRO B 2 404 ? 121.937 158.423 157.319 1.00 61.09  ? 404  PRO B CD    1 
ATOM   10550 N  N     . ASP B 2 405 ? 123.696 161.899 159.644 1.00 66.10  ? 405  ASP B N     1 
ATOM   10551 C  CA    . ASP B 2 405 ? 123.593 162.584 160.928 1.00 65.14  ? 405  ASP B CA    1 
ATOM   10552 C  C     . ASP B 2 405 ? 122.151 162.887 161.311 1.00 67.64  ? 405  ASP B C     1 
ATOM   10553 O  O     . ASP B 2 405 ? 121.821 162.901 162.502 1.00 70.20  ? 405  ASP B O     1 
ATOM   10554 C  CB    . ASP B 2 405 ? 124.403 163.877 160.895 1.00 66.42  ? 405  ASP B CB    1 
ATOM   10555 C  CG    . ASP B 2 405 ? 123.884 164.861 159.869 1.00 72.99  ? 405  ASP B CG    1 
ATOM   10556 O  OD1   . ASP B 2 405 ? 123.274 164.416 158.874 1.00 71.80  ? 405  ASP B OD1   1 
ATOM   10557 O  OD2   . ASP B 2 405 ? 124.084 166.079 160.056 1.00 73.41  ? 405  ASP B OD2   1 
ATOM   10558 N  N     . TYR B 2 406 ? 121.281 163.135 160.335 1.00 64.85  ? 406  TYR B N     1 
ATOM   10559 C  CA    . TYR B 2 406 ? 119.912 163.516 160.652 1.00 64.50  ? 406  TYR B CA    1 
ATOM   10560 C  C     . TYR B 2 406 ? 119.035 162.329 161.029 1.00 64.23  ? 406  TYR B C     1 
ATOM   10561 O  O     . TYR B 2 406 ? 117.880 162.534 161.416 1.00 66.79  ? 406  TYR B O     1 
ATOM   10562 C  CB    . TYR B 2 406 ? 119.287 164.289 159.485 1.00 63.73  ? 406  TYR B CB    1 
ATOM   10563 C  CG    . TYR B 2 406 ? 119.273 163.567 158.158 1.00 65.88  ? 406  TYR B CG    1 
ATOM   10564 C  CD1   . TYR B 2 406 ? 120.335 163.681 157.273 1.00 65.59  ? 406  TYR B CD1   1 
ATOM   10565 C  CD2   . TYR B 2 406 ? 118.185 162.796 157.777 1.00 65.83  ? 406  TYR B CD2   1 
ATOM   10566 C  CE1   . TYR B 2 406 ? 120.320 163.034 156.054 1.00 64.21  ? 406  TYR B CE1   1 
ATOM   10567 C  CE2   . TYR B 2 406 ? 118.162 162.144 156.562 1.00 64.94  ? 406  TYR B CE2   1 
ATOM   10568 C  CZ    . TYR B 2 406 ? 119.232 162.266 155.705 1.00 65.30  ? 406  TYR B CZ    1 
ATOM   10569 O  OH    . TYR B 2 406 ? 119.209 161.617 154.493 1.00 65.28  ? 406  TYR B OH    1 
ATOM   10570 N  N     . LEU B 2 407 ? 119.546 161.104 160.932 1.00 63.02  ? 407  LEU B N     1 
ATOM   10571 C  CA    . LEU B 2 407 ? 118.832 159.918 161.385 1.00 62.47  ? 407  LEU B CA    1 
ATOM   10572 C  C     . LEU B 2 407 ? 119.411 159.373 162.687 1.00 66.24  ? 407  LEU B C     1 
ATOM   10573 O  O     . LEU B 2 407 ? 119.285 158.182 162.977 1.00 66.50  ? 407  LEU B O     1 
ATOM   10574 C  CB    . LEU B 2 407 ? 118.839 158.837 160.308 1.00 60.14  ? 407  LEU B CB    1 
ATOM   10575 C  CG    . LEU B 2 407 ? 117.971 159.099 159.079 1.00 62.41  ? 407  LEU B CG    1 
ATOM   10576 C  CD1   . LEU B 2 407 ? 117.977 157.895 158.160 1.00 61.28  ? 407  LEU B CD1   1 
ATOM   10577 C  CD2   . LEU B 2 407 ? 116.553 159.450 159.495 1.00 66.22  ? 407  LEU B CD2   1 
ATOM   10578 N  N     . PHE B 2 408 ? 120.054 160.231 163.480 1.00 62.86  ? 408  PHE B N     1 
ATOM   10579 C  CA    . PHE B 2 408 ? 120.597 159.804 164.763 1.00 55.03  ? 408  PHE B CA    1 
ATOM   10580 C  C     . PHE B 2 408 ? 119.527 159.631 165.829 1.00 53.60  ? 408  PHE B C     1 
ATOM   10581 O  O     . PHE B 2 408 ? 119.833 159.121 166.911 1.00 58.26  ? 408  PHE B O     1 
ATOM   10582 C  CB    . PHE B 2 408 ? 121.655 160.792 165.253 1.00 53.57  ? 408  PHE B CB    1 
ATOM   10583 C  CG    . PHE B 2 408 ? 122.984 160.636 164.579 1.00 52.60  ? 408  PHE B CG    1 
ATOM   10584 C  CD1   . PHE B 2 408 ? 123.162 159.698 163.579 1.00 54.04  ? 408  PHE B CD1   1 
ATOM   10585 C  CD2   . PHE B 2 408 ? 124.060 161.418 164.954 1.00 55.21  ? 408  PHE B CD2   1 
ATOM   10586 C  CE1   . PHE B 2 408 ? 124.379 159.551 162.961 1.00 55.92  ? 408  PHE B CE1   1 
ATOM   10587 C  CE2   . PHE B 2 408 ? 125.281 161.272 164.339 1.00 56.93  ? 408  PHE B CE2   1 
ATOM   10588 C  CZ    . PHE B 2 408 ? 125.439 160.337 163.340 1.00 56.18  ? 408  PHE B CZ    1 
ATOM   10589 N  N     . ASN B 2 409 ? 118.291 160.046 165.554 1.00 63.98  ? 409  ASN B N     1 
ATOM   10590 C  CA    . ASN B 2 409 ? 117.171 159.727 166.428 1.00 65.06  ? 409  ASN B CA    1 
ATOM   10591 C  C     . ASN B 2 409 ? 116.721 158.282 166.284 1.00 63.99  ? 409  ASN B C     1 
ATOM   10592 O  O     . ASN B 2 409 ? 115.836 157.849 167.028 1.00 63.33  ? 409  ASN B O     1 
ATOM   10593 C  CB    . ASN B 2 409 ? 115.999 160.664 166.142 1.00 62.98  ? 409  ASN B CB    1 
ATOM   10594 C  CG    . ASN B 2 409 ? 116.357 162.118 166.343 1.00 63.87  ? 409  ASN B CG    1 
ATOM   10595 O  OD1   . ASN B 2 409 ? 117.187 162.452 167.187 1.00 66.72  ? 409  ASN B OD1   1 
ATOM   10596 N  ND2   . ASN B 2 409 ? 115.734 162.995 165.567 1.00 64.34  ? 409  ASN B ND2   1 
ATOM   10597 N  N     . THR B 2 410 ? 117.297 157.543 165.345 1.00 63.54  ? 410  THR B N     1 
ATOM   10598 C  CA    . THR B 2 410 ? 116.925 156.152 165.137 1.00 63.34  ? 410  THR B CA    1 
ATOM   10599 C  C     . THR B 2 410 ? 117.342 155.312 166.337 1.00 66.12  ? 410  THR B C     1 
ATOM   10600 O  O     . THR B 2 410 ? 118.496 155.395 166.773 1.00 72.49  ? 410  THR B O     1 
ATOM   10601 C  CB    . THR B 2 410 ? 117.587 155.611 163.872 1.00 64.78  ? 410  THR B CB    1 
ATOM   10602 O  OG1   . THR B 2 410 ? 117.299 156.478 162.769 1.00 69.20  ? 410  THR B OG1   1 
ATOM   10603 C  CG2   . THR B 2 410 ? 117.077 154.218 163.556 1.00 66.62  ? 410  THR B CG2   1 
ATOM   10604 N  N     . PRO B 2 411 ? 116.441 154.515 166.906 1.00 63.09  ? 411  PRO B N     1 
ATOM   10605 C  CA    . PRO B 2 411 ? 116.856 153.557 167.935 1.00 61.43  ? 411  PRO B CA    1 
ATOM   10606 C  C     . PRO B 2 411 ? 117.848 152.553 167.371 1.00 62.74  ? 411  PRO B C     1 
ATOM   10607 O  O     . PRO B 2 411 ? 117.776 152.166 166.204 1.00 65.77  ? 411  PRO B O     1 
ATOM   10608 C  CB    . PRO B 2 411 ? 115.542 152.881 168.340 1.00 61.78  ? 411  PRO B CB    1 
ATOM   10609 C  CG    . PRO B 2 411 ? 114.484 153.864 167.968 1.00 65.28  ? 411  PRO B CG    1 
ATOM   10610 C  CD    . PRO B 2 411 ? 114.981 154.541 166.728 1.00 63.23  ? 411  PRO B CD    1 
ATOM   10611 N  N     . VAL B 2 412 ? 118.792 152.137 168.210 1.00 57.70  ? 412  VAL B N     1 
ATOM   10612 C  CA    . VAL B 2 412 ? 119.791 151.151 167.815 1.00 58.86  ? 412  VAL B CA    1 
ATOM   10613 C  C     . VAL B 2 412 ? 119.232 149.774 168.159 1.00 58.50  ? 412  VAL B C     1 
ATOM   10614 O  O     . VAL B 2 412 ? 119.264 149.341 169.310 1.00 61.25  ? 412  VAL B O     1 
ATOM   10615 C  CB    . VAL B 2 412 ? 121.141 151.399 168.486 1.00 57.63  ? 412  VAL B CB    1 
ATOM   10616 C  CG1   . VAL B 2 412 ? 122.140 150.370 168.024 1.00 59.09  ? 412  VAL B CG1   1 
ATOM   10617 C  CG2   . VAL B 2 412 ? 121.641 152.783 168.160 1.00 57.27  ? 412  VAL B CG2   1 
ATOM   10618 N  N     . ASP B 2 413 ? 118.712 149.087 167.148 1.00 58.36  ? 413  ASP B N     1 
ATOM   10619 C  CA    . ASP B 2 413 ? 118.191 147.739 167.296 1.00 53.97  ? 413  ASP B CA    1 
ATOM   10620 C  C     . ASP B 2 413 ? 118.315 147.044 165.948 1.00 55.33  ? 413  ASP B C     1 
ATOM   10621 O  O     . ASP B 2 413 ? 118.815 147.620 164.978 1.00 60.58  ? 413  ASP B O     1 
ATOM   10622 C  CB    . ASP B 2 413 ? 116.748 147.756 167.806 1.00 58.76  ? 413  ASP B CB    1 
ATOM   10623 C  CG    . ASP B 2 413 ? 115.826 148.565 166.920 1.00 60.88  ? 413  ASP B CG    1 
ATOM   10624 O  OD1   . ASP B 2 413 ? 115.399 148.044 165.869 1.00 62.45  ? 413  ASP B OD1   1 
ATOM   10625 O  OD2   . ASP B 2 413 ? 115.528 149.724 167.273 1.00 60.99  ? 413  ASP B OD2   1 
ATOM   10626 N  N     . TYR B 2 414 ? 117.868 145.790 165.889 1.00 50.13  ? 414  TYR B N     1 
ATOM   10627 C  CA    . TYR B 2 414 ? 118.016 145.027 164.655 1.00 48.72  ? 414  TYR B CA    1 
ATOM   10628 C  C     . TYR B 2 414 ? 117.153 145.603 163.540 1.00 53.22  ? 414  TYR B C     1 
ATOM   10629 O  O     . TYR B 2 414 ? 117.649 145.892 162.444 1.00 52.99  ? 414  TYR B O     1 
ATOM   10630 C  CB    . TYR B 2 414 ? 117.679 143.556 164.902 1.00 47.76  ? 414  TYR B CB    1 
ATOM   10631 C  CG    . TYR B 2 414 ? 118.754 142.833 165.677 1.00 49.15  ? 414  TYR B CG    1 
ATOM   10632 C  CD1   . TYR B 2 414 ? 120.039 142.716 165.166 1.00 49.56  ? 414  TYR B CD1   1 
ATOM   10633 C  CD2   . TYR B 2 414 ? 118.491 142.278 166.918 1.00 47.09  ? 414  TYR B CD2   1 
ATOM   10634 C  CE1   . TYR B 2 414 ? 121.031 142.067 165.869 1.00 46.59  ? 414  TYR B CE1   1 
ATOM   10635 C  CE2   . TYR B 2 414 ? 119.478 141.624 167.628 1.00 49.66  ? 414  TYR B CE2   1 
ATOM   10636 C  CZ    . TYR B 2 414 ? 120.745 141.522 167.098 1.00 50.58  ? 414  TYR B CZ    1 
ATOM   10637 O  OH    . TYR B 2 414 ? 121.731 140.871 167.799 1.00 50.09  ? 414  TYR B OH    1 
ATOM   10638 N  N     . GLU B 2 415 ? 115.866 145.815 163.815 1.00 63.38  ? 415  GLU B N     1 
ATOM   10639 C  CA    . GLU B 2 415 ? 114.948 146.227 162.760 1.00 59.19  ? 415  GLU B CA    1 
ATOM   10640 C  C     . GLU B 2 415 ? 115.212 147.658 162.311 1.00 59.68  ? 415  GLU B C     1 
ATOM   10641 O  O     . GLU B 2 415 ? 115.176 147.949 161.112 1.00 63.11  ? 415  GLU B O     1 
ATOM   10642 C  CB    . GLU B 2 415 ? 113.504 146.064 163.232 1.00 57.18  ? 415  GLU B CB    1 
ATOM   10643 C  CG    . GLU B 2 415 ? 113.186 144.676 163.770 1.00 61.48  ? 415  GLU B CG    1 
ATOM   10644 C  CD    . GLU B 2 415 ? 113.320 143.583 162.723 1.00 62.67  ? 415  GLU B CD    1 
ATOM   10645 O  OE1   . GLU B 2 415 ? 113.194 143.884 161.518 1.00 62.98  ? 415  GLU B OE1   1 
ATOM   10646 O  OE2   . GLU B 2 415 ? 113.545 142.417 163.108 1.00 60.09  ? 415  GLU B OE2   1 
ATOM   10647 N  N     . SER B 2 416 ? 115.491 148.561 163.253 1.00 58.45  ? 416  SER B N     1 
ATOM   10648 C  CA    . SER B 2 416 ? 115.705 149.961 162.898 1.00 61.87  ? 416  SER B CA    1 
ATOM   10649 C  C     . SER B 2 416 ? 116.956 150.136 162.045 1.00 61.84  ? 416  SER B C     1 
ATOM   10650 O  O     . SER B 2 416 ? 116.921 150.803 161.004 1.00 64.41  ? 416  SER B O     1 
ATOM   10651 C  CB    . SER B 2 416 ? 115.794 150.814 164.161 1.00 62.79  ? 416  SER B CB    1 
ATOM   10652 O  OG    . SER B 2 416 ? 114.620 150.697 164.941 1.00 65.19  ? 416  SER B OG    1 
ATOM   10653 N  N     . VAL B 2 417 ? 118.072 149.540 162.467 1.00 56.84  ? 417  VAL B N     1 
ATOM   10654 C  CA    . VAL B 2 417 ? 119.310 149.665 161.705 1.00 58.89  ? 417  VAL B CA    1 
ATOM   10655 C  C     . VAL B 2 417 ? 119.197 148.927 160.376 1.00 59.16  ? 417  VAL B C     1 
ATOM   10656 O  O     . VAL B 2 417 ? 119.711 149.392 159.352 1.00 57.15  ? 417  VAL B O     1 
ATOM   10657 C  CB    . VAL B 2 417 ? 120.505 149.172 162.542 1.00 56.48  ? 417  VAL B CB    1 
ATOM   10658 C  CG1   . VAL B 2 417 ? 121.790 149.227 161.736 1.00 55.27  ? 417  VAL B CG1   1 
ATOM   10659 C  CG2   . VAL B 2 417 ? 120.647 150.016 163.794 1.00 56.82  ? 417  VAL B CG2   1 
ATOM   10660 N  N     . THR B 2 418 ? 118.513 147.779 160.364 1.00 59.96  ? 418  THR B N     1 
ATOM   10661 C  CA    . THR B 2 418 ? 118.310 147.055 159.112 1.00 61.44  ? 418  THR B CA    1 
ATOM   10662 C  C     . THR B 2 418 ? 117.500 147.878 158.117 1.00 62.92  ? 418  THR B C     1 
ATOM   10663 O  O     . THR B 2 418 ? 117.839 147.943 156.930 1.00 60.18  ? 418  THR B O     1 
ATOM   10664 C  CB    . THR B 2 418 ? 117.618 145.719 159.388 1.00 60.39  ? 418  THR B CB    1 
ATOM   10665 O  OG1   . THR B 2 418 ? 118.465 144.899 160.203 1.00 60.70  ? 418  THR B OG1   1 
ATOM   10666 C  CG2   . THR B 2 418 ? 117.311 144.987 158.093 1.00 59.05  ? 418  THR B CG2   1 
ATOM   10667 N  N     . ALA B 2 419 ? 116.433 148.528 158.584 1.00 67.11  ? 419  ALA B N     1 
ATOM   10668 C  CA    . ALA B 2 419 ? 115.568 149.289 157.693 1.00 66.02  ? 419  ALA B CA    1 
ATOM   10669 C  C     . ALA B 2 419 ? 116.181 150.620 157.287 1.00 67.33  ? 419  ALA B C     1 
ATOM   10670 O  O     . ALA B 2 419 ? 115.843 151.148 156.223 1.00 68.56  ? 419  ALA B O     1 
ATOM   10671 C  CB    . ALA B 2 419 ? 114.209 149.520 158.352 1.00 64.60  ? 419  ALA B CB    1 
ATOM   10672 N  N     . THR B 2 420 ? 117.064 151.182 158.117 1.00 59.09  ? 420  THR B N     1 
ATOM   10673 C  CA    . THR B 2 420 ? 117.684 152.458 157.773 1.00 60.83  ? 420  THR B CA    1 
ATOM   10674 C  C     . THR B 2 420 ? 118.562 152.328 156.534 1.00 60.72  ? 420  THR B C     1 
ATOM   10675 O  O     . THR B 2 420 ? 118.582 153.221 155.680 1.00 59.71  ? 420  THR B O     1 
ATOM   10676 C  CB    . THR B 2 420 ? 118.494 152.984 158.956 1.00 62.81  ? 420  THR B CB    1 
ATOM   10677 O  OG1   . THR B 2 420 ? 117.654 153.057 160.114 1.00 61.33  ? 420  THR B OG1   1 
ATOM   10678 C  CG2   . THR B 2 420 ? 119.035 154.368 158.656 1.00 63.37  ? 420  THR B CG2   1 
ATOM   10679 N  N     . GLY B 2 421 ? 119.275 151.215 156.408 1.00 57.28  ? 421  GLY B N     1 
ATOM   10680 C  CA    . GLY B 2 421 ? 120.135 150.998 155.263 1.00 59.82  ? 421  GLY B CA    1 
ATOM   10681 C  C     . GLY B 2 421 ? 121.409 150.262 155.617 1.00 59.35  ? 421  GLY B C     1 
ATOM   10682 O  O     . GLY B 2 421 ? 122.064 149.684 154.745 1.00 57.94  ? 421  GLY B O     1 
ATOM   10683 N  N     . ALA B 2 422 ? 121.767 150.268 156.897 1.00 55.14  ? 422  ALA B N     1 
ATOM   10684 C  CA    . ALA B 2 422 ? 122.942 149.567 157.382 1.00 50.84  ? 422  ALA B CA    1 
ATOM   10685 C  C     . ALA B 2 422 ? 122.544 148.203 157.942 1.00 49.72  ? 422  ALA B C     1 
ATOM   10686 O  O     . ALA B 2 422 ? 121.394 147.771 157.850 1.00 55.85  ? 422  ALA B O     1 
ATOM   10687 C  CB    . ALA B 2 422 ? 123.666 150.404 158.435 1.00 51.46  ? 422  ALA B CB    1 
ATOM   10688 N  N     . ILE B 2 423 ? 123.524 147.507 158.515 1.00 39.09  ? 423  ILE B N     1 
ATOM   10689 C  CA    . ILE B 2 423 ? 123.298 146.242 159.199 1.00 40.08  ? 423  ILE B CA    1 
ATOM   10690 C  C     . ILE B 2 423 ? 124.148 146.223 160.461 1.00 41.09  ? 423  ILE B C     1 
ATOM   10691 O  O     . ILE B 2 423 ? 125.104 146.986 160.604 1.00 40.63  ? 423  ILE B O     1 
ATOM   10692 C  CB    . ILE B 2 423 ? 123.613 145.021 158.305 1.00 43.38  ? 423  ILE B CB    1 
ATOM   10693 C  CG1   . ILE B 2 423 ? 124.844 145.285 157.434 1.00 41.91  ? 423  ILE B CG1   1 
ATOM   10694 C  CG2   . ILE B 2 423 ? 122.415 144.674 157.441 1.00 42.58  ? 423  ILE B CG2   1 
ATOM   10695 C  CD1   . ILE B 2 423 ? 126.153 144.846 158.052 1.00 35.21  ? 423  ILE B CD1   1 
ATOM   10696 N  N     . MET B 2 424 ? 123.772 145.347 161.395 1.00 41.27  ? 424  MET B N     1 
ATOM   10697 C  CA    . MET B 2 424 ? 124.530 145.232 162.637 1.00 41.69  ? 424  MET B CA    1 
ATOM   10698 C  C     . MET B 2 424 ? 125.951 144.757 162.371 1.00 38.94  ? 424  MET B C     1 
ATOM   10699 O  O     . MET B 2 424 ? 126.907 145.286 162.951 1.00 37.94  ? 424  MET B O     1 
ATOM   10700 C  CB    . MET B 2 424 ? 123.818 144.291 163.605 1.00 41.55  ? 424  MET B CB    1 
ATOM   10701 C  CG    . MET B 2 424 ? 122.698 144.946 164.385 1.00 40.78  ? 424  MET B CG    1 
ATOM   10702 S  SD    . MET B 2 424 ? 123.302 146.232 165.491 1.00 53.38  ? 424  MET B SD    1 
ATOM   10703 C  CE    . MET B 2 424 ? 121.786 146.703 166.313 1.00 46.33  ? 424  MET B CE    1 
ATOM   10704 N  N     . GLY B 2 425 ? 126.108 143.770 161.491 1.00 40.59  ? 425  GLY B N     1 
ATOM   10705 C  CA    . GLY B 2 425 ? 127.425 143.296 161.105 1.00 37.97  ? 425  GLY B CA    1 
ATOM   10706 C  C     . GLY B 2 425 ? 128.211 142.788 162.292 1.00 44.03  ? 425  GLY B C     1 
ATOM   10707 O  O     . GLY B 2 425 ? 127.685 142.103 163.175 1.00 54.88  ? 425  GLY B O     1 
ATOM   10708 N  N     . SER B 2 426 ? 129.499 143.127 162.315 1.00 34.04  ? 426  SER B N     1 
ATOM   10709 C  CA    . SER B 2 426 ? 130.314 142.809 163.480 1.00 34.58  ? 426  SER B CA    1 
ATOM   10710 C  C     . SER B 2 426 ? 129.819 143.559 164.708 1.00 34.56  ? 426  SER B C     1 
ATOM   10711 O  O     . SER B 2 426 ? 129.720 142.986 165.798 1.00 42.14  ? 426  SER B O     1 
ATOM   10712 C  CB    . SER B 2 426 ? 131.777 143.140 163.200 1.00 37.02  ? 426  SER B CB    1 
ATOM   10713 O  OG    . SER B 2 426 ? 131.936 144.514 162.904 1.00 35.33  ? 426  SER B OG    1 
ATOM   10714 N  N     . GLY B 2 427 ? 129.473 144.829 164.542 1.00 32.94  ? 427  GLY B N     1 
ATOM   10715 C  CA    . GLY B 2 427 ? 129.077 145.656 165.660 1.00 35.16  ? 427  GLY B CA    1 
ATOM   10716 C  C     . GLY B 2 427 ? 129.982 146.859 165.803 1.00 39.02  ? 427  GLY B C     1 
ATOM   10717 O  O     . GLY B 2 427 ? 130.164 147.384 166.903 1.00 45.60  ? 427  GLY B O     1 
ATOM   10718 N  N     . GLY B 2 428 ? 130.565 147.298 164.694 1.00 37.47  ? 428  GLY B N     1 
ATOM   10719 C  CA    . GLY B 2 428 ? 131.487 148.419 164.697 1.00 39.96  ? 428  GLY B CA    1 
ATOM   10720 C  C     . GLY B 2 428 ? 130.824 149.686 164.187 1.00 42.37  ? 428  GLY B C     1 
ATOM   10721 O  O     . GLY B 2 428 ? 130.085 149.662 163.204 1.00 42.50  ? 428  GLY B O     1 
ATOM   10722 N  N     . MET B 2 429 ? 131.095 150.788 164.875 1.00 47.32  ? 429  MET B N     1 
ATOM   10723 C  CA    . MET B 2 429 ? 130.654 152.113 164.458 1.00 42.63  ? 429  MET B CA    1 
ATOM   10724 C  C     . MET B 2 429 ? 131.890 152.918 164.086 1.00 43.57  ? 429  MET B C     1 
ATOM   10725 O  O     . MET B 2 429 ? 132.712 153.238 164.951 1.00 49.69  ? 429  MET B O     1 
ATOM   10726 C  CB    . MET B 2 429 ? 129.859 152.809 165.561 1.00 43.49  ? 429  MET B CB    1 
ATOM   10727 C  CG    . MET B 2 429 ? 128.523 152.165 165.875 1.00 45.03  ? 429  MET B CG    1 
ATOM   10728 S  SD    . MET B 2 429 ? 127.533 153.167 166.994 1.00 56.60  ? 429  MET B SD    1 
ATOM   10729 C  CE    . MET B 2 429 ? 126.123 152.096 167.243 1.00 49.46  ? 429  MET B CE    1 
ATOM   10730 N  N     . VAL B 2 430 ? 132.026 153.236 162.804 1.00 49.74  ? 430  VAL B N     1 
ATOM   10731 C  CA    . VAL B 2 430 ? 133.095 154.099 162.321 1.00 49.33  ? 430  VAL B CA    1 
ATOM   10732 C  C     . VAL B 2 430 ? 132.503 155.483 162.104 1.00 47.38  ? 430  VAL B C     1 
ATOM   10733 O  O     . VAL B 2 430 ? 131.608 155.664 161.272 1.00 53.36  ? 430  VAL B O     1 
ATOM   10734 C  CB    . VAL B 2 430 ? 133.730 153.553 161.035 1.00 52.24  ? 430  VAL B CB    1 
ATOM   10735 C  CG1   . VAL B 2 430 ? 134.933 154.391 160.648 1.00 50.78  ? 430  VAL B CG1   1 
ATOM   10736 C  CG2   . VAL B 2 430 ? 134.130 152.101 161.219 1.00 50.27  ? 430  VAL B CG2   1 
ATOM   10737 N  N     . VAL B 2 431 ? 133.001 156.455 162.856 1.00 54.86  ? 431  VAL B N     1 
ATOM   10738 C  CA    . VAL B 2 431 ? 132.461 157.808 162.849 1.00 55.89  ? 431  VAL B CA    1 
ATOM   10739 C  C     . VAL B 2 431 ? 133.105 158.591 161.714 1.00 58.98  ? 431  VAL B C     1 
ATOM   10740 O  O     . VAL B 2 431 ? 134.332 158.710 161.645 1.00 61.45  ? 431  VAL B O     1 
ATOM   10741 C  CB    . VAL B 2 431 ? 132.694 158.499 164.199 1.00 58.71  ? 431  VAL B CB    1 
ATOM   10742 C  CG1   . VAL B 2 431 ? 132.452 159.993 164.086 1.00 60.82  ? 431  VAL B CG1   1 
ATOM   10743 C  CG2   . VAL B 2 431 ? 131.795 157.886 165.247 1.00 58.41  ? 431  VAL B CG2   1 
ATOM   10744 N  N     . MET B 2 432 ? 132.275 159.129 160.830 1.00 60.70  ? 432  MET B N     1 
ATOM   10745 C  CA    . MET B 2 432 ? 132.727 159.933 159.708 1.00 62.19  ? 432  MET B CA    1 
ATOM   10746 C  C     . MET B 2 432 ? 132.181 161.345 159.853 1.00 65.05  ? 432  MET B C     1 
ATOM   10747 O  O     . MET B 2 432 ? 131.004 161.536 160.170 1.00 66.87  ? 432  MET B O     1 
ATOM   10748 C  CB    . MET B 2 432 ? 132.286 159.308 158.384 1.00 61.79  ? 432  MET B CB    1 
ATOM   10749 C  CG    . MET B 2 432 ? 132.874 157.927 158.149 1.00 63.80  ? 432  MET B CG    1 
ATOM   10750 S  SD    . MET B 2 432 ? 131.903 156.932 157.008 1.00 72.21  ? 432  MET B SD    1 
ATOM   10751 C  CE    . MET B 2 432 ? 130.350 156.846 157.893 1.00 61.66  ? 432  MET B CE    1 
ATOM   10752 N  N     . ASP B 2 433 ? 133.039 162.329 159.622 1.00 73.14  ? 433  ASP B N     1 
ATOM   10753 C  CA    . ASP B 2 433 ? 132.736 163.728 159.884 1.00 75.50  ? 433  ASP B CA    1 
ATOM   10754 C  C     . ASP B 2 433 ? 132.770 164.527 158.581 1.00 78.50  ? 433  ASP B C     1 
ATOM   10755 O  O     . ASP B 2 433 ? 132.810 163.966 157.482 1.00 78.41  ? 433  ASP B O     1 
ATOM   10756 C  CB    . ASP B 2 433 ? 133.704 164.292 160.926 1.00 78.51  ? 433  ASP B CB    1 
ATOM   10757 C  CG    . ASP B 2 433 ? 135.146 163.941 160.631 1.00 77.62  ? 433  ASP B CG    1 
ATOM   10758 O  OD1   . ASP B 2 433 ? 135.385 162.877 160.027 1.00 74.20  ? 433  ASP B OD1   1 
ATOM   10759 O  OD2   . ASP B 2 433 ? 136.041 164.726 161.005 1.00 77.69  ? 433  ASP B OD2   1 
ATOM   10760 N  N     . GLU B 2 434 ? 132.720 165.856 158.720 1.00 82.29  ? 434  GLU B N     1 
ATOM   10761 C  CA    . GLU B 2 434 ? 132.690 166.743 157.561 1.00 82.85  ? 434  GLU B CA    1 
ATOM   10762 C  C     . GLU B 2 434 ? 133.956 166.630 156.717 1.00 82.53  ? 434  GLU B C     1 
ATOM   10763 O  O     . GLU B 2 434 ? 133.908 166.831 155.498 1.00 82.85  ? 434  GLU B O     1 
ATOM   10764 C  CB    . GLU B 2 434 ? 132.480 168.185 158.025 1.00 82.35  ? 434  GLU B CB    1 
ATOM   10765 C  CG    . GLU B 2 434 ? 132.216 169.184 156.910 1.00 82.90  ? 434  GLU B CG    1 
ATOM   10766 C  CD    . GLU B 2 434 ? 133.483 169.839 156.396 1.00 84.76  ? 434  GLU B CD    1 
ATOM   10767 O  OE1   . GLU B 2 434 ? 134.541 169.676 157.040 1.00 82.65  ? 434  GLU B OE1   1 
ATOM   10768 O  OE2   . GLU B 2 434 ? 133.422 170.515 155.348 1.00 86.06  ? 434  GLU B OE2   1 
ATOM   10769 N  N     . ASP B 2 435 ? 135.091 166.308 157.338 1.00 81.56  ? 435  ASP B N     1 
ATOM   10770 C  CA    . ASP B 2 435 ? 136.348 166.162 156.612 1.00 83.90  ? 435  ASP B CA    1 
ATOM   10771 C  C     . ASP B 2 435 ? 136.401 164.899 155.758 1.00 85.27  ? 435  ASP B C     1 
ATOM   10772 O  O     . ASP B 2 435 ? 137.300 164.774 154.920 1.00 87.63  ? 435  ASP B O     1 
ATOM   10773 C  CB    . ASP B 2 435 ? 137.509 166.171 157.610 1.00 85.95  ? 435  ASP B CB    1 
ATOM   10774 C  CG    . ASP B 2 435 ? 138.864 166.190 156.935 1.00 86.53  ? 435  ASP B CG    1 
ATOM   10775 O  OD1   . ASP B 2 435 ? 139.253 167.254 156.410 1.00 84.19  ? 435  ASP B OD1   1 
ATOM   10776 O  OD2   . ASP B 2 435 ? 139.537 165.139 156.926 1.00 85.34  ? 435  ASP B OD2   1 
ATOM   10777 N  N     . THR B 2 436 ? 135.458 163.977 155.926 1.00 73.90  ? 436  THR B N     1 
ATOM   10778 C  CA    . THR B 2 436 ? 135.522 162.673 155.281 1.00 72.76  ? 436  THR B CA    1 
ATOM   10779 C  C     . THR B 2 436 ? 134.777 162.688 153.951 1.00 76.40  ? 436  THR B C     1 
ATOM   10780 O  O     . THR B 2 436 ? 133.633 163.146 153.877 1.00 75.22  ? 436  THR B O     1 
ATOM   10781 C  CB    . THR B 2 436 ? 134.938 161.602 156.204 1.00 71.02  ? 436  THR B CB    1 
ATOM   10782 O  OG1   . THR B 2 436 ? 135.833 161.375 157.299 1.00 73.31  ? 436  THR B OG1   1 
ATOM   10783 C  CG2   . THR B 2 436 ? 134.723 160.301 155.461 1.00 72.39  ? 436  THR B CG2   1 
ATOM   10784 N  N     . CYS B 2 437 ? 135.433 162.189 152.904 1.00 68.41  ? 437  CYS B N     1 
ATOM   10785 C  CA    . CYS B 2 437 ? 134.801 161.989 151.606 1.00 64.49  ? 437  CYS B CA    1 
ATOM   10786 C  C     . CYS B 2 437 ? 134.128 160.624 151.598 1.00 61.02  ? 437  CYS B C     1 
ATOM   10787 O  O     . CYS B 2 437 ? 134.777 159.604 151.850 1.00 59.40  ? 437  CYS B O     1 
ATOM   10788 C  CB    . CYS B 2 437 ? 135.823 162.091 150.475 1.00 66.51  ? 437  CYS B CB    1 
ATOM   10789 S  SG    . CYS B 2 437 ? 135.148 161.848 148.814 1.00 67.55  ? 437  CYS B SG    1 
ATOM   10790 N  N     . MET B 2 438 ? 132.829 160.608 151.310 1.00 54.45  ? 438  MET B N     1 
ATOM   10791 C  CA    . MET B 2 438 ? 132.064 159.372 151.392 1.00 54.74  ? 438  MET B CA    1 
ATOM   10792 C  C     . MET B 2 438 ? 132.350 158.433 150.227 1.00 55.18  ? 438  MET B C     1 
ATOM   10793 O  O     . MET B 2 438 ? 132.269 157.210 150.391 1.00 57.58  ? 438  MET B O     1 
ATOM   10794 C  CB    . MET B 2 438 ? 130.573 159.695 151.463 1.00 55.33  ? 438  MET B CB    1 
ATOM   10795 C  CG    . MET B 2 438 ? 130.199 160.604 152.613 1.00 57.08  ? 438  MET B CG    1 
ATOM   10796 S  SD    . MET B 2 438 ? 130.727 159.941 154.201 1.00 60.64  ? 438  MET B SD    1 
ATOM   10797 C  CE    . MET B 2 438 ? 129.799 158.414 154.249 1.00 55.92  ? 438  MET B CE    1 
ATOM   10798 N  N     . VAL B 2 439 ? 132.679 158.976 149.054 1.00 52.84  ? 439  VAL B N     1 
ATOM   10799 C  CA    . VAL B 2 439 ? 132.998 158.128 147.910 1.00 53.13  ? 439  VAL B CA    1 
ATOM   10800 C  C     . VAL B 2 439 ? 134.268 157.328 148.176 1.00 50.47  ? 439  VAL B C     1 
ATOM   10801 O  O     . VAL B 2 439 ? 134.347 156.135 147.857 1.00 56.04  ? 439  VAL B O     1 
ATOM   10802 C  CB    . VAL B 2 439 ? 133.112 158.980 146.633 1.00 54.52  ? 439  VAL B CB    1 
ATOM   10803 C  CG1   . VAL B 2 439 ? 133.309 158.095 145.416 1.00 48.85  ? 439  VAL B CG1   1 
ATOM   10804 C  CG2   . VAL B 2 439 ? 131.874 159.838 146.467 1.00 53.16  ? 439  VAL B CG2   1 
ATOM   10805 N  N     . ASP B 2 440 ? 135.274 157.965 148.780 1.00 42.81  ? 440  ASP B N     1 
ATOM   10806 C  CA    . ASP B 2 440 ? 136.497 157.250 149.131 1.00 47.50  ? 440  ASP B CA    1 
ATOM   10807 C  C     . ASP B 2 440 ? 136.229 156.172 150.176 1.00 53.46  ? 440  ASP B C     1 
ATOM   10808 O  O     . ASP B 2 440 ? 136.836 155.098 150.137 1.00 53.73  ? 440  ASP B O     1 
ATOM   10809 C  CB    . ASP B 2 440 ? 137.553 158.234 149.633 1.00 51.66  ? 440  ASP B CB    1 
ATOM   10810 C  CG    . ASP B 2 440 ? 138.901 157.581 149.843 1.00 50.57  ? 440  ASP B CG    1 
ATOM   10811 O  OD1   . ASP B 2 440 ? 139.603 157.332 148.843 1.00 50.62  ? 440  ASP B OD1   1 
ATOM   10812 O  OD2   . ASP B 2 440 ? 139.260 157.314 151.008 1.00 50.40  ? 440  ASP B OD2   1 
ATOM   10813 N  N     . VAL B 2 441 ? 135.328 156.443 151.122 1.00 45.68  ? 441  VAL B N     1 
ATOM   10814 C  CA    . VAL B 2 441 ? 134.976 155.450 152.135 1.00 42.01  ? 441  VAL B CA    1 
ATOM   10815 C  C     . VAL B 2 441 ? 134.290 154.248 151.495 1.00 38.81  ? 441  VAL B C     1 
ATOM   10816 O  O     . VAL B 2 441 ? 134.587 153.088 151.826 1.00 44.62  ? 441  VAL B O     1 
ATOM   10817 C  CB    . VAL B 2 441 ? 134.100 156.102 153.220 1.00 40.78  ? 441  VAL B CB    1 
ATOM   10818 C  CG1   . VAL B 2 441 ? 133.308 155.060 153.983 1.00 38.14  ? 441  VAL B CG1   1 
ATOM   10819 C  CG2   . VAL B 2 441 ? 134.964 156.905 154.167 1.00 42.48  ? 441  VAL B CG2   1 
