data_15488 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, 13CO and 13CA resonance assignment of ABL kinase domain in complex with imatinib ; _BMRB_accession_number 15488 _BMRB