ATOM   10820 N  N     . ALA B 2 442 ? 133.363 154.507 150.571 1.00 33.28  ? 442  ALA B N     1 
ATOM   10821 C  CA    . ALA B 2 442 ? 132.726 153.422 149.834 1.00 37.62  ? 442  ALA B CA    1 
ATOM   10822 C  C     . ALA B 2 442 ? 133.756 152.613 149.060 1.00 37.23  ? 442  ALA B C     1 
ATOM   10823 O  O     . ALA B 2 442 ? 133.681 151.380 149.015 1.00 41.64  ? 442  ALA B O     1 
ATOM   10824 C  CB    . ALA B 2 442 ? 131.661 153.982 148.893 1.00 39.40  ? 442  ALA B CB    1 
ATOM   10825 N  N     . LYS B 2 443 ? 134.735 153.292 148.457 1.00 36.59  ? 443  LYS B N     1 
ATOM   10826 C  CA    . LYS B 2 443 ? 135.786 152.588 147.729 1.00 34.57  ? 443  LYS B CA    1 
ATOM   10827 C  C     . LYS B 2 443 ? 136.631 151.731 148.665 1.00 35.41  ? 443  LYS B C     1 
ATOM   10828 O  O     . LYS B 2 443 ? 137.028 150.620 148.306 1.00 43.93  ? 443  LYS B O     1 
ATOM   10829 C  CB    . LYS B 2 443 ? 136.665 153.586 146.977 1.00 36.35  ? 443  LYS B CB    1 
ATOM   10830 C  CG    . LYS B 2 443 ? 137.386 152.990 145.783 1.00 38.80  ? 443  LYS B CG    1 
ATOM   10831 C  CD    . LYS B 2 443 ? 138.461 153.920 145.260 1.00 40.22  ? 443  LYS B CD    1 
ATOM   10832 C  CE    . LYS B 2 443 ? 139.620 154.009 146.230 1.00 38.77  ? 443  LYS B CE    1 
ATOM   10833 N  NZ    . LYS B 2 443 ? 140.717 154.858 145.701 1.00 37.92  ? 443  LYS B NZ    1 
ATOM   10834 N  N     . PHE B 2 444 ? 136.922 152.237 149.864 1.00 31.88  ? 444  PHE B N     1 
ATOM   10835 C  CA    . PHE B 2 444 ? 137.692 151.477 150.847 1.00 36.95  ? 444  PHE B CA    1 
ATOM   10836 C  C     . PHE B 2 444 ? 136.966 150.193 151.240 1.00 38.58  ? 444  PHE B C     1 
ATOM   10837 O  O     . PHE B 2 444 ? 137.558 149.103 151.274 1.00 41.08  ? 444  PHE B O     1 
ATOM   10838 C  CB    . PHE B 2 444 ? 137.946 152.361 152.071 1.00 34.94  ? 444  PHE B CB    1 
ATOM   10839 C  CG    . PHE B 2 444 ? 138.855 151.754 153.099 1.00 42.89  ? 444  PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 2 444 ? 138.344 150.990 154.134 1.00 40.34  ? 444  PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 2 444 ? 140.219 151.981 153.053 1.00 43.50  ? 444  PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 2 444 ? 139.177 150.445 155.085 1.00 41.09  ? 444  PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 2 444 ? 141.057 151.440 154.003 1.00 42.27  ? 444  PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 2 444 ? 140.535 150.670 155.020 1.00 42.55  ? 444  PHE B CZ    1 
ATOM   10845 N  N     . PHE B 2 445 ? 135.669 150.303 151.524 1.00 30.91  ? 445  PHE B N     1 
ATOM   10846 C  CA    . PHE B 2 445 ? 134.920 149.117 151.928 1.00 25.79  ? 445  PHE B CA    1 
ATOM   10847 C  C     . PHE B 2 445 ? 134.734 148.143 150.770 1.00 25.40  ? 445  PHE B C     1 
ATOM   10848 O  O     . PHE B 2 445 ? 134.780 146.922 150.972 1.00 29.09  ? 445  PHE B O     1 
ATOM   10849 C  CB    . PHE B 2 445 ? 133.581 149.534 152.526 1.00 27.89  ? 445  PHE B CB    1 
ATOM   10850 C  CG    . PHE B 2 445 ? 133.719 150.278 153.818 1.00 38.37  ? 445  PHE B CG    1 
ATOM   10851 C  CD1   . PHE B 2 445 ? 134.815 150.059 154.636 1.00 35.89  ? 445  PHE B CD1   1 
ATOM   10852 C  CD2   . PHE B 2 445 ? 132.775 151.205 154.209 1.00 33.44  ? 445  PHE B CD2   1 
ATOM   10853 C  CE1   . PHE B 2 445 ? 134.961 150.741 155.821 1.00 35.14  ? 445  PHE B CE1   1 
ATOM   10854 C  CE2   . PHE B 2 445 ? 132.918 151.891 155.396 1.00 31.24  ? 445  PHE B CE2   1 
ATOM   10855 C  CZ    . PHE B 2 445 ? 134.014 151.657 156.202 1.00 34.11  ? 445  PHE B CZ    1 
ATOM   10856 N  N     . LEU B 2 446 ? 134.561 148.655 149.551 1.00 30.72  ? 446  LEU B N     1 
ATOM   10857 C  CA    . LEU B 2 446 ? 134.462 147.768 148.399 1.00 22.92  ? 446  LEU B CA    1 
ATOM   10858 C  C     . LEU B 2 446 ? 135.792 147.094 148.094 1.00 20.58  ? 446  LEU B C     1 
ATOM   10859 O  O     . LEU B 2 446 ? 135.809 145.949 147.636 1.00 29.41  ? 446  LEU B O     1 
ATOM   10860 C  CB    . LEU B 2 446 ? 133.955 148.540 147.183 1.00 26.46  ? 446  LEU B CB    1 
ATOM   10861 C  CG    . LEU B 2 446 ? 132.451 148.434 146.923 1.00 28.66  ? 446  LEU B CG    1 
ATOM   10862 C  CD1   . LEU B 2 446 ? 132.092 147.043 146.438 1.00 29.30  ? 446  LEU B CD1   1 
ATOM   10863 C  CD2   . LEU B 2 446 ? 131.655 148.777 148.170 1.00 28.52  ? 446  LEU B CD2   1 
ATOM   10864 N  N     . ASP B 2 447 ? 136.911 147.777 148.341 1.00 24.59  ? 447  ASP B N     1 
ATOM   10865 C  CA    . ASP B 2 447 ? 138.217 147.147 148.190 1.00 22.96  ? 447  ASP B CA    1 
ATOM   10866 C  C     . ASP B 2 447 ? 138.403 146.024 149.200 1.00 24.02  ? 447  ASP B C     1 
ATOM   10867 O  O     . ASP B 2 447 ? 138.930 144.956 148.861 1.00 35.55  ? 447  ASP B O     1 
ATOM   10868 C  CB    . ASP B 2 447 ? 139.323 148.191 148.337 1.00 29.16  ? 447  ASP B CB    1 
ATOM   10869 C  CG    . ASP B 2 447 ? 140.708 147.594 148.210 1.00 37.90  ? 447  ASP B CG    1 
ATOM   10870 O  OD1   . ASP B 2 447 ? 141.127 147.294 147.075 1.00 38.59  ? 447  ASP B OD1   1 
ATOM   10871 O  OD2   . ASP B 2 447 ? 141.378 147.424 149.248 1.00 40.64  ? 447  ASP B OD2   1 
ATOM   10872 N  N     . PHE B 2 448 ? 137.975 146.244 150.447 1.00 25.63  ? 448  PHE B N     1 
ATOM   10873 C  CA    . PHE B 2 448 ? 138.052 145.166 151.428 1.00 28.75  ? 448  PHE B CA    1 
ATOM   10874 C  C     . PHE B 2 448 ? 137.174 143.988 151.023 1.00 20.83  ? 448  PHE B C     1 
ATOM   10875 O  O     . PHE B 2 448 ? 137.567 142.828 151.188 1.00 25.38  ? 448  PHE B O     1 
ATOM   10876 C  CB    . PHE B 2 448 ? 137.663 145.659 152.820 1.00 27.68  ? 448  PHE B CB    1 
ATOM   10877 C  CG    . PHE B 2 448 ? 137.875 144.631 153.896 1.00 25.28  ? 448  PHE B CG    1 
ATOM   10878 C  CD1   . PHE B 2 448 ? 139.118 144.472 154.483 1.00 33.97  ? 448  PHE B CD1   1 
ATOM   10879 C  CD2   . PHE B 2 448 ? 136.843 143.806 154.302 1.00 27.57  ? 448  PHE B CD2   1 
ATOM   10880 C  CE1   . PHE B 2 448 ? 139.320 143.520 155.463 1.00 34.16  ? 448  PHE B CE1   1 
ATOM   10881 C  CE2   . PHE B 2 448 ? 137.040 142.857 155.281 1.00 32.35  ? 448  PHE B CE2   1 
ATOM   10882 C  CZ    . PHE B 2 448 ? 138.280 142.714 155.861 1.00 26.69  ? 448  PHE B CZ    1 
ATOM   10883 N  N     . THR B 2 449 ? 135.977 144.264 150.503 1.00 24.01  ? 449  THR B N     1 
ATOM   10884 C  CA    . THR B 2 449 ? 135.107 143.178 150.058 1.00 20.36  ? 449  THR B CA    1 
ATOM   10885 C  C     . THR B 2 449 ? 135.703 142.430 148.867 1.00 15.32  ? 449  THR B C     1 
ATOM   10886 O  O     . THR B 2 449 ? 135.606 141.199 148.790 1.00 22.76  ? 449  THR B O     1 
ATOM   10887 C  CB    . THR B 2 449 ? 133.722 143.722 149.718 1.00 26.68  ? 449  THR B CB    1 
ATOM   10888 O  OG1   . THR B 2 449 ? 133.141 144.315 150.884 1.00 26.84  ? 449  THR B OG1   1 
ATOM   10889 C  CG2   . THR B 2 449 ? 132.831 142.606 149.250 1.00 24.40  ? 449  THR B CG2   1 
ATOM   10890 N  N     . VAL B 2 450 ? 136.318 143.153 147.928 1.00 24.19  ? 450  VAL B N     1 
ATOM   10891 C  CA    . VAL B 2 450 ? 136.952 142.516 146.775 1.00 23.01  ? 450  VAL B CA    1 
ATOM   10892 C  C     . VAL B 2 450 ? 138.098 141.623 147.226 1.00 21.99  ? 450  VAL B C     1 
ATOM   10893 O  O     . VAL B 2 450 ? 138.276 140.509 146.718 1.00 33.55  ? 450  VAL B O     1 
ATOM   10894 C  CB    . VAL B 2 450 ? 137.426 143.585 145.770 1.00 22.46  ? 450  VAL B CB    1 
ATOM   10895 C  CG1   . VAL B 2 450 ? 138.471 143.018 144.827 1.00 23.58  ? 450  VAL B CG1   1 
ATOM   10896 C  CG2   . VAL B 2 450 ? 136.259 144.120 144.975 1.00 18.23  ? 450  VAL B CG2   1 
ATOM   10897 N  N     . LYS B 2 451 ? 138.892 142.097 148.187 1.00 12.25  ? 451  LYS B N     1 
ATOM   10898 C  CA    . LYS B 2 451 ? 140.022 141.312 148.671 1.00 18.99  ? 451  LYS B CA    1 
ATOM   10899 C  C     . LYS B 2 451 ? 139.563 140.030 149.357 1.00 22.82  ? 451  LYS B C     1 
ATOM   10900 O  O     . LYS B 2 451 ? 140.168 138.969 149.171 1.00 23.67  ? 451  LYS B O     1 
ATOM   10901 C  CB    . LYS B 2 451 ? 140.863 142.154 149.627 1.00 27.45  ? 451  LYS B CB    1 
ATOM   10902 C  CG    . LYS B 2 451 ? 142.325 141.772 149.672 1.00 26.49  ? 451  LYS B CG    1 
ATOM   10903 C  CD    . LYS B 2 451 ? 143.050 142.275 148.441 1.00 28.56  ? 451  LYS B CD    1 
ATOM   10904 C  CE    . LYS B 2 451 ? 142.911 143.780 148.312 1.00 29.67  ? 451  LYS B CE    1 
ATOM   10905 N  NZ    . LYS B 2 451 ? 143.332 144.479 149.557 1.00 27.72  ? 451  LYS B NZ    1 
ATOM   10906 N  N     . GLU B 2 452 ? 138.494 140.104 150.143 1.00 26.69  ? 452  GLU B N     1 
ATOM   10907 C  CA    . GLU B 2 452 ? 138.092 139.009 151.015 1.00 22.53  ? 452  GLU B CA    1 
ATOM   10908 C  C     . GLU B 2 452 ? 137.077 138.064 150.387 1.00 26.19  ? 452  GLU B C     1 
ATOM   10909 O  O     . GLU B 2 452 ? 136.620 137.138 151.063 1.00 35.98  ? 452  GLU B O     1 
ATOM   10910 C  CB    . GLU B 2 452 ? 137.527 139.567 152.323 1.00 20.77  ? 452  GLU B CB    1 
ATOM   10911 C  CG    . GLU B 2 452 ? 138.511 140.419 153.110 1.00 31.22  ? 452  GLU B CG    1 
ATOM   10912 C  CD    . GLU B 2 452 ? 139.796 139.685 153.451 1.00 36.26  ? 452  GLU B CD    1 
ATOM   10913 O  OE1   . GLU B 2 452 ? 140.742 139.714 152.635 1.00 31.00  ? 452  GLU B OE1   1 
ATOM   10914 O  OE2   . GLU B 2 452 ? 139.864 139.080 154.541 1.00 39.59  ? 452  GLU B OE2   1 
ATOM   10915 N  N     . SER B 2 453 ? 136.708 138.274 149.128 1.00 21.95  ? 453  SER B N     1 
ATOM   10916 C  CA    . SER B 2 453 ? 135.798 137.357 148.457 1.00 17.62  ? 453  SER B CA    1 
ATOM   10917 C  C     . SER B 2 453 ? 136.495 136.032 148.171 1.00 18.24  ? 453  SER B C     1 
ATOM   10918 O  O     . SER B 2 453 ? 137.676 135.997 147.819 1.00 27.16  ? 453  SER B O     1 
ATOM   10919 C  CB    . SER B 2 453 ? 135.288 137.977 147.158 1.00 9.70   ? 453  SER B CB    1 
ATOM   10920 O  OG    . SER B 2 453 ? 134.575 137.032 146.385 1.00 17.14  ? 453  SER B OG    1 
ATOM   10921 N  N     . CYS B 2 454 ? 135.757 134.934 148.333 1.00 6.36   ? 454  CYS B N     1 
ATOM   10922 C  CA    . CYS B 2 454 ? 136.309 133.618 148.040 1.00 6.13   ? 454  CYS B CA    1 
ATOM   10923 C  C     . CYS B 2 454 ? 136.376 133.329 146.546 1.00 17.40  ? 454  CYS B C     1 
ATOM   10924 O  O     . CYS B 2 454 ? 137.147 132.459 146.131 1.00 31.16  ? 454  CYS B O     1 
ATOM   10925 C  CB    . CYS B 2 454 ? 135.492 132.529 148.738 1.00 13.44  ? 454  CYS B CB    1 
ATOM   10926 S  SG    . CYS B 2 454 ? 133.808 132.342 148.130 1.00 27.07  ? 454  CYS B SG    1 
ATOM   10927 N  N     . GLY B 2 455 ? 135.599 134.039 145.735 1.00 9.46   ? 455  GLY B N     1 
ATOM   10928 C  CA    . GLY B 2 455 ? 135.636 133.832 144.302 1.00 15.84  ? 455  GLY B CA    1 
ATOM   10929 C  C     . GLY B 2 455 ? 134.831 132.656 143.804 1.00 18.48  ? 455  GLY B C     1 
ATOM   10930 O  O     . GLY B 2 455 ? 135.206 132.040 142.803 1.00 16.10  ? 455  GLY B O     1 
ATOM   10931 N  N     . LYS B 2 456 ? 133.728 132.324 144.471 1.00 17.85  ? 456  LYS B N     1 
ATOM   10932 C  CA    . LYS B 2 456 ? 132.909 131.193 144.050 1.00 15.08  ? 456  LYS B CA    1 
ATOM   10933 C  C     . LYS B 2 456 ? 131.781 131.631 143.118 1.00 25.84  ? 456  LYS B C     1 
ATOM   10934 O  O     . LYS B 2 456 ? 131.738 131.220 141.955 1.00 38.30  ? 456  LYS B O     1 
ATOM   10935 C  CB    . LYS B 2 456 ? 132.352 130.466 145.279 1.00 10.72  ? 456  LYS B CB    1 
ATOM   10936 C  CG    . LYS B 2 456 ? 131.577 129.208 144.954 1.00 12.08  ? 456  LYS B CG    1 
ATOM   10937 C  CD    . LYS B 2 456 ? 131.137 128.486 146.214 1.00 14.49  ? 456  LYS B CD    1 
ATOM   10938 C  CE    . LYS B 2 456 ? 130.254 127.301 145.878 1.00 24.57  ? 456  LYS B CE    1 
ATOM   10939 N  NZ    . LYS B 2 456 ? 129.876 126.521 147.082 1.00 22.69  ? 456  LYS B NZ    1 
ATOM   10940 N  N     . CYS B 2 457 ? 130.882 132.482 143.599 1.00 19.57  ? 457  CYS B N     1 
ATOM   10941 C  CA    . CYS B 2 457 ? 129.730 132.886 142.808 1.00 7.35   ? 457  CYS B CA    1 
ATOM   10942 C  C     . CYS B 2 457 ? 130.089 134.053 141.896 1.00 19.39  ? 457  CYS B C     1 
ATOM   10943 O  O     . CYS B 2 457 ? 130.969 134.861 142.203 1.00 32.50  ? 457  CYS B O     1 
ATOM   10944 C  CB    . CYS B 2 457 ? 128.548 133.253 143.706 1.00 0.00   ? 457  CYS B CB    1 
ATOM   10945 S  SG    . CYS B 2 457 ? 128.639 134.869 144.477 1.00 10.50  ? 457  CYS B SG    1 
ATOM   10946 N  N     . THR B 2 458 ? 129.399 134.123 140.756 1.00 21.81  ? 458  THR B N     1 
ATOM   10947 C  CA    . THR B 2 458 ? 129.752 135.103 139.735 1.00 17.17  ? 458  THR B CA    1 
ATOM   10948 C  C     . THR B 2 458 ? 129.446 136.524 140.188 1.00 19.07  ? 458  THR B C     1 
ATOM   10949 O  O     . THR B 2 458 ? 130.222 137.446 139.912 1.00 24.24  ? 458  THR B O     1 
ATOM   10950 C  CB    . THR B 2 458 ? 129.022 134.796 138.428 1.00 14.56  ? 458  THR B CB    1 
ATOM   10951 O  OG1   . THR B 2 458 ? 127.620 134.654 138.680 1.00 13.17  ? 458  THR B OG1   1 
ATOM   10952 C  CG2   . THR B 2 458 ? 129.555 133.517 137.811 1.00 24.90  ? 458  THR B CG2   1 
ATOM   10953 N  N     . PHE B 2 459 ? 128.327 136.719 140.889 1.00 24.03  ? 459  PHE B N     1 
ATOM   10954 C  CA    . PHE B 2 459 ? 127.908 138.070 141.249 1.00 20.04  ? 459  PHE B CA    1 
ATOM   10955 C  C     . PHE B 2 459 ? 128.923 138.744 142.163 1.00 12.68  ? 459  PHE B C     1 
ATOM   10956 O  O     . PHE B 2 459 ? 129.403 139.835 141.856 1.00 19.48  ? 459  PHE B O     1 
ATOM   10957 C  CB    . PHE B 2 459 ? 126.521 138.047 141.889 1.00 20.49  ? 459  PHE B CB    1 
ATOM   10958 C  CG    . PHE B 2 459 ? 125.403 138.279 140.911 1.00 18.49  ? 459  PHE B CG    1 
ATOM   10959 C  CD1   . PHE B 2 459 ? 125.162 139.543 140.407 1.00 16.20  ? 459  PHE B CD1   1 
ATOM   10960 C  CD2   . PHE B 2 459 ? 124.598 137.235 140.494 1.00 18.28  ? 459  PHE B CD2   1 
ATOM   10961 C  CE1   . PHE B 2 459 ? 124.139 139.762 139.510 1.00 19.37  ? 459  PHE B CE1   1 
ATOM   10962 C  CE2   . PHE B 2 459 ? 123.572 137.448 139.599 1.00 15.06  ? 459  PHE B CE2   1 
ATOM   10963 C  CZ    . PHE B 2 459 ? 123.343 138.713 139.106 1.00 19.49  ? 459  PHE B CZ    1 
ATOM   10964 N  N     . CYS B 2 460 ? 129.304 138.094 143.262 1.00 14.02  ? 460  CYS B N     1 
ATOM   10965 C  CA    . CYS B 2 460 ? 130.313 138.687 144.135 1.00 10.00  ? 460  CYS B CA    1 
ATOM   10966 C  C     . CYS B 2 460 ? 131.625 138.886 143.385 1.00 12.77  ? 460  CYS B C     1 
ATOM   10967 O  O     . CYS B 2 460 ? 132.058 140.022 143.166 1.00 25.74  ? 460  CYS B O     1 
ATOM   10968 C  CB    . CYS B 2 460 ? 130.522 137.822 145.378 1.00 16.21  ? 460  CYS B CB    1 
ATOM   10969 S  SG    . CYS B 2 460 ? 131.666 138.528 146.590 1.00 14.42  ? 460  CYS B SG    1 
ATOM   10970 N  N     . ARG B 2 461 ? 132.209 137.785 142.899 1.00 7.34   ? 461  ARG B N     1 
ATOM   10971 C  CA    . ARG B 2 461 ? 133.538 137.797 142.289 1.00 8.54   ? 461  ARG B CA    1 
ATOM   10972 C  C     . ARG B 2 461 ? 133.670 138.848 141.192 1.00 20.32  ? 461  ARG B C     1 
ATOM   10973 O  O     . ARG B 2 461 ? 134.683 139.551 141.113 1.00 17.50  ? 461  ARG B O     1 
ATOM   10974 C  CB    . ARG B 2 461 ? 133.846 136.404 141.731 1.00 12.83  ? 461  ARG B CB    1 
ATOM   10975 C  CG    . ARG B 2 461 ? 135.165 136.287 140.998 1.00 17.50  ? 461  ARG B CG    1 
ATOM   10976 C  CD    . ARG B 2 461 ? 135.430 134.857 140.534 1.00 13.74  ? 461  ARG B CD    1 
ATOM   10977 N  NE    . ARG B 2 461 ? 134.733 134.518 139.299 1.00 18.16  ? 461  ARG B NE    1 
ATOM   10978 C  CZ    . ARG B 2 461 ? 133.685 133.710 139.225 1.00 14.96  ? 461  ARG B CZ    1 
ATOM   10979 N  NH1   . ARG B 2 461 ? 133.179 133.135 140.302 1.00 14.03  ? 461  ARG B NH1   1 
ATOM   10980 N  NH2   . ARG B 2 461 ? 133.136 133.468 138.040 1.00 25.01  ? 461  ARG B NH2   1 
ATOM   10981 N  N     . LEU B 2 462 ? 132.649 138.988 140.350 1.00 25.07  ? 462  LEU B N     1 
ATOM   10982 C  CA    . LEU B 2 462 ? 132.717 139.870 139.193 1.00 12.77  ? 462  LEU B CA    1 
ATOM   10983 C  C     . LEU B 2 462 ? 132.102 141.240 139.449 1.00 21.19  ? 462  LEU B C     1 
ATOM   10984 O  O     . LEU B 2 462 ? 132.733 142.260 139.162 1.00 28.86  ? 462  LEU B O     1 
ATOM   10985 C  CB    . LEU B 2 462 ? 132.033 139.195 137.999 1.00 15.29  ? 462  LEU B CB    1 
ATOM   10986 C  CG    . LEU B 2 462 ? 132.695 137.889 137.557 1.00 11.10  ? 462  LEU B CG    1 
ATOM   10987 C  CD1   . LEU B 2 462 ? 131.800 137.114 136.616 1.00 18.62  ? 462  LEU B CD1   1 
ATOM   10988 C  CD2   . LEU B 2 462 ? 134.034 138.174 136.904 1.00 15.91  ? 462  LEU B CD2   1 
ATOM   10989 N  N     . GLY B 2 463 ? 130.870 141.287 139.959 1.00 22.24  ? 463  GLY B N     1 
ATOM   10990 C  CA    . GLY B 2 463 ? 130.217 142.554 140.207 1.00 25.80  ? 463  GLY B CA    1 
ATOM   10991 C  C     . GLY B 2 463 ? 130.875 143.392 141.282 1.00 20.66  ? 463  GLY B C     1 
ATOM   10992 O  O     . GLY B 2 463 ? 130.824 144.617 141.213 1.00 30.10  ? 463  GLY B O     1 
ATOM   10993 N  N     . THR B 2 464 ? 131.488 142.765 142.294 1.00 17.11  ? 464  THR B N     1 
ATOM   10994 C  CA    . THR B 2 464 ? 132.206 143.554 143.286 1.00 24.78  ? 464  THR B CA    1 
ATOM   10995 C  C     . THR B 2 464 ? 133.423 144.226 142.665 1.00 31.53  ? 464  THR B C     1 
ATOM   10996 O  O     . THR B 2 464 ? 133.706 145.397 142.943 1.00 32.99  ? 464  THR B O     1 
ATOM   10997 C  CB    . THR B 2 464 ? 132.610 142.669 144.465 1.00 26.15  ? 464  THR B CB    1 
ATOM   10998 O  OG1   . THR B 2 464 ? 131.568 141.723 144.725 1.00 24.71  ? 464  THR B OG1   1 
ATOM   10999 C  CG2   . THR B 2 464 ? 132.805 143.507 145.705 1.00 29.83  ? 464  THR B CG2   1 
ATOM   11000 N  N     . LYS B 2 465 ? 134.136 143.505 141.796 1.00 22.70  ? 465  LYS B N     1 
ATOM   11001 C  CA    . LYS B 2 465 ? 135.254 144.099 141.072 1.00 19.17  ? 465  LYS B CA    1 
ATOM   11002 C  C     . LYS B 2 465 ? 134.781 145.203 140.133 1.00 29.75  ? 465  LYS B C     1 
ATOM   11003 O  O     . LYS B 2 465 ? 135.442 146.237 140.001 1.00 39.43  ? 465  LYS B O     1 
ATOM   11004 C  CB    . LYS B 2 465 ? 136.002 143.016 140.298 1.00 17.40  ? 465  LYS B CB    1 
ATOM   11005 C  CG    . LYS B 2 465 ? 137.416 143.383 139.895 1.00 14.12  ? 465  LYS B CG    1 
ATOM   11006 C  CD    . LYS B 2 465 ? 138.293 143.594 141.110 1.00 22.60  ? 465  LYS B CD    1 
ATOM   11007 C  CE    . LYS B 2 465 ? 139.757 143.425 140.758 1.00 28.76  ? 465  LYS B CE    1 
ATOM   11008 N  NZ    . LYS B 2 465 ? 140.139 144.242 139.582 1.00 29.13  ? 465  LYS B NZ    1 
ATOM   11009 N  N     . ARG B 2 466 ? 133.636 145.003 139.475 1.00 24.48  ? 466  ARG B N     1 
ATOM   11010 C  CA    . ARG B 2 466 ? 133.103 146.037 138.589 1.00 20.19  ? 466  ARG B CA    1 
ATOM   11011 C  C     . ARG B 2 466 ? 132.665 147.274 139.368 1.00 20.56  ? 466  ARG B C     1 
ATOM   11012 O  O     . ARG B 2 466 ? 132.904 148.405 138.931 1.00 29.17  ? 466  ARG B O     1 
ATOM   11013 C  CB    . ARG B 2 466 ? 131.945 145.480 137.762 1.00 19.68  ? 466  ARG B CB    1 
ATOM   11014 C  CG    . ARG B 2 466 ? 132.344 144.364 136.811 1.00 21.54  ? 466  ARG B CG    1 
ATOM   11015 C  CD    . ARG B 2 466 ? 133.663 144.660 136.131 1.00 30.06  ? 466  ARG B CD    1 
ATOM   11016 N  NE    . ARG B 2 466 ? 134.173 143.508 135.400 1.00 26.79  ? 466  ARG B NE    1 
ATOM   11017 C  CZ    . ARG B 2 466 ? 135.459 143.271 135.190 1.00 23.55  ? 466  ARG B CZ    1 
ATOM   11018 N  NH1   . ARG B 2 466 ? 136.394 144.077 135.663 1.00 11.53  ? 466  ARG B NH1   1 
ATOM   11019 N  NH2   . ARG B 2 466 ? 135.817 142.196 134.496 1.00 26.96  ? 466  ARG B NH2   1 
ATOM   11020 N  N     . MET B 2 467 ? 132.027 147.081 140.524 1.00 23.31  ? 467  MET B N     1 
ATOM   11021 C  CA    . MET B 2 467 ? 131.654 148.207 141.373 1.00 27.74  ? 467  MET B CA    1 
ATOM   11022 C  C     . MET B 2 467 ? 132.885 148.955 141.863 1.00 22.30  ? 467  MET B C     1 
ATOM   11023 O  O     . MET B 2 467 ? 132.893 150.190 141.912 1.00 23.95  ? 467  MET B O     1 
ATOM   11024 C  CB    . MET B 2 467 ? 130.817 147.723 142.557 1.00 29.18  ? 467  MET B CB    1 
ATOM   11025 C  CG    . MET B 2 467 ? 129.403 147.313 142.199 1.00 26.88  ? 467  MET B CG    1 
ATOM   11026 S  SD    . MET B 2 467 ? 128.420 146.814 143.621 1.00 43.88  ? 467  MET B SD    1 
ATOM   11027 C  CE    . MET B 2 467 ? 128.317 148.363 144.506 1.00 21.92  ? 467  MET B CE    1 
ATOM   11028 N  N     . TRP B 2 468 ? 133.938 148.222 142.231 1.00 9.22   ? 468  TRP B N     1 
ATOM   11029 C  CA    . TRP B 2 468 ? 135.168 148.873 142.664 1.00 19.98  ? 468  TRP B CA    1 
ATOM   11030 C  C     . TRP B 2 468 ? 135.828 149.637 141.520 1.00 34.06  ? 468  TRP B C     1 
ATOM   11031 O  O     . TRP B 2 468 ? 136.384 150.721 141.731 1.00 49.34  ? 468  TRP B O     1 
ATOM   11032 C  CB    . TRP B 2 468 ? 136.127 147.842 143.252 1.00 23.54  ? 468  TRP B CB    1 
ATOM   11033 C  CG    . TRP B 2 468 ? 137.399 148.445 143.723 1.00 27.30  ? 468  TRP B CG    1 
ATOM   11034 C  CD1   . TRP B 2 468 ? 137.626 149.040 144.925 1.00 26.61  ? 468  TRP B CD1   1 
ATOM   11035 C  CD2   . TRP B 2 468 ? 138.626 148.528 142.994 1.00 29.50  ? 468  TRP B CD2   1 
ATOM   11036 N  NE1   . TRP B 2 468 ? 138.922 149.486 144.994 1.00 34.03  ? 468  TRP B NE1   1 
ATOM   11037 C  CE2   . TRP B 2 468 ? 139.557 149.183 143.818 1.00 33.80  ? 468  TRP B CE2   1 
ATOM   11038 C  CE3   . TRP B 2 468 ? 139.028 148.111 141.722 1.00 28.04  ? 468  TRP B CE3   1 
ATOM   11039 C  CZ2   . TRP B 2 468 ? 140.863 149.431 143.415 1.00 35.04  ? 468  TRP B CZ2   1 
ATOM   11040 C  CZ3   . TRP B 2 468 ? 140.322 148.358 141.324 1.00 30.97  ? 468  TRP B CZ3   1 
ATOM   11041 C  CH2   . TRP B 2 468 ? 141.226 149.011 142.167 1.00 36.12  ? 468  TRP B CH2   1 
ATOM   11042 N  N     . GLU B 2 469 ? 135.787 149.085 140.305 1.00 28.87  ? 469  GLU B N     1 
ATOM   11043 C  CA    . GLU B 2 469 ? 136.311 149.803 139.147 1.00 26.55  ? 469  GLU B CA    1 
ATOM   11044 C  C     . GLU B 2 469 ? 135.527 151.083 138.893 1.00 31.75  ? 469  GLU B C     1 
ATOM   11045 O  O     . GLU B 2 469 ? 136.110 152.127 138.583 1.00 33.01  ? 469  GLU B O     1 
ATOM   11046 C  CB    . GLU B 2 469 ? 136.279 148.906 137.909 1.00 30.91  ? 469  GLU B CB    1 
ATOM   11047 C  CG    . GLU B 2 469 ? 137.307 147.789 137.911 1.00 33.62  ? 469  GLU B CG    1 
ATOM   11048 C  CD    . GLU B 2 469 ? 138.727 148.297 137.758 1.00 38.72  ? 469  GLU B CD    1 
ATOM   11049 O  OE1   . GLU B 2 469 ? 138.911 149.411 137.224 1.00 42.61  ? 469  GLU B OE1   1 
ATOM   11050 O  OE2   . GLU B 2 469 ? 139.662 147.580 138.173 1.00 32.92  ? 469  GLU B OE2   1 
ATOM   11051 N  N     . LEU B 2 470 ? 134.200 151.020 139.021 1.00 29.83  ? 470  LEU B N     1 
ATOM   11052 C  CA    . LEU B 2 470 ? 133.381 152.217 138.860 1.00 27.79  ? 470  LEU B CA    1 
ATOM   11053 C  C     . LEU B 2 470 ? 133.705 153.256 139.927 1.00 38.75  ? 470  LEU B C     1 
ATOM   11054 O  O     . LEU B 2 470 ? 133.769 154.457 139.638 1.00 43.86  ? 470  LEU B O     1 
ATOM   11055 C  CB    . LEU B 2 470 ? 131.900 151.844 138.901 1.00 30.01  ? 470  LEU B CB    1 
ATOM   11056 C  CG    . LEU B 2 470 ? 131.382 151.015 137.726 1.00 28.83  ? 470  LEU B CG    1 
ATOM   11057 C  CD1   . LEU B 2 470 ? 130.022 150.426 138.042 1.00 32.60  ? 470  LEU B CD1   1 
ATOM   11058 C  CD2   . LEU B 2 470 ? 131.314 151.860 136.470 1.00 36.07  ? 470  LEU B CD2   1 
ATOM   11059 N  N     . LEU B 2 471 ? 133.916 152.813 141.167 1.00 33.75  ? 471  LEU B N     1 
ATOM   11060 C  CA    . LEU B 2 471 ? 134.229 153.749 142.243 1.00 31.76  ? 471  LEU B CA    1 
ATOM   11061 C  C     . LEU B 2 471 ? 135.603 154.382 142.057 1.00 33.91  ? 471  LEU B C     1 
ATOM   11062 O  O     . LEU B 2 471 ? 135.792 155.561 142.371 1.00 44.77  ? 471  LEU B O     1 
ATOM   11063 C  CB    . LEU B 2 471 ? 134.140 153.048 143.594 1.00 37.54  ? 471  LEU B CB    1 
ATOM   11064 C  CG    . LEU B 2 471 ? 132.730 152.927 144.161 1.00 37.29  ? 471  LEU B CG    1 
ATOM   11065 C  CD1   . LEU B 2 471 ? 132.773 152.227 145.501 1.00 34.49  ? 471  LEU B CD1   1 
ATOM   11066 C  CD2   . LEU B 2 471 ? 132.105 154.301 144.290 1.00 35.19  ? 471  LEU B CD2   1 
ATOM   11067 N  N     . ASP B 2 472 ? 136.576 153.614 141.564 1.00 24.33  ? 472  ASP B N     1 
ATOM   11068 C  CA    . ASP B 2 472 ? 137.887 154.189 141.281 1.00 34.16  ? 472  ASP B CA    1 
ATOM   11069 C  C     . ASP B 2 472 ? 137.838 155.119 140.074 1.00 43.56  ? 472  ASP B C     1 
ATOM   11070 O  O     . ASP B 2 472 ? 138.605 156.086 140.007 1.00 45.17  ? 472  ASP B O     1 
ATOM   11071 C  CB    . ASP B 2 472 ? 138.914 153.078 141.061 1.00 42.99  ? 472  ASP B CB    1 
ATOM   11072 C  CG    . ASP B 2 472 ? 140.345 153.572 141.174 1.00 42.26  ? 472  ASP B CG    1 
ATOM   11073 O  OD1   . ASP B 2 472 ? 140.742 154.003 142.275 1.00 41.72  ? 472  ASP B OD1   1 
ATOM   11074 O  OD2   . ASP B 2 472 ? 141.076 153.521 140.165 1.00 44.65  ? 472  ASP B OD2   1 
ATOM   11075 N  N     . LYS B 2 473 ? 136.959 154.836 139.111 1.00 46.86  ? 473  LYS B N     1 
ATOM   11076 C  CA    . LYS B 2 473 ? 136.752 155.751 137.993 1.00 43.15  ? 473  LYS B CA    1 
ATOM   11077 C  C     . LYS B 2 473 ? 136.147 157.069 138.462 1.00 41.84  ? 473  LYS B C     1 
ATOM   11078 O  O     . LYS B 2 473 ? 136.564 158.144 138.014 1.00 50.21  ? 473  LYS B O     1 
ATOM   11079 C  CB    . LYS B 2 473 ? 135.859 155.092 136.943 1.00 40.79  ? 473  LYS B CB    1 
ATOM   11080 C  CG    . LYS B 2 473 ? 135.497 155.987 135.778 1.00 44.29  ? 473  LYS B CG    1 
ATOM   11081 C  CD    . LYS B 2 473 ? 134.520 155.307 134.838 1.00 42.42  ? 473  LYS B CD    1 
ATOM   11082 C  CE    . LYS B 2 473 ? 135.165 154.148 134.107 1.00 48.67  ? 473  LYS B CE    1 
ATOM   11083 N  NZ    . LYS B 2 473 ? 136.258 154.607 133.211 1.00 49.53  ? 473  LYS B NZ    1 
ATOM   11084 N  N     . ILE B 2 474 ? 135.162 157.005 139.358 1.00 37.33  ? 474  ILE B N     1 
ATOM   11085 C  CA    . ILE B 2 474 ? 134.557 158.223 139.889 1.00 40.56  ? 474  ILE B CA    1 
ATOM   11086 C  C     . ILE B 2 474 ? 135.556 158.995 140.746 1.00 39.72  ? 474  ILE B C     1 
ATOM   11087 O  O     . ILE B 2 474 ? 135.651 160.224 140.654 1.00 47.97  ? 474  ILE B O     1 
ATOM   11088 C  CB    . ILE B 2 474 ? 133.276 157.888 140.675 1.00 40.46  ? 474  ILE B CB    1 
ATOM   11089 C  CG1   . ILE B 2 474 ? 132.229 157.265 139.755 1.00 43.22  ? 474  ILE B CG1   1 
ATOM   11090 C  CG2   . ILE B 2 474 ? 132.706 159.132 141.330 1.00 37.52  ? 474  ILE B CG2   1 
ATOM   11091 C  CD1   . ILE B 2 474 ? 130.980 156.831 140.473 1.00 43.68  ? 474  ILE B CD1   1 
ATOM   11092 N  N     . THR B 2 475 ? 136.314 158.289 141.589 1.00 35.06  ? 475  THR B N     1 
ATOM   11093 C  CA    . THR B 2 475 ? 137.217 158.955 142.525 1.00 38.58  ? 475  THR B CA    1 
ATOM   11094 C  C     . THR B 2 475 ? 138.329 159.706 141.804 1.00 44.18  ? 475  THR B C     1 
ATOM   11095 O  O     . THR B 2 475 ? 138.704 160.807 142.225 1.00 54.58  ? 475  THR B O     1 
ATOM   11096 C  CB    . THR B 2 475 ? 137.797 157.933 143.505 1.00 43.04  ? 475  THR B CB    1 
ATOM   11097 O  OG1   . THR B 2 475 ? 136.733 157.343 144.262 1.00 40.69  ? 475  THR B OG1   1 
ATOM   11098 C  CG2   . THR B 2 475 ? 138.773 158.590 144.466 1.00 45.61  ? 475  THR B CG2   1 
ATOM   11099 N  N     . LYS B 2 476 ? 138.852 159.152 140.713 1.00 46.85  ? 476  LYS B N     1 
ATOM   11100 C  CA    . LYS B 2 476 ? 139.855 159.856 139.925 1.00 49.58  ? 476  LYS B CA    1 
ATOM   11101 C  C     . LYS B 2 476 ? 139.262 160.952 139.049 1.00 51.17  ? 476  LYS B C     1 
ATOM   11102 O  O     . LYS B 2 476 ? 140.010 161.607 138.315 1.00 50.45  ? 476  LYS B O     1 
ATOM   11103 C  CB    . LYS B 2 476 ? 140.639 158.867 139.061 1.00 50.01  ? 476  LYS B CB    1 
ATOM   11104 C  CG    . LYS B 2 476 ? 141.571 157.967 139.851 1.00 51.95  ? 476  LYS B CG    1 
ATOM   11105 C  CD    . LYS B 2 476 ? 142.337 157.029 138.936 1.00 53.07  ? 476  LYS B CD    1 
ATOM   11106 C  CE    . LYS B 2 476 ? 141.393 156.155 138.126 1.00 51.66  ? 476  LYS B CE    1 
ATOM   11107 N  NZ    . LYS B 2 476 ? 142.129 155.231 137.221 1.00 46.25  ? 476  LYS B NZ    1 
ATOM   11108 N  N     . GLY B 2 477 ? 137.950 161.168 139.107 1.00 49.41  ? 477  GLY B N     1 
ATOM   11109 C  CA    . GLY B 2 477 ? 137.316 162.224 138.350 1.00 46.84  ? 477  GLY B CA    1 
ATOM   11110 C  C     . GLY B 2 477 ? 136.997 161.884 136.915 1.00 53.72  ? 477  GLY B C     1 
ATOM   11111 O  O     . GLY B 2 477 ? 136.567 162.769 136.168 1.00 56.00  ? 477  GLY B O     1 
ATOM   11112 N  N     . GLU B 2 478 ? 137.192 160.633 136.503 1.00 48.89  ? 478  GLU B N     1 
ATOM   11113 C  CA    . GLU B 2 478 ? 136.924 160.211 135.135 1.00 43.47  ? 478  GLU B CA    1 
ATOM   11114 C  C     . GLU B 2 478 ? 135.527 159.630 134.966 1.00 46.55  ? 478  GLU B C     1 
ATOM   11115 O  O     . GLU B 2 478 ? 135.309 158.793 134.081 1.00 53.58  ? 478  GLU B O     1 
ATOM   11116 C  CB    . GLU B 2 478 ? 137.984 159.204 134.689 1.00 42.32  ? 478  GLU B CB    1 
ATOM   11117 C  CG    . GLU B 2 478 ? 139.402 159.704 134.884 1.00 45.80  ? 478  GLU B CG    1 
ATOM   11118 C  CD    . GLU B 2 478 ? 140.442 158.688 134.472 1.00 50.10  ? 478  GLU B CD    1 
ATOM   11119 O  OE1   . GLU B 2 478 ? 140.059 157.614 133.964 1.00 53.22  ? 478  GLU B OE1   1 
ATOM   11120 O  OE2   . GLU B 2 478 ? 141.646 158.963 134.656 1.00 48.70  ? 478  GLU B OE2   1 
ATOM   11121 N  N     . GLY B 2 479 ? 134.571 160.056 135.792 1.00 46.99  ? 479  GLY B N     1 
ATOM   11122 C  CA    . GLY B 2 479 ? 133.233 159.514 135.768 1.00 45.61  ? 479  GLY B CA    1 
ATOM   11123 C  C     . GLY B 2 479 ? 132.224 160.428 135.087 1.00 46.89  ? 479  GLY B C     1 
ATOM   11124 O  O     . GLY B 2 479 ? 132.530 161.520 134.617 1.00 49.12  ? 479  GLY B O     1 
ATOM   11125 N  N     . ALA B 2 480 ? 130.986 159.943 135.046 1.00 53.83  ? 480  ALA B N     1 
ATOM   11126 C  CA    . ALA B 2 480 ? 129.867 160.672 134.466 1.00 53.53  ? 480  ALA B CA    1 
ATOM   11127 C  C     . ALA B 2 480 ? 128.584 160.151 135.104 1.00 53.63  ? 480  ALA B C     1 
ATOM   11128 O  O     . ALA B 2 480 ? 128.611 159.253 135.949 1.00 57.28  ? 480  ALA B O     1 
ATOM   11129 C  CB    . ALA B 2 480 ? 129.843 160.526 132.943 1.00 54.63  ? 480  ALA B CB    1 
ATOM   11130 N  N     . LEU B 2 481 ? 127.451 160.727 134.694 1.00 53.29  ? 481  LEU B N     1 
ATOM   11131 C  CA    . LEU B 2 481 ? 126.159 160.266 135.193 1.00 54.13  ? 481  LEU B CA    1 
ATOM   11132 C  C     . LEU B 2 481 ? 125.850 158.839 134.761 1.00 55.17  ? 481  LEU B C     1 
ATOM   11133 O  O     . LEU B 2 481 ? 125.083 158.148 135.443 1.00 50.26  ? 481  LEU B O     1 
ATOM   11134 C  CB    . LEU B 2 481 ? 125.040 161.200 134.727 1.00 52.71  ? 481  LEU B CB    1 
ATOM   11135 C  CG    . LEU B 2 481 ? 124.802 162.497 135.506 1.00 57.20  ? 481  LEU B CG    1 
ATOM   11136 C  CD1   . LEU B 2 481 ? 125.884 163.530 135.238 1.00 56.82  ? 481  LEU B CD1   1 
ATOM   11137 C  CD2   . LEU B 2 481 ? 123.432 163.063 135.177 1.00 56.98  ? 481  LEU B CD2   1 
ATOM   11138 N  N     . GLU B 2 482 ? 126.431 158.384 133.650 1.00 54.80  ? 482  GLU B N     1 
ATOM   11139 C  CA    . GLU B 2 482 ? 126.245 157.002 133.225 1.00 52.09  ? 482  GLU B CA    1 
ATOM   11140 C  C     . GLU B 2 482 ? 126.863 156.028 134.220 1.00 55.65  ? 482  GLU B C     1 
ATOM   11141 O  O     . GLU B 2 482 ? 126.303 154.958 134.472 1.00 59.06  ? 482  GLU B O     1 
ATOM   11142 C  CB    . GLU B 2 482 ? 126.841 156.800 131.833 1.00 55.86  ? 482  GLU B CB    1 
ATOM   11143 C  CG    . GLU B 2 482 ? 126.419 157.855 130.828 1.00 55.60  ? 482  GLU B CG    1 
ATOM   11144 C  CD    . GLU B 2 482 ? 124.918 157.905 130.627 1.00 59.04  ? 482  GLU B CD    1 
ATOM   11145 O  OE1   . GLU B 2 482 ? 124.275 156.834 130.646 1.00 56.49  ? 482  GLU B OE1   1 
ATOM   11146 O  OE2   . GLU B 2 482 ? 124.379 159.017 130.453 1.00 60.82  ? 482  GLU B OE2   1 
ATOM   11147 N  N     . ASP B 2 483 ? 128.023 156.374 134.785 1.00 52.29  ? 483  ASP B N     1 
ATOM   11148 C  CA    . ASP B 2 483 ? 128.644 155.515 135.789 1.00 49.82  ? 483  ASP B CA    1 
ATOM   11149 C  C     . ASP B 2 483 ? 127.796 155.433 137.050 1.00 45.49  ? 483  ASP B C     1 
ATOM   11150 O  O     . ASP B 2 483 ? 127.663 154.359 137.649 1.00 48.94  ? 483  ASP B O     1 
ATOM   11151 C  CB    . ASP B 2 483 ? 130.047 156.020 136.116 1.00 49.25  ? 483  ASP B CB    1 
ATOM   11152 C  CG    . ASP B 2 483 ? 130.978 155.943 134.929 1.00 52.70  ? 483  ASP B CG    1 
ATOM   11153 O  OD1   . ASP B 2 483 ? 130.947 154.921 134.214 1.00 53.42  ? 483  ASP B OD1   1 
ATOM   11154 O  OD2   . ASP B 2 483 ? 131.731 156.909 134.702 1.00 50.67  ? 483  ASP B OD2   1 
ATOM   11155 N  N     . ILE B 2 484 ? 127.214 156.558 137.468 1.00 43.78  ? 484  ILE B N     1 
ATOM   11156 C  CA    . ILE B 2 484 ? 126.313 156.553 138.616 1.00 45.18  ? 484  ILE B CA    1 
ATOM   11157 C  C     . ILE B 2 484 ? 125.085 155.699 138.321 1.00 45.86  ? 484  ILE B C     1 
ATOM   11158 O  O     . ILE B 2 484 ? 124.608 154.954 139.185 1.00 45.13  ? 484  ILE B O     1 
ATOM   11159 C  CB    . ILE B 2 484 ? 125.938 157.997 139.009 1.00 45.25  ? 484  ILE B CB    1 
ATOM   11160 C  CG1   . ILE B 2 484 ? 126.997 158.606 139.931 1.00 47.59  ? 484  ILE B CG1   1 
ATOM   11161 C  CG2   . ILE B 2 484 ? 124.581 158.054 139.691 1.00 42.31  ? 484  ILE B CG2   1 
ATOM   11162 C  CD1   . ILE B 2 484 ? 128.260 159.046 139.236 1.00 44.32  ? 484  ILE B CD1   1 
ATOM   11163 N  N     . GLU B 2 485 ? 124.560 155.786 137.095 1.00 48.84  ? 485  GLU B N     1 
ATOM   11164 C  CA    . GLU B 2 485 ? 123.425 154.949 136.713 1.00 53.54  ? 485  GLU B CA    1 
ATOM   11165 C  C     . GLU B 2 485 ? 123.794 153.470 136.742 1.00 50.55  ? 485  GLU B C     1 
ATOM   11166 O  O     . GLU B 2 485 ? 123.007 152.631 137.201 1.00 47.42  ? 485  GLU B O     1 
ATOM   11167 C  CB    . GLU B 2 485 ? 122.925 155.350 135.327 1.00 48.08  ? 485  GLU B CB    1 
ATOM   11168 C  CG    . GLU B 2 485 ? 121.495 155.854 135.296 1.00 45.09  ? 485  GLU B CG    1 
ATOM   11169 C  CD    . GLU B 2 485 ? 121.328 157.193 135.986 1.00 51.42  ? 485  GLU B CD    1 
ATOM   11170 O  OE1   . GLU B 2 485 ? 122.327 157.929 136.121 1.00 55.91  ? 485  GLU B OE1   1 
ATOM   11171 O  OE2   . GLU B 2 485 ? 120.192 157.512 136.394 1.00 53.34  ? 485  GLU B OE2   1 
ATOM   11172 N  N     . LYS B 2 486 ? 124.991 153.133 136.258 1.00 40.38  ? 486  LYS B N     1 
ATOM   11173 C  CA    . LYS B 2 486 ? 125.447 151.749 136.295 1.00 35.27  ? 486  LYS B CA    1 
ATOM   11174 C  C     . LYS B 2 486 ? 125.600 151.258 137.727 1.00 35.58  ? 486  LYS B C     1 
ATOM   11175 O  O     . LYS B 2 486 ? 125.282 150.106 138.027 1.00 29.97  ? 486  LYS B O     1 
ATOM   11176 C  CB    . LYS B 2 486 ? 126.763 151.602 135.533 1.00 33.49  ? 486  LYS B CB    1 
ATOM   11177 C  CG    . LYS B 2 486 ? 126.626 151.785 134.036 1.00 36.72  ? 486  LYS B CG    1 
ATOM   11178 C  CD    . LYS B 2 486 ? 127.950 151.584 133.322 1.00 34.10  ? 486  LYS B CD    1 
ATOM   11179 C  CE    . LYS B 2 486 ? 128.390 150.139 133.378 1.00 37.36  ? 486  LYS B CE    1 
ATOM   11180 N  NZ    . LYS B 2 486 ? 129.625 149.917 132.584 1.00 33.49  ? 486  LYS B NZ    1 
ATOM   11181 N  N     . LEU B 2 487 ? 126.091 152.115 138.625 1.00 40.03  ? 487  LEU B N     1 
ATOM   11182 C  CA    . LEU B 2 487 ? 126.188 151.736 140.033 1.00 26.52  ? 487  LEU B CA    1 
ATOM   11183 C  C     . LEU B 2 487 ? 124.813 151.524 140.654 1.00 29.44  ? 487  LEU B C     1 
ATOM   11184 O  O     . LEU B 2 487 ? 124.595 150.545 141.378 1.00 36.25  ? 487  LEU B O     1 
ATOM   11185 C  CB    . LEU B 2 487 ? 126.963 152.795 140.813 1.00 26.28  ? 487  LEU B CB    1 
ATOM   11186 C  CG    . LEU B 2 487 ? 128.479 152.631 140.852 1.00 27.53  ? 487  LEU B CG    1 
ATOM   11187 C  CD1   . LEU B 2 487 ? 129.113 153.793 141.588 1.00 29.20  ? 487  LEU B CD1   1 
ATOM   11188 C  CD2   . LEU B 2 487 ? 128.838 151.315 141.514 1.00 33.25  ? 487  LEU B CD2   1 
ATOM   11189 N  N     . GLU B 2 488 ? 123.873 152.433 140.386 1.00 37.48  ? 488  GLU B N     1 
ATOM   11190 C  CA    . GLU B 2 488 ? 122.530 152.305 140.935 1.00 36.01  ? 488  GLU B CA    1 
ATOM   11191 C  C     . GLU B 2 488 ? 121.794 151.100 140.376 1.00 34.42  ? 488  GLU B C     1 
ATOM   11192 O  O     . GLU B 2 488 ? 120.873 150.597 141.025 1.00 40.22  ? 488  GLU B O     1 
ATOM   11193 C  CB    . GLU B 2 488 ? 121.717 153.571 140.670 1.00 36.93  ? 488  GLU B CB    1 
ATOM   11194 C  CG    . GLU B 2 488 ? 122.200 154.783 141.433 1.00 42.45  ? 488  GLU B CG    1 
ATOM   11195 C  CD    . GLU B 2 488 ? 121.317 155.987 141.216 1.00 48.36  ? 488  GLU B CD    1 
ATOM   11196 O  OE1   . GLU B 2 488 ? 120.323 155.865 140.472 1.00 44.24  ? 488  GLU B OE1   1 
ATOM   11197 O  OE2   . GLU B 2 488 ? 121.614 157.054 141.788 1.00 43.06  ? 488  GLU B OE2   1 
ATOM   11198 N  N     . LYS B 2 489 ? 122.162 150.641 139.182 1.00 29.10  ? 489  LYS B N     1 
ATOM   11199 C  CA    . LYS B 2 489 ? 121.617 149.384 138.688 1.00 27.66  ? 489  LYS B CA    1 
ATOM   11200 C  C     . LYS B 2 489 ? 122.326 148.189 139.316 1.00 30.03  ? 489  LYS B C     1 
ATOM   11201 O  O     . LYS B 2 489 ? 121.677 147.248 139.781 1.00 33.08  ? 489  LYS B O     1 
ATOM   11202 C  CB    . LYS B 2 489 ? 121.717 149.328 137.163 1.00 34.34  ? 489  LYS B CB    1 
ATOM   11203 C  CG    . LYS B 2 489 ? 121.174 148.046 136.557 1.00 28.72  ? 489  LYS B CG    1 
ATOM   11204 C  CD    . LYS B 2 489 ? 121.257 148.066 135.043 1.00 31.21  ? 489  LYS B CD    1 
ATOM   11205 C  CE    . LYS B 2 489 ? 122.690 148.212 134.578 1.00 30.20  ? 489  LYS B CE    1 
ATOM   11206 N  NZ    . LYS B 2 489 ? 123.549 147.116 135.099 1.00 31.91  ? 489  LYS B NZ    1 
ATOM   11207 N  N     . LEU B 2 490 ? 123.658 148.234 139.378 1.00 29.78  ? 490  LEU B N     1 
ATOM   11208 C  CA    . LEU B 2 490 ? 124.453 147.054 139.699 1.00 22.08  ? 490  LEU B CA    1 
ATOM   11209 C  C     . LEU B 2 490 ? 124.386 146.700 141.180 1.00 29.55  ? 490  LEU B C     1 
ATOM   11210 O  O     . LEU B 2 490 ? 124.330 145.517 141.532 1.00 31.71  ? 490  LEU B O     1 
ATOM   11211 C  CB    . LEU B 2 490 ? 125.900 147.286 139.262 1.00 16.98  ? 490  LEU B CB    1 
ATOM   11212 C  CG    . LEU B 2 490 ? 126.919 146.152 139.369 1.00 26.79  ? 490  LEU B CG    1 
ATOM   11213 C  CD1   . LEU B 2 490 ? 126.445 144.920 138.623 1.00 24.87  ? 490  LEU B CD1   1 
ATOM   11214 C  CD2   . LEU B 2 490 ? 128.256 146.616 138.828 1.00 21.72  ? 490  LEU B CD2   1 
ATOM   11215 N  N     . ALA B 2 491 ? 124.403 147.701 142.063 1.00 27.23  ? 491  ALA B N     1 
ATOM   11216 C  CA    . ALA B 2 491 ? 124.447 147.423 143.499 1.00 9.77   ? 491  ALA B CA    1 
ATOM   11217 C  C     . ALA B 2 491 ? 123.244 146.627 144.005 1.00 24.01  ? 491  ALA B C     1 
ATOM   11218 O  O     . ALA B 2 491 ? 123.453 145.653 144.753 1.00 20.57  ? 491  ALA B O     1 
ATOM   11219 C  CB    . ALA B 2 491 ? 124.628 148.739 144.264 1.00 23.09  ? 491  ALA B CB    1 
ATOM   11220 N  N     . PRO B 2 492 ? 121.990 146.958 143.661 1.00 29.04  ? 492  PRO B N     1 
ATOM   11221 C  CA    . PRO B 2 492 ? 120.885 146.060 144.041 1.00 23.88  ? 492  PRO B CA    1 
ATOM   11222 C  C     . PRO B 2 492 ? 121.018 144.668 143.455 1.00 28.34  ? 492  PRO B C     1 
ATOM   11223 O  O     . PRO B 2 492 ? 120.622 143.688 144.099 1.00 30.14  ? 492  PRO B O     1 
ATOM   11224 C  CB    . PRO B 2 492 ? 119.643 146.779 143.497 1.00 26.92  ? 492  PRO B CB    1 
ATOM   11225 C  CG    . PRO B 2 492 ? 120.038 148.191 143.389 1.00 27.68  ? 492  PRO B CG    1 
ATOM   11226 C  CD    . PRO B 2 492 ? 121.475 148.170 142.998 1.00 19.53  ? 492  PRO B CD    1 
ATOM   11227 N  N     . LEU B 2 493 ? 121.584 144.551 142.254 1.00 25.38  ? 493  LEU B N     1 
ATOM   11228 C  CA    . LEU B 2 493 ? 121.750 143.240 141.639 1.00 22.28  ? 493  LEU B CA    1 
ATOM   11229 C  C     . LEU B 2 493 ? 122.808 142.416 142.361 1.00 23.71  ? 493  LEU B C     1 
ATOM   11230 O  O     . LEU B 2 493 ? 122.640 141.206 142.538 1.00 36.82  ? 493  LEU B O     1 
ATOM   11231 C  CB    . LEU B 2 493 ? 122.099 143.401 140.162 1.00 24.51  ? 493  LEU B CB    1 
ATOM   11232 C  CG    . LEU B 2 493 ? 121.063 144.197 139.369 1.00 19.00  ? 493  LEU B CG    1 
ATOM   11233 C  CD1   . LEU B 2 493 ? 121.531 144.441 137.954 1.00 18.92  ? 493  LEU B CD1   1 
ATOM   11234 C  CD2   . LEU B 2 493 ? 119.716 143.509 139.374 1.00 26.26  ? 493  LEU B CD2   1 
ATOM   11235 N  N     . VAL B 2 494 ? 123.906 143.048 142.781 1.00 18.12  ? 494  VAL B N     1 
ATOM   11236 C  CA    . VAL B 2 494 ? 124.922 142.323 143.539 1.00 23.00  ? 494  VAL B CA    1 
ATOM   11237 C  C     . VAL B 2 494 ? 124.386 141.932 144.910 1.00 20.87  ? 494  VAL B C     1 
ATOM   11238 O  O     . VAL B 2 494 ? 124.713 140.857 145.428 1.00 16.57  ? 494  VAL B O     1 
ATOM   11239 C  CB    . VAL B 2 494 ? 126.216 143.153 143.638 1.00 24.30  ? 494  VAL B CB    1 
ATOM   11240 C  CG1   . VAL B 2 494 ? 127.261 142.436 144.479 1.00 5.29   ? 494  VAL B CG1   1 
ATOM   11241 C  CG2   . VAL B 2 494 ? 126.767 143.426 142.254 1.00 23.36  ? 494  VAL B CG2   1 
ATOM   11242 N  N     . LYS B 2 495 ? 123.558 142.784 145.520 1.00 25.37  ? 495  LYS B N     1 
ATOM   11243 C  CA    . LYS B 2 495 ? 122.943 142.419 146.793 1.00 24.64  ? 495  LYS B CA    1 
ATOM   11244 C  C     . LYS B 2 495 ? 121.989 141.238 146.639 1.00 25.21  ? 495  LYS B C     1 
ATOM   11245 O  O     . LYS B 2 495 ? 121.993 140.318 147.464 1.00 32.24  ? 495  LYS B O     1 
ATOM   11246 C  CB    . LYS B 2 495 ? 122.213 143.624 147.384 1.00 23.30  ? 495  LYS B CB    1 
ATOM   11247 C  CG    . LYS B 2 495 ? 121.238 143.274 148.489 1.00 23.63  ? 495  LYS B CG    1 
ATOM   11248 C  CD    . LYS B 2 495 ? 120.559 144.509 149.040 1.00 26.72  ? 495  LYS B CD    1 
ATOM   11249 C  CE    . LYS B 2 495 ? 121.508 145.314 149.895 1.00 26.51  ? 495  LYS B CE    1 
ATOM   11250 N  NZ    . LYS B 2 495 ? 121.933 144.553 151.098 1.00 28.94  ? 495  LYS B NZ    1 
ATOM   11251 N  N     . THR B 2 496 ? 121.166 141.243 145.591 1.00 25.73  ? 496  THR B N     1 
ATOM   11252 C  CA    . THR B 2 496 ? 120.156 140.202 145.445 1.00 30.17  ? 496  THR B CA    1 
ATOM   11253 C  C     . THR B 2 496 ? 120.754 138.885 144.964 1.00 30.18  ? 496  THR B C     1 
ATOM   11254 O  O     . THR B 2 496 ? 120.324 137.811 145.400 1.00 33.27  ? 496  THR B O     1 
ATOM   11255 C  CB    . THR B 2 496 ? 119.062 140.672 144.485 1.00 28.72  ? 496  THR B CB    1 
ATOM   11256 O  OG1   . THR B 2 496 ? 118.580 141.954 144.902 1.00 31.01  ? 496  THR B OG1   1 
ATOM   11257 C  CG2   . THR B 2 496 ? 117.904 139.695 144.475 1.00 31.11  ? 496  THR B CG2   1 
ATOM   11258 N  N     . GLY B 2 497 ? 121.748 138.941 144.084 1.00 21.60  ? 497  GLY B N     1 
ATOM   11259 C  CA    . GLY B 2 497 ? 122.238 137.769 143.394 1.00 14.89  ? 497  GLY B CA    1 
ATOM   11260 C  C     . GLY B 2 497 ? 123.458 137.086 143.969 1.00 21.21  ? 497  GLY B C     1 
ATOM   11261 O  O     . GLY B 2 497 ? 124.005 136.196 143.311 1.00 30.64  ? 497  GLY B O     1 
ATOM   11262 N  N     . SER B 2 498 ? 123.912 137.461 145.157 1.00 19.91  ? 498  SER B N     1 
ATOM   11263 C  CA    . SER B 2 498 ? 125.054 136.788 145.757 1.00 18.56  ? 498  SER B CA    1 
ATOM   11264 C  C     . SER B 2 498 ? 124.595 135.593 146.590 1.00 22.11  ? 498  SER B C     1 
ATOM   11265 O  O     . SER B 2 498 ? 123.419 135.448 146.925 1.00 30.90  ? 498  SER B O     1 
ATOM   11266 C  CB    . SER B 2 498 ? 125.866 137.761 146.608 1.00 17.82  ? 498  SER B CB    1 
ATOM   11267 O  OG    . SER B 2 498 ? 126.505 138.726 145.796 1.00 21.87  ? 498  SER B OG    1 
ATOM   11268 N  N     . LEU B 2 499 ? 125.549 134.727 146.925 1.00 20.70  ? 499  LEU B N     1 
ATOM   11269 C  CA    . LEU B 2 499 ? 125.262 133.473 147.612 1.00 24.34  ? 499  LEU B CA    1 
ATOM   11270 C  C     . LEU B 2 499 ? 125.459 133.548 149.119 1.00 25.53  ? 499  LEU B C     1 
ATOM   11271 O  O     . LEU B 2 499 ? 124.629 133.030 149.870 1.00 33.50  ? 499  LEU B O     1 
ATOM   11272 C  CB    . LEU B 2 499 ? 126.133 132.350 147.043 1.00 21.18  ? 499  LEU B CB    1 
ATOM   11273 C  CG    . LEU B 2 499 ? 125.984 130.967 147.677 1.00 10.09  ? 499  LEU B CG    1 
ATOM   11274 C  CD1   . LEU B 2 499 ? 124.552 130.485 147.583 1.00 20.17  ? 499  LEU B CD1   1 
ATOM   11275 C  CD2   . LEU B 2 499 ? 126.922 129.983 147.014 1.00 15.83  ? 499  LEU B CD2   1 
ATOM   11276 N  N     . CYS B 2 500 ? 126.535 134.167 149.585 1.00 21.60  ? 500  CYS B N     1 
ATOM   11277 C  CA    . CYS B 2 500 ? 126.781 134.310 151.010 1.00 14.10  ? 500  CYS B CA    1 
ATOM   11278 C  C     . CYS B 2 500 ? 126.635 135.771 151.411 1.00 12.26  ? 500  CYS B C     1 
ATOM   11279 O  O     . CYS B 2 500 ? 126.536 136.666 150.570 1.00 23.28  ? 500  CYS B O     1 
ATOM   11280 C  CB    . CYS B 2 500 ? 128.167 133.775 151.388 1.00 19.69  ? 500  CYS B CB    1 
ATOM   11281 S  SG    . CYS B 2 500 ? 129.507 134.963 151.263 1.00 12.59  ? 500  CYS B SG    1 
ATOM   11282 N  N     . GLY B 2 501 ? 126.623 136.004 152.724 1.00 14.42  ? 501  GLY B N     1 
ATOM   11283 C  CA    . GLY B 2 501 ? 126.354 137.333 153.241 1.00 18.88  ? 501  GLY B CA    1 
ATOM   11284 C  C     . GLY B 2 501 ? 127.414 138.363 152.914 1.00 15.96  ? 501  GLY B C     1 
ATOM   11285 O  O     . GLY B 2 501 ? 127.145 139.561 153.026 1.00 23.67  ? 501  GLY B O     1 
ATOM   11286 N  N     . LEU B 2 502 ? 128.610 137.928 152.512 1.00 10.39  ? 502  LEU B N     1 
ATOM   11287 C  CA    . LEU B 2 502 ? 129.656 138.875 152.138 1.00 14.56  ? 502  LEU B CA    1 
ATOM   11288 C  C     . LEU B 2 502 ? 129.260 139.667 150.898 1.00 14.44  ? 502  LEU B C     1 
ATOM   11289 O  O     . LEU B 2 502 ? 129.393 140.895 150.864 1.00 35.02  ? 502  LEU B O     1 
ATOM   11290 C  CB    . LEU B 2 502 ? 130.975 138.133 151.918 1.00 20.68  ? 502  LEU B CB    1 
ATOM   11291 C  CG    . LEU B 2 502 ? 132.274 138.901 151.666 1.00 13.07  ? 502  LEU B CG    1 
ATOM   11292 C  CD1   . LEU B 2 502 ? 133.429 138.125 152.251 1.00 17.80  ? 502  LEU B CD1   1 
ATOM   11293 C  CD2   . LEU B 2 502 ? 132.510 139.112 150.187 1.00 10.92  ? 502  LEU B CD2   1 
ATOM   11294 N  N     . GLY B 2 503 ? 128.769 138.981 149.866 1.00 8.37   ? 503  GLY B N     1 
ATOM   11295 C  CA    . GLY B 2 503 ? 128.317 139.677 148.676 1.00 9.71   ? 503  GLY B CA    1 
ATOM   11296 C  C     . GLY B 2 503 ? 126.966 140.332 148.839 1.00 20.08  ? 503  GLY B C     1 
ATOM   11297 O  O     . GLY B 2 503 ? 126.684 141.342 148.189 1.00 27.94  ? 503  GLY B O     1 
ATOM   11298 N  N     . GLN B 2 504 ? 126.112 139.773 149.698 1.00 23.10  ? 504  GLN B N     1 
ATOM   11299 C  CA    . GLN B 2 504 ? 124.812 140.379 149.949 1.00 13.57  ? 504  GLN B CA    1 
ATOM   11300 C  C     . GLN B 2 504 ? 124.943 141.673 150.742 1.00 26.25  ? 504  GLN B C     1 
ATOM   11301 O  O     . GLN B 2 504 ? 124.121 142.582 150.585 1.00 38.39  ? 504  GLN B O     1 
ATOM   11302 C  CB    . GLN B 2 504 ? 123.909 139.385 150.678 1.00 13.21  ? 504  GLN B CB    1 
ATOM   11303 C  CG    . GLN B 2 504 ? 123.674 138.091 149.913 1.00 13.12  ? 504  GLN B CG    1 
ATOM   11304 C  CD    . GLN B 2 504 ? 122.810 137.110 150.677 1.00 22.31  ? 504  GLN B CD    1 
ATOM   11305 O  OE1   . GLN B 2 504 ? 122.385 137.383 151.798 1.00 33.32  ? 504  GLN B OE1   1 
ATOM   11306 N  NE2   . GLN B 2 504 ? 122.546 135.959 150.075 1.00 13.11  ? 504  GLN B NE2   1 
ATOM   11307 N  N     . THR B 2 505 ? 125.955 141.774 151.597 1.00 22.17  ? 505  THR B N     1 
ATOM   11308 C  CA    . THR B 2 505 ? 126.260 143.005 152.309 1.00 21.31  ? 505  THR B CA    1 
ATOM   11309 C  C     . THR B 2 505 ? 127.340 143.826 151.617 1.00 25.61  ? 505  THR B C     1 
ATOM   11310 O  O     . THR B 2 505 ? 127.671 144.915 152.092 1.00 38.62  ? 505  THR B O     1 
ATOM   11311 C  CB    . THR B 2 505 ? 126.684 142.690 153.747 1.00 30.68  ? 505  THR B CB    1 
ATOM   11312 O  OG1   . THR B 2 505 ? 127.807 141.801 153.732 1.00 22.39  ? 505  THR B OG1   1 
ATOM   11313 C  CG2   . THR B 2 505 ? 125.544 142.035 154.506 1.00 27.17  ? 505  THR B CG2   1 
ATOM   11314 N  N     . ALA B 2 506 ? 127.890 143.327 150.512 1.00 21.01  ? 506  ALA B N     1 
ATOM   11315 C  CA    . ALA B 2 506 ? 128.902 144.070 149.763 1.00 16.26  ? 506  ALA B CA    1 
ATOM   11316 C  C     . ALA B 2 506 ? 128.418 145.416 149.232 1.00 28.85  ? 506  ALA B C     1 
ATOM   11317 O  O     . ALA B 2 506 ? 129.159 146.404 149.372 1.00 35.38  ? 506  ALA B O     1 
ATOM   11318 C  CB    . ALA B 2 506 ? 129.433 143.198 148.621 1.00 21.52  ? 506  ALA B CB    1 
ATOM   11319 N  N     . PRO B 2 507 ? 127.243 145.541 148.604 1.00 27.30  ? 507  PRO B N     1 
ATOM   11320 C  CA    . PRO B 2 507 ? 126.849 146.845 148.057 1.00 21.41  ? 507  PRO B CA    1 
ATOM   11321 C  C     . PRO B 2 507 ? 126.304 147.819 149.086 1.00 25.83  ? 507  PRO B C     1 
ATOM   11322 O  O     . PRO B 2 507 ? 125.931 148.933 148.704 1.00 31.68  ? 507  PRO B O     1 
ATOM   11323 C  CB    . PRO B 2 507 ? 125.761 146.477 147.032 1.00 28.01  ? 507  PRO B CB    1 
ATOM   11324 C  CG    . PRO B 2 507 ? 125.798 144.989 146.912 1.00 28.14  ? 507  PRO B CG    1 
ATOM   11325 C  CD    . PRO B 2 507 ? 126.251 144.518 148.231 1.00 27.76  ? 507  PRO B CD    1 
ATOM   11326 N  N     . ASN B 2 508 ? 126.242 147.435 150.362 1.00 28.16  ? 508  ASN B N     1 
ATOM   11327 C  CA    . ASN B 2 508 ? 125.663 148.307 151.383 1.00 27.29  ? 508  ASN B CA    1 
ATOM   11328 C  C     . ASN B 2 508 ? 126.336 149.673 151.482 1.00 28.17  ? 508  ASN B C     1 
ATOM   11329 O  O     . ASN B 2 508 ? 125.609 150.681 151.534 1.00 41.51  ? 508  ASN B O     1 
ATOM   11330 C  CB    . ASN B 2 508 ? 125.669 147.594 152.740 1.00 24.32  ? 508  ASN B CB    1 
ATOM   11331 C  CG    . ASN B 2 508 ? 124.627 146.504 152.829 1.00 32.11  ? 508  ASN B CG    1 
ATOM   11332 O  OD1   . ASN B 2 508 ? 123.727 146.423 151.998 1.00 37.85  ? 508  ASN B OD1   1 
ATOM   11333 N  ND2   . ASN B 2 508 ? 124.737 145.665 153.849 1.00 27.45  ? 508  ASN B ND2   1 
ATOM   11334 N  N     . PRO B 2 509 ? 127.673 149.798 151.525 1.00 23.75  ? 509  PRO B N     1 
ATOM   11335 C  CA    . PRO B 2 509 ? 128.253 151.151 151.605 1.00 29.19  ? 509  PRO B CA    1 
ATOM   11336 C  C     . PRO B 2 509 ? 127.906 152.026 150.416 1.00 33.38  ? 509  PRO B C     1 
ATOM   11337 O  O     . PRO B 2 509 ? 127.540 153.193 150.600 1.00 37.78  ? 509  PRO B O     1 
ATOM   11338 C  CB    . PRO B 2 509 ? 129.762 150.883 151.687 1.00 30.81  ? 509  PRO B CB    1 
ATOM   11339 C  CG    . PRO B 2 509 ? 129.878 149.503 152.187 1.00 32.95  ? 509  PRO B CG    1 
ATOM   11340 C  CD    . PRO B 2 509 ? 128.729 148.770 151.587 1.00 28.01  ? 509  PRO B CD    1 
ATOM   11341 N  N     . VAL B 2 510 ? 127.997 151.485 149.199 1.00 33.62  ? 510  VAL B N     1 
ATOM   11342 C  CA    . VAL B 2 510 ? 127.672 152.257 148.003 1.00 29.61  ? 510  VAL B CA    1 
ATOM   11343 C  C     . VAL B 2 510 ? 126.206 152.659 148.014 1.00 32.54  ? 510  VAL B C     1 
ATOM   11344 O  O     . VAL B 2 510 ? 125.856 153.808 147.721 1.00 40.43  ? 510  VAL B O     1 
ATOM   11345 C  CB    . VAL B 2 510 ? 128.020 151.454 146.737 1.00 31.19  ? 510  VAL B CB    1 
ATOM   11346 C  CG1   . VAL B 2 510 ? 127.512 152.165 145.496 1.00 29.52  ? 510  VAL B CG1   1 
ATOM   11347 C  CG2   . VAL B 2 510 ? 129.507 151.241 146.651 1.00 37.66  ? 510  VAL B CG2   1 
ATOM   11348 N  N     . LEU B 2 511 ? 125.327 151.711 148.346 1.00 34.85  ? 511  LEU B N     1 
ATOM   11349 C  CA    . LEU B 2 511 ? 123.898 151.994 148.356 1.00 37.19  ? 511  LEU B CA    1 
ATOM   11350 C  C     . LEU B 2 511 ? 123.560 153.088 149.358 1.00 32.54  ? 511  LEU B C     1 
ATOM   11351 O  O     . LEU B 2 511 ? 122.808 154.015 149.042 1.00 34.34  ? 511  LEU B O     1 
ATOM   11352 C  CB    . LEU B 2 511 ? 123.115 150.720 148.670 1.00 30.51  ? 511  LEU B CB    1 
ATOM   11353 C  CG    . LEU B 2 511 ? 122.993 149.697 147.542 1.00 25.76  ? 511  LEU B CG    1 
ATOM   11354 C  CD1   . LEU B 2 511 ? 122.471 148.382 148.078 1.00 23.79  ? 511  LEU B CD1   1 
ATOM   11355 C  CD2   . LEU B 2 511 ? 122.080 150.226 146.455 1.00 35.99  ? 511  LEU B CD2   1 
ATOM   11356 N  N     . THR B 2 512 ? 124.127 153.012 150.563 1.00 29.95  ? 512  THR B N     1 
ATOM   11357 C  CA    . THR B 2 512 ? 123.806 154.006 151.581 1.00 33.53  ? 512  THR B CA    1 
ATOM   11358 C  C     . THR B 2 512 ? 124.419 155.362 151.251 1.00 37.55  ? 512  THR B C     1 
ATOM   11359 O  O     . THR B 2 512 ? 123.806 156.403 151.515 1.00 47.86  ? 512  THR B O     1 
ATOM   11360 C  CB    . THR B 2 512 ? 124.263 153.521 152.953 1.00 36.60  ? 512  THR B CB    1 
ATOM   11361 O  OG1   . THR B 2 512 ? 125.647 153.158 152.899 1.00 36.29  ? 512  THR B OG1   1 
ATOM   11362 C  CG2   . THR B 2 512 ? 123.443 152.319 153.373 1.00 38.98  ? 512  THR B CG2   1 
ATOM   11363 N  N     . THR B 2 513 ? 125.621 155.374 150.670 1.00 36.70  ? 513  THR B N     1 
ATOM   11364 C  CA    . THR B 2 513 ? 126.220 156.637 150.255 1.00 37.50  ? 513  THR B CA    1 
ATOM   11365 C  C     . THR B 2 513 ? 125.407 157.296 149.146 1.00 36.37  ? 513  THR B C     1 
ATOM   11366 O  O     . THR B 2 513 ? 125.217 158.517 149.149 1.00 43.01  ? 513  THR B O     1 
ATOM   11367 C  CB    . THR B 2 513 ? 127.664 156.409 149.809 1.00 40.65  ? 513  THR B CB    1 
ATOM   11368 O  OG1   . THR B 2 513 ? 128.385 155.737 150.848 1.00 40.69  ? 513  THR B OG1   1 
ATOM   11369 C  CG2   . THR B 2 513 ? 128.342 157.728 149.526 1.00 45.12  ? 513  THR B CG2   1 
ATOM   11370 N  N     . LEU B 2 514 ? 124.919 156.507 148.186 1.00 42.54  ? 514  LEU B N     1 
ATOM   11371 C  CA    . LEU B 2 514 ? 124.036 157.050 147.158 1.00 40.14  ? 514  LEU B CA    1 
ATOM   11372 C  C     . LEU B 2 514 ? 122.740 157.568 147.763 1.00 42.67  ? 514  LEU B C     1 
ATOM   11373 O  O     . LEU B 2 514 ? 122.249 158.638 147.384 1.00 48.45  ? 514  LEU B O     1 
ATOM   11374 C  CB    . LEU B 2 514 ? 123.731 155.984 146.106 1.00 43.55  ? 514  LEU B CB    1 
ATOM   11375 C  CG    . LEU B 2 514 ? 124.807 155.597 145.096 1.00 43.40  ? 514  LEU B CG    1 
ATOM   11376 C  CD1   . LEU B 2 514 ? 124.407 154.316 144.395 1.00 40.72  ? 514  LEU B CD1   1 
ATOM   11377 C  CD2   . LEU B 2 514 ? 125.008 156.708 144.087 1.00 45.35  ? 514  LEU B CD2   1 
ATOM   11378 N  N     . LYS B 2 515 ? 122.170 156.816 148.706 1.00 49.97  ? 515  LYS B N     1 
ATOM   11379 C  CA    . LYS B 2 515 ? 120.876 157.171 149.273 1.00 49.61  ? 515  LYS B CA    1 
ATOM   11380 C  C     . LYS B 2 515 ? 120.968 158.402 150.164 1.00 48.49  ? 515  LYS B C     1 
ATOM   11381 O  O     . LYS B 2 515 ? 119.980 159.128 150.318 1.00 52.03  ? 515  LYS B O     1 
ATOM   11382 C  CB    . LYS B 2 515 ? 120.321 155.978 150.053 1.00 45.17  ? 515  LYS B CB    1 
ATOM   11383 C  CG    . LYS B 2 515 ? 118.905 156.142 150.563 1.00 48.87  ? 515  LYS B CG    1 
ATOM   11384 C  CD    . LYS B 2 515 ? 118.482 154.926 151.364 1.00 47.79  ? 515  LYS B CD    1 
ATOM   11385 C  CE    . LYS B 2 515 ? 117.099 155.107 151.956 1.00 50.95  ? 515  LYS B CE    1 
ATOM   11386 N  NZ    . LYS B 2 515 ? 116.684 153.917 152.746 1.00 53.05  ? 515  LYS B NZ    1 
ATOM   11387 N  N     . TYR B 2 516 ? 122.135 158.666 150.738 1.00 45.05  ? 516  TYR B N     1 
ATOM   11388 C  CA    . TYR B 2 516 ? 122.267 159.735 151.715 1.00 49.36  ? 516  TYR B CA    1 
ATOM   11389 C  C     . TYR B 2 516 ? 123.239 160.837 151.322 1.00 53.63  ? 516  TYR B C     1 
ATOM   11390 O  O     . TYR B 2 516 ? 123.048 161.977 151.748 1.00 57.80  ? 516  TYR B O     1 
ATOM   11391 C  CB    . TYR B 2 516 ? 122.695 159.155 153.070 1.00 47.30  ? 516  TYR B CB    1 
ATOM   11392 C  CG    . TYR B 2 516 ? 121.662 158.247 153.696 1.00 50.38  ? 516  TYR B CG    1 
ATOM   11393 C  CD1   . TYR B 2 516 ? 120.342 158.651 153.822 1.00 53.12  ? 516  TYR B CD1   1 
ATOM   11394 C  CD2   . TYR B 2 516 ? 122.006 156.983 154.148 1.00 49.16  ? 516  TYR B CD2   1 
ATOM   11395 C  CE1   . TYR B 2 516 ? 119.397 157.827 154.392 1.00 51.70  ? 516  TYR B CE1   1 
ATOM   11396 C  CE2   . TYR B 2 516 ? 121.067 156.152 154.720 1.00 49.56  ? 516  TYR B CE2   1 
ATOM   11397 C  CZ    . TYR B 2 516 ? 119.764 156.578 154.838 1.00 54.02  ? 516  TYR B CZ    1 
ATOM   11398 O  OH    . TYR B 2 516 ? 118.824 155.753 155.405 1.00 54.59  ? 516  TYR B OH    1 
ATOM   11399 N  N     . PHE B 2 517 ? 124.265 160.544 150.529 1.00 47.87  ? 517  PHE B N     1 
ATOM   11400 C  CA    . PHE B 2 517 ? 125.320 161.511 150.231 1.00 48.46  ? 517  PHE B CA    1 
ATOM   11401 C  C     . PHE B 2 517 ? 125.613 161.550 148.741 1.00 49.89  ? 517  PHE B C     1 
ATOM   11402 O  O     . PHE B 2 517 ? 126.763 161.481 148.302 1.00 48.78  ? 517  PHE B O     1 
ATOM   11403 C  CB    . PHE B 2 517 ? 126.577 161.193 151.026 1.00 43.26  ? 517  PHE B CB    1 
ATOM   11404 C  CG    . PHE B 2 517 ? 126.350 161.162 152.499 1.00 48.02  ? 517  PHE B CG    1 
ATOM   11405 C  CD1   . PHE B 2 517 ? 126.315 162.336 153.225 1.00 51.41  ? 517  PHE B CD1   1 
ATOM   11406 C  CD2   . PHE B 2 517 ? 126.144 159.964 153.156 1.00 47.99  ? 517  PHE B CD2   1 
ATOM   11407 C  CE1   . PHE B 2 517 ? 126.092 162.316 154.579 1.00 51.21  ? 517  PHE B CE1   1 
ATOM   11408 C  CE2   . PHE B 2 517 ? 125.922 159.938 154.510 1.00 47.64  ? 517  PHE B CE2   1 
ATOM   11409 C  CZ    . PHE B 2 517 ? 125.894 161.118 155.222 1.00 51.72  ? 517  PHE B CZ    1 
ATOM   11410 N  N     . LYS B 2 518 ? 124.558 161.668 147.936 1.00 51.17  ? 518  LYS B N     1 
ATOM   11411 C  CA    . LYS B 2 518 ? 124.727 161.783 146.495 1.00 52.36  ? 518  LYS B CA    1 
ATOM   11412 C  C     . LYS B 2 518 ? 125.310 163.126 146.076 1.00 59.79  ? 518  LYS B C     1 
ATOM   11413 O  O     . LYS B 2 518 ? 125.657 163.289 144.902 1.00 65.32  ? 518  LYS B O     1 
ATOM   11414 C  CB    . LYS B 2 518 ? 123.388 161.554 145.793 1.00 51.65  ? 518  LYS B CB    1 
ATOM   11415 C  CG    . LYS B 2 518 ? 123.521 160.947 144.412 1.00 54.54  ? 518  LYS B CG    1 
ATOM   11416 C  CD    . LYS B 2 518 ? 122.180 160.827 143.728 1.00 54.58  ? 518  LYS B CD    1 
ATOM   11417 C  CE    . LYS B 2 518 ? 122.335 160.207 142.356 1.00 57.04  ? 518  LYS B CE    1 
ATOM   11418 N  NZ    . LYS B 2 518 ? 123.334 160.939 141.539 1.00 54.09  ? 518  LYS B NZ    1 
ATOM   11419 N  N     . ASP B 2 519 ? 125.416 164.089 146.996 1.00 64.94  ? 519  ASP B N     1 
ATOM   11420 C  CA    . ASP B 2 519 ? 126.013 165.378 146.661 1.00 62.53  ? 519  ASP B CA    1 
ATOM   11421 C  C     . ASP B 2 519 ? 127.470 165.216 146.252 1.00 63.94  ? 519  ASP B C     1 
ATOM   11422 O  O     . ASP B 2 519 ? 127.902 165.755 145.229 1.00 66.50  ? 519  ASP B O     1 
ATOM   11423 C  CB    . ASP B 2 519 ? 125.891 166.337 147.844 1.00 60.50  ? 519  ASP B CB    1 
ATOM   11424 C  CG    . ASP B 2 519 ? 124.455 166.638 148.200 1.00 64.77  ? 519  ASP B CG    1 
ATOM   11425 O  OD1   . ASP B 2 519 ? 123.607 166.645 147.285 1.00 65.76  ? 519  ASP B OD1   1 
ATOM   11426 O  OD2   . ASP B 2 519 ? 124.172 166.866 149.394 1.00 66.43  ? 519  ASP B OD2   1 
ATOM   11427 N  N     . GLU B 2 520 ? 128.242 164.458 147.034 1.00 67.53  ? 520  GLU B N     1 
ATOM   11428 C  CA    . GLU B 2 520 ? 129.622 164.187 146.648 1.00 66.30  ? 520  GLU B CA    1 
ATOM   11429 C  C     . GLU B 2 520 ? 129.691 163.288 145.422 1.00 67.81  ? 520  GLU B C     1 
ATOM   11430 O  O     . GLU B 2 520 ? 130.629 163.407 144.627 1.00 72.92  ? 520  GLU B O     1 
ATOM   11431 C  CB    . GLU B 2 520 ? 130.390 163.567 147.813 1.00 69.44  ? 520  GLU B CB    1 
ATOM   11432 C  CG    . GLU B 2 520 ? 130.752 164.554 148.908 1.00 70.08  ? 520  GLU B CG    1 
ATOM   11433 C  CD    . GLU B 2 520 ? 131.641 163.945 149.971 1.00 72.83  ? 520  GLU B CD    1 
ATOM   11434 O  OE1   . GLU B 2 520 ? 131.675 162.702 150.077 1.00 71.46  ? 520  GLU B OE1   1 
ATOM   11435 O  OE2   . GLU B 2 520 ? 132.311 164.707 150.697 1.00 73.26  ? 520  GLU B OE2   1 
ATOM   11436 N  N     . TYR B 2 521 ? 128.707 162.399 145.246 1.00 59.69  ? 521  TYR B N     1 
ATOM   11437 C  CA    . TYR B 2 521 ? 128.642 161.588 144.034 1.00 61.56  ? 521  TYR B CA    1 
ATOM   11438 C  C     . TYR B 2 521 ? 128.561 162.466 142.793 1.00 64.34  ? 521  TYR B C     1 
ATOM   11439 O  O     . TYR B 2 521 ? 129.326 162.288 141.839 1.00 64.82  ? 521  TYR B O     1 
ATOM   11440 C  CB    . TYR B 2 521 ? 127.438 160.647 144.093 1.00 56.57  ? 521  TYR B CB    1 
ATOM   11441 C  CG    . TYR B 2 521 ? 127.772 159.225 144.467 1.00 61.07  ? 521  TYR B CG    1 
ATOM   11442 C  CD1   . TYR B 2 521 ? 128.245 158.331 143.518 1.00 62.16  ? 521  TYR B CD1   1 
ATOM   11443 C  CD2   . TYR B 2 521 ? 127.602 158.770 145.766 1.00 62.08  ? 521  TYR B CD2   1 
ATOM   11444 C  CE1   . TYR B 2 521 ? 128.549 157.027 143.855 1.00 60.39  ? 521  TYR B CE1   1 
ATOM   11445 C  CE2   . TYR B 2 521 ? 127.901 157.469 146.110 1.00 59.28  ? 521  TYR B CE2   1 
ATOM   11446 C  CZ    . TYR B 2 521 ? 128.374 156.603 145.154 1.00 62.22  ? 521  TYR B CZ    1 
ATOM   11447 O  OH    . TYR B 2 521 ? 128.673 155.306 145.499 1.00 62.78  ? 521  TYR B OH    1 
ATOM   11448 N  N     . LEU B 2 522 ? 127.640 163.430 142.796 1.00 60.75  ? 522  LEU B N     1 
ATOM   11449 C  CA    . LEU B 2 522 ? 127.508 164.337 141.662 1.00 58.43  ? 522  LEU B CA    1 
ATOM   11450 C  C     . LEU B 2 522 ? 128.687 165.294 141.557 1.00 59.12  ? 522  LEU B C     1 
ATOM   11451 O  O     . LEU B 2 522 ? 129.078 165.670 140.447 1.00 64.94  ? 522  LEU B O     1 
ATOM   11452 C  CB    . LEU B 2 522 ? 126.203 165.121 141.769 1.00 60.74  ? 522  LEU B CB    1 
ATOM   11453 C  CG    . LEU B 2 522 ? 124.934 164.298 141.575 1.00 57.86  ? 522  LEU B CG    1 
ATOM   11454 C  CD1   . LEU B 2 522 ? 123.708 165.184 141.695 1.00 58.73  ? 522  LEU B CD1   1 
ATOM   11455 C  CD2   . LEU B 2 522 ? 124.971 163.599 140.228 1.00 57.50  ? 522  LEU B CD2   1 
ATOM   11456 N  N     . ALA B 2 523 ? 129.264 165.699 142.690 1.00 63.85  ? 523  ALA B N     1 
ATOM   11457 C  CA    . ALA B 2 523 ? 130.356 166.664 142.660 1.00 67.97  ? 523  ALA B CA    1 
ATOM   11458 C  C     . ALA B 2 523 ? 131.648 166.048 142.142 1.00 68.53  ? 523  ALA B C     1 
ATOM   11459 O  O     . ALA B 2 523 ? 132.463 166.749 141.532 1.00 68.54  ? 523  ALA B O     1 
ATOM   11460 C  CB    . ALA B 2 523 ? 130.570 167.257 144.051 1.00 67.69  ? 523  ALA B CB    1 
ATOM   11461 N  N     . HIS B 2 524 ? 131.862 164.752 142.378 1.00 70.95  ? 524  HIS B N     1 
ATOM   11462 C  CA    . HIS B 2 524 ? 133.066 164.106 141.872 1.00 66.54  ? 524  HIS B CA    1 
ATOM   11463 C  C     . HIS B 2 524 ? 133.039 163.943 140.359 1.00 66.78  ? 524  HIS B C     1 
ATOM   11464 O  O     . HIS B 2 524 ? 134.091 163.710 139.755 1.00 70.72  ? 524  HIS B O     1 
ATOM   11465 C  CB    . HIS B 2 524 ? 133.263 162.751 142.553 1.00 65.10  ? 524  HIS B CB    1 
ATOM   11466 C  CG    . HIS B 2 524 ? 133.771 162.852 143.957 1.00 64.13  ? 524  HIS B CG    1 
ATOM   11467 N  ND1   . HIS B 2 524 ? 132.973 163.232 145.014 1.00 65.06  ? 524  HIS B ND1   1 
ATOM   11468 C  CD2   . HIS B 2 524 ? 135.002 162.630 144.478 1.00 68.21  ? 524  HIS B CD2   1 
ATOM   11469 C  CE1   . HIS B 2 524 ? 133.688 163.237 146.125 1.00 68.64  ? 524  HIS B CE1   1 
ATOM   11470 N  NE2   . HIS B 2 524 ? 134.923 162.876 145.827 1.00 68.48  ? 524  HIS B NE2   1 
ATOM   11471 N  N     . ILE B 2 525 ? 131.865 164.060 139.737 1.00 67.20  ? 525  ILE B N     1 
ATOM   11472 C  CA    . ILE B 2 525 ? 131.795 164.102 138.280 1.00 70.19  ? 525  ILE B CA    1 
ATOM   11473 C  C     . ILE B 2 525 ? 132.442 165.378 137.755 1.00 75.78  ? 525  ILE B C     1 
ATOM   11474 O  O     . ILE B 2 525 ? 133.111 165.370 136.714 1.00 74.45  ? 525  ILE B O     1 
ATOM   11475 C  CB    . ILE B 2 525 ? 130.333 163.972 137.818 1.00 69.56  ? 525  ILE B CB    1 
ATOM   11476 C  CG1   . ILE B 2 525 ? 129.749 162.638 138.277 1.00 70.07  ? 525  ILE B CG1   1 
ATOM   11477 C  CG2   . ILE B 2 525 ? 130.226 164.100 136.308 1.00 70.00  ? 525  ILE B CG2   1 
ATOM   11478 C  CD1   . ILE B 2 525 ? 128.301 162.457 137.899 1.00 73.38  ? 525  ILE B CD1   1 
ATOM   11479 N  N     . GLU B 2 526 ? 132.273 166.486 138.473 1.00 82.13  ? 526  GLU B N     1 
ATOM   11480 C  CA    . GLU B 2 526 ? 132.783 167.785 138.053 1.00 78.54  ? 526  GLU B CA    1 
ATOM   11481 C  C     . GLU B 2 526 ? 134.264 167.974 138.358 1.00 80.43  ? 526  GLU B C     1 
ATOM   11482 O  O     . GLU B 2 526 ? 134.771 169.090 138.210 1.00 82.23  ? 526  GLU B O     1 
ATOM   11483 C  CB    . GLU B 2 526 ? 131.978 168.905 138.719 1.00 78.17  ? 526  GLU B CB    1 
ATOM   11484 C  CG    . GLU B 2 526 ? 130.559 168.518 139.103 1.00 79.74  ? 526  GLU B CG    1 
ATOM   11485 C  CD    . GLU B 2 526 ? 129.685 168.203 137.905 1.00 82.09  ? 526  GLU B CD    1 
ATOM   11486 O  OE1   . GLU B 2 526 ? 129.922 168.780 136.823 1.00 83.26  ? 526  GLU B OE1   1 
ATOM   11487 O  OE2   . GLU B 2 526 ? 128.761 167.374 138.047 1.00 81.41  ? 526  GLU B OE2   1 
ATOM   11488 N  N     . GLY B 2 527 ? 134.965 166.925 138.780 1.00 82.03  ? 527  GLY B N     1 
ATOM   11489 C  CA    . GLY B 2 527 ? 136.376 167.045 139.082 1.00 80.00  ? 527  GLY B CA    1 
ATOM   11490 C  C     . GLY B 2 527 ? 136.692 167.724 140.392 1.00 82.18  ? 527  GLY B C     1 
ATOM   11491 O  O     . GLY B 2 527 ? 137.820 168.189 140.578 1.00 85.12  ? 527  GLY B O     1 
ATOM   11492 N  N     . ARG B 2 528 ? 135.733 167.793 141.312 1.00 81.91  ? 528  ARG B N     1 
ATOM   11493 C  CA    . ARG B 2 528 ? 135.910 168.480 142.584 1.00 82.63  ? 528  ARG B CA    1 
ATOM   11494 C  C     . ARG B 2 528 ? 135.550 167.542 143.725 1.00 83.05  ? 528  ARG B C     1 
ATOM   11495 O  O     . ARG B 2 528 ? 134.496 166.900 143.696 1.00 77.97  ? 528  ARG B O     1 
ATOM   11496 C  CB    . ARG B 2 528 ? 135.047 169.743 142.646 1.00 80.97  ? 528  ARG B CB    1 
ATOM   11497 C  CG    . ARG B 2 528 ? 135.114 170.482 143.970 1.00 80.57  ? 528  ARG B CG    1 
ATOM   11498 C  CD    . ARG B 2 528 ? 134.092 171.609 144.034 1.00 80.98  ? 528  ARG B CD    1 
ATOM   11499 N  NE    . ARG B 2 528 ? 132.720 171.115 144.087 1.00 81.11  ? 528  ARG B NE    1 
ATOM   11500 C  CZ    . ARG B 2 528 ? 131.906 171.044 143.043 1.00 81.96  ? 528  ARG B CZ    1 
ATOM   11501 N  NH1   . ARG B 2 528 ? 132.292 171.426 141.837 1.00 80.82  ? 528  ARG B NH1   1 
ATOM   11502 N  NH2   . ARG B 2 528 ? 130.672 170.578 143.214 1.00 83.13  ? 528  ARG B NH2   1 
ATOM   11503 N  N     . CYS B 2 529 ? 136.426 167.468 144.726 1.00 86.45  ? 529  CYS B N     1 
ATOM   11504 C  CA    . CYS B 2 529 ? 136.166 166.703 145.941 1.00 81.49  ? 529  CYS B CA    1 
ATOM   11505 C  C     . CYS B 2 529 ? 135.890 167.660 147.090 1.00 82.92  ? 529  CYS B C     1 
ATOM   11506 O  O     . CYS B 2 529 ? 136.816 168.350 147.547 1.00 84.09  ? 529  CYS B O     1 
ATOM   11507 C  CB    . CYS B 2 529 ? 137.350 165.797 146.279 1.00 83.38  ? 529  CYS B CB    1 
ATOM   11508 S  SG    . CYS B 2 529 ? 137.195 164.971 147.879 1.00 92.99  ? 529  CYS B SG    1 
ATOM   11509 N  N     . PRO B 2 530 ? 134.651 167.747 147.580 1.00 82.64  ? 530  PRO B N     1 
ATOM   11510 C  CA    . PRO B 2 530 ? 134.356 168.692 148.670 1.00 84.02  ? 530  PRO B CA    1 
ATOM   11511 C  C     . PRO B 2 530 ? 135.147 168.442 149.943 1.00 84.01  ? 530  PRO B C     1 
ATOM   11512 O  O     . PRO B 2 530 ? 135.489 169.403 150.644 1.00 84.94  ? 530  PRO B O     1 
ATOM   11513 C  CB    . PRO B 2 530 ? 132.850 168.498 148.894 1.00 81.85  ? 530  PRO B CB    1 
ATOM   11514 C  CG    . PRO B 2 530 ? 132.341 167.992 147.586 1.00 82.12  ? 530  PRO B CG    1 
ATOM   11515 C  CD    . PRO B 2 530 ? 133.432 167.116 147.049 1.00 81.51  ? 530  PRO B CD    1 
ATOM   11516 N  N     . ALA B 2 531 ? 135.454 167.186 150.267 1.00 83.68  ? 531  ALA B N     1 
ATOM   11517 C  CA    . ALA B 2 531 ? 136.207 166.888 151.479 1.00 83.87  ? 531  ALA B CA    1 
ATOM   11518 C  C     . ALA B 2 531 ? 137.708 167.077 151.311 1.00 84.50  ? 531  ALA B C     1 
ATOM   11519 O  O     . ALA B 2 531 ? 138.431 167.028 152.312 1.00 85.77  ? 531  ALA B O     1 
ATOM   11520 C  CB    . ALA B 2 531 ? 135.921 165.460 151.941 1.00 85.15  ? 531  ALA B CB    1 
ATOM   11521 N  N     . LYS B 2 532 ? 138.183 167.284 150.081 1.00 82.76  ? 532  LYS B N     1 
ATOM   11522 C  CA    . LYS B 2 532 ? 139.592 167.562 149.795 1.00 82.93  ? 532  LYS B CA    1 
ATOM   11523 C  C     . LYS B 2 532 ? 140.508 166.457 150.322 1.00 83.20  ? 532  LYS B C     1 
ATOM   11524 O  O     . LYS B 2 532 ? 141.499 166.713 151.008 1.00 83.38  ? 532  LYS B O     1 
ATOM   11525 C  CB    . LYS B 2 532 ? 140.003 168.928 150.351 1.00 84.65  ? 532  LYS B CB    1 
ATOM   11526 C  CG    . LYS B 2 532 ? 139.253 170.094 149.732 1.00 85.59  ? 532  LYS B CG    1 
ATOM   11527 C  CD    . LYS B 2 532 ? 139.697 171.419 150.329 1.00 84.62  ? 532  LYS B CD    1 
ATOM   11528 C  CE    . LYS B 2 532 ? 139.418 171.473 151.822 1.00 84.38  ? 532  LYS B CE    1 
ATOM   11529 N  NZ    . LYS B 2 532 ? 137.969 171.307 152.122 1.00 84.68  ? 532  LYS B NZ    1 
ATOM   11530 N  N     . VAL B 2 533 ? 140.168 165.212 149.993 1.00 85.17  ? 533  VAL B N     1 
ATOM   11531 C  CA    . VAL B 2 533 ? 141.014 164.078 150.355 1.00 85.69  ? 533  VAL B CA    1 
ATOM   11532 C  C     . VAL B 2 533 ? 141.350 163.176 149.178 1.00 85.95  ? 533  VAL B C     1 
ATOM   11533 O  O     . VAL B 2 533 ? 142.317 162.395 149.265 1.00 85.69  ? 533  VAL B O     1 
ATOM   11534 C  CB    . VAL B 2 533 ? 140.365 163.255 151.493 1.00 85.61  ? 533  VAL B CB    1 
ATOM   11535 C  CG1   . VAL B 2 533 ? 139.418 162.205 150.933 1.00 82.01  ? 533  VAL B CG1   1 
ATOM   11536 C  CG2   . VAL B 2 533 ? 141.434 162.615 152.368 1.00 85.21  ? 533  VAL B CG2   1 
ATOM   11537 N  N     . CYS B 2 534 ? 140.622 163.228 148.064 1.00 80.98  ? 534  CYS B N     1 
ATOM   11538 C  CA    . CYS B 2 534 ? 140.963 162.408 146.908 1.00 78.69  ? 534  CYS B CA    1 
ATOM   11539 C  C     . CYS B 2 534 ? 142.204 162.978 146.235 1.00 77.57  ? 534  CYS B C     1 
ATOM   11540 O  O     . CYS B 2 534 ? 142.220 164.147 145.840 1.00 82.73  ? 534  CYS B O     1 
ATOM   11541 C  CB    . CYS B 2 534 ? 139.793 162.352 145.928 1.00 76.88  ? 534  CYS B CB    1 
ATOM   11542 S  SG    . CYS B 2 534 ? 138.293 161.587 146.584 1.00 72.06  ? 534  CYS B SG    1 
ATOM   11543 N  N     . LYS B 2 535 ? 143.241 162.150 146.109 1.00 81.02  ? 535  LYS B N     1 
ATOM   11544 C  CA    . LYS B 2 535 ? 144.526 162.626 145.598 1.00 84.43  ? 535  LYS B CA    1 
ATOM   11545 C  C     . LYS B 2 535 ? 144.460 163.189 144.181 1.00 87.94  ? 535  LYS B C     1 
ATOM   11546 O  O     . LYS B 2 535 ? 144.982 164.296 143.964 1.00 88.81  ? 535  LYS B O     1 
ATOM   11547 C  CB    . LYS B 2 535 ? 145.561 161.500 145.705 1.00 88.21  ? 535  LYS B CB    1 
ATOM   11548 C  CG    . LYS B 2 535 ? 145.797 161.012 147.120 1.00 87.35  ? 535  LYS B CG    1 
ATOM   11549 C  CD    . LYS B 2 535 ? 146.453 159.640 147.127 1.00 88.26  ? 535  LYS B CD    1 
ATOM   11550 C  CE    . LYS B 2 535 ? 147.692 159.608 146.247 1.00 87.65  ? 535  LYS B CE    1 
ATOM   11551 N  NZ    . LYS B 2 535 ? 148.715 160.590 146.689 1.00 87.90  ? 535  LYS B NZ    1 
ATOM   11552 N  N     . PRO B 2 536 ? 143.865 162.520 143.184 1.00 85.01  ? 536  PRO B N     1 
ATOM   11553 C  CA    . PRO B 2 536 ? 143.891 163.094 141.828 1.00 81.24  ? 536  PRO B CA    1 
ATOM   11554 C  C     . PRO B 2 536 ? 142.980 164.295 141.643 1.00 80.73  ? 536  PRO B C     1 
ATOM   11555 O  O     . PRO B 2 536 ? 143.173 165.045 140.678 1.00 84.54  ? 536  PRO B O     1 
ATOM   11556 C  CB    . PRO B 2 536 ? 143.450 161.923 140.943 1.00 82.75  ? 536  PRO B CB    1 
ATOM   11557 C  CG    . PRO B 2 536 ? 142.600 161.111 141.824 1.00 82.31  ? 536  PRO B CG    1 
ATOM   11558 C  CD    . PRO B 2 536 ? 143.217 161.193 143.182 1.00 85.36  ? 536  PRO B CD    1 
ATOM   11559 N  N     . LEU B 2 537 ? 142.001 164.506 142.518 1.00 79.93  ? 537  LEU B N     1 
ATOM   11560 C  CA    . LEU B 2 537 ? 141.067 165.616 142.373 1.00 81.84  ? 537  LEU B CA    1 
ATOM   11561 C  C     . LEU B 2 537 ? 141.494 166.870 143.124 1.00 82.26  ? 537  LEU B C     1 
ATOM   11562 O  O     . LEU B 2 537 ? 140.800 167.888 143.037 1.00 82.15  ? 537  LEU B O     1 
ATOM   11563 C  CB    . LEU B 2 537 ? 139.672 165.195 142.837 1.00 81.49  ? 537  LEU B CB    1 
ATOM   11564 C  CG    . LEU B 2 537 ? 138.971 164.177 141.941 1.00 80.05  ? 537  LEU B CG    1 
ATOM   11565 C  CD1   . LEU B 2 537 ? 137.558 163.930 142.424 1.00 78.07  ? 537  LEU B CD1   1 
ATOM   11566 C  CD2   . LEU B 2 537 ? 138.972 164.663 140.504 1.00 81.36  ? 537  LEU B CD2   1 
ATOM   11567 N  N     . ILE B 2 538 ? 142.601 166.826 143.866 1.00 91.86  ? 538  ILE B N     1 
ATOM   11568 C  CA    . ILE B 2 538 ? 143.123 167.984 144.582 1.00 93.03  ? 538  ILE B CA    1 
ATOM   11569 C  C     . ILE B 2 538 ? 144.628 168.058 144.360 1.00 94.86  ? 538  ILE B C     1 
ATOM   11570 O  O     . ILE B 2 538 ? 145.244 167.154 143.796 1.00 91.66  ? 538  ILE B O     1 
ATOM   11571 C  CB    . ILE B 2 538 ? 142.822 167.940 146.096 1.00 90.70  ? 538  ILE B CB    1 
ATOM   11572 C  CG1   . ILE B 2 538 ? 143.648 166.843 146.768 1.00 91.16  ? 538  ILE B CG1   1 
ATOM   11573 C  CG2   . ILE B 2 538 ? 141.335 167.753 146.360 1.00 90.49  ? 538  ILE B CG2   1 
ATOM   11574 C  CD1   . ILE B 2 538 ? 143.379 166.691 148.241 1.00 91.74  ? 538  ILE B CD1   1 
ATOM   11575 N  N     . LYS B 2 539 ? 145.214 169.164 144.811 1.00 113.64 ? 539  LYS B N     1 
ATOM   11576 C  CA    . LYS B 2 539 ? 146.660 169.326 144.868 1.00 112.97 ? 539  LYS B CA    1 
ATOM   11577 C  C     . LYS B 2 539 ? 146.992 170.022 146.182 1.00 112.75 ? 539  LYS B C     1 
ATOM   11578 O  O     . LYS B 2 539 ? 146.133 170.186 147.052 1.00 111.14 ? 539  LYS B O     1 
ATOM   11579 C  CB    . LYS B 2 539 ? 147.180 170.095 143.647 1.00 112.19 ? 539  LYS B CB    1 
ATOM   11580 C  CG    . LYS B 2 539 ? 146.669 171.518 143.539 1.00 111.96 ? 539  LYS B CG    1 
ATOM   11581 C  CD    . LYS B 2 539 ? 147.253 172.212 142.321 1.00 112.28 ? 539  LYS B CD    1 
ATOM   11582 C  CE    . LYS B 2 539 ? 146.721 173.628 142.183 1.00 113.08 ? 539  LYS B CE    1 
ATOM   11583 N  NZ    . LYS B 2 539 ? 147.285 174.317 140.990 1.00 112.23 ? 539  LYS B NZ    1 
ATOM   11584 N  N     . TYR B 2 540 ? 148.250 170.427 146.339 1.00 117.63 ? 540  TYR B N     1 
ATOM   11585 C  CA    . TYR B 2 540 ? 148.688 171.128 147.541 1.00 118.52 ? 540  TYR B CA    1 
ATOM   11586 C  C     . TYR B 2 540 ? 149.531 172.323 147.131 1.00 119.13 ? 540  TYR B C     1 
ATOM   11587 O  O     . TYR B 2 540 ? 150.524 172.168 146.414 1.00 119.06 ? 540  TYR B O     1 
ATOM   11588 C  CB    . TYR B 2 540 ? 149.475 170.201 148.472 1.00 119.01 ? 540  TYR B CB    1 
ATOM   11589 C  CG    . TYR B 2 540 ? 148.597 169.333 149.347 1.00 119.91 ? 540  TYR B CG    1 
ATOM   11590 C  CD1   . TYR B 2 540 ? 148.063 168.144 148.868 1.00 119.40 ? 540  TYR B CD1   1 
ATOM   11591 C  CD2   . TYR B 2 540 ? 148.299 169.707 150.651 1.00 118.12 ? 540  TYR B CD2   1 
ATOM   11592 C  CE1   . TYR B 2 540 ? 147.259 167.352 149.664 1.00 118.36 ? 540  TYR B CE1   1 
ATOM   11593 C  CE2   . TYR B 2 540 ? 147.497 168.921 151.453 1.00 118.30 ? 540  TYR B CE2   1 
ATOM   11594 C  CZ    . TYR B 2 540 ? 146.980 167.746 150.955 1.00 118.83 ? 540  TYR B CZ    1 
ATOM   11595 O  OH    . TYR B 2 540 ? 146.180 166.960 151.753 1.00 118.02 ? 540  TYR B OH    1 
ATOM   11596 N  N     . VAL B 2 541 ? 149.139 173.507 147.592 1.00 125.27 ? 541  VAL B N     1 
ATOM   11597 C  CA    . VAL B 2 541 ? 149.825 174.748 147.266 1.00 124.71 ? 541  VAL B CA    1 
ATOM   11598 C  C     . VAL B 2 541 ? 150.212 175.444 148.561 1.00 125.94 ? 541  VAL B C     1 
ATOM   11599 O  O     . VAL B 2 541 ? 149.558 175.284 149.597 1.00 125.71 ? 541  VAL B O     1 
ATOM   11600 C  CB    . VAL B 2 541 ? 148.954 175.674 146.387 1.00 124.32 ? 541  VAL B CB    1 
ATOM   11601 C  CG1   . VAL B 2 541 ? 148.673 175.019 145.048 1.00 125.23 ? 541  VAL B CG1   1 
ATOM   11602 C  CG2   . VAL B 2 541 ? 147.652 176.013 147.095 1.00 124.80 ? 541  VAL B CG2   1 
ATOM   11603 N  N     . ILE B 2 542 ? 151.290 176.220 148.500 1.00 132.60 ? 542  ILE B N     1 
ATOM   11604 C  CA    . ILE B 2 542 ? 151.795 176.960 149.649 1.00 132.72 ? 542  ILE B CA    1 
ATOM   11605 C  C     . ILE B 2 542 ? 151.502 178.439 149.438 1.00 133.21 ? 542  ILE B C     1 
ATOM   11606 O  O     . ILE B 2 542 ? 151.842 179.005 148.391 1.00 133.10 ? 542  ILE B O     1 
ATOM   11607 C  CB    . ILE B 2 542 ? 153.299 176.709 149.856 1.00 132.57 ? 542  ILE B CB    1 
ATOM   11608 C  CG1   . ILE B 2 542 ? 153.902 177.756 150.804 1.00 133.36 ? 542  ILE B CG1   1 
ATOM   11609 C  CG2   . ILE B 2 542 ? 154.026 176.631 148.513 1.00 133.01 ? 542  ILE B CG2   1 
ATOM   11610 C  CD1   . ILE B 2 542 ? 154.840 178.754 150.142 1.00 133.01 ? 542  ILE B CD1   1 
ATOM   11611 N  N     . ILE B 2 543 ? 150.864 179.063 150.423 1.00 130.46 ? 543  ILE B N     1 
ATOM   11612 C  CA    . ILE B 2 543 ? 150.529 180.479 150.354 1.00 130.40 ? 543  ILE B CA    1 
ATOM   11613 C  C     . ILE B 2 543 ? 151.676 181.288 150.943 1.00 130.27 ? 543  ILE B C     1 
ATOM   11614 O  O     . ILE B 2 543 ? 152.136 181.016 152.059 1.00 129.78 ? 543  ILE B O     1 
ATOM   11615 C  CB    . ILE B 2 543 ? 149.205 180.773 151.080 1.00 130.29 ? 543  ILE B CB    1 
ATOM   11616 C  CG1   . ILE B 2 543 ? 149.139 180.029 152.415 1.00 130.61 ? 543  ILE B CG1   1 
ATOM   11617 C  CG2   . ILE B 2 543 ? 148.024 180.402 150.198 1.00 130.03 ? 543  ILE B CG2   1 
ATOM   11618 C  CD1   . ILE B 2 543 ? 147.868 180.284 153.195 1.00 129.78 ? 543  ILE B CD1   1 
ATOM   11619 N  N     . THR B 2 544 ? 152.148 182.278 150.182 1.00 130.76 ? 544  THR B N     1 
ATOM   11620 C  CA    . THR B 2 544 ? 153.265 183.103 150.631 1.00 131.04 ? 544  THR B CA    1 
ATOM   11621 C  C     . THR B 2 544 ? 152.867 184.006 151.793 1.00 131.34 ? 544  THR B C     1 
ATOM   11622 O  O     . THR B 2 544 ? 153.707 184.330 152.641 1.00 131.09 ? 544  THR B O     1 
ATOM   11623 C  CB    . THR B 2 544 ? 153.792 183.935 149.459 1.00 131.14 ? 544  THR B CB    1 
ATOM   11624 O  OG1   . THR B 2 544 ? 154.042 183.076 148.339 1.00 130.93 ? 544  THR B OG1   1 
ATOM   11625 C  CG2   . THR B 2 544 ? 155.083 184.650 149.829 1.00 130.58 ? 544  THR B CG2   1 
ATOM   11626 N  N     . GLU B 2 545 ? 151.594 184.401 151.860 1.00 126.80 ? 545  GLU B N     1 
ATOM   11627 C  CA    . GLU B 2 545 ? 151.149 185.360 152.865 1.00 125.63 ? 545  GLU B CA    1 
ATOM   11628 C  C     . GLU B 2 545 ? 151.256 184.822 154.286 1.00 125.67 ? 545  GLU B C     1 
ATOM   11629 O  O     . GLU B 2 545 ? 151.294 185.616 155.233 1.00 126.19 ? 545  GLU B O     1 
ATOM   11630 C  CB    . GLU B 2 545 ? 149.707 185.781 152.581 1.00 125.28 ? 545  GLU B CB    1 
ATOM   11631 C  CG    . GLU B 2 545 ? 148.714 184.630 152.578 1.00 126.00 ? 545  GLU B CG    1 
ATOM   11632 C  CD    . GLU B 2 545 ? 147.294 185.083 152.299 1.00 125.90 ? 545  GLU B CD    1 
ATOM   11633 O  OE1   . GLU B 2 545 ? 147.082 186.301 152.117 1.00 125.43 ? 545  GLU B OE1   1 
ATOM   11634 O  OE2   . GLU B 2 545 ? 146.390 184.222 152.261 1.00 125.67 ? 545  GLU B OE2   1 
ATOM   11635 N  N     . LYS B 2 546 ? 151.305 183.500 154.465 1.00 129.43 ? 546  LYS B N     1 
ATOM   11636 C  CA    . LYS B 2 546 ? 151.342 182.914 155.798 1.00 130.10 ? 546  LYS B CA    1 
ATOM   11637 C  C     . LYS B 2 546 ? 152.528 181.980 156.009 1.00 130.61 ? 546  LYS B C     1 
ATOM   11638 O  O     . LYS B 2 546 ? 152.683 181.438 157.110 1.00 131.51 ? 546  LYS B O     1 
ATOM   11639 C  CB    . LYS B 2 546 ? 150.039 182.159 156.088 1.00 129.90 ? 546  LYS B CB    1 
ATOM   11640 C  CG    . LYS B 2 546 ? 148.788 183.020 156.027 1.00 129.71 ? 546  LYS B CG    1 
ATOM   11641 C  CD    . LYS B 2 546 ? 147.552 182.216 156.397 1.00 130.04 ? 546  LYS B CD    1 
ATOM   11642 C  CE    . LYS B 2 546 ? 146.294 183.064 156.312 1.00 129.79 ? 546  LYS B CE    1 
ATOM   11643 N  NZ    . LYS B 2 546 ? 146.060 183.574 154.933 1.00 129.68 ? 546  LYS B NZ    1 
ATOM   11644 N  N     . CYS B 2 547 ? 153.367 181.776 154.999 1.00 134.55 ? 547  CYS B N     1 
ATOM   11645 C  CA    . CYS B 2 547 ? 154.460 180.827 155.119 1.00 134.89 ? 547  CYS B CA    1 
ATOM   11646 C  C     . CYS B 2 547 ? 155.636 181.451 155.866 1.00 135.01 ? 547  CYS B C     1 
ATOM   11647 O  O     . CYS B 2 547 ? 155.749 182.671 156.005 1.00 135.08 ? 547  CYS B O     1 
ATOM   11648 C  CB    . CYS B 2 547 ? 154.895 180.327 153.743 1.00 135.39 ? 547  CYS B CB    1 
ATOM   11649 S  SG    . CYS B 2 547 ? 156.159 179.035 153.811 1.00 136.12 ? 547  CYS B SG    1 
ATOM   11650 N  N     . THR B 2 548 ? 156.530 180.591 156.352 1.00 137.96 ? 548  THR B N     1 
ATOM   11651 C  CA    . THR B 2 548 ? 157.733 181.026 157.048 1.00 138.69 ? 548  THR B CA    1 
ATOM   11652 C  C     . THR B 2 548 ? 158.932 180.206 156.591 1.00 138.48 ? 548  THR B C     1 
ATOM   11653 O  O     . THR B 2 548 ? 158.840 179.451 155.618 1.00 137.86 ? 548  THR B O     1 
ATOM   11654 C  CB    . THR B 2 548 ? 157.560 180.911 158.565 1.00 138.74 ? 548  THR B CB    1 
ATOM   11655 O  OG1   . THR B 2 548 ? 156.940 179.659 158.885 1.00 139.00 ? 548  THR B OG1   1 
ATOM   11656 C  CG2   . THR B 2 548 ? 156.708 182.054 159.102 1.00 138.14 ? 548  THR B CG2   1 
ATOM   11657 N  N     . GLY B 2 549 ? 160.058 180.346 157.284 1.00 140.10 ? 549  GLY B N     1 
ATOM   11658 C  CA    . GLY B 2 549 ? 161.266 179.638 156.909 1.00 139.99 ? 549  GLY B CA    1 
ATOM   11659 C  C     . GLY B 2 549 ? 161.429 178.293 157.584 1.00 140.82 ? 549  GLY B C     1 
ATOM   11660 O  O     . GLY B 2 549 ? 162.359 178.101 158.374 1.00 140.10 ? 549  GLY B O     1 
ATOM   11661 N  N     . CYS B 2 550 ? 160.525 177.354 157.290 1.00 148.85 ? 550  CYS B N     1 
ATOM   11662 C  CA    . CYS B 2 550 ? 160.641 176.013 157.855 1.00 149.01 ? 550  CYS B CA    1 
ATOM   11663 C  C     . CYS B 2 550 ? 161.895 175.300 157.372 1.00 148.93 ? 550  CYS B C     1 
ATOM   11664 O  O     . CYS B 2 550 ? 162.560 174.623 158.165 1.00 148.44 ? 550  CYS B O     1 
ATOM   11665 C  CB    . CYS B 2 550 ? 159.406 175.182 157.509 1.00 149.24 ? 550  CYS B CB    1 
ATOM   11666 S  SG    . CYS B 2 550 ? 158.278 174.910 158.889 1.00 148.75 ? 550  CYS B SG    1 
ATOM   11667 N  N     . THR B 2 551 ? 162.198 175.400 156.072 1.00 146.89 ? 551  THR B N     1 
ATOM   11668 C  CA    . THR B 2 551 ? 163.373 174.813 155.427 1.00 146.95 ? 551  THR B CA    1 
ATOM   11669 C  C     . THR B 2 551 ? 163.297 173.287 155.431 1.00 146.81 ? 551  THR B C     1 
ATOM   11670 O  O     . THR B 2 551 ? 164.170 172.612 154.876 1.00 146.63 ? 551  THR B O     1 
ATOM   11671 C  CB    . THR B 2 551 ? 164.673 175.297 156.087 1.00 146.58 ? 551  THR B CB    1 
ATOM   11672 O  OG1   . THR B 2 551 ? 164.501 176.640 156.558 1.00 146.03 ? 551  THR B OG1   1 
ATOM   11673 C  CG2   . THR B 2 551 ? 165.825 175.278 155.089 1.00 146.40 ? 551  THR B CG2   1 
ATOM   11674 N  N     . ALA B 2 552 ? 162.250 172.737 156.041 1.00 145.41 ? 552  ALA B N     1 
ATOM   11675 C  CA    . ALA B 2 552 ? 161.981 171.308 156.041 1.00 145.31 ? 552  ALA B CA    1 
ATOM   11676 C  C     . ALA B 2 552 ? 160.602 170.974 155.491 1.00 145.18 ? 552  ALA B C     1 
ATOM   11677 O  O     . ALA B 2 552 ? 160.186 169.812 155.560 1.00 144.86 ? 552  ALA B O     1 
ATOM   11678 C  CB    . ALA B 2 552 ? 162.138 170.742 157.454 1.00 145.12 ? 552  ALA B CB    1 
ATOM   11679 N  N     . CYS B 2 553 ? 159.886 171.970 154.959 1.00 144.05 ? 553  CYS B N     1 
ATOM   11680 C  CA    . CYS B 2 553 ? 158.574 171.718 154.373 1.00 144.56 ? 553  CYS B CA    1 
ATOM   11681 C  C     . CYS B 2 553 ? 158.676 170.772 153.184 1.00 144.74 ? 553  CYS B C     1 
ATOM   11682 O  O     . CYS B 2 553 ? 157.872 169.845 153.044 1.00 144.29 ? 553  CYS B O     1 
ATOM   11683 C  CB    . CYS B 2 553 ? 157.924 173.037 153.956 1.00 144.32 ? 553  CYS B CB    1 
ATOM   11684 S  SG    . CYS B 2 553 ? 156.509 172.843 152.849 1.00 145.34 ? 553  CYS B SG    1 
ATOM   11685 N  N     . ALA B 2 554 ? 159.664 170.988 152.318 1.00 137.67 ? 554  ALA B N     1 
ATOM   11686 C  CA    . ALA B 2 554 ? 159.925 170.103 151.193 1.00 136.41 ? 554  ALA B CA    1 
ATOM   11687 C  C     . ALA B 2 554 ? 160.989 169.059 151.508 1.00 136.36 ? 554  ALA B C     1 
ATOM   11688 O  O     . ALA B 2 554 ? 161.327 168.251 150.637 1.00 136.52 ? 554  ALA B O     1 
ATOM   11689 C  CB    . ALA B 2 554 ? 160.336 170.917 149.965 1.00 135.76 ? 554  ALA B CB    1 
ATOM   11690 N  N     . ILE B 2 555 ? 161.521 169.057 152.729 1.00 134.91 ? 555  ILE B N     1 
ATOM   11691 C  CA    . ILE B 2 555 ? 162.556 168.094 153.096 1.00 135.42 ? 555  ILE B CA    1 
ATOM   11692 C  C     . ILE B 2 555 ? 161.949 166.908 153.835 1.00 135.28 ? 555  ILE B C     1 
ATOM   11693 O  O     . ILE B 2 555 ? 162.261 165.748 153.540 1.00 134.76 ? 555  ILE B O     1 
ATOM   11694 C  CB    . ILE B 2 555 ? 163.654 168.777 153.931 1.00 135.04 ? 555  ILE B CB    1 
ATOM   11695 C  CG1   . ILE B 2 555 ? 164.347 169.862 153.106 1.00 135.15 ? 555  ILE B CG1   1 
ATOM   11696 C  CG2   . ILE B 2 555 ? 164.665 167.754 154.426 1.00 134.76 ? 555  ILE B CG2   1 
ATOM   11697 C  CD1   . ILE B 2 555 ? 164.991 169.347 151.838 1.00 134.59 ? 555  ILE B CD1   1 
ATOM   11698 N  N     . MET B 2 556 ? 161.083 167.183 154.814 1.00 132.57 ? 556  MET B N     1 
ATOM   11699 C  CA    . MET B 2 556 ? 160.365 166.121 155.509 1.00 132.35 ? 556  MET B CA    1 
ATOM   11700 C  C     . MET B 2 556 ? 159.541 165.299 154.526 1.00 131.75 ? 556  MET B C     1 
ATOM   11701 O  O     . MET B 2 556 ? 159.586 164.063 154.529 1.00 131.54 ? 556  MET B O     1 
ATOM   11702 C  CB    . MET B 2 556 ? 159.471 166.723 156.598 1.00 131.70 ? 556  MET B CB    1 
ATOM   11703 C  CG    . MET B 2 556 ? 160.231 167.396 157.729 1.00 132.27 ? 556  MET B CG    1 
ATOM   11704 S  SD    . MET B 2 556 ? 159.147 168.312 158.841 1.00 133.57 ? 556  MET B SD    1 
ATOM   11705 C  CE    . MET B 2 556 ? 160.312 168.859 160.086 1.00 131.88 ? 556  MET B CE    1 
ATOM   11706 N  N     . CYS B 2 557 ? 158.789 165.982 153.673 1.00 129.16 ? 557  CYS B N     1 
ATOM   11707 C  CA    . CYS B 2 557 ? 158.071 165.351 152.577 1.00 129.12 ? 557  CYS B CA    1 
ATOM   11708 C  C     . CYS B 2 557 ? 159.060 164.904 151.507 1.00 129.33 ? 557  CYS B C     1 
ATOM   11709 O  O     . CYS B 2 557 ? 159.923 165.688 151.092 1.00 129.48 ? 557  CYS B O     1 
ATOM   11710 C  CB    . CYS B 2 557 ? 157.035 166.314 151.997 1.00 129.56 ? 557  CYS B CB    1 
ATOM   11711 S  SG    . CYS B 2 557 ? 156.963 166.356 150.202 1.00 127.64 ? 557  CYS B SG    1 
ATOM   11712 N  N     . PRO B 2 558 ? 158.989 163.647 151.063 1.00 132.06 ? 558  PRO B N     1 
ATOM   11713 C  CA    . PRO B 2 558 ? 159.901 163.196 149.999 1.00 132.65 ? 558  PRO B CA    1 
ATOM   11714 C  C     . PRO B 2 558 ? 159.745 163.959 148.695 1.00 133.20 ? 558  PRO B C     1 
ATOM   11715 O  O     . PRO B 2 558 ? 160.742 164.151 147.986 1.00 131.50 ? 558  PRO B O     1 
ATOM   11716 C  CB    . PRO B 2 558 ? 159.534 161.714 149.832 1.00 132.33 ? 558  PRO B CB    1 
ATOM   11717 C  CG    . PRO B 2 558 ? 158.883 161.331 151.123 1.00 132.15 ? 558  PRO B CG    1 
ATOM   11718 C  CD    . PRO B 2 558 ? 158.147 162.555 151.574 1.00 132.06 ? 558  PRO B CD    1 
ATOM   11719 N  N     . VAL B 2 559 ? 158.530 164.396 148.365 1.00 133.23 ? 559  VAL B N     1 
ATOM   11720 C  CA    . VAL B 2 559 ? 158.226 165.093 147.113 1.00 133.16 ? 559  VAL B CA    1 
ATOM   11721 C  C     . VAL B 2 559 ? 158.673 164.277 145.902 1.00 133.48 ? 559  VAL B C     1 
ATOM   11722 O  O     . VAL B 2 559 ? 158.113 163.220 145.613 1.00 133.00 ? 559  VAL B O     1 
ATOM   11723 C  CB    . VAL B 2 559 ? 158.853 166.510 147.091 1.00 132.66 ? 559  VAL B CB    1 
ATOM   11724 C  CG1   . VAL B 2 559 ? 159.950 166.608 146.036 1.00 132.36 ? 559  VAL B CG1   1 
ATOM   11725 C  CG2   . VAL B 2 559 ? 157.781 167.561 146.851 1.00 132.45 ? 559  VAL B CG2   1 
ATOM   11726 N  N     . ARG B 2 566 ? 165.082 178.333 151.845 1.00 136.05 ? 566  ARG B N     1 
ATOM   11727 C  CA    . ARG B 2 566 ? 165.893 178.648 153.014 1.00 136.54 ? 566  ARG B CA    1 
ATOM   11728 C  C     . ARG B 2 566 ? 165.461 179.979 153.621 1.00 136.87 ? 566  ARG B C     1 
ATOM   11729 O  O     . ARG B 2 566 ? 165.838 181.044 153.132 1.00 137.16 ? 566  ARG B O     1 
ATOM   11730 C  CB    . ARG B 2 566 ? 167.377 178.692 152.644 1.00 136.12 ? 566  ARG B CB    1 
ATOM   11731 C  CG    . ARG B 2 566 ? 168.292 177.940 153.602 1.00 136.15 ? 566  ARG B CG    1 
ATOM   11732 C  CD    . ARG B 2 566 ? 168.165 178.455 155.027 1.00 136.35 ? 566  ARG B CD    1 
ATOM   11733 N  NE    . ARG B 2 566 ? 168.324 179.902 155.100 1.00 136.87 ? 566  ARG B NE    1 
ATOM   11734 C  CZ    . ARG B 2 566 ? 169.485 180.522 155.261 1.00 136.60 ? 566  ARG B CZ    1 
ATOM   11735 N  NH1   . ARG B 2 566 ? 170.618 179.849 155.371 1.00 136.64 ? 566  ARG B NH1   1 
ATOM   11736 N  NH2   . ARG B 2 566 ? 169.509 181.851 155.313 1.00 135.85 ? 566  ARG B NH2   1 
ATOM   11737 N  N     . GLY B 2 567 ? 164.668 179.910 154.688 1.00 139.19 ? 567  GLY B N     1 
ATOM   11738 C  CA    . GLY B 2 567 ? 164.179 181.116 155.325 1.00 138.99 ? 567  GLY B CA    1 
ATOM   11739 C  C     . GLY B 2 567 ? 163.160 181.882 154.517 1.00 139.31 ? 567  GLY B C     1 
ATOM   11740 O  O     . GLY B 2 567 ? 162.852 183.029 154.850 1.00 138.81 ? 567  GLY B O     1 
ATOM   11741 N  N     . LYS B 2 568 ? 162.628 181.279 153.464 1.00 134.29 ? 568  LYS B N     1 
ATOM   11742 C  CA    . LYS B 2 568 ? 161.681 181.911 152.562 1.00 134.25 ? 568  LYS B CA    1 
ATOM   11743 C  C     . LYS B 2 568 ? 160.577 180.915 152.252 1.00 134.07 ? 568  LYS B C     1 
ATOM   11744 O  O     . LYS B 2 568 ? 160.761 179.705 152.429 1.00 133.09 ? 568  LYS B O     1 
ATOM   11745 C  CB    . LYS B 2 568 ? 162.368 182.370 151.268 1.00 133.53 ? 568  LYS B CB    1 
ATOM   11746 C  CG    . LYS B 2 568 ? 163.005 181.246 150.467 1.00 133.45 ? 568  LYS B CG    1 
ATOM   11747 C  CD    . LYS B 2 568 ? 162.249 180.992 149.173 1.00 133.47 ? 568  LYS B CD    1 
ATOM   11748 C  CE    . LYS B 2 568 ? 162.835 179.815 148.411 1.00 133.26 ? 568  LYS B CE    1 
ATOM   11749 N  NZ    . LYS B 2 568 ? 162.736 178.549 149.189 1.00 132.91 ? 568  LYS B NZ    1 
ATOM   11750 N  N     . PRO B 2 569 ? 159.408 181.391 151.821 1.00 136.31 ? 569  PRO B N     1 
ATOM   11751 C  CA    . PRO B 2 569 ? 158.346 180.467 151.392 1.00 136.40 ? 569  PRO B CA    1 
ATOM   11752 C  C     . PRO B 2 569 ? 158.820 179.565 150.263 1.00 136.94 ? 569  PRO B C     1 
ATOM   11753 O  O     . PRO B 2 569 ? 159.127 180.025 149.161 1.00 136.68 ? 569  PRO B O     1 
ATOM   11754 C  CB    . PRO B 2 569 ? 157.225 181.410 150.943 1.00 135.71 ? 569  PRO B CB    1 
ATOM   11755 C  CG    . PRO B 2 569 ? 157.437 182.635 151.761 1.00 135.82 ? 569  PRO B CG    1 
ATOM   11756 C  CD    . PRO B 2 569 ? 158.927 182.783 151.888 1.00 135.92 ? 569  PRO B CD    1 
ATOM   11757 N  N     . HIS B 2 570 ? 158.870 178.266 150.547 1.00 137.99 ? 570  HIS B N     1 
ATOM   11758 C  CA    . HIS B 2 570 ? 159.462 177.299 149.637 1.00 137.67 ? 570  HIS B CA    1 
ATOM   11759 C  C     . HIS B 2 570 ? 158.521 176.998 148.472 1.00 137.56 ? 570  HIS B C     1 
ATOM   11760 O  O     . HIS B 2 570 ? 157.399 177.506 148.388 1.00 137.07 ? 570  HIS B O     1 
ATOM   11761 C  CB    . HIS B 2 570 ? 159.831 176.023 150.390 1.00 136.76 ? 570  HIS B CB    1 
ATOM   11762 C  CG    . HIS B 2 570 ? 161.038 176.166 151.264 1.00 136.66 ? 570  HIS B CG    1 
ATOM   11763 N  ND1   . HIS B 2 570 ? 161.116 177.095 152.280 1.00 136.29 ? 570  HIS B ND1   1 
ATOM   11764 C  CD2   . HIS B 2 570 ? 162.217 175.501 151.272 1.00 137.37 ? 570  HIS B CD2   1 
ATOM   11765 C  CE1   . HIS B 2 570 ? 162.290 176.994 152.876 1.00 136.73 ? 570  HIS B CE1   1 
ATOM   11766 N  NE2   . HIS B 2 570 ? 162.977 176.034 152.284 1.00 137.43 ? 570  HIS B NE2   1 
ATOM   11767 N  N     . LEU B 2 571 ? 158.991 176.150 147.562 1.00 136.48 ? 571  LEU B N     1 
ATOM   11768 C  CA    . LEU B 2 571 ? 158.286 175.826 146.333 1.00 135.82 ? 571  LEU B CA    1 
ATOM   11769 C  C     . LEU B 2 571 ? 157.734 174.407 146.389 1.00 136.08 ? 571  LEU B C     1 
ATOM   11770 O  O     . LEU B 2 571 ? 158.298 173.526 147.044 1.00 135.26 ? 571  LEU B O     1 
ATOM   11771 C  CB    . LEU B 2 571 ? 159.208 175.984 145.118 1.00 135.27 ? 571  LEU B CB    1 
ATOM   11772 C  CG    . LEU B 2 571 ? 160.715 175.798 145.336 1.00 135.04 ? 571  LEU B CG    1 
ATOM   11773 C  CD1   . LEU B 2 571 ? 161.086 174.343 145.596 1.00 134.60 ? 571  LEU B CD1   1 
ATOM   11774 C  CD2   . LEU B 2 571 ? 161.497 176.348 144.152 1.00 135.07 ? 571  LEU B CD2   1 
ATOM   11775 N  N     . ILE B 2 572 ? 156.616 174.200 145.698 1.00 136.04 ? 572  ILE B N     1 
ATOM   11776 C  CA    . ILE B 2 572 ? 155.968 172.898 145.603 1.00 135.33 ? 572  ILE B CA    1 
ATOM   11777 C  C     . ILE B 2 572 ? 155.772 172.578 144.128 1.00 135.60 ? 572  ILE B C     1 
ATOM   11778 O  O     . ILE B 2 572 ? 155.141 173.354 143.401 1.00 135.76 ? 572  ILE B O     1 
ATOM   11779 C  CB    . ILE B 2 572 ? 154.625 172.866 146.351 1.00 134.77 ? 572  ILE B CB    1 
ATOM   11780 C  CG1   . ILE B 2 572 ? 154.854 172.937 147.862 1.00 135.13 ? 572  ILE B CG1   1 
ATOM   11781 C  CG2   . ILE B 2 572 ? 153.837 171.621 145.987 1.00 134.09 ? 572  ILE B CG2   1 
ATOM   11782 C  CD1   . ILE B 2 572 ? 153.580 172.873 148.676 1.00 134.96 ? 572  ILE B CD1   1 
ATOM   11783 N  N     . ASN B 2 573 ? 156.312 171.441 143.688 1.00 132.87 ? 573  ASN B N     1 
ATOM   11784 C  CA    . ASN B 2 573 ? 156.188 171.004 142.298 1.00 132.27 ? 573  ASN B CA    1 
ATOM   11785 C  C     . ASN B 2 573 ? 154.843 170.303 142.133 1.00 132.03 ? 573  ASN B C     1 
ATOM   11786 O  O     . ASN B 2 573 ? 154.714 169.083 142.264 1.00 131.77 ? 573  ASN B O     1 
ATOM   11787 C  CB    . ASN B 2 573 ? 157.347 170.096 141.912 1.00 132.15 ? 573  ASN B CB    1 
ATOM   11788 C  CG    . ASN B 2 573 ? 158.690 170.786 142.024 1.00 132.48 ? 573  ASN B CG    1 
ATOM   11789 O  OD1   . ASN B 2 573 ? 159.167 171.398 141.068 1.00 131.78 ? 573  ASN B OD1   1 
ATOM   11790 N  ND2   . ASN B 2 573 ? 159.309 170.691 143.194 1.00 132.81 ? 573  ASN B ND2   1 
ATOM   11791 N  N     . GLN B 2 574 ? 153.817 171.107 141.839 1.00 128.39 ? 574  GLN B N     1 
ATOM   11792 C  CA    . GLN B 2 574 ? 152.469 170.570 141.683 1.00 129.08 ? 574  GLN B CA    1 
ATOM   11793 C  C     . GLN B 2 574 ? 152.365 169.652 140.473 1.00 129.69 ? 574  GLN B C     1 
ATOM   11794 O  O     . GLN B 2 574 ? 151.488 168.781 140.429 1.00 129.33 ? 574  GLN B O     1 
ATOM   11795 C  CB    . GLN B 2 574 ? 151.464 171.714 141.566 1.00 128.45 ? 574  GLN B CB    1 
ATOM   11796 C  CG    . GLN B 2 574 ? 151.587 172.752 142.664 1.00 127.97 ? 574  GLN B CG    1 
ATOM   11797 C  CD    . GLN B 2 574 ? 150.856 174.035 142.332 1.00 128.10 ? 574  GLN B CD    1 
ATOM   11798 O  OE1   . GLN B 2 574 ? 149.927 174.043 141.526 1.00 128.48 ? 574  GLN B OE1   1 
ATOM   11799 N  NE2   . GLN B 2 574 ? 151.281 175.133 142.946 1.00 128.06 ? 574  GLN B NE2   1 
ATOM   11800 N  N     . GLU B 2 575 ? 153.239 169.834 139.482 1.00 132.02 ? 575  GLU B N     1 
ATOM   11801 C  CA    . GLU B 2 575 ? 153.209 168.981 138.299 1.00 132.21 ? 575  GLU B CA    1 
ATOM   11802 C  C     . GLU B 2 575 ? 153.601 167.548 138.637 1.00 132.24 ? 575  GLU B C     1 
ATOM   11803 O  O     . GLU B 2 575 ? 153.016 166.598 138.103 1.00 132.25 ? 575  GLU B O     1 
ATOM   11804 C  CB    . GLU B 2 575 ? 154.132 169.547 137.217 1.00 132.17 ? 575  GLU B CB    1 
ATOM   11805 C  CG    . GLU B 2 575 ? 153.719 170.911 136.677 1.00 131.87 ? 575  GLU B CG    1 
ATOM   11806 C  CD    . GLU B 2 575 ? 154.172 172.060 137.559 1.00 131.84 ? 575  GLU B CD    1 
ATOM   11807 O  OE1   . GLU B 2 575 ? 154.900 171.807 138.542 1.00 131.66 ? 575  GLU B OE1   1 
ATOM   11808 O  OE2   . GLU B 2 575 ? 153.801 173.216 137.268 1.00 131.56 ? 575  GLU B OE2   1 
ATOM   11809 N  N     . ALA B 2 576 ? 154.585 167.370 139.520 1.00 136.86 ? 576  ALA B N     1 
ATOM   11810 C  CA    . ALA B 2 576 ? 155.099 166.048 139.859 1.00 137.23 ? 576  ALA B CA    1 
ATOM   11811 C  C     . ALA B 2 576 ? 154.860 165.687 141.322 1.00 138.50 ? 576  ALA B C     1 
ATOM   11812 O  O     . ALA B 2 576 ? 155.546 164.813 141.859 1.00 139.20 ? 576  ALA B O     1 
ATOM   11813 C  CB    . ALA B 2 576 ? 156.590 165.955 139.529 1.00 136.49 ? 576  ALA B CB    1 
ATOM   11814 N  N     . CYS B 2 577 ? 153.905 166.340 141.977 1.00 134.19 ? 577  CYS B N     1 
ATOM   11815 C  CA    . CYS B 2 577 ? 153.606 166.027 143.365 1.00 133.15 ? 577  CYS B CA    1 
ATOM   11816 C  C     . CYS B 2 577 ? 152.893 164.683 143.474 1.00 133.16 ? 577  CYS B C     1 
ATOM   11817 O  O     . CYS B 2 577 ? 152.225 164.222 142.545 1.00 133.59 ? 577  CYS B O     1 
ATOM   11818 C  CB    . CYS B 2 577 ? 152.748 167.122 143.996 1.00 132.73 ? 577  CYS B CB    1 
ATOM   11819 S  SG    . CYS B 2 577 ? 153.603 168.104 145.243 1.00 134.21 ? 577  CYS B SG    1 
ATOM   11820 N  N     . ILE B 2 578 ? 153.046 164.053 144.638 1.00 131.96 ? 578  ILE B N     1 
ATOM   11821 C  CA    . ILE B 2 578 ? 152.412 162.765 144.887 1.00 131.35 ? 578  ILE B CA    1 
ATOM   11822 C  C     . ILE B 2 578 ? 151.006 162.916 145.459 1.00 131.02 ? 578  ILE B C     1 
ATOM   11823 O  O     . ILE B 2 578 ? 150.236 161.944 145.448 1.00 131.48 ? 578  ILE B O     1 
ATOM   11824 C  CB    . ILE B 2 578 ? 153.279 161.915 145.835 1.00 131.31 ? 578  ILE B CB    1 
ATOM   11825 C  CG1   . ILE B 2 578 ? 154.766 162.152 145.559 1.00 131.09 ? 578  ILE B CG1   1 
ATOM   11826 C  CG2   . ILE B 2 578 ? 152.967 160.432 145.680 1.00 130.59 ? 578  ILE B CG2   1 
ATOM   11827 C  CD1   . ILE B 2 578 ? 155.247 161.592 144.235 1.00 131.63 ? 578  ILE B CD1   1 
ATOM   11828 N  N     . LYS B 2 579 ? 150.645 164.112 145.934 1.00 126.45 ? 579  LYS B N     1 
ATOM   11829 C  CA    . LYS B 2 579 ? 149.401 164.341 146.674 1.00 125.95 ? 579  LYS B CA    1 
ATOM   11830 C  C     . LYS B 2 579 ? 149.304 163.404 147.874 1.00 125.61 ? 579  LYS B C     1 
ATOM   11831 O  O     . LYS B 2 579 ? 148.232 162.899 148.212 1.00 124.98 ? 579  LYS B O     1 
ATOM   11832 C  CB    . LYS B 2 579 ? 148.171 164.218 145.772 1.00 124.91 ? 579  LYS B CB    1 
ATOM   11833 C  CG    . LYS B 2 579 ? 147.695 165.544 145.196 1.00 125.01 ? 579  LYS B CG    1 
ATOM   11834 C  CD    . LYS B 2 579 ? 148.731 166.172 144.280 1.00 124.44 ? 579  LYS B CD    1 
ATOM   11835 C  CE    . LYS B 2 579 ? 148.999 165.295 143.071 1.00 124.37 ? 579  LYS B CE    1 
ATOM   11836 N  NZ    . LYS B 2 579 ? 147.766 165.081 142.266 1.00 124.84 ? 579  LYS B NZ    1 
ATOM   11837 N  N     . CYS B 2 580 ? 150.446 163.172 148.522 1.00 129.19 ? 580  CYS B N     1 
ATOM   11838 C  CA    . CYS B 2 580 ? 150.506 162.290 149.681 1.00 128.24 ? 580  CYS B CA    1 
ATOM   11839 C  C     . CYS B 2 580 ? 149.919 162.964 150.914 1.00 129.02 ? 580  CYS B C     1 
ATOM   11840 O  O     . CYS B 2 580 ? 148.941 162.481 151.494 1.00 128.71 ? 580  CYS B O     1 
ATOM   11841 C  CB    . CYS B 2 580 ? 151.955 161.873 149.930 1.00 128.10 ? 580  CYS B CB    1 
ATOM   11842 S  SG    . CYS B 2 580 ? 153.125 163.214 149.645 1.00 129.21 ? 580  CYS B SG    1 
ATOM   11843 N  N     . GLY B 2 581 ? 150.506 164.082 151.328 1.00 132.18 ? 581  GLY B N     1 
ATOM   11844 C  CA    . GLY B 2 581 ? 149.955 164.841 152.428 1.00 131.37 ? 581  GLY B CA    1 
ATOM   11845 C  C     . GLY B 2 581 ? 150.886 165.008 153.607 1.00 131.58 ? 581  GLY B C     1 
ATOM   11846 O  O     . GLY B 2 581 ? 150.446 165.416 154.686 1.00 131.54 ? 581  GLY B O     1 
ATOM   11847 N  N     . THR B 2 582 ? 152.170 164.704 153.432 1.00 131.95 ? 582  THR B N     1 
ATOM   11848 C  CA    . THR B 2 582 ? 153.125 164.877 154.526 1.00 133.11 ? 582  THR B CA    1 
ATOM   11849 C  C     . THR B 2 582 ? 153.730 166.278 154.516 1.00 133.61 ? 582  THR B C     1 
ATOM   11850 O  O     . THR B 2 582 ? 154.938 166.472 154.641 1.00 133.02 ? 582  THR B O     1 
ATOM   11851 C  CB    . THR B 2 582 ? 154.210 163.810 154.440 1.00 132.06 ? 582  THR B CB    1 
ATOM   11852 O  OG1   . THR B 2 582 ? 153.652 162.605 153.902 1.00 131.78 ? 582  THR B OG1   1 
ATOM   11853 C  CG2   . THR B 2 582 ? 154.778 163.512 155.822 1.00 132.20 ? 582  THR B CG2   1 
ATOM   11854 N  N     . CYS B 2 583 ? 152.873 167.266 154.352 1.00 132.97 ? 583  CYS B N     1 
ATOM   11855 C  CA    . CYS B 2 583 ? 153.167 168.674 154.579 1.00 132.53 ? 583  CYS B CA    1 
ATOM   11856 C  C     . CYS B 2 583 ? 152.101 169.361 155.414 1.00 132.49 ? 583  CYS B C     1 
ATOM   11857 O  O     . CYS B 2 583 ? 152.429 170.203 156.251 1.00 132.78 ? 583  CYS B O     1 
ATOM   11858 C  CB    . CYS B 2 583 ? 153.321 169.403 153.239 1.00 30.00  ? 583  CYS B CB    1 
ATOM   11859 S  SG    . CYS B 2 583 ? 154.882 169.107 152.395 1.00 30.00  ? 583  CYS B SG    1 
ATOM   11860 N  N     . TYR B 2 584 ? 150.829 169.011 155.208 1.00 128.59 ? 584  TYR B N     1 
ATOM   11861 C  CA    . TYR B 2 584 ? 149.732 169.693 155.880 1.00 128.52 ? 584  TYR B CA    1 
ATOM   11862 C  C     . TYR B 2 584 ? 149.614 169.294 157.342 1.00 129.33 ? 584  TYR B C     1 
ATOM   11863 O  O     . TYR B 2 584 ? 149.095 170.075 158.145 1.00 129.28 ? 584  TYR B O     1 
ATOM   11864 C  CB    . TYR B 2 584 ? 148.423 169.409 155.142 1.00 127.84 ? 584  TYR B CB    1 
ATOM   11865 C  CG    . TYR B 2 584 ? 147.234 170.173 155.670 1.00 128.63 ? 584  TYR B CG    1 
ATOM   11866 C  CD1   . TYR B 2 584 ? 147.181 171.555 155.583 1.00 129.08 ? 584  TYR B CD1   1 
ATOM   11867 C  CD2   . TYR B 2 584 ? 146.157 169.510 156.243 1.00 128.98 ? 584  TYR B CD2   1 
ATOM   11868 C  CE1   . TYR B 2 584 ? 146.093 172.260 156.061 1.00 129.23 ? 584  TYR B CE1   1 
ATOM   11869 C  CE2   . TYR B 2 584 ? 145.063 170.206 156.723 1.00 128.80 ? 584  TYR B CE2   1 
ATOM   11870 C  CZ    . TYR B 2 584 ? 145.037 171.581 156.629 1.00 129.08 ? 584  TYR B CZ    1 
ATOM   11871 O  OH    . TYR B 2 584 ? 143.952 172.279 157.105 1.00 129.60 ? 584  TYR B OH    1 
ATOM   11872 N  N     . GLU B 2 585 ? 150.081 168.101 157.704 1.00 133.19 ? 585  GLU B N     1 
ATOM   11873 C  CA    . GLU B 2 585 ? 150.104 167.686 159.099 1.00 133.65 ? 585  GLU B CA    1 
ATOM   11874 C  C     . GLU B 2 585 ? 151.360 168.167 159.812 1.00 134.03 ? 585  GLU B C     1 
ATOM   11875 O  O     . GLU B 2 585 ? 151.274 168.721 160.913 1.00 133.08 ? 585  GLU B O     1 
ATOM   11876 C  CB    . GLU B 2 585 ? 149.997 166.161 159.198 1.00 132.83 ? 585  GLU B CB    1 
ATOM   11877 C  CG    . GLU B 2 585 ? 150.083 165.603 160.616 1.00 133.04 ? 585  GLU B CG    1 
ATOM   11878 C  CD    . GLU B 2 585 ? 148.782 165.732 161.392 1.00 133.28 ? 585  GLU B CD    1 
ATOM   11879 O  OE1   . GLU B 2 585 ? 148.294 166.867 161.575 1.00 132.76 ? 585  GLU B OE1   1 
ATOM   11880 O  OE2   . GLU B 2 585 ? 148.243 164.689 161.819 1.00 133.40 ? 585  GLU B OE2   1 
ATOM   11881 N  N     . VAL B 2 586 ? 152.526 167.966 159.205 1.00 140.91 ? 586  VAL B N     1 
ATOM   11882 C  CA    . VAL B 2 586 ? 153.786 168.477 159.767 1.00 141.05 ? 586  VAL B CA    1 
ATOM   11883 C  C     . VAL B 2 586 ? 153.990 169.855 159.148 1.00 140.70 ? 586  VAL B C     1 
ATOM   11884 O  O     . VAL B 2 586 ? 154.681 170.037 158.142 1.00 140.67 ? 586  VAL B O     1 
ATOM   11885 C  CB    . VAL B 2 586 ? 154.961 167.528 159.511 1.00 140.65 ? 586  VAL B CB    1 
ATOM   11886 C  CG1   . VAL B 2 586 ? 156.048 167.743 160.550 1.00 139.38 ? 586  VAL B CG1   1 
ATOM   11887 C  CG2   . VAL B 2 586 ? 154.485 166.083 159.514 1.00 139.75 ? 586  VAL B CG2   1 
ATOM   11888 N  N     . CYS B 2 587 ? 153.367 170.855 159.766 1.00 145.21 ? 587  CYS B N     1 
ATOM   11889 C  CA    . CYS B 2 587 ? 153.420 172.223 159.273 1.00 145.71 ? 587  CYS B CA    1 
ATOM   11890 C  C     . CYS B 2 587 ? 153.560 173.182 160.444 1.00 145.53 ? 587  CYS B C     1 
ATOM   11891 O  O     . CYS B 2 587 ? 153.155 172.879 161.569 1.00 144.84 ? 587  CYS B O     1 
ATOM   11892 C  CB    . CYS B 2 587 ? 152.171 172.580 158.457 1.00 30.00  ? 587  CYS B CB    1 
ATOM   11893 S  SG    . CYS B 2 587 ? 152.120 174.293 157.883 1.00 30.00  ? 587  CYS B SG    1 
ATOM   11894 N  N     . ARG B 2 588 ? 154.139 174.345 160.165 1.00 149.03 ? 588  ARG B N     1 
ATOM   11895 C  CA    . ARG B 2 588 ? 154.272 175.413 161.146 1.00 149.12 ? 588  ARG B CA    1 
ATOM   11896 C  C     . ARG B 2 588 ? 153.298 176.528 160.794 1.00 149.32 ? 588  ARG B C     1 
ATOM   11897 O  O     . ARG B 2 588 ? 153.238 176.961 159.638 1.00 148.74 ? 588  ARG B O     1 
ATOM   11898 C  CB    . ARG B 2 588 ? 155.705 175.941 161.192 1.00 149.24 ? 588  ARG B CB    1 
ATOM   11899 C  CG    . ARG B 2 588 ? 155.987 176.872 162.357 1.00 149.27 ? 588  ARG B CG    1 
ATOM   11900 C  CD    . ARG B 2 588 ? 155.717 176.206 163.700 1.00 149.51 ? 588  ARG B CD    1 
ATOM   11901 N  NE    . ARG B 2 588 ? 156.524 175.008 163.899 1.00 149.47 ? 588  ARG B NE    1 
ATOM   11902 C  CZ    . ARG B 2 588 ? 156.040 173.774 163.948 1.00 148.98 ? 588  ARG B CZ    1 
ATOM   11903 N  NH1   . ARG B 2 588 ? 154.743 173.535 163.840 1.00 149.07 ? 588  ARG B NH1   1 
ATOM   11904 N  NH2   . ARG B 2 588 ? 156.877 172.754 164.116 1.00 148.77 ? 588  ARG B NH2   1 
ATOM   11905 N  N     . PHE B 2 589 ? 152.544 176.979 161.790 1.00 143.80 ? 589  PHE B N     1 
ATOM   11906 C  CA    . PHE B 2 589 ? 151.424 177.924 161.626 1.00 143.28 ? 589  PHE B CA    1 
ATOM   11907 C  C     . PHE B 2 589 ? 150.417 177.262 160.679 1.00 142.74 ? 589  PHE B C     1 
ATOM   11908 O  O     . PHE B 2 589 ? 150.175 176.050 160.782 1.00 143.13 ? 589  PHE B O     1 
ATOM   11909 C  CB    . PHE B 2 589 ? 151.926 179.285 161.176 1.00 143.09 ? 589  PHE B CB    1 
ATOM   11910 C  CG    . PHE B 2 589 ? 153.115 179.781 161.946 1.00 143.10 ? 589  PHE B CG    1 
ATOM   11911 C  CD1   . PHE B 2 589 ? 152.993 180.154 163.274 1.00 142.67 ? 589  PHE B CD1   1 
ATOM   11912 C  CD2   . PHE B 2 589 ? 154.353 179.890 161.336 1.00 143.12 ? 589  PHE B CD2   1 
ATOM   11913 C  CE1   . PHE B 2 589 ? 154.087 180.615 163.983 1.00 142.65 ? 589  PHE B CE1   1 
ATOM   11914 C  CE2   . PHE B 2 589 ? 155.451 180.352 162.038 1.00 143.30 ? 589  PHE B CE2   1 
ATOM   11915 C  CZ    . PHE B 2 589 ? 155.317 180.714 163.364 1.00 143.10 ? 589  PHE B CZ    1 
ATOM   11916 N  N     . ASN B 2 590 ? 149.818 178.014 159.758 1.00 138.75 ? 590  ASN B N     1 
ATOM   11917 C  CA    . ASN B 2 590 ? 148.915 177.476 158.741 1.00 138.73 ? 590  ASN B CA    1 
ATOM   11918 C  C     . ASN B 2 590 ? 149.381 178.056 157.409 1.00 138.63 ? 590  ASN B C     1 
ATOM   11919 O  O     . ASN B 2 590 ? 148.938 179.128 156.991 1.00 138.56 ? 590  ASN B O     1 
ATOM   11920 C  CB    . ASN B 2 590 ? 147.459 177.818 159.049 1.00 138.99 ? 590  ASN B CB    1 
ATOM   11921 C  CG    . ASN B 2 590 ? 147.276 179.260 159.481 1.00 139.08 ? 590  ASN B CG    1 
ATOM   11922 O  OD1   . ASN B 2 590 ? 148.188 179.876 160.032 1.00 139.18 ? 590  ASN B OD1   1 
ATOM   11923 N  ND2   . ASN B 2 590 ? 146.091 179.806 159.232 1.00 138.59 ? 590  ASN B ND2   1 
ATOM   11924 N  N     . ALA B 2 591 ? 150.285 177.341 156.742 1.00 134.64 ? 591  ALA B N     1 
ATOM   11925 C  CA    . ALA B 2 591 ? 150.960 177.864 155.568 1.00 135.03 ? 591  ALA B CA    1 
ATOM   11926 C  C     . ALA B 2 591 ? 150.647 177.124 154.276 1.00 135.14 ? 591  ALA B C     1 
ATOM   11927 O  O     . ALA B 2 591 ? 151.087 177.573 153.212 1.00 135.38 ? 591  ALA B O     1 
ATOM   11928 C  CB    . ALA B 2 591 ? 152.480 177.852 155.784 1.00 134.80 ? 591  ALA B CB    1 
ATOM   11929 N  N     . ILE B 2 592 ? 149.919 176.011 154.327 1.00 127.95 ? 592  ILE B N     1 
ATOM   11930 C  CA    . ILE B 2 592 ? 149.646 175.195 153.147 1.00 127.30 ? 592  ILE B CA    1 
ATOM   11931 C  C     . ILE B 2 592 ? 148.147 174.931 153.098 1.00 127.30 ? 592  ILE B C     1 
ATOM   11932 O  O     . ILE B 2 592 ? 147.640 174.061 153.814 1.00 127.53 ? 592  ILE B O     1 
ATOM   11933 C  CB    . ILE B 2 592 ? 150.436 173.882 153.150 1.00 126.82 ? 592  ILE B CB    1 
ATOM   11934 C  CG1   . ILE B 2 592 ? 151.935 174.167 153.176 1.00 126.76 ? 592  ILE B CG1   1 
ATOM   11935 C  CG2   . ILE B 2 592 ? 150.092 173.049 151.929 1.00 126.53 ? 592  ILE B CG2   1 
ATOM   11936 C  CD1   . ILE B 2 592 ? 152.790 172.938 153.180 1.00 126.14 ? 592  ILE B CD1   1 
ATOM   11937 N  N     . GLU B 2 593 ? 147.433 175.683 152.267 1.00 121.51 ? 593  GLU B N     1 
ATOM   11938 C  CA    . GLU B 2 593 ? 146.069 175.322 151.927 1.00 120.28 ? 593  GLU B CA    1 
ATOM   11939 C  C     . GLU B 2 593 ? 146.081 174.198 150.893 1.00 120.60 ? 593  GLU B C     1 
ATOM   11940 O  O     . GLU B 2 593 ? 147.099 173.917 150.255 1.00 119.38 ? 593  GLU B O     1 
ATOM   11941 C  CB    . GLU B 2 593 ? 145.306 176.533 151.399 1.00 120.05 ? 593  GLU B CB    1 
ATOM   11942 C  CG    . GLU B 2 593 ? 145.902 177.128 150.138 1.00 121.10 ? 593  GLU B CG    1 
ATOM   11943 C  CD    . GLU B 2 593 ? 145.114 178.316 149.627 1.00 121.21 ? 593  GLU B CD    1 
ATOM   11944 O  OE1   . GLU B 2 593 ? 144.157 178.735 150.310 1.00 121.68 ? 593  GLU B OE1   1 
ATOM   11945 O  OE2   . GLU B 2 593 ? 145.451 178.828 148.539 1.00 120.95 ? 593  GLU B OE2   1 
ATOM   11946 N  N     . ILE B 2 594 ? 144.935 173.545 150.725 1.00 118.47 ? 594  ILE B N     1 
ATOM   11947 C  CA    . ILE B 2 594 ? 144.879 172.389 149.838 1.00 117.55 ? 594  ILE B CA    1 
ATOM   11948 C  C     . ILE B 2 594 ? 144.415 172.814 148.452 1.00 117.29 ? 594  ILE B C     1 
ATOM   11949 O  O     . ILE B 2 594 ? 145.179 172.730 147.483 1.00 116.26 ? 594  ILE B O     1 
ATOM   11950 C  CB    . ILE B 2 594 ? 143.963 171.295 150.416 1.00 116.67 ? 594  ILE B CB    1 
ATOM   11951 C  CG1   . ILE B 2 594 ? 144.499 170.814 151.765 1.00 117.58 ? 594  ILE B CG1   1 
ATOM   11952 C  CG2   . ILE B 2 594 ? 143.844 170.134 149.445 1.00 115.23 ? 594  ILE B CG2   1 
ATOM   11953 C  CD1   . ILE B 2 594 ? 143.675 169.711 152.393 1.00 117.96 ? 594  ILE B CD1   1 
ATOM   11954 N  N     . THR B 2 595 ? 143.169 173.289 148.356 1.00 115.21 ? 595  THR B N     1 
ATOM   11955 C  CA    . THR B 2 595 ? 142.541 173.744 147.114 1.00 114.72 ? 595  THR B CA    1 
ATOM   11956 C  C     . THR B 2 595 ? 142.473 172.658 146.043 1.00 112.49 ? 595  THR B C     1 
ATOM   11957 O  O     . THR B 2 595 ? 143.051 171.576 146.190 1.00 110.38 ? 595  THR B O     1 
ATOM   11958 C  CB    . THR B 2 595 ? 143.254 174.980 146.549 1.00 115.98 ? 595  THR B CB    1 
ATOM   11959 O  OG1   . THR B 2 595 ? 144.565 174.623 146.090 1.00 115.56 ? 595  THR B OG1   1 
ATOM   11960 C  CG2   . THR B 2 595 ? 143.365 176.064 147.608 1.00 114.96 ? 595  THR B CG2   1 
ATOM   11961 N  N     . ASP B 2 596 ? 141.749 172.937 144.965 1.00 109.38 ? 596  ASP B N     1 
ATOM   11962 C  CA    . ASP B 2 596 ? 141.596 171.991 143.875 1.00 109.89 ? 596  ASP B CA    1 
ATOM   11963 C  C     . ASP B 2 596 ? 142.753 172.118 142.887 1.00 111.69 ? 596  ASP B C     1 
ATOM   11964 O  O     . ASP B 2 596 ? 143.582 173.028 142.967 1.00 112.55 ? 596  ASP B O     1 
ATOM   11965 C  CB    . ASP B 2 596 ? 140.263 172.212 143.167 1.00 109.84 ? 596  ASP B CB    1 
ATOM   11966 C  CG    . ASP B 2 596 ? 139.095 172.217 144.124 1.00 110.02 ? 596  ASP B CG    1 
ATOM   11967 O  OD1   . ASP B 2 596 ? 139.101 171.401 145.069 1.00 109.09 ? 596  ASP B OD1   1 
ATOM   11968 O  OD2   . ASP B 2 596 ? 138.177 173.041 143.940 1.00 111.37 ? 596  ASP B OD2   1 
ATOM   11969 N  N     . ALA B 2 597 ? 142.802 171.185 141.942 1.00 113.91 ? 597  ALA B N     1 
ATOM   11970 C  CA    . ALA B 2 597 ? 143.826 171.202 140.905 1.00 113.40 ? 597  ALA B CA    1 
ATOM   11971 C  C     . ALA B 2 597 ? 143.200 171.449 139.539 1.00 113.97 ? 597  ALA B C     1 
ATOM   11972 O  O     . ALA B 2 597 ? 141.978 171.434 139.397 1.00 114.43 ? 597  ALA B O     1 
ATOM   11973 C  CB    . ALA B 2 597 ? 144.606 169.899 140.904 1.00 113.15 ? 597  ALA B CB    1 
ATOM   11974 N  N     . ILE C 3 3   ? 164.699 113.407 160.139 1.00 95.61  ? 3    ILE C N     1 
ATOM   11975 C  CA    . ILE C 3 3   ? 164.429 114.358 159.071 1.00 96.67  ? 3    ILE C CA    1 
ATOM   11976 C  C     . ILE C 3 3   ? 163.420 115.386 159.573 1.00 95.45  ? 3    ILE C C     1 
ATOM   11977 O  O     . ILE C 3 3   ? 162.757 115.168 160.585 1.00 93.73  ? 3    ILE C O     1 
ATOM   11978 C  CB    . ILE C 3 3   ? 163.933 113.639 157.798 1.00 95.82  ? 3    ILE C CB    1 
ATOM   11979 C  CG1   . ILE C 3 3   ? 164.228 114.476 156.550 1.00 94.89  ? 3    ILE C CG1   1 
ATOM   11980 C  CG2   . ILE C 3 3   ? 162.449 113.321 157.901 1.00 94.87  ? 3    ILE C CG2   1 
ATOM   11981 C  CD1   . ILE C 3 3   ? 163.813 113.816 155.255 1.00 94.34  ? 3    ILE C CD1   1 
ATOM   11982 N  N     . GLN C 3 4   ? 163.314 116.513 158.866 1.00 90.36  ? 4    GLN C N     1 
ATOM   11983 C  CA    . GLN C 3 4   ? 162.419 117.584 159.289 1.00 90.83  ? 4    GLN C CA    1 
ATOM   11984 C  C     . GLN C 3 4   ? 160.950 117.203 159.165 1.00 89.89  ? 4    GLN C C     1 
ATOM   11985 O  O     . GLN C 3 4   ? 160.105 117.836 159.804 1.00 87.05  ? 4    GLN C O     1 
ATOM   11986 C  CB    . GLN C 3 4   ? 162.686 118.853 158.478 1.00 90.54  ? 4    GLN C CB    1 
ATOM   11987 C  CG    . GLN C 3 4   ? 164.122 119.351 158.519 1.00 89.20  ? 4    GLN C CG    1 
ATOM   11988 C  CD    . GLN C 3 4   ? 165.004 118.687 157.481 1.00 89.47  ? 4    GLN C CD    1 
ATOM   11989 O  OE1   . GLN C 3 4   ? 164.592 117.739 156.815 1.00 88.72  ? 4    GLN C OE1   1 
ATOM   11990 N  NE2   . GLN C 3 4   ? 166.226 119.185 157.339 1.00 88.33  ? 4    GLN C NE2   1 
ATOM   11991 N  N     . LEU C 3 5   ? 160.628 116.186 158.370 1.00 84.10  ? 5    LEU C N     1 
ATOM   11992 C  CA    . LEU C 3 5   ? 159.251 115.772 158.134 1.00 81.97  ? 5    LEU C CA    1 
ATOM   11993 C  C     . LEU C 3 5   ? 158.702 114.867 159.234 1.00 82.45  ? 5    LEU C C     1 
ATOM   11994 O  O     . LEU C 3 5   ? 157.679 114.206 159.024 1.00 82.54  ? 5    LEU C O     1 
ATOM   11995 C  CB    . LEU C 3 5   ? 159.143 115.074 156.775 1.00 82.83  ? 5    LEU C CB    1 
ATOM   11996 C  CG    . LEU C 3 5   ? 158.832 115.919 155.535 1.00 83.70  ? 5    LEU C CG    1 
ATOM   11997 C  CD1   . LEU C 3 5   ? 159.627 117.212 155.495 1.00 83.65  ? 5    LEU C CD1   1 
ATOM   11998 C  CD2   . LEU C 3 5   ? 159.102 115.108 154.283 1.00 82.28  ? 5    LEU C CD2   1 
ATOM   11999 N  N     . GLU C 3 6   ? 159.357 114.826 160.396 1.00 80.51  ? 6    GLU C N     1 
ATOM   12000 C  CA    . GLU C 3 6   ? 158.880 114.015 161.511 1.00 78.93  ? 6    GLU C CA    1 
ATOM   12001 C  C     . GLU C 3 6   ? 157.638 114.601 162.168 1.00 79.88  ? 6    GLU C C     1 
ATOM   12002 O  O     . GLU C 3 6   ? 156.936 113.882 162.885 1.00 82.64  ? 6    GLU C O     1 
ATOM   12003 C  CB    . GLU C 3 6   ? 159.986 113.862 162.555 1.00 80.05  ? 6    GLU C CB    1 
ATOM   12004 C  CG    . GLU C 3 6   ? 160.307 112.428 162.926 1.00 82.05  ? 6    GLU C CG    1 
ATOM   12005 C  CD    . GLU C 3 6   ? 161.091 111.709 161.848 1.00 83.21  ? 6    GLU C CD    1 
ATOM   12006 O  OE1   . GLU C 3 6   ? 161.712 112.392 161.007 1.00 82.51  ? 6    GLU C OE1   1 
ATOM   12007 O  OE2   . GLU C 3 6   ? 161.088 110.461 161.842 1.00 82.49  ? 6    GLU C OE2   1 
ATOM   12008 N  N     . TYR C 3 7   ? 157.358 115.888 161.948 1.00 69.61  ? 7    TYR C N     1 
ATOM   12009 C  CA    . TYR C 3 7   ? 156.199 116.525 162.562 1.00 68.29  ? 7    TYR C CA    1 
ATOM   12010 C  C     . TYR C 3 7   ? 154.883 115.984 162.022 1.00 66.47  ? 7    TYR C C     1 
ATOM   12011 O  O     . TYR C 3 7   ? 153.864 116.069 162.713 1.00 64.41  ? 7    TYR C O     1 
ATOM   12012 C  CB    . TYR C 3 7   ? 156.258 118.039 162.347 1.00 65.74  ? 7    TYR C CB    1 
ATOM   12013 C  CG    . TYR C 3 7   ? 156.047 118.462 160.911 1.00 66.45  ? 7    TYR C CG    1 
ATOM   12014 C  CD1   . TYR C 3 7   ? 157.100 118.475 160.013 1.00 62.78  ? 7    TYR C CD1   1 
ATOM   12015 C  CD2   . TYR C 3 7   ? 154.796 118.852 160.456 1.00 70.39  ? 7    TYR C CD2   1 
ATOM   12016 C  CE1   . TYR C 3 7   ? 156.915 118.858 158.702 1.00 59.22  ? 7    TYR C CE1   1 
ATOM   12017 C  CE2   . TYR C 3 7   ? 154.602 119.233 159.147 1.00 71.61  ? 7    TYR C CE2   1 
ATOM   12018 C  CZ    . TYR C 3 7   ? 155.665 119.235 158.276 1.00 64.27  ? 7    TYR C CZ    1 
ATOM   12019 O  OH    . TYR C 3 7   ? 155.477 119.618 156.969 1.00 64.36  ? 7    TYR C OH    1 
ATOM   12020 N  N     . ILE C 3 8   ? 154.885 115.440 160.803 1.00 69.72  ? 8    ILE C N     1 
ATOM   12021 C  CA    . ILE C 3 8   ? 153.654 114.958 160.186 1.00 68.41  ? 8    ILE C CA    1 
ATOM   12022 C  C     . ILE C 3 8   ? 153.082 113.781 160.959 1.00 72.25  ? 8    ILE C C     1 
ATOM   12023 O  O     . ILE C 3 8   ? 151.866 113.556 160.956 1.00 72.04  ? 8    ILE C O     1 
ATOM   12024 C  CB    . ILE C 3 8   ? 153.915 114.594 158.711 1.00 65.93  ? 8    ILE C CB    1 
ATOM   12025 C  CG1   . ILE C 3 8   ? 154.702 115.709 158.025 1.00 68.59  ? 8    ILE C CG1   1 
ATOM   12026 C  CG2   . ILE C 3 8   ? 152.610 114.349 157.977 1.00 62.89  ? 8    ILE C CG2   1 
ATOM   12027 C  CD1   . ILE C 3 8   ? 154.911 115.490 156.555 1.00 67.77  ? 8    ILE C CD1   1 
ATOM   12028 N  N     . TYR C 3 9   ? 153.933 113.024 161.643 1.00 75.30  ? 9    TYR C N     1 
ATOM   12029 C  CA    . TYR C 3 9   ? 153.506 111.794 162.293 1.00 74.77  ? 9    TYR C CA    1 
ATOM   12030 C  C     . TYR C 3 9   ? 152.953 112.013 163.694 1.00 75.72  ? 9    TYR C C     1 
ATOM   12031 O  O     . TYR C 3 9   ? 152.419 111.069 164.286 1.00 77.19  ? 9    TYR C O     1 
ATOM   12032 C  CB    . TYR C 3 9   ? 154.669 110.799 162.319 1.00 74.93  ? 9    TYR C CB    1 
ATOM   12033 C  CG    . TYR C 3 9   ? 155.036 110.322 160.933 1.00 75.55  ? 9    TYR C CG    1 
ATOM   12034 C  CD1   . TYR C 3 9   ? 155.865 111.076 160.114 1.00 74.67  ? 9    TYR C CD1   1 
ATOM   12035 C  CD2   . TYR C 3 9   ? 154.531 109.132 160.432 1.00 76.37  ? 9    TYR C CD2   1 
ATOM   12036 C  CE1   . TYR C 3 9   ? 156.189 110.653 158.842 1.00 74.84  ? 9    TYR C CE1   1 
ATOM   12037 C  CE2   . TYR C 3 9   ? 154.851 108.701 159.161 1.00 76.74  ? 9    TYR C CE2   1 
ATOM   12038 C  CZ    . TYR C 3 9   ? 155.679 109.466 158.371 1.00 78.08  ? 9    TYR C CZ    1 
ATOM   12039 O  OH    . TYR C 3 9   ? 156.003 109.040 157.105 1.00 79.57  ? 9    TYR C OH    1 
ATOM   12040 N  N     . HIS C 3 10  ? 153.053 113.226 164.232 1.00 74.28  ? 10   HIS C N     1 
ATOM   12041 C  CA    . HIS C 3 10  ? 152.366 113.576 165.467 1.00 73.58  ? 10   HIS C CA    1 
ATOM   12042 C  C     . HIS C 3 10  ? 150.932 114.026 165.231 1.00 73.45  ? 10   HIS C C     1 
ATOM   12043 O  O     . HIS C 3 10  ? 150.174 114.162 166.196 1.00 73.12  ? 10   HIS C O     1 
ATOM   12044 C  CB    . HIS C 3 10  ? 153.128 114.680 166.206 1.00 74.70  ? 10   HIS C CB    1 
ATOM   12045 C  CG    . HIS C 3 10  ? 154.528 114.304 166.581 1.00 77.32  ? 10   HIS C CG    1 
ATOM   12046 N  ND1   . HIS C 3 10  ? 155.460 115.230 166.995 1.00 76.11  ? 10   HIS C ND1   1 
ATOM   12047 C  CD2   . HIS C 3 10  ? 155.153 113.103 166.608 1.00 75.26  ? 10   HIS C CD2   1 
ATOM   12048 C  CE1   . HIS C 3 10  ? 156.600 114.617 167.258 1.00 76.66  ? 10   HIS C CE1   1 
ATOM   12049 N  NE2   . HIS C 3 10  ? 156.440 113.326 167.031 1.00 74.51  ? 10   HIS C NE2   1 
ATOM   12050 N  N     . TYR C 3 11  ? 150.548 114.264 163.982 1.00 65.56  ? 11   TYR C N     1 
ATOM   12051 C  CA    . TYR C 3 11  ? 149.186 114.628 163.630 1.00 61.07  ? 11   TYR C CA    1 
ATOM   12052 C  C     . TYR C 3 11  ? 148.433 113.407 163.122 1.00 60.15  ? 11   TYR C C     1 
ATOM   12053 O  O     . TYR C 3 11  ? 149.009 112.517 162.492 1.00 62.91  ? 11   TYR C O     1 
ATOM   12054 C  CB    . TYR C 3 11  ? 149.164 115.725 162.567 1.00 58.13  ? 11   TYR C CB    1 
ATOM   12055 C  CG    . TYR C 3 11  ? 149.553 117.090 163.079 1.00 58.87  ? 11   TYR C CG    1 
ATOM   12056 C  CD1   . TYR C 3 11  ? 148.615 117.925 163.667 1.00 61.40  ? 11   TYR C CD1   1 
ATOM   12057 C  CD2   . TYR C 3 11  ? 150.856 117.548 162.966 1.00 59.27  ? 11   TYR C CD2   1 
ATOM   12058 C  CE1   . TYR C 3 11  ? 148.966 119.173 164.130 1.00 62.75  ? 11   TYR C CE1   1 
ATOM   12059 C  CE2   . TYR C 3 11  ? 151.215 118.794 163.423 1.00 60.91  ? 11   TYR C CE2   1 
ATOM   12060 C  CZ    . TYR C 3 11  ? 150.267 119.603 164.005 1.00 64.80  ? 11   TYR C CZ    1 
ATOM   12061 O  OH    . TYR C 3 11  ? 150.625 120.847 164.466 1.00 63.80  ? 11   TYR C OH    1 
ATOM   12062 N  N     . GLU C 3 12  ? 147.140 113.378 163.407 1.00 56.88  ? 12   GLU C N     1 
ATOM   12063 C  CA    . GLU C 3 12  ? 146.312 112.250 163.013 1.00 57.22  ? 12   GLU C CA    1 
ATOM   12064 C  C     . GLU C 3 12  ? 146.241 112.161 161.491 1.00 60.41  ? 12   GLU C C     1 
ATOM   12065 O  O     . GLU C 3 12  ? 145.957 113.168 160.829 1.00 62.50  ? 12   GLU C O     1 
ATOM   12066 C  CB    . GLU C 3 12  ? 144.911 112.397 163.600 1.00 58.29  ? 12   GLU C CB    1 
ATOM   12067 C  CG    . GLU C 3 12  ? 143.960 111.284 163.218 1.00 61.36  ? 12   GLU C CG    1 
ATOM   12068 C  CD    . GLU C 3 12  ? 142.613 111.417 163.897 1.00 65.30  ? 12   GLU C CD    1 
ATOM   12069 O  OE1   . GLU C 3 12  ? 142.415 112.401 164.639 1.00 62.71  ? 12   GLU C OE1   1 
ATOM   12070 O  OE2   . GLU C 3 12  ? 141.752 110.537 163.689 1.00 64.36  ? 12   GLU C OE2   1 
ATOM   12071 N  N     . PRO C 3 13  ? 146.492 110.992 160.901 1.00 60.69  ? 13   PRO C N     1 
ATOM   12072 C  CA    . PRO C 3 13  ? 146.434 110.879 159.438 1.00 58.45  ? 13   PRO C CA    1 
ATOM   12073 C  C     . PRO C 3 13  ? 145.017 110.959 158.895 1.00 59.42  ? 13   PRO C C     1 
ATOM   12074 O  O     . PRO C 3 13  ? 144.501 109.993 158.327 1.00 58.97  ? 13   PRO C O     1 
ATOM   12075 C  CB    . PRO C 3 13  ? 147.063 109.508 159.168 1.00 55.45  ? 13   PRO C CB    1 
ATOM   12076 C  CG    . PRO C 3 13  ? 146.832 108.742 160.418 1.00 57.15  ? 13   PRO C CG    1 
ATOM   12077 C  CD    . PRO C 3 13  ? 146.928 109.738 161.536 1.00 58.79  ? 13   PRO C CD    1 
ATOM   12078 N  N     . ASN C 3 14  ? 144.385 112.117 159.064 1.00 53.39  ? 14   ASN C N     1 
ATOM   12079 C  CA    . ASN C 3 14  ? 143.084 112.444 158.515 1.00 51.29  ? 14   ASN C CA    1 
ATOM   12080 C  C     . ASN C 3 14  ? 143.178 113.731 157.708 1.00 49.47  ? 14   ASN C C     1 
ATOM   12081 O  O     . ASN C 3 14  ? 144.036 114.575 157.982 1.00 48.20  ? 14   ASN C O     1 
ATOM   12082 C  CB    . ASN C 3 14  ? 142.032 112.609 159.619 1.00 46.60  ? 14   ASN C CB    1 
ATOM   12083 C  CG    . ASN C 3 14  ? 141.481 111.286 160.095 1.00 52.54  ? 14   ASN C CG    1 
ATOM   12084 O  OD1   . ASN C 3 14  ? 141.593 110.272 159.409 1.00 53.21  ? 14   ASN C OD1   1 
ATOM   12085 N  ND2   . ASN C 3 14  ? 140.871 111.289 161.272 1.00 53.23  ? 14   ASN C ND2   1 
ATOM   12086 N  N     . PRO C 3 15  ? 142.328 113.901 156.693 1.00 41.78  ? 15   PRO C N     1 
ATOM   12087 C  CA    . PRO C 3 15  ? 142.399 115.120 155.872 1.00 39.26  ? 15   PRO C CA    1 
ATOM   12088 C  C     . PRO C 3 15  ? 142.122 116.401 156.637 1.00 44.47  ? 15   PRO C C     1 
ATOM   12089 O  O     . PRO C 3 15  ? 142.576 117.466 156.204 1.00 49.05  ? 15   PRO C O     1 
ATOM   12090 C  CB    . PRO C 3 15  ? 141.338 114.874 154.792 1.00 45.19  ? 15   PRO C CB    1 
ATOM   12091 C  CG    . PRO C 3 15  ? 141.207 113.393 154.727 1.00 44.04  ? 15   PRO C CG    1 
ATOM   12092 C  CD    . PRO C 3 15  ? 141.388 112.917 156.130 1.00 45.14  ? 15   PRO C CD    1 
ATOM   12093 N  N     . SER C 3 16  ? 141.386 116.344 157.751 1.00 42.80  ? 16   SER C N     1 
ATOM   12094 C  CA    . SER C 3 16  ? 141.117 117.554 158.518 1.00 37.15  ? 16   SER C CA    1 
ATOM   12095 C  C     . SER C 3 16  ? 142.372 118.113 159.170 1.00 38.35  ? 16   SER C C     1 
ATOM   12096 O  O     . SER C 3 16  ? 142.410 119.305 159.491 1.00 40.18  ? 16   SER C O     1 
ATOM   12097 C  CB    . SER C 3 16  ? 140.061 117.285 159.588 1.00 32.27  ? 16   SER C CB    1 
ATOM   12098 O  OG    . SER C 3 16  ? 140.643 116.662 160.717 1.00 35.29  ? 16   SER C OG    1 
ATOM   12099 N  N     . SER C 3 17  ? 143.398 117.287 159.366 1.00 35.41  ? 17   SER C N     1 
ATOM   12100 C  CA    . SER C 3 17  ? 144.665 117.747 159.918 1.00 37.13  ? 17   SER C CA    1 
ATOM   12101 C  C     . SER C 3 17  ? 145.484 118.554 158.925 1.00 37.31  ? 17   SER C C     1 
ATOM   12102 O  O     . SER C 3 17  ? 146.608 118.940 159.258 1.00 39.59  ? 17   SER C O     1 
ATOM   12103 C  CB    . SER C 3 17  ? 145.485 116.554 160.410 1.00 36.97  ? 17   SER C CB    1 
ATOM   12104 O  OG    . SER C 3 17  ? 144.783 115.830 161.401 1.00 41.90  ? 17   SER C OG    1 
ATOM   12105 N  N     . LEU C 3 18  ? 144.951 118.814 157.730 1.00 33.06  ? 18   LEU C N     1 
ATOM   12106 C  CA    . LEU C 3 18  ? 145.713 119.504 156.694 1.00 30.07  ? 18   LEU C CA    1 
ATOM   12107 C  C     . LEU C 3 18  ? 146.076 120.922 157.119 1.00 38.21  ? 18   LEU C C     1 
ATOM   12108 O  O     . LEU C 3 18  ? 147.249 121.310 157.081 1.00 39.32  ? 18   LEU C O     1 
ATOM   12109 C  CB    . LEU C 3 18  ? 144.906 119.516 155.395 1.00 28.48  ? 18   LEU C CB    1 
ATOM   12110 C  CG    . LEU C 3 18  ? 145.517 120.147 154.147 1.00 27.07  ? 18   LEU C CG    1 
ATOM   12111 C  CD1   . LEU C 3 18  ? 146.790 119.428 153.751 1.00 35.39  ? 18   LEU C CD1   1 
ATOM   12112 C  CD2   . LEU C 3 18  ? 144.511 120.118 153.015 1.00 31.79  ? 18   LEU C CD2   1 
ATOM   12113 N  N     . ILE C 3 19  ? 145.081 121.710 157.534 1.00 40.54  ? 19   ILE C N     1 
ATOM   12114 C  CA    . ILE C 3 19  ? 145.348 123.097 157.923 1.00 31.48  ? 19   ILE C CA    1 
ATOM   12115 C  C     . ILE C 3 19  ? 146.270 123.189 159.134 1.00 44.37  ? 19   ILE C C     1 
ATOM   12116 O  O     . ILE C 3 19  ? 147.202 124.011 159.108 1.00 50.76  ? 19   ILE C O     1 
ATOM   12117 C  CB    . ILE C 3 19  ? 144.023 123.859 158.109 1.00 36.41  ? 19   ILE C CB    1 
ATOM   12118 C  CG1   . ILE C 3 19  ? 143.235 123.865 156.801 1.00 38.22  ? 19   ILE C CG1   1 
ATOM   12119 C  CG2   . ILE C 3 19  ? 144.284 125.281 158.575 1.00 39.58  ? 19   ILE C CG2   1 
ATOM   12120 C  CD1   . ILE C 3 19  ? 142.034 124.769 156.816 1.00 35.16  ? 19   ILE C CD1   1 
ATOM   12121 N  N     . PRO C 3 20  ? 146.082 122.409 160.212 1.00 48.00  ? 20   PRO C N     1 
ATOM   12122 C  CA    . PRO C 3 20  ? 147.125 122.378 161.253 1.00 41.18  ? 20   PRO C CA    1 
ATOM   12123 C  C     . PRO C 3 20  ? 148.486 121.937 160.739 1.00 43.05  ? 20   PRO C C     1 
ATOM   12124 O  O     . PRO C 3 20  ? 149.507 122.491 161.162 1.00 42.32  ? 20   PRO C O     1 
ATOM   12125 C  CB    . PRO C 3 20  ? 146.557 121.390 162.281 1.00 36.85  ? 20   PRO C CB    1 
ATOM   12126 C  CG    . PRO C 3 20  ? 145.102 121.497 162.121 1.00 37.36  ? 20   PRO C CG    1 
ATOM   12127 C  CD    . PRO C 3 20  ? 144.881 121.673 160.652 1.00 42.83  ? 20   PRO C CD    1 
ATOM   12128 N  N     . LEU C 3 21  ? 148.531 120.962 159.827 1.00 38.62  ? 21   LEU C N     1 
ATOM   12129 C  CA    . LEU C 3 21  ? 149.810 120.531 159.268 1.00 37.58  ? 21   LEU C CA    1 
ATOM   12130 C  C     . LEU C 3 21  ? 150.440 121.619 158.409 1.00 38.61  ? 21   LEU C C     1 
ATOM   12131 O  O     . LEU C 3 21  ? 151.660 121.804 158.436 1.00 45.94  ? 21   LEU C O     1 
ATOM   12132 C  CB    . LEU C 3 21  ? 149.631 119.250 158.454 1.00 40.73  ? 21   LEU C CB    1 
ATOM   12133 C  CG    . LEU C 3 21  ? 149.868 117.936 159.194 1.00 36.37  ? 21   LEU C CG    1 
ATOM   12134 C  CD1   . LEU C 3 21  ? 149.380 116.759 158.377 1.00 34.68  ? 21   LEU C CD1   1 
ATOM   12135 C  CD2   . LEU C 3 21  ? 151.341 117.792 159.497 1.00 46.06  ? 21   LEU C CD2   1 
ATOM   12136 N  N     . LEU C 3 22  ? 149.629 122.339 157.631 1.00 34.81  ? 22   LEU C N     1 
ATOM   12137 C  CA    . LEU C 3 22  ? 150.155 123.446 156.838 1.00 34.49  ? 22   LEU C CA    1 
ATOM   12138 C  C     . LEU C 3 22  ? 150.697 124.554 157.732 1.00 37.65  ? 22   LEU C C     1 
ATOM   12139 O  O     . LEU C 3 22  ? 151.751 125.134 157.448 1.00 40.09  ? 22   LEU C O     1 
ATOM   12140 C  CB    . LEU C 3 22  ? 149.072 123.989 155.905 1.00 37.61  ? 22   LEU C CB    1 
ATOM   12141 C  CG    . LEU C 3 22  ? 148.616 123.081 154.762 1.00 36.23  ? 22   LEU C CG    1 
ATOM   12142 C  CD1   . LEU C 3 22  ? 147.443 123.687 154.013 1.00 32.25  ? 22   LEU C CD1   1 
ATOM   12143 C  CD2   . LEU C 3 22  ? 149.765 122.806 153.816 1.00 37.53  ? 22   LEU C CD2   1 
ATOM   12144 N  N     . GLN C 3 23  ? 149.989 124.857 158.823 1.00 46.25  ? 23   GLN C N     1 
ATOM   12145 C  CA    . GLN C 3 23  ? 150.469 125.864 159.764 1.00 44.13  ? 23   GLN C CA    1 
ATOM   12146 C  C     . GLN C 3 23  ? 151.760 125.421 160.442 1.00 51.33  ? 23   GLN C C     1 
ATOM   12147 O  O     . GLN C 3 23  ? 152.679 126.227 160.632 1.00 53.93  ? 23   GLN C O     1 
ATOM   12148 C  CB    . GLN C 3 23  ? 149.384 126.165 160.796 1.00 42.24  ? 23   GLN C CB    1 
ATOM   12149 C  CG    . GLN C 3 23  ? 148.179 126.883 160.215 1.00 43.40  ? 23   GLN C CG    1 
ATOM   12150 C  CD    . GLN C 3 23  ? 146.969 126.825 161.118 1.00 50.35  ? 23   GLN C CD    1 
ATOM   12151 O  OE1   . GLN C 3 23  ? 146.899 126.002 162.029 1.00 52.73  ? 23   GLN C OE1   1 
ATOM   12152 N  NE2   . GLN C 3 23  ? 146.005 127.700 160.871 1.00 48.80  ? 23   GLN C NE2   1 
ATOM   12153 N  N     . LYS C 3 24  ? 151.857 124.139 160.799 1.00 50.50  ? 24   LYS C N     1 
ATOM   12154 C  CA    . LYS C 3 24  ? 153.081 123.634 161.413 1.00 48.82  ? 24   LYS C CA    1 
ATOM   12155 C  C     . LYS C 3 24  ? 154.241 123.640 160.424 1.00 47.95  ? 24   LYS C C     1 
ATOM   12156 O  O     . LYS C 3 24  ? 155.385 123.895 160.808 1.00 52.67  ? 24   LYS C O     1 
ATOM   12157 C  CB    . LYS C 3 24  ? 152.850 122.230 161.969 1.00 50.07  ? 24   LYS C CB    1 
ATOM   12158 C  CG    . LYS C 3 24  ? 153.987 121.716 162.829 1.00 51.50  ? 24   LYS C CG    1 
ATOM   12159 C  CD    . LYS C 3 24  ? 154.219 122.619 164.025 1.00 50.69  ? 24   LYS C CD    1 
ATOM   12160 C  CE    . LYS C 3 24  ? 155.475 122.227 164.773 1.00 54.22  ? 24   LYS C CE    1 
ATOM   12161 N  NZ    . LYS C 3 24  ? 155.419 120.819 165.249 1.00 52.38  ? 24   LYS C NZ    1 
ATOM   12162 N  N     . THR C 3 25  ? 153.967 123.362 159.149 1.00 50.84  ? 25   THR C N     1 
ATOM   12163 C  CA    . THR C 3 25  ? 155.013 123.433 158.133 1.00 52.65  ? 25   THR C CA    1 
ATOM   12164 C  C     . THR C 3 25  ? 155.489 124.867 157.936 1.00 50.47  ? 25   THR C C     1 
ATOM   12165 O  O     . THR C 3 25  ? 156.693 125.116 157.789 1.00 54.61  ? 25   THR C O     1 
ATOM   12166 C  CB    . THR C 3 25  ? 154.502 122.852 156.816 1.00 51.89  ? 25   THR C CB    1 
ATOM   12167 O  OG1   . THR C 3 25  ? 153.915 121.568 157.053 1.00 52.12  ? 25   THR C OG1   1 
ATOM   12168 C  CG2   . THR C 3 25  ? 155.637 122.697 155.833 1.00 50.67  ? 25   THR C CG2   1 
ATOM   12169 N  N     . GLN C 3 26  ? 154.553 125.820 157.929 1.00 52.84  ? 26   GLN C N     1 
ATOM   12170 C  CA    . GLN C 3 26  ? 154.918 127.230 157.853 1.00 51.45  ? 26   GLN C CA    1 
ATOM   12171 C  C     . GLN C 3 26  ? 155.734 127.657 159.066 1.00 56.35  ? 26   GLN C C     1 
ATOM   12172 O  O     . GLN C 3 26  ? 156.615 128.515 158.951 1.00 59.81  ? 26   GLN C O     1 
ATOM   12173 C  CB    . GLN C 3 26  ? 153.655 128.084 157.724 1.00 51.88  ? 26   GLN C CB    1 
ATOM   12174 C  CG    . GLN C 3 26  ? 153.899 129.571 157.529 1.00 55.35  ? 26   GLN C CG    1 
ATOM   12175 C  CD    . GLN C 3 26  ? 153.926 129.974 156.071 1.00 55.79  ? 26   GLN C CD    1 
ATOM   12176 O  OE1   . GLN C 3 26  ? 153.867 129.129 155.182 1.00 59.41  ? 26   GLN C OE1   1 
ATOM   12177 N  NE2   . GLN C 3 26  ? 154.008 131.273 155.818 1.00 49.81  ? 26   GLN C NE2   1 
ATOM   12178 N  N     . GLU C 3 27  ? 155.451 127.081 160.236 1.00 59.32  ? 27   GLU C N     1 
ATOM   12179 C  CA    . GLU C 3 27  ? 156.291 127.331 161.404 1.00 60.28  ? 27   GLU C CA    1 
ATOM   12180 C  C     . GLU C 3 27  ? 157.679 126.721 161.237 1.00 60.90  ? 27   GLU C C     1 
ATOM   12181 O  O     . GLU C 3 27  ? 158.687 127.350 161.580 1.00 60.99  ? 27   GLU C O     1 
ATOM   12182 C  CB    . GLU C 3 27  ? 155.622 126.779 162.662 1.00 55.80  ? 27   GLU C CB    1 
ATOM   12183 C  CG    . GLU C 3 27  ? 154.414 127.563 163.121 1.00 58.39  ? 27   GLU C CG    1 
ATOM   12184 C  CD    . GLU C 3 27  ? 154.790 128.871 163.780 1.00 63.75  ? 27   GLU C CD    1 
ATOM   12185 O  OE1   . GLU C 3 27  ? 155.958 129.011 164.200 1.00 65.83  ? 27   GLU C OE1   1 
ATOM   12186 O  OE2   . GLU C 3 27  ? 153.920 129.761 163.880 1.00 61.86  ? 27   GLU C OE2   1 
ATOM   12187 N  N     . THR C 3 28  ? 157.747 125.498 160.712 1.00 60.68  ? 28   THR C N     1 
ATOM   12188 C  CA    . THR C 3 28  ? 158.999 124.748 160.715 1.00 59.36  ? 28   THR C CA    1 
ATOM   12189 C  C     . THR C 3 28  ? 159.985 125.285 159.684 1.00 59.44  ? 28   THR C C     1 
ATOM   12190 O  O     . THR C 3 28  ? 161.180 125.415 159.973 1.00 64.27  ? 28   THR C O     1 
ATOM   12191 C  CB    . THR C 3 28  ? 158.718 123.265 160.468 1.00 60.95  ? 28   THR C CB    1 
ATOM   12192 O  OG1   . THR C 3 28  ? 157.842 122.764 161.485 1.00 59.26  ? 28   THR C OG1   1 
ATOM   12193 C  CG2   . THR C 3 28  ? 160.009 122.462 160.490 1.00 62.94  ? 28   THR C CG2   1 
ATOM   12194 N  N     . PHE C 3 29  ? 159.513 125.607 158.479 1.00 60.86  ? 29   PHE C N     1 
ATOM   12195 C  CA    . PHE C 3 29  ? 160.408 126.024 157.409 1.00 62.54  ? 29   PHE C CA    1 
ATOM   12196 C  C     . PHE C 3 29  ? 160.280 127.491 157.028 1.00 61.71  ? 29   PHE C C     1 
ATOM   12197 O  O     . PHE C 3 29  ? 161.147 128.002 156.312 1.00 59.08  ? 29   PHE C O     1 
ATOM   12198 C  CB    . PHE C 3 29  ? 160.173 125.173 156.154 1.00 62.21  ? 29   PHE C CB    1 
ATOM   12199 C  CG    . PHE C 3 29  ? 160.246 123.698 156.398 1.00 59.78  ? 29   PHE C CG    1 
ATOM   12200 C  CD1   . PHE C 3 29  ? 161.461 123.044 156.407 1.00 60.38  ? 29   PHE C CD1   1 
ATOM   12201 C  CD2   . PHE C 3 29  ? 159.094 122.962 156.605 1.00 61.14  ? 29   PHE C CD2   1 
ATOM   12202 C  CE1   . PHE C 3 29  ? 161.526 121.687 156.624 1.00 62.71  ? 29   PHE C CE1   1 
ATOM   12203 C  CE2   . PHE C 3 29  ? 159.153 121.605 156.824 1.00 62.58  ? 29   PHE C CE2   1 
ATOM   12204 C  CZ    . PHE C 3 29  ? 160.370 120.967 156.834 1.00 62.47  ? 29   PHE C CZ    1 
ATOM   12205 N  N     . GLY C 3 30  ? 159.239 128.180 157.483 1.00 64.59  ? 30   GLY C N     1 
ATOM   12206 C  CA    . GLY C 3 30  ? 158.926 129.500 156.987 1.00 64.85  ? 30   GLY C CA    1 
ATOM   12207 C  C     . GLY C 3 30  ? 158.087 129.509 155.730 1.00 66.34  ? 30   GLY C C     1 
ATOM   12208 O  O     . GLY C 3 30  ? 157.708 130.591 155.265 1.00 68.83  ? 30   GLY C O     1 
ATOM   12209 N  N     . TYR C 3 31  ? 157.786 128.343 155.170 1.00 60.59  ? 31   TYR C N     1 
ATOM   12210 C  CA    . TYR C 3 31  ? 157.019 128.215 153.938 1.00 60.56  ? 31   TYR C CA    1 
ATOM   12211 C  C     . TYR C 3 31  ? 156.533 126.774 153.836 1.00 62.06  ? 31   TYR C C     1 
ATOM   12212 O  O     . TYR C 3 31  ? 156.596 126.010 154.804 1.00 67.78  ? 31   TYR C O     1 
ATOM   12213 C  CB    . TYR C 3 31  ? 157.853 128.621 152.720 1.00 61.54  ? 31   TYR C CB    1 
ATOM   12214 C  CG    . TYR C 3 31  ? 159.021 127.707 152.426 1.00 66.52  ? 31   TYR C CG    1 
ATOM   12215 C  CD1   . TYR C 3 31  ? 160.165 127.730 153.215 1.00 67.86  ? 31   TYR C CD1   1 
ATOM   12216 C  CD2   . TYR C 3 31  ? 158.991 126.835 151.349 1.00 64.32  ? 31   TYR C CD2   1 
ATOM   12217 C  CE1   . TYR C 3 31  ? 161.236 126.904 152.946 1.00 63.33  ? 31   TYR C CE1   1 
ATOM   12218 C  CE2   . TYR C 3 31  ? 160.059 126.008 151.073 1.00 65.24  ? 31   TYR C CE2   1 
ATOM   12219 C  CZ    . TYR C 3 31  ? 161.178 126.046 151.875 1.00 63.66  ? 31   TYR C CZ    1 
ATOM   12220 O  OH    . TYR C 3 31  ? 162.245 125.222 151.606 1.00 62.70  ? 31   TYR C OH    1 
ATOM   12221 N  N     . LEU C 3 32  ? 156.041 126.401 152.657 1.00 57.56  ? 32   LEU C N     1 
ATOM   12222 C  CA    . LEU C 3 32  ? 155.599 125.035 152.402 1.00 57.78  ? 32   LEU C CA    1 
ATOM   12223 C  C     . LEU C 3 32  ? 156.492 124.392 151.349 1.00 60.08  ? 32   LEU C C     1 
ATOM   12224 O  O     . LEU C 3 32  ? 156.321 124.652 150.148 1.00 62.21  ? 32   LEU C O     1 
ATOM   12225 C  CB    . LEU C 3 32  ? 154.137 125.025 151.949 1.00 57.58  ? 32   LEU C CB    1 
ATOM   12226 C  CG    . LEU C 3 32  ? 153.157 125.770 152.857 1.00 56.78  ? 32   LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 3 32  ? 151.743 125.611 152.352 1.00 56.07  ? 32   LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 3 32  ? 153.268 125.281 154.287 1.00 57.00  ? 32   LEU C CD2   1 
ATOM   12229 N  N     . PRO C 3 33  ? 157.459 123.563 151.737 1.00 64.81  ? 33   PRO C N     1 
ATOM   12230 C  CA    . PRO C 3 33  ? 158.343 122.936 150.749 1.00 66.64  ? 33   PRO C CA    1 
ATOM   12231 C  C     . PRO C 3 33  ? 157.615 121.907 149.901 1.00 64.65  ? 33   PRO C C     1 
ATOM   12232 O  O     . PRO C 3 33  ? 156.597 121.339 150.296 1.00 65.83  ? 33   PRO C O     1 
ATOM   12233 C  CB    . PRO C 3 33  ? 159.423 122.270 151.610 1.00 64.48  ? 33   PRO C CB    1 
ATOM   12234 C  CG    . PRO C 3 33  ? 159.339 122.951 152.933 1.00 63.42  ? 33   PRO C CG    1 
ATOM   12235 C  CD    . PRO C 3 33  ? 157.899 123.292 153.113 1.00 61.12  ? 33   PRO C CD    1 
ATOM   12236 N  N     . LYS C 3 34  ? 158.171 121.667 148.711 1.00 57.74  ? 34   LYS C N     1 
ATOM   12237 C  CA    . LYS C 3 34  ? 157.582 120.699 147.790 1.00 58.01  ? 34   LYS C CA    1 
ATOM   12238 C  C     . LYS C 3 34  ? 157.544 119.304 148.400 1.00 62.37  ? 34   LYS C C     1 
ATOM   12239 O  O     . LYS C 3 34  ? 156.512 118.622 148.356 1.00 62.67  ? 34   LYS C O     1 
ATOM   12240 C  CB    . LYS C 3 34  ? 158.370 120.681 146.480 1.00 60.86  ? 34   LYS C CB    1 
ATOM   12241 C  CG    . LYS C 3 34  ? 158.099 121.848 145.554 1.00 59.37  ? 34   LYS C CG    1 
ATOM   12242 C  CD    . LYS C 3 34  ? 156.885 121.585 144.690 1.00 59.81  ? 34   LYS C CD    1 
ATOM   12243 C  CE    . LYS C 3 34  ? 156.700 122.682 143.662 1.00 61.35  ? 34   LYS C CE    1 
ATOM   12244 N  NZ    . LYS C 3 34  ? 155.522 122.423 142.791 1.00 60.26  ? 34   LYS C NZ    1 
ATOM   12245 N  N     . GLU C 3 35  ? 158.662 118.864 148.983 1.00 68.98  ? 35   GLU C N     1 
ATOM   12246 C  CA    . GLU C 3 35  ? 158.722 117.507 149.517 1.00 67.97  ? 35   GLU C CA    1 
ATOM   12247 C  C     . GLU C 3 35  ? 157.867 117.365 150.770 1.00 69.54  ? 35   GLU C C     1 
ATOM   12248 O  O     . GLU C 3 35  ? 157.245 116.319 150.986 1.00 70.17  ? 35   GLU C O     1 
ATOM   12249 C  CB    . GLU C 3 35  ? 160.172 117.112 149.799 1.00 66.62  ? 35   GLU C CB    1 
ATOM   12250 C  CG    . GLU C 3 35  ? 160.931 118.077 150.679 1.00 68.54  ? 35   GLU C CG    1 
ATOM   12251 C  CD    . GLU C 3 35  ? 162.247 117.504 151.155 1.00 71.82  ? 35   GLU C CD    1 
ATOM   12252 O  OE1   . GLU C 3 35  ? 162.549 116.345 150.805 1.00 70.42  ? 35   GLU C OE1   1 
ATOM   12253 O  OE2   . GLU C 3 35  ? 162.977 118.211 151.881 1.00 72.76  ? 35   GLU C OE2   1 
ATOM   12254 N  N     . ALA C 3 36  ? 157.822 118.405 151.606 1.00 68.33  ? 36   ALA C N     1 
ATOM   12255 C  CA    . ALA C 3 36  ? 156.953 118.370 152.775 1.00 62.11  ? 36   ALA C CA    1 
ATOM   12256 C  C     . ALA C 3 36  ? 155.491 118.285 152.365 1.00 64.14  ? 36   ALA C C     1 
ATOM   12257 O  O     . ALA C 3 36  ? 154.717 117.523 152.953 1.00 66.81  ? 36   ALA C O     1 
ATOM   12258 C  CB    . ALA C 3 36  ? 157.196 119.596 153.651 1.00 62.40  ? 36   ALA C CB    1 
ATOM   12259 N  N     . LEU C 3 37  ? 155.097 119.055 151.349 1.00 61.43  ? 37   LEU C N     1 
ATOM   12260 C  CA    . LEU C 3 37  ? 153.723 118.994 150.866 1.00 58.98  ? 37   LEU C CA    1 
ATOM   12261 C  C     . LEU C 3 37  ? 153.411 117.633 150.260 1.00 61.25  ? 37   LEU C C     1 
ATOM   12262 O  O     . LEU C 3 37  ? 152.301 117.116 150.421 1.00 61.40  ? 37   LEU C O     1 
ATOM   12263 C  CB    . LEU C 3 37  ? 153.471 120.112 149.856 1.00 58.03  ? 37   LEU C CB    1 
ATOM   12264 C  CG    . LEU C 3 37  ? 153.462 121.523 150.450 1.00 59.75  ? 37   LEU C CG    1 
ATOM   12265 C  CD1   . LEU C 3 37  ? 153.177 122.562 149.384 1.00 61.84  ? 37   LEU C CD1   1 
ATOM   12266 C  CD2   . LEU C 3 37  ? 152.457 121.621 151.582 1.00 61.58  ? 37   LEU C CD2   1 
ATOM   12267 N  N     . GLU C 3 38  ? 154.381 117.029 149.567 1.00 59.42  ? 38   GLU C N     1 
ATOM   12268 C  CA    . GLU C 3 38  ? 154.167 115.694 149.013 1.00 60.88  ? 38   GLU C CA    1 
ATOM   12269 C  C     . GLU C 3 38  ? 154.007 114.647 150.110 1.00 61.23  ? 38   GLU C C     1 
ATOM   12270 O  O     . GLU C 3 38  ? 153.167 113.746 149.998 1.00 60.42  ? 38   GLU C O     1 
ATOM   12271 C  CB    . GLU C 3 38  ? 155.318 115.318 148.083 1.00 63.52  ? 38   GLU C CB    1 
ATOM   12272 C  CG    . GLU C 3 38  ? 155.120 115.740 146.638 1.00 62.62  ? 38   GLU C CG    1 
ATOM   12273 C  CD    . GLU C 3 38  ? 154.192 114.811 145.872 1.00 67.43  ? 38   GLU C CD    1 
ATOM   12274 O  OE1   . GLU C 3 38  ? 153.565 113.928 146.494 1.00 66.77  ? 38   GLU C OE1   1 
ATOM   12275 O  OE2   . GLU C 3 38  ? 154.094 114.963 144.636 1.00 69.57  ? 38   GLU C OE2   1 
ATOM   12276 N  N     . GLU C 3 39  ? 154.813 114.736 151.169 1.00 65.34  ? 39   GLU C N     1 
ATOM   12277 C  CA    . GLU C 3 39  ? 154.658 113.805 152.281 1.00 64.41  ? 39   GLU C CA    1 
ATOM   12278 C  C     . GLU C 3 39  ? 153.345 114.027 153.018 1.00 61.03  ? 39   GLU C C     1 
ATOM   12279 O  O     . GLU C 3 39  ? 152.740 113.067 153.505 1.00 58.46  ? 39   GLU C O     1 
ATOM   12280 C  CB    . GLU C 3 39  ? 155.837 113.926 153.242 1.00 62.57  ? 39   GLU C CB    1 
ATOM   12281 C  CG    . GLU C 3 39  ? 155.912 112.809 154.265 1.00 63.27  ? 39   GLU C CG    1 
ATOM   12282 C  CD    . GLU C 3 39  ? 156.147 111.453 153.631 1.00 64.63  ? 39   GLU C CD    1 
ATOM   12283 O  OE1   . GLU C 3 39  ? 156.811 111.394 152.576 1.00 60.63  ? 39   GLU C OE1   1 
ATOM   12284 O  OE2   . GLU C 3 39  ? 155.664 110.445 154.186 1.00 65.79  ? 39   GLU C OE2   1 
ATOM   12285 N  N     . ILE C 3 40  ? 152.894 115.278 153.113 1.00 64.19  ? 40   ILE C N     1 
ATOM   12286 C  CA    . ILE C 3 40  ? 151.571 115.562 153.664 1.00 64.40  ? 40   ILE C CA    1 
ATOM   12287 C  C     . ILE C 3 40  ? 150.491 114.927 152.797 1.00 62.04  ? 40   ILE C C     1 
ATOM   12288 O  O     . ILE C 3 40  ? 149.516 114.360 153.304 1.00 62.59  ? 40   ILE C O     1 
ATOM   12289 C  CB    . ILE C 3 40  ? 151.374 117.084 153.803 1.00 59.44  ? 40   ILE C CB    1 
ATOM   12290 C  CG1   . ILE C 3 40  ? 152.233 117.637 154.938 1.00 58.19  ? 40   ILE C CG1   1 
ATOM   12291 C  CG2   . ILE C 3 40  ? 149.918 117.428 154.035 1.00 56.35  ? 40   ILE C CG2   1 
ATOM   12292 C  CD1   . ILE C 3 40  ? 152.114 119.130 155.106 1.00 58.45  ? 40   ILE C CD1   1 
ATOM   12293 N  N     . SER C 3 41  ? 150.651 115.006 151.475 1.00 59.24  ? 41   SER C N     1 
ATOM   12294 C  CA    . SER C 3 41  ? 149.682 114.404 150.566 1.00 57.96  ? 41   SER C CA    1 
ATOM   12295 C  C     . SER C 3 41  ? 149.647 112.886 150.703 1.00 60.28  ? 41   SER C C     1 
ATOM   12296 O  O     . SER C 3 41  ? 148.573 112.278 150.652 1.00 62.81  ? 41   SER C O     1 
ATOM   12297 C  CB    . SER C 3 41  ? 149.999 114.805 149.127 1.00 57.89  ? 41   SER C CB    1 
ATOM   12298 O  OG    . SER C 3 41  ? 149.136 114.149 148.217 1.00 56.82  ? 41   SER C OG    1 
ATOM   12299 N  N     . ARG C 3 42  ? 150.810 112.255 150.863 1.00 63.54  ? 42   ARG C N     1 
ATOM   12300 C  CA    . ARG C 3 42  ? 150.839 110.800 150.996 1.00 64.39  ? 42   ARG C CA    1 
ATOM   12301 C  C     . ARG C 3 42  ? 150.319 110.348 152.357 1.00 66.44  ? 42   ARG C C     1 
ATOM   12302 O  O     . ARG C 3 42  ? 149.583 109.359 152.447 1.00 65.74  ? 42   ARG C O     1 
ATOM   12303 C  CB    . ARG C 3 42  ? 152.254 110.272 150.769 1.00 62.14  ? 42   ARG C CB    1 
ATOM   12304 C  CG    . ARG C 3 42  ? 152.722 110.357 149.333 1.00 61.43  ? 42   ARG C CG    1 
ATOM   12305 C  CD    . ARG C 3 42  ? 154.089 109.729 149.169 1.00 66.68  ? 42   ARG C CD    1 
ATOM   12306 N  NE    . ARG C 3 42  ? 155.107 110.434 149.936 1.00 66.94  ? 42   ARG C NE    1 
ATOM   12307 C  CZ    . ARG C 3 42  ? 155.833 111.439 149.466 1.00 66.58  ? 42   ARG C CZ    1 
ATOM   12308 N  NH1   . ARG C 3 42  ? 155.676 111.885 148.230 1.00 65.83  ? 42   ARG C NH1   1 
ATOM   12309 N  NH2   . ARG C 3 42  ? 156.740 112.009 150.253 1.00 62.27  ? 42   ARG C NH2   1 
ATOM   12310 N  N     . TYR C 3 43  ? 150.696 111.051 153.425 1.00 61.42  ? 43   TYR C N     1 
ATOM   12311 C  CA    . TYR C 3 43  ? 150.317 110.636 154.773 1.00 58.31  ? 43   TYR C CA    1 
ATOM   12312 C  C     . TYR C 3 43  ? 148.827 110.833 155.014 1.00 61.96  ? 43   TYR C C     1 
ATOM   12313 O  O     . TYR C 3 43  ? 148.148 109.942 155.534 1.00 68.60  ? 43   TYR C O     1 
ATOM   12314 C  CB    . TYR C 3 43  ? 151.139 111.414 155.799 1.00 61.95  ? 43   TYR C CB    1 
ATOM   12315 C  CG    . TYR C 3 43  ? 150.984 110.948 157.228 1.00 67.96  ? 43   TYR C CG    1 
ATOM   12316 C  CD1   . TYR C 3 43  ? 151.533 109.747 157.651 1.00 66.22  ? 43   TYR C CD1   1 
ATOM   12317 C  CD2   . TYR C 3 43  ? 150.315 111.723 158.162 1.00 67.46  ? 43   TYR C CD2   1 
ATOM   12318 C  CE1   . TYR C 3 43  ? 151.404 109.325 158.958 1.00 66.74  ? 43   TYR C CE1   1 
ATOM   12319 C  CE2   . TYR C 3 43  ? 150.185 111.312 159.471 1.00 65.66  ? 43   TYR C CE2   1 
ATOM   12320 C  CZ    . TYR C 3 43  ? 150.731 110.113 159.864 1.00 65.88  ? 43   TYR C CZ    1 
ATOM   12321 O  OH    . TYR C 3 43  ? 150.600 109.701 161.168 1.00 64.57  ? 43   TYR C OH    1 
ATOM   12322 N  N     . LEU C 3 44  ? 148.300 111.997 154.645 1.00 57.43  ? 44   LEU C N     1 
ATOM   12323 C  CA    . LEU C 3 44  ? 146.873 112.254 154.767 1.00 55.23  ? 44   LEU C CA    1 
ATOM   12324 C  C     . LEU C 3 44  ? 146.061 111.569 153.681 1.00 57.49  ? 44   LEU C C     1 
ATOM   12325 O  O     . LEU C 3 44  ? 144.834 111.493 153.810 1.00 61.67  ? 44   LEU C O     1 
ATOM   12326 C  CB    . LEU C 3 44  ? 146.605 113.759 154.734 1.00 57.22  ? 44   LEU C CB    1 
ATOM   12327 C  CG    . LEU C 3 44  ? 147.378 114.603 155.746 1.00 55.60  ? 44   LEU C CG    1 
ATOM   12328 C  CD1   . LEU C 3 44  ? 146.956 116.054 155.659 1.00 52.90  ? 44   LEU C CD1   1 
ATOM   12329 C  CD2   . LEU C 3 44  ? 147.176 114.066 157.151 1.00 53.85  ? 44   LEU C CD2   1 
ATOM   12330 N  N     . LYS C 3 45  ? 146.720 111.064 152.634 1.00 56.95  ? 45   LYS C N     1 
ATOM   12331 C  CA    . LYS C 3 45  ? 146.066 110.434 151.486 1.00 55.95  ? 45   LYS C CA    1 
ATOM   12332 C  C     . LYS C 3 45  ? 145.056 111.382 150.843 1.00 58.49  ? 45   LYS C C     1 
ATOM   12333 O  O     . LYS C 3 45  ? 143.916 111.017 150.551 1.00 64.50  ? 45   LYS C O     1 
ATOM   12334 C  CB    . LYS C 3 45  ? 145.419 109.105 151.877 1.00 59.03  ? 45   LYS C CB    1 
ATOM   12335 C  CG    . LYS C 3 45  ? 146.417 108.073 152.361 1.00 60.63  ? 45   LYS C CG    1 
ATOM   12336 C  CD    . LYS C 3 45  ? 145.732 106.777 152.749 1.00 58.22  ? 45   LYS C CD    1 
ATOM   12337 C  CE    . LYS C 3 45  ? 146.743 105.745 153.217 1.00 59.26  ? 45   LYS C CE    1 
ATOM   12338 N  NZ    . LYS C 3 45  ? 146.089 104.465 153.602 1.00 57.52  ? 45   LYS C NZ    1 
ATOM   12339 N  N     . VAL C 3 46  ? 145.491 112.618 150.629 1.00 42.07  ? 46   VAL C N     1 
ATOM   12340 C  CA    . VAL C 3 46  ? 144.664 113.635 149.990 1.00 43.47  ? 46   VAL C CA    1 
ATOM   12341 C  C     . VAL C 3 46  ? 145.414 114.108 148.748 1.00 43.73  ? 46   VAL C C     1 
ATOM   12342 O  O     . VAL C 3 46  ? 146.653 114.076 148.730 1.00 42.99  ? 46   VAL C O     1 
ATOM   12343 C  CB    . VAL C 3 46  ? 144.338 114.777 150.970 1.00 44.92  ? 46   VAL C CB    1 
ATOM   12344 C  CG1   . VAL C 3 46  ? 145.175 116.012 150.694 1.00 40.07  ? 46   VAL C CG1   1 
ATOM   12345 C  CG2   . VAL C 3 46  ? 142.852 115.105 150.946 1.00 42.63  ? 46   VAL C CG2   1 
ATOM   12346 N  N     . PRO C 3 47  ? 144.720 114.496 147.678 1.00 42.56  ? 47   PRO C N     1 
ATOM   12347 C  CA    . PRO C 3 47  ? 145.423 114.910 146.460 1.00 38.56  ? 47   PRO C CA    1 
ATOM   12348 C  C     . PRO C 3 47  ? 146.274 116.147 146.693 1.00 38.36  ? 47   PRO C C     1 
ATOM   12349 O  O     . PRO C 3 47  ? 145.952 117.007 147.515 1.00 46.69  ? 47   PRO C O     1 
ATOM   12350 C  CB    . PRO C 3 47  ? 144.286 115.193 145.473 1.00 35.38  ? 47   PRO C CB    1 
ATOM   12351 C  CG    . PRO C 3 47  ? 143.141 114.408 145.982 1.00 41.45  ? 47   PRO C CG    1 
ATOM   12352 C  CD    . PRO C 3 47  ? 143.264 114.431 147.470 1.00 39.51  ? 47   PRO C CD    1 
ATOM   12353 N  N     . LEU C 3 48  ? 147.384 116.219 145.960 1.00 31.31  ? 48   LEU C N     1 
ATOM   12354 C  CA    . LEU C 3 48  ? 148.262 117.377 146.067 1.00 24.71  ? 48   LEU C CA    1 
ATOM   12355 C  C     . LEU C 3 48  ? 147.575 118.640 145.569 1.00 31.57  ? 48   LEU C C     1 
ATOM   12356 O  O     . LEU C 3 48  ? 147.876 119.742 146.045 1.00 45.61  ? 48   LEU C O     1 
ATOM   12357 C  CB    . LEU C 3 48  ? 149.552 117.117 145.292 1.00 31.42  ? 48   LEU C CB    1 
ATOM   12358 C  CG    . LEU C 3 48  ? 150.788 117.909 145.710 1.00 31.97  ? 48   LEU C CG    1 
ATOM   12359 C  CD1   . LEU C 3 48  ? 151.056 117.728 147.188 1.00 39.31  ? 48   LEU C CD1   1 
ATOM   12360 C  CD2   . LEU C 3 48  ? 151.986 117.468 144.898 1.00 34.24  ? 48   LEU C CD2   1 
ATOM   12361 N  N     . SER C 3 49  ? 146.643 118.495 144.625 1.00 30.89  ? 49   SER C N     1 
ATOM   12362 C  CA    . SER C 3 49  ? 145.902 119.646 144.126 1.00 29.16  ? 49   SER C CA    1 
ATOM   12363 C  C     . SER C 3 49  ? 145.059 120.280 145.225 1.00 37.03  ? 49   SER C C     1 
ATOM   12364 O  O     . SER C 3 49  ? 144.951 121.506 145.300 1.00 38.68  ? 49   SER C O     1 
ATOM   12365 C  CB    . SER C 3 49  ? 145.032 119.232 142.940 1.00 31.34  ? 49   SER C CB    1 
ATOM   12366 O  OG    . SER C 3 49  ? 144.368 118.011 143.197 1.00 40.79  ? 49   SER C OG    1 
ATOM   12367 N  N     . ARG C 3 50  ? 144.466 119.463 146.099 1.00 34.14  ? 50   ARG C N     1 
ATOM   12368 C  CA    . ARG C 3 50  ? 143.695 120.019 147.206 1.00 34.39  ? 50   ARG C CA    1 
ATOM   12369 C  C     . ARG C 3 50  ? 144.595 120.655 148.261 1.00 25.58  ? 50   ARG C C     1 
ATOM   12370 O  O     . ARG C 3 50  ? 144.222 121.671 148.860 1.00 32.19  ? 50   ARG C O     1 
ATOM   12371 C  CB    . ARG C 3 50  ? 142.812 118.937 147.824 1.00 36.23  ? 50   ARG C CB    1 
ATOM   12372 C  CG    . ARG C 3 50  ? 141.866 119.446 148.891 1.00 34.79  ? 50   ARG C CG    1 
ATOM   12373 C  CD    . ARG C 3 50  ? 140.514 118.764 148.806 1.00 30.39  ? 50   ARG C CD    1 
ATOM   12374 N  NE    . ARG C 3 50  ? 139.735 119.232 147.668 1.00 29.98  ? 50   ARG C NE    1 
ATOM   12375 C  CZ    . ARG C 3 50  ? 138.503 118.829 147.390 1.00 35.40  ? 50   ARG C CZ    1 
ATOM   12376 N  NH1   . ARG C 3 50  ? 137.882 117.941 148.147 1.00 30.72  ? 50   ARG C NH1   1 
ATOM   12377 N  NH2   . ARG C 3 50  ? 137.880 119.330 146.328 1.00 33.46  ? 50   ARG C NH2   1 
ATOM   12378 N  N     . VAL C 3 51  ? 145.782 120.085 148.490 1.00 17.68  ? 51   VAL C N     1 
ATOM   12379 C  CA    . VAL C 3 51  ? 146.756 120.715 149.380 1.00 23.73  ? 51   VAL C CA    1 
ATOM   12380 C  C     . VAL C 3 51  ? 147.112 122.104 148.870 1.00 29.72  ? 51   VAL C C     1 
ATOM   12381 O  O     . VAL C 3 51  ? 147.123 123.085 149.625 1.00 32.08  ? 51   VAL C O     1 
ATOM   12382 C  CB    . VAL C 3 51  ? 148.012 119.835 149.513 1.00 19.20  ? 51   VAL C CB    1 
ATOM   12383 C  CG1   . VAL C 3 51  ? 149.096 120.570 150.282 1.00 24.42  ? 51   VAL C CG1   1 
ATOM   12384 C  CG2   . VAL C 3 51  ? 147.675 118.527 150.184 1.00 27.50  ? 51   VAL C CG2   1 
ATOM   12385 N  N     . TYR C 3 52  ? 147.385 122.210 147.569 1.00 30.36  ? 52   TYR C N     1 
ATOM   12386 C  CA    . TYR C 3 52  ? 147.737 123.507 147.009 1.00 26.27  ? 52   TYR C CA    1 
ATOM   12387 C  C     . TYR C 3 52  ? 146.544 124.451 146.967 1.00 28.92  ? 52   TYR C C     1 
ATOM   12388 O  O     . TYR C 3 52  ? 146.716 125.657 147.147 1.00 37.40  ? 52   TYR C O     1 
ATOM   12389 C  CB    . TYR C 3 52  ? 148.350 123.332 145.623 1.00 21.15  ? 52   TYR C CB    1 
ATOM   12390 C  CG    . TYR C 3 52  ? 149.828 123.032 145.681 1.00 22.16  ? 52   TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 3 52  ? 150.289 121.728 145.764 1.00 29.61  ? 52   TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 3 52  ? 150.762 124.058 145.671 1.00 26.37  ? 52   TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 3 52  ? 151.638 121.453 145.826 1.00 28.28  ? 52   TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 3 52  ? 152.113 123.792 145.729 1.00 30.88  ? 52   TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 3 52  ? 152.544 122.488 145.807 1.00 32.99  ? 52   TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 3 52  ? 153.888 122.218 145.868 1.00 37.92  ? 52   TYR C OH    1 
ATOM   12397 N  N     . GLY C 3 53  ? 145.335 123.932 146.754 1.00 19.96  ? 53   GLY C N     1 
ATOM   12398 C  CA    . GLY C 3 53  ? 144.159 124.786 146.804 1.00 19.08  ? 53   GLY C CA    1 
ATOM   12399 C  C     . GLY C 3 53  ? 143.942 125.395 148.175 1.00 21.40  ? 53   GLY C C     1 
ATOM   12400 O  O     . GLY C 3 53  ? 143.678 126.595 148.298 1.00 27.40  ? 53   GLY C O     1 
ATOM   12401 N  N     . VAL C 3 54  ? 144.072 124.581 149.224 1.00 30.24  ? 54   VAL C N     1 
ATOM   12402 C  CA    . VAL C 3 54  ? 143.936 125.092 150.583 1.00 22.06  ? 54   VAL C CA    1 
ATOM   12403 C  C     . VAL C 3 54  ? 145.055 126.077 150.903 1.00 15.89  ? 54   VAL C C     1 
ATOM   12404 O  O     . VAL C 3 54  ? 144.821 127.120 151.524 1.00 21.00  ? 54   VAL C O     1 
ATOM   12405 C  CB    . VAL C 3 54  ? 143.892 123.925 151.586 1.00 16.26  ? 54   VAL C CB    1 
ATOM   12406 C  CG1   . VAL C 3 54  ? 143.890 124.441 153.011 1.00 19.53  ? 54   VAL C CG1   1 
ATOM   12407 C  CG2   . VAL C 3 54  ? 142.665 123.072 151.337 1.00 22.18  ? 54   VAL C CG2   1 
ATOM   12408 N  N     . ALA C 3 55  ? 146.283 125.771 150.478 1.00 16.20  ? 55   ALA C N     1 
ATOM   12409 C  CA    . ALA C 3 55  ? 147.404 126.660 150.766 1.00 20.77  ? 55   ALA C CA    1 
ATOM   12410 C  C     . ALA C 3 55  ? 147.267 127.997 150.043 1.00 27.80  ? 55   ALA C C     1 
ATOM   12411 O  O     . ALA C 3 55  ? 147.603 129.047 150.602 1.00 30.01  ? 55   ALA C O     1 
ATOM   12412 C  CB    . ALA C 3 55  ? 148.716 125.974 150.395 1.00 22.07  ? 55   ALA C CB    1 
ATOM   12413 N  N     . THR C 3 56  ? 146.780 127.984 148.804 1.00 28.30  ? 56   THR C N     1 
ATOM   12414 C  CA    . THR C 3 56  ? 146.622 129.217 148.045 1.00 19.36  ? 56   THR C CA    1 
ATOM   12415 C  C     . THR C 3 56  ? 145.366 129.990 148.422 1.00 27.83  ? 56   THR C C     1 
ATOM   12416 O  O     . THR C 3 56  ? 145.285 131.185 148.122 1.00 30.89  ? 56   THR C O     1 
ATOM   12417 C  CB    . THR C 3 56  ? 146.598 128.916 146.546 1.00 19.69  ? 56   THR C CB    1 
ATOM   12418 O  OG1   . THR C 3 56  ? 145.601 127.926 146.271 1.00 15.24  ? 56   THR C OG1   1 
ATOM   12419 C  CG2   . THR C 3 56  ? 147.950 128.412 146.083 1.00 21.93  ? 56   THR C CG2   1 
ATOM   12420 N  N     . PHE C 3 57  ? 144.388 129.342 149.060 1.00 20.16  ? 57   PHE C N     1 
ATOM   12421 C  CA    . PHE C 3 57  ? 143.186 130.057 149.481 1.00 14.66  ? 57   PHE C CA    1 
ATOM   12422 C  C     . PHE C 3 57  ? 143.501 131.106 150.542 1.00 29.01  ? 57   PHE C C     1 
ATOM   12423 O  O     . PHE C 3 57  ? 142.957 132.214 150.506 1.00 38.26  ? 57   PHE C O     1 
ATOM   12424 C  CB    . PHE C 3 57  ? 142.141 129.070 149.997 1.00 15.72  ? 57   PHE C CB    1 
ATOM   12425 C  CG    . PHE C 3 57  ? 140.818 129.700 150.331 1.00 14.92  ? 57   PHE C CG    1 
ATOM   12426 C  CD1   . PHE C 3 57  ? 139.870 129.914 149.346 1.00 15.93  ? 57   PHE C CD1   1 
ATOM   12427 C  CD2   . PHE C 3 57  ? 140.515 130.065 151.629 1.00 23.63  ? 57   PHE C CD2   1 
ATOM   12428 C  CE1   . PHE C 3 57  ? 138.653 130.485 149.648 1.00 14.49  ? 57   PHE C CE1   1 
ATOM   12429 C  CE2   . PHE C 3 57  ? 139.300 130.638 151.935 1.00 27.46  ? 57   PHE C CE2   1 
ATOM   12430 C  CZ    . PHE C 3 57  ? 138.368 130.846 150.943 1.00 22.06  ? 57   PHE C CZ    1 
ATOM   12431 N  N     . TYR C 3 58  ? 144.370 130.779 151.492 1.00 26.02  ? 58   TYR C N     1 
ATOM   12432 C  CA    . TYR C 3 58  ? 144.704 131.697 152.571 1.00 24.29  ? 58   TYR C CA    1 
ATOM   12433 C  C     . TYR C 3 58  ? 145.938 132.510 152.207 1.00 30.84  ? 58   TYR C C     1 
ATOM   12434 O  O     . TYR C 3 58  ? 146.911 131.979 151.665 1.00 33.75  ? 58   TYR C O     1 
ATOM   12435 C  CB    . TYR C 3 58  ? 144.925 130.932 153.875 1.00 27.22  ? 58   TYR C CB    1 
ATOM   12436 C  CG    . TYR C 3 58  ? 143.715 130.135 154.305 1.00 24.76  ? 58   TYR C CG    1 
ATOM   12437 C  CD1   . TYR C 3 58  ? 142.699 130.724 155.043 1.00 24.38  ? 58   TYR C CD1   1 
ATOM   12438 C  CD2   . TYR C 3 58  ? 143.581 128.799 153.959 1.00 25.44  ? 58   TYR C CD2   1 
ATOM   12439 C  CE1   . TYR C 3 58  ? 141.591 130.001 155.433 1.00 26.48  ? 58   TYR C CE1   1 
ATOM   12440 C  CE2   . TYR C 3 58  ? 142.476 128.071 154.341 1.00 22.47  ? 58   TYR C CE2   1 
ATOM   12441 C  CZ    . TYR C 3 58  ? 141.485 128.677 155.078 1.00 26.64  ? 58   TYR C CZ    1 
ATOM   12442 O  OH    . TYR C 3 58  ? 140.383 127.956 155.462 1.00 30.52  ? 58   TYR C OH    1 
ATOM   12443 N  N     . ALA C 3 59  ? 145.887 133.808 152.504 1.00 25.47  ? 59   ALA C N     1 
ATOM   12444 C  CA    . ALA C 3 59  ? 146.914 134.733 152.044 1.00 31.26  ? 59   ALA C CA    1 
ATOM   12445 C  C     . ALA C 3 59  ? 148.213 134.640 152.833 1.00 37.30  ? 59   ALA C C     1 
ATOM   12446 O  O     . ALA C 3 59  ? 149.250 135.092 152.338 1.00 37.68  ? 59   ALA C O     1 
ATOM   12447 C  CB    . ALA C 3 59  ? 146.387 136.168 152.101 1.00 26.88  ? 59   ALA C CB    1 
ATOM   12448 N  N     . GLN C 3 60  ? 148.190 134.074 154.039 1.00 35.69  ? 60   GLN C N     1 
ATOM   12449 C  CA    . GLN C 3 60  ? 149.408 133.993 154.837 1.00 33.46  ? 60   GLN C CA    1 
ATOM   12450 C  C     . GLN C 3 60  ? 150.371 132.919 154.347 1.00 34.24  ? 60   GLN C C     1 
ATOM   12451 O  O     . GLN C 3 60  ? 151.575 133.029 154.597 1.00 37.33  ? 60   GLN C O     1 
ATOM   12452 C  CB    . GLN C 3 60  ? 149.066 133.739 156.307 1.00 32.46  ? 60   GLN C CB    1 
ATOM   12453 C  CG    . GLN C 3 60  ? 148.371 132.419 156.574 1.00 32.53  ? 60   GLN C CG    1 
ATOM   12454 C  CD    . GLN C 3 60  ? 148.515 131.973 158.015 1.00 36.64  ? 60   GLN C CD    1 
ATOM   12455 O  OE1   . GLN C 3 60  ? 149.040 132.705 158.851 1.00 35.00  ? 60   GLN C OE1   1 
ATOM   12456 N  NE2   . GLN C 3 60  ? 148.055 130.765 158.310 1.00 34.25  ? 60   GLN C NE2   1 
ATOM   12457 N  N     . PHE C 3 61  ? 149.876 131.895 153.657 1.00 36.28  ? 61   PHE C N     1 
ATOM   12458 C  CA    . PHE C 3 61  ? 150.706 130.769 153.247 1.00 37.35  ? 61   PHE C CA    1 
ATOM   12459 C  C     . PHE C 3 61  ? 151.604 131.156 152.080 1.00 41.17  ? 61   PHE C C     1 
ATOM   12460 O  O     . PHE C 3 61  ? 151.133 131.691 151.072 1.00 43.15  ? 61   PHE C O     1 
ATOM   12461 C  CB    . PHE C 3 61  ? 149.827 129.582 152.863 1.00 37.44  ? 61   PHE C CB    1 
ATOM   12462 C  CG    . PHE C 3 61  ? 149.095 128.966 154.019 1.00 33.21  ? 61   PHE C CG    1 
ATOM   12463 C  CD1   . PHE C 3 61  ? 149.735 128.751 155.226 1.00 33.80  ? 61   PHE C CD1   1 
ATOM   12464 C  CD2   . PHE C 3 61  ? 147.767 128.597 153.896 1.00 29.16  ? 61   PHE C CD2   1 
ATOM   12465 C  CE1   . PHE C 3 61  ? 149.064 128.181 156.287 1.00 35.59  ? 61   PHE C CE1   1 
ATOM   12466 C  CE2   . PHE C 3 61  ? 147.091 128.026 154.954 1.00 30.86  ? 61   PHE C CE2   1 
ATOM   12467 C  CZ    . PHE C 3 61  ? 147.740 127.818 156.151 1.00 32.44  ? 61   PHE C CZ    1 
ATOM   12468 N  N     . ARG C 3 62  ? 152.895 130.866 152.209 1.00 51.12  ? 62   ARG C N     1 
ATOM   12469 C  CA    . ARG C 3 62  ? 153.888 131.230 151.211 1.00 50.94  ? 62   ARG C CA    1 
ATOM   12470 C  C     . ARG C 3 62  ? 154.587 129.979 150.699 1.00 50.32  ? 62   ARG C C     1 
ATOM   12471 O  O     . ARG C 3 62  ? 154.792 129.016 151.442 1.00 53.61  ? 62   ARG C O     1 
ATOM   12472 C  CB    . ARG C 3 62  ? 154.917 132.208 151.788 1.00 51.08  ? 62   ARG C CB    1 
ATOM   12473 C  CG    . ARG C 3 62  ? 154.311 133.268 152.692 1.00 52.24  ? 62   ARG C CG    1 
ATOM   12474 C  CD    . ARG C 3 62  ? 155.370 134.121 153.367 1.00 52.05  ? 62   ARG C CD    1 
ATOM   12475 N  NE    . ARG C 3 62  ? 155.714 135.291 152.571 1.00 57.52  ? 62   ARG C NE    1 
ATOM   12476 C  CZ    . ARG C 3 62  ? 156.705 135.333 151.692 1.00 58.64  ? 62   ARG C CZ    1 
ATOM   12477 N  NH1   . ARG C 3 62  ? 157.478 134.283 151.472 1.00 56.21  ? 62   ARG C NH1   1 
ATOM   12478 N  NH2   . ARG C 3 62  ? 156.926 136.457 151.017 1.00 57.20  ? 62   ARG C NH2   1 
ATOM   12479 N  N     . PHE C 3 63  ? 154.945 129.996 149.416 1.00 48.41  ? 63   PHE C N     1 
ATOM   12480 C  CA    . PHE C 3 63  ? 155.582 128.855 148.772 1.00 49.16  ? 63   PHE C CA    1 
ATOM   12481 C  C     . PHE C 3 63  ? 157.047 129.074 148.449 1.00 52.67  ? 63   PHE C C     1 
ATOM   12482 O  O     . PHE C 3 63  ? 157.804 128.103 148.399 1.00 47.86  ? 63   PHE C O     1 
ATOM   12483 C  CB    . PHE C 3 63  ? 154.846 128.490 147.479 1.00 45.72  ? 63   PHE C CB    1 
ATOM   12484 C  CG    . PHE C 3 63  ? 153.401 128.182 147.681 1.00 46.13  ? 63   PHE C CG    1 
ATOM   12485 C  CD1   . PHE C 3 63  ? 152.994 126.905 148.022 1.00 46.30  ? 63   PHE C CD1   1 
ATOM   12486 C  CD2   . PHE C 3 63  ? 152.446 129.169 147.538 1.00 48.38  ? 63   PHE C CD2   1 
ATOM   12487 C  CE1   . PHE C 3 63  ? 151.663 126.623 148.211 1.00 47.30  ? 63   PHE C CE1   1 
ATOM   12488 C  CE2   . PHE C 3 63  ? 151.117 128.891 147.729 1.00 47.60  ? 63   PHE C CE2   1 
ATOM   12489 C  CZ    . PHE C 3 63  ? 150.725 127.616 148.065 1.00 45.20  ? 63   PHE C CZ    1 
ATOM   12490 N  N     . GLU C 3 64  ? 157.459 130.313 148.212 1.00 68.75  ? 64   GLU C N     1 
ATOM   12491 C  CA    . GLU C 3 64  ? 158.871 130.599 148.061 1.00 67.81  ? 64   GLU C CA    1 
ATOM   12492 C  C     . GLU C 3 64  ? 159.579 130.364 149.393 1.00 71.00  ? 64   GLU C C     1 
ATOM   12493 O  O     . GLU C 3 64  ? 158.968 130.499 150.455 1.00 69.34  ? 64   GLU C O     1 
ATOM   12494 C  CB    . GLU C 3 64  ? 159.076 132.039 147.598 1.00 66.25  ? 64   GLU C CB    1 
ATOM   12495 C  CG    . GLU C 3 64  ? 158.419 133.079 148.488 1.00 68.12  ? 64   GLU C CG    1 
ATOM   12496 C  CD    . GLU C 3 64  ? 158.646 134.494 147.995 1.00 70.47  ? 64   GLU C CD    1 
ATOM   12497 O  OE1   . GLU C 3 64  ? 159.334 134.664 146.967 1.00 71.52  ? 64   GLU C OE1   1 
ATOM   12498 O  OE2   . GLU C 3 64  ? 158.135 135.437 148.635 1.00 69.08  ? 64   GLU C OE2   1 
ATOM   12499 N  N     . PRO C 3 65  ? 160.867 130.007 149.366 1.00 74.00  ? 65   PRO C N     1 
ATOM   12500 C  CA    . PRO C 3 65  ? 161.573 129.679 150.617 1.00 70.35  ? 65   PRO C CA    1 
ATOM   12501 C  C     . PRO C 3 65  ? 161.567 130.786 151.664 1.00 68.43  ? 65   PRO C C     1 
ATOM   12502 O  O     . PRO C 3 65  ? 161.990 130.531 152.799 1.00 70.86  ? 65   PRO C O     1 
ATOM   12503 C  CB    . PRO C 3 65  ? 162.999 129.377 150.142 1.00 70.84  ? 65   PRO C CB    1 
ATOM   12504 C  CG    . PRO C 3 65  ? 162.822 128.897 148.749 1.00 68.74  ? 65   PRO C CG    1 
ATOM   12505 C  CD    . PRO C 3 65  ? 161.693 129.711 148.182 1.00 67.17  ? 65   PRO C CD    1 
ATOM   12506 N  N     . LEU C 3 66  ? 161.106 131.988 151.334 1.00 30.00  ? 66   LEU C N     1 
ATOM   12507 C  CA    . LEU C 3 66  ? 160.978 133.053 152.320 1.00 30.00  ? 66   LEU C CA    1 
ATOM   12508 C  C     . LEU C 3 66  ? 159.812 132.775 153.260 1.00 30.00  ? 66   LEU C C     1 
ATOM   12509 O  O     . LEU C 3 66  ? 159.001 131.884 153.010 1.00 30.00  ? 66   LEU C O     1 
ATOM   12510 C  CB    . LEU C 3 66  ? 160.792 134.408 151.636 1.00 30.00  ? 66   LEU C CB    1 
ATOM   12511 C  CG    . LEU C 3 66  ? 162.060 135.139 151.200 1.00 30.00  ? 66   LEU C CG    1 
ATOM   12512 C  CD1   . LEU C 3 66  ? 163.069 135.167 152.339 1.00 30.00  ? 66   LEU C CD1   1 
ATOM   12513 C  CD2   . LEU C 3 66  ? 162.665 134.520 149.947 1.00 30.00  ? 66   LEU C CD2   1 
HETATM 12514 FE FE1   . SF4 D 4 .   ? 136.236 126.386 134.518 1.00 37.02  ? 1001 SF4 A FE1   1 
HETATM 12515 FE FE2   . SF4 D 4 .   ? 133.868 125.089 134.966 1.00 35.81  ? 1001 SF4 A FE2   1 
HETATM 12516 FE FE3   . SF4 D 4 .   ? 136.235 123.737 135.193 1.00 36.93  ? 1001 SF4 A FE3   1 
HETATM 12517 FE FE4   . SF4 D 4 .   ? 135.333 124.521 132.731 1.00 33.19  ? 1001 SF4 A FE4   1 
HETATM 12518 S  S1    . SF4 D 4 .   ? 134.345 123.023 134.137 1.00 16.53  ? 1001 SF4 A S1    1 
HETATM 12519 S  S2    . SF4 D 4 .   ? 137.456 124.726 133.541 1.00 23.72  ? 1001 SF4 A S2    1 
HETATM 12520 S  S3    . SF4 D 4 .   ? 134.348 126.508 133.249 1.00 25.57  ? 1001 SF4 A S3    1 
HETATM 12521 S  S4    . SF4 D 4 .   ? 135.527 125.477 136.484 1.00 29.75  ? 1001 SF4 A S4    1 
HETATM 12522 FE FE1   . SF4 E 4 .   ? 132.744 135.441 101.841 1.00 86.49  ? 1002 SF4 A FE1   1 
HETATM 12523 FE FE2   . SF4 E 4 .   ? 133.918 136.375 99.551  1.00 85.26  ? 1002 SF4 A FE2   1 
HETATM 12524 FE FE3   . SF4 E 4 .   ? 134.041 133.711 100.166 1.00 93.41  ? 1002 SF4 A FE3   1 
HETATM 12525 FE FE4   . SF4 E 4 .   ? 135.471 135.519 101.634 1.00 94.53  ? 1002 SF4 A FE4   1 
HETATM 12526 S  S1    . SF4 E 4 .   ? 135.753 135.027 99.428  1.00 52.17  ? 1002 SF4 A S1    1 
HETATM 12527 S  S2    . SF4 E 4 .   ? 134.209 133.797 102.435 1.00 71.67  ? 1002 SF4 A S2    1 
HETATM 12528 S  S3    . SF4 E 4 .   ? 134.047 137.299 101.632 1.00 59.08  ? 1002 SF4 A S3    1 
HETATM 12529 S  S4    . SF4 E 4 .   ? 132.168 134.924 99.697  1.00 70.50  ? 1002 SF4 A S4    1 
HETATM 12530 FE FE1   . SF4 F 4 .   ? 141.920 131.003 109.682 1.00 30.98  ? 1003 SF4 A FE1   1 
HETATM 12531 FE FE2   . SF4 F 4 .   ? 141.792 132.843 111.700 1.00 36.10  ? 1003 SF4 A FE2   1 
HETATM 12532 FE FE3   . SF4 F 4 .   ? 139.805 132.735 109.822 1.00 22.43  ? 1003 SF4 A FE3   1 
HETATM 12533 FE FE4   . SF4 F 4 .   ? 142.287 133.659 109.135 1.00 19.66  ? 1003 SF4 A FE4   1 
HETATM 12534 S  S1    . SF4 F 4 .   ? 140.833 134.606 110.617 1.00 31.57  ? 1003 SF4 A S1    1 
HETATM 12535 S  S2    . SF4 F 4 .   ? 141.007 132.187 107.961 1.00 21.86  ? 1003 SF4 A S2    1 
HETATM 12536 S  S3    . SF4 F 4 .   ? 143.616 132.332 110.426 1.00 7.51   ? 1003 SF4 A S3    1 
HETATM 12537 S  S4    . SF4 F 4 .   ? 140.351 131.119 111.332 1.00 8.91   ? 1003 SF4 A S4    1 
HETATM 12538 FE FE1   . SF4 G 4 .   ? 132.072 130.396 124.476 1.00 38.96  ? 1004 SF4 A FE1   1 
HETATM 12539 FE FE2   . SF4 G 4 .   ? 132.632 132.291 122.588 1.00 52.18  ? 1004 SF4 A FE2   1 
HETATM 12540 FE FE3   . SF4 G 4 .   ? 134.471 130.349 123.166 1.00 29.49  ? 1004 SF4 A FE3   1 
HETATM 12541 FE FE4   . SF4 G 4 .   ? 133.940 132.335 124.990 1.00 40.24  ? 1004 SF4 A FE4   1 
HETATM 12542 S  S1    . SF4 G 4 .   ? 134.869 132.584 122.922 1.00 25.22  ? 1004 SF4 A S1    1 
HETATM 12543 S  S2    . SF4 G 4 .   ? 134.132 130.099 125.401 1.00 15.59  ? 1004 SF4 A S2    1 
HETATM 12544 S  S3    . SF4 G 4 .   ? 131.709 132.642 124.641 1.00 32.06  ? 1004 SF4 A S3    1 
HETATM 12545 S  S4    . SF4 G 4 .   ? 132.405 130.045 122.250 1.00 13.14  ? 1004 SF4 A S4    1 
HETATM 12546 P  PA    . FAD H 5 .   ? 121.570 141.730 88.598  1.00 27.10  ? 1005 FAD A PA    1 
HETATM 12547 O  O1A   . FAD H 5 .   ? 122.583 140.653 88.499  1.00 31.17  ? 1005 FAD A O1A   1 
HETATM 12548 O  O2A   . FAD H 5 .   ? 122.122 143.152 88.542  1.00 35.63  ? 1005 FAD A O2A   1 
HETATM 12549 O  O5B   . FAD H 5 .   ? 120.459 141.559 87.504  1.00 27.86  ? 1005 FAD A O5B   1 
HETATM 12550 C  C5B   . FAD H 5 .   ? 119.068 141.783 87.814  1.00 30.28  ? 1005 FAD A C5B   1 
HETATM 12551 C  C4B   . FAD H 5 .   ? 118.218 140.842 87.001  1.00 28.97  ? 1005 FAD A C4B   1 
HETATM 12552 O  O4B   . FAD H 5 .   ? 116.867 141.352 86.924  1.00 30.37  ? 1005 FAD A O4B   1 
HETATM 12553 C  C3B   . FAD H 5 .   ? 118.686 140.622 85.562  1.00 31.19  ? 1005 FAD A C3B   1 
HETATM 12554 O  O3B   . FAD H 5 .   ? 118.656 139.241 85.222  1.00 42.36  ? 1005 FAD A O3B   1 
HETATM 12555 C  C2B   . FAD H 5 .   ? 117.688 141.440 84.737  1.00 32.23  ? 1005 FAD A C2B   1 
HETATM 12556 O  O2B   . FAD H 5 .   ? 117.475 140.874 83.449  1.00 47.76  ? 1005 FAD A O2B   1 
HETATM 12557 C  C1B   . FAD H 5 .   ? 116.428 141.326 85.586  1.00 24.93  ? 1005 FAD A C1B   1 
HETATM 12558 N  N9A   . FAD H 5 .   ? 115.479 142.416 85.387  1.00 25.18  ? 1005 FAD A N9A   1 
HETATM 12559 C  C8A   . FAD H 5 .   ? 115.764 143.751 85.284  1.00 30.13  ? 1005 FAD A C8A   1 
HETATM 12560 N  N7A   . FAD H 5 .   ? 114.711 144.511 85.103  1.00 36.38  ? 1005 FAD A N7A   1 
HETATM 12561 C  C5A   . FAD H 5 .   ? 113.658 143.610 85.081  1.00 33.17  ? 1005 FAD A C5A   1 
HETATM 12562 C  C6A   . FAD H 5 .   ? 112.269 143.777 84.921  1.00 31.46  ? 1005 FAD A C6A   1 
HETATM 12563 N  N6A   . FAD H 5 .   ? 111.679 144.963 84.745  1.00 35.35  ? 1005 FAD A N6A   1 
HETATM 12564 N  N1A   . FAD H 5 .   ? 111.497 142.669 84.948  1.00 31.60  ? 1005 FAD A N1A   1 
HETATM 12565 C  C2A   . FAD H 5 .   ? 112.081 141.482 85.123  1.00 32.28  ? 1005 FAD A C2A   1 
HETATM 12566 N  N3A   . FAD H 5 .   ? 113.375 141.201 85.284  1.00 33.89  ? 1005 FAD A N3A   1 
HETATM 12567 C  C4A   . FAD H 5 .   ? 114.116 142.315 85.253  1.00 32.16  ? 1005 FAD A C4A   1 
HETATM 12568 N  N1    . FAD H 5 .   ? 127.694 145.024 87.825  1.00 38.74  ? 1005 FAD A N1    1 
HETATM 12569 C  C2    . FAD H 5 .   ? 127.622 145.634 86.608  1.00 37.35  ? 1005 FAD A C2    1 
HETATM 12570 O  O2    . FAD H 5 .   ? 126.562 146.099 86.176  1.00 40.23  ? 1005 FAD A O2    1 
HETATM 12571 N  N3    . FAD H 5 .   ? 128.757 145.745 85.830  1.00 34.33  ? 1005 FAD A N3    1 
HETATM 12572 C  C4    . FAD H 5 .   ? 130.011 145.288 86.156  1.00 30.60  ? 1005 FAD A C4    1 
HETATM 12573 O  O4    . FAD H 5 .   ? 130.945 145.452 85.376  1.00 35.21  ? 1005 FAD A O4    1 
HETATM 12574 C  C4X   . FAD H 5 .   ? 130.080 144.638 87.451  1.00 32.83  ? 1005 FAD A C4X   1 
HETATM 12575 N  N5    . FAD H 5 .   ? 131.232 144.170 87.842  1.00 32.03  ? 1005 FAD A N5    1 
HETATM 12576 C  C5X   . FAD H 5 .   ? 131.296 143.547 89.080  1.00 31.64  ? 1005 FAD A C5X   1 
HETATM 12577 C  C6    . FAD H 5 .   ? 132.518 143.043 89.515  1.00 33.50  ? 1005 FAD A C6    1 
HETATM 12578 C  C7    . FAD H 5 .   ? 132.632 142.410 90.748  1.00 26.17  ? 1005 FAD A C7    1 
HETATM 12579 C  C7M   . FAD H 5 .   ? 133.967 141.878 91.190  1.00 28.92  ? 1005 FAD A C7M   1 
HETATM 12580 C  C8    . FAD H 5 .   ? 131.500 142.274 91.566  1.00 23.06  ? 1005 FAD A C8    1 
HETATM 12581 C  C8M   . FAD H 5 .   ? 131.593 141.591 92.904  1.00 22.51  ? 1005 FAD A C8M   1 
HETATM 12582 C  C9    . FAD H 5 .   ? 130.278 142.777 91.136  1.00 30.06  ? 1005 FAD A C9    1 
HETATM 12583 C  C9A   . FAD H 5 .   ? 130.170 143.408 89.903  1.00 29.93  ? 1005 FAD A C9A   1 
HETATM 12584 N  N10   . FAD H 5 .   ? 128.944 143.922 89.440  1.00 35.66  ? 1005 FAD A N10   1 
HETATM 12585 C  C10   . FAD H 5 .   ? 128.864 144.551 88.215  1.00 38.44  ? 1005 FAD A C10   1 
HETATM 12586 C  "C1'" . FAD H 5 .   ? 127.733 143.816 90.267  1.00 33.32  ? 1005 FAD A "C1'" 1 
HETATM 12587 C  "C2'" . FAD H 5 .   ? 126.767 142.738 89.792  1.00 29.68  ? 1005 FAD A "C2'" 1 
HETATM 12588 O  "O2'" . FAD H 5 .   ? 125.605 143.348 89.231  1.00 21.56  ? 1005 FAD A "O2'" 1 
HETATM 12589 C  "C3'" . FAD H 5 .   ? 126.331 141.891 90.984  1.00 27.20  ? 1005 FAD A "C3'" 1 
HETATM 12590 O  "O3'" . FAD H 5 .   ? 125.938 140.616 90.492  1.00 20.75  ? 1005 FAD A "O3'" 1 
HETATM 12591 C  "C4'" . FAD H 5 .   ? 125.165 142.496 91.764  1.00 29.45  ? 1005 FAD A "C4'" 1 
HETATM 12592 O  "O4'" . FAD H 5 .   ? 125.618 142.905 93.055  1.00 35.11  ? 1005 FAD A "O4'" 1 
HETATM 12593 C  "C5'" . FAD H 5 .   ? 123.990 141.551 91.889  1.00 24.05  ? 1005 FAD A "C5'" 1 
HETATM 12594 O  "O5'" . FAD H 5 .   ? 122.907 142.038 91.071  1.00 25.85  ? 1005 FAD A "O5'" 1 
HETATM 12595 P  P     . FAD H 5 .   ? 121.411 141.666 91.388  1.00 20.60  ? 1005 FAD A P     1 
HETATM 12596 O  O1P   . FAD H 5 .   ? 121.315 140.271 92.013  1.00 24.40  ? 1005 FAD A O1P   1 
HETATM 12597 O  O2P   . FAD H 5 .   ? 120.773 142.743 92.175  1.00 30.79  ? 1005 FAD A O2P   1 
HETATM 12598 O  O3P   . FAD H 5 .   ? 120.758 141.588 89.950  1.00 34.57  ? 1005 FAD A O3P   1 
HETATM 12599 FE FE1   . SF4 I 4 .   ? 137.252 102.694 129.167 1.00 87.09  ? 1006 SF4 A FE1   1 
HETATM 12600 FE FE2   . SF4 I 4 .   ? 134.635 101.924 129.384 1.00 84.43  ? 1006 SF4 A FE2   1 
HETATM 12601 FE FE3   . SF4 I 4 .   ? 136.607 100.036 129.234 1.00 75.04  ? 1006 SF4 A FE3   1 
HETATM 12602 FE FE4   . SF4 I 4 .   ? 135.986 101.541 127.035 1.00 78.53  ? 1006 SF4 A FE4   1 
HETATM 12603 S  S1    . SF4 I 4 .   ? 134.633 100.045 128.095 1.00 70.12  ? 1006 SF4 A S1    1 
HETATM 12604 S  S2    . SF4 I 4 .   ? 138.072 101.054 127.816 1.00 68.32  ? 1006 SF4 A S2    1 
HETATM 12605 S  S3    . SF4 I 4 .   ? 135.477 103.538 128.011 1.00 68.05  ? 1006 SF4 A S3    1 
HETATM 12606 S  S4    . SF4 I 4 .   ? 136.298 101.560 130.902 1.00 68.63  ? 1006 SF4 A S4    1 
HETATM 12607 FE FE1   . FES J 6 .   ? 124.718 127.713 139.105 1.00 31.57  ? 1007 FES A FE1   1 
HETATM 12608 FE FE2   . FES J 6 .   ? 122.267 127.389 140.180 1.00 40.91  ? 1007 FES A FE2   1 
HETATM 12609 S  S1    . FES J 6 .   ? 123.089 126.425 138.375 1.00 37.25  ? 1007 FES A S1    1 
HETATM 12610 S  S2    . FES J 6 .   ? 123.809 128.847 140.761 1.00 21.87  ? 1007 FES A S2    1 
HETATM 12611 FE FE1   . SF4 K 4 .   ? 130.035 134.838 149.072 1.00 32.01  ? 701  SF4 B FE1   1 
HETATM 12612 FE FE2   . SF4 K 4 .   ? 131.508 136.425 147.401 1.00 23.55  ? 701  SF4 B FE2   1 
HETATM 12613 FE FE3   . SF4 K 4 .   ? 129.837 134.532 146.361 1.00 13.52  ? 701  SF4 B FE3   1 
HETATM 12614 FE FE4   . SF4 K 4 .   ? 132.118 133.770 147.667 1.00 34.29  ? 701  SF4 B FE4   1 
HETATM 12615 S  S1    . SF4 K 4 .   ? 131.986 134.956 145.726 1.00 8.47   ? 701  SF4 B S1    1 
HETATM 12616 S  S2    . SF4 K 4 .   ? 130.035 132.873 147.914 1.00 0.63   ? 701  SF4 B S2    1 
HETATM 12617 S  S3    . SF4 K 4 .   ? 132.241 135.372 149.285 1.00 3.14   ? 701  SF4 B S3    1 
HETATM 12618 S  S4    . SF4 K 4 .   ? 129.236 136.360 147.578 1.00 30.02  ? 701  SF4 B S4    1 
HETATM 12619 N  N1    . FMN L 7 .   ? 129.600 135.378 162.923 1.00 21.21  ? 702  FMN B N1    1 
HETATM 12620 C  C2    . FMN L 7 .   ? 130.388 135.431 164.047 1.00 25.13  ? 702  FMN B C2    1 
HETATM 12621 O  O2    . FMN L 7 .   ? 129.931 135.081 165.131 1.00 40.14  ? 702  FMN B O2    1 
HETATM 12622 N  N3    . FMN L 7 .   ? 131.686 135.876 163.961 1.00 19.50  ? 702  FMN B N3    1 
HETATM 12623 C  C4    . FMN L 7 .   ? 132.190 136.267 162.743 1.00 19.01  ? 702  FMN B C4    1 
HETATM 12624 O  O4    . FMN L 7 .   ? 133.340 136.666 162.669 1.00 33.36  ? 702  FMN B O4    1 
HETATM 12625 C  C4A   . FMN L 7 .   ? 131.404 136.216 161.603 1.00 20.77  ? 702  FMN B C4A   1 
HETATM 12626 N  N5    . FMN L 7 .   ? 131.913 136.607 160.384 1.00 24.29  ? 702  FMN B N5    1 
HETATM 12627 C  C5A   . FMN L 7 .   ? 131.116 136.550 159.259 1.00 20.22  ? 702  FMN B C5A   1 
HETATM 12628 C  C6    . FMN L 7 .   ? 131.622 136.942 158.025 1.00 19.62  ? 702  FMN B C6    1 
HETATM 12629 C  C7    . FMN L 7 .   ? 130.816 136.881 156.897 1.00 21.81  ? 702  FMN B C7    1 
HETATM 12630 C  C7M   . FMN L 7 .   ? 131.350 137.301 155.563 1.00 19.70  ? 702  FMN B C7M   1 
HETATM 12631 C  C8    . FMN L 7 .   ? 129.509 136.432 157.002 1.00 23.43  ? 702  FMN B C8    1 
HETATM 12632 C  C8M   . FMN L 7 .   ? 128.635 136.365 155.791 1.00 21.90  ? 702  FMN B C8M   1 
HETATM 12633 C  C9    . FMN L 7 .   ? 129.006 136.040 158.230 1.00 23.86  ? 702  FMN B C9    1 
HETATM 12634 C  C9A   . FMN L 7 .   ? 129.808 136.097 159.359 1.00 19.46  ? 702  FMN B C9A   1 
HETATM 12635 N  N10   . FMN L 7 .   ? 129.304 135.705 160.581 1.00 18.15  ? 702  FMN B N10   1 
HETATM 12636 C  C10   . FMN L 7 .   ? 130.100 135.767 161.701 1.00 21.68  ? 702  FMN B C10   1 
HETATM 12637 C  "C1'" . FMN L 7 .   ? 127.892 135.218 160.706 1.00 17.51  ? 702  FMN B "C1'" 1 
HETATM 12638 C  "C2'" . FMN L 7 .   ? 127.853 133.698 160.613 1.00 21.39  ? 702  FMN B "C2'" 1 
HETATM 12639 O  "O2'" . FMN L 7 .   ? 127.642 133.315 159.275 1.00 31.11  ? 702  FMN B "O2'" 1 
HETATM 12640 C  "C3'" . FMN L 7 .   ? 126.735 133.137 161.478 1.00 20.58  ? 702  FMN B "C3'" 1 
HETATM 12641 O  "O3'" . FMN L 7 .   ? 125.553 133.865 161.246 1.00 34.32  ? 702  FMN B "O3'" 1 
HETATM 12642 C  "C4'" . FMN L 7 .   ? 127.099 133.232 162.951 1.00 22.19  ? 702  FMN B "C4'" 1 
HETATM 12643 O  "O4'" . FMN L 7 .   ? 128.052 132.246 163.269 1.00 22.00  ? 702  FMN B "O4'" 1 
HETATM 12644 C  "C5'" . FMN L 7 .   ? 125.869 133.041 163.821 1.00 17.95  ? 702  FMN B "C5'" 1 
HETATM 12645 O  "O5'" . FMN L 7 .   ? 126.188 133.349 165.155 1.00 18.23  ? 702  FMN B "O5'" 1 
HETATM 12646 P  P     . FMN L 7 .   ? 125.022 133.877 166.124 1.00 27.50  ? 702  FMN B P     1 
HETATM 12647 O  O1P   . FMN L 7 .   ? 124.086 132.735 166.428 1.00 34.04  ? 702  FMN B O1P   1 
HETATM 12648 O  O2P   . FMN L 7 .   ? 124.273 134.972 165.409 1.00 21.24  ? 702  FMN B O2P   1 
HETATM 12649 O  O3P   . FMN L 7 .   ? 125.616 134.405 167.404 1.00 28.98  ? 702  FMN B O3P   1 
HETATM 12650 FE FE1   . SF4 M 4 .   ? 156.518 174.469 154.425 1.00 158.99 ? 703  SF4 B FE1   1 
HETATM 12651 FE FE2   . SF4 M 4 .   ? 154.619 175.479 156.116 1.00 158.87 ? 703  SF4 B FE2   1 
HETATM 12652 FE FE3   . SF4 M 4 .   ? 156.490 177.141 155.013 1.00 158.32 ? 703  SF4 B FE3   1 
HETATM 12653 FE FE4   . SF4 M 4 .   ? 157.227 175.325 156.924 1.00 161.17 ? 703  SF4 B FE4   1 
HETATM 12654 S  S1    . SF4 M 4 .   ? 155.813 177.093 157.192 1.00 156.92 ? 703  SF4 B S1    1 
HETATM 12655 S  S2    . SF4 M 4 .   ? 158.312 175.769 154.965 1.00 156.18 ? 703  SF4 B S2    1 
HETATM 12656 S  S3    . SF4 M 4 .   ? 155.850 173.583 156.417 1.00 155.38 ? 703  SF4 B S3    1 
HETATM 12657 S  S4    . SF4 M 4 .   ? 154.885 175.970 153.905 1.00 154.89 ? 703  SF4 B S4    1 
HETATM 12658 FE FE1   . SF4 N 4 .   ? 152.768 165.381 149.064 1.00 126.92 ? 704  SF4 B FE1   1 
HETATM 12659 FE FE2   . SF4 N 4 .   ? 152.330 167.953 149.901 1.00 122.22 ? 704  SF4 B FE2   1 
HETATM 12660 FE FE3   . SF4 N 4 .   ? 153.349 167.482 147.407 1.00 126.68 ? 704  SF4 B FE3   1 
HETATM 12661 FE FE4   . SF4 N 4 .   ? 154.883 167.012 149.622 1.00 128.89 ? 704  SF4 B FE4   1 
HETATM 12662 S  S1    . SF4 N 4 .   ? 154.082 169.028 148.914 1.00 126.81 ? 704  SF4 B S1    1 
HETATM 12663 S  S2    . SF4 N 4 .   ? 154.648 165.654 147.809 1.00 123.10 ? 704  SF4 B S2    1 
HETATM 12664 S  S3    . SF4 N 4 .   ? 153.307 166.268 151.089 1.00 123.55 ? 704  SF4 B S3    1 
HETATM 12665 S  S4    . SF4 N 4 .   ? 151.291 166.884 148.181 1.00 117.89 ? 704  SF4 B S4    1 
HETATM 12666 P  PA    . NAD O 8 .   ? 124.062 134.665 157.875 1.00 32.07  ? 705  NAD B PA    1 
HETATM 12667 O  O1A   . NAD O 8 .   ? 124.506 133.478 158.663 1.00 11.16  ? 705  NAD B O1A   1 
HETATM 12668 O  O2A   . NAD O 8 .   ? 124.161 134.608 156.388 1.00 37.93  ? 705  NAD B O2A   1 
HETATM 12669 O  O5B   . NAD O 8 .   ? 124.824 135.972 158.405 1.00 30.04  ? 705  NAD B O5B   1 
HETATM 12670 C  C5B   . NAD O 8 .   ? 124.572 137.218 157.713 1.00 24.22  ? 705  NAD B C5B   1 
HETATM 12671 C  C4B   . NAD O 8 .   ? 124.976 138.378 158.589 1.00 26.96  ? 705  NAD B C4B   1 
HETATM 12672 O  O4B   . NAD O 8 .   ? 126.405 138.387 158.798 1.00 40.18  ? 705  NAD B O4B   1 
HETATM 12673 C  C3B   . NAD O 8 .   ? 124.718 139.783 158.033 1.00 27.14  ? 705  NAD B C3B   1 
HETATM 12674 O  O3B   . NAD O 8 .   ? 123.373 140.213 158.202 1.00 22.90  ? 705  NAD B O3B   1 
HETATM 12675 C  C2B   . NAD O 8 .   ? 125.749 140.649 158.773 1.00 36.78  ? 705  NAD B C2B   1 
HETATM 12676 O  O2B   . NAD O 8 .   ? 125.165 141.443 159.782 1.00 48.30  ? 705  NAD B O2B   1 
HETATM 12677 C  C1B   . NAD O 8 .   ? 126.701 139.626 159.396 1.00 23.27  ? 705  NAD B C1B   1 
HETATM 12678 N  N9A   . NAD O 8 .   ? 128.116 139.925 159.207 1.00 19.65  ? 705  NAD B N9A   1 
HETATM 12679 C  C8A   . NAD O 8 .   ? 128.729 140.366 158.061 1.00 18.24  ? 705  NAD B C8A   1 
HETATM 12680 N  N7A   . NAD O 8 .   ? 130.017 140.557 158.203 1.00 23.63  ? 705  NAD B N7A   1 
HETATM 12681 C  C5A   . NAD O 8 .   ? 130.272 140.231 159.527 1.00 27.03  ? 705  NAD B C5A   1 
HETATM 12682 C  C6A   . NAD O 8 .   ? 131.450 140.229 160.299 1.00 28.81  ? 705  NAD B C6A   1 
HETATM 12683 N  N6A   . NAD O 8 .   ? 132.643 140.579 159.831 1.00 29.08  ? 705  NAD B N6A   1 
HETATM 12684 N  N1A   . NAD O 8 .   ? 131.353 139.849 161.594 1.00 27.23  ? 705  NAD B N1A   1 
HETATM 12685 C  C2A   . NAD O 8 .   ? 130.152 139.498 162.065 1.00 25.34  ? 705  NAD B C2A   1 
HETATM 12686 N  N3A   . NAD O 8 .   ? 128.982 139.463 161.436 1.00 24.09  ? 705  NAD B N3A   1 
HETATM 12687 C  C4A   . NAD O 8 .   ? 129.106 139.844 160.156 1.00 24.58  ? 705  NAD B C4A   1 
HETATM 12688 O  O3    . NAD O 8 .   ? 122.552 135.025 158.284 1.00 37.58  ? 705  NAD B O3    1 
HETATM 12689 P  PN    . NAD O 8 .   ? 121.149 134.248 158.278 1.00 50.53  ? 705  NAD B PN    1 
HETATM 12690 O  O1N   . NAD O 8 .   ? 120.088 135.174 158.774 1.00 32.45  ? 705  NAD B O1N   1 
HETATM 12691 O  O2N   . NAD O 8 .   ? 120.949 133.594 156.952 1.00 34.92  ? 705  NAD B O2N   1 
HETATM 12692 O  O5D   . NAD O 8 .   ? 121.424 133.123 159.384 1.00 32.25  ? 705  NAD B O5D   1 
HETATM 12693 C  C5D   . NAD O 8 .   ? 121.796 133.544 160.717 1.00 31.48  ? 705  NAD B C5D   1 
HETATM 12694 C  C4D   . NAD O 8 .   ? 121.986 132.324 161.581 1.00 29.19  ? 705  NAD B C4D   1 
HETATM 12695 O  O4D   . NAD O 8 .   ? 120.723 131.632 161.690 1.00 34.43  ? 705  NAD B O4D   1 
HETATM 12696 C  C3D   . NAD O 8 .   ? 122.993 131.286 161.056 1.00 26.68  ? 705  NAD B C3D   1 
HETATM 12697 O  O3D   . NAD O 8 .   ? 123.787 130.792 162.124 1.00 25.12  ? 705  NAD B O3D   1 
HETATM 12698 C  C2D   . NAD O 8 .   ? 122.089 130.186 160.489 1.00 23.55  ? 705  NAD B C2D   1 
HETATM 12699 O  O2D   . NAD O 8 .   ? 122.680 128.896 160.465 1.00 26.85  ? 705  NAD B O2D   1 
HETATM 12700 C  C1D   . NAD O 8 .   ? 120.923 130.246 161.473 1.00 26.44  ? 705  NAD B C1D   1 
HETATM 12701 N  N1N   . NAD O 8 .   ? 119.678 129.707 160.898 1.00 27.87  ? 705  NAD B N1N   1 
HETATM 12702 C  C2N   . NAD O 8 .   ? 119.286 128.419 161.185 1.00 21.60  ? 705  NAD B C2N   1 
HETATM 12703 C  C3N   . NAD O 8 .   ? 118.110 127.926 160.632 1.00 23.00  ? 705  NAD B C3N   1 
HETATM 12704 C  C7N   . NAD O 8 .   ? 117.683 126.527 160.942 1.00 34.19  ? 705  NAD B C7N   1 
HETATM 12705 O  O7N   . NAD O 8 .   ? 118.376 125.825 161.695 1.00 34.39  ? 705  NAD B O7N   1 
HETATM 12706 N  N7N   . NAD O 8 .   ? 116.566 126.080 160.385 1.00 34.50  ? 705  NAD B N7N   1 
HETATM 12707 C  C4N   . NAD O 8 .   ? 117.340 128.724 159.801 1.00 26.18  ? 705  NAD B C4N   1 
HETATM 12708 C  C5N   . NAD O 8 .   ? 117.748 130.012 159.522 1.00 28.88  ? 705  NAD B C5N   1 
HETATM 12709 C  C6N   . NAD O 8 .   ? 118.916 130.494 160.071 1.00 26.35  ? 705  NAD B C6N   1 
HETATM 12710 ZN ZN    . ZN  P 9 .   ? 136.471 162.875 147.209 1.00 77.93  ? 706  ZN  B ZN    1 
HETATM 12711 ZN ZN    . ZN  Q 9 .   ? 140.230 147.350 174.796 1.00 126.86 ? 707  ZN  B ZN    1 
# 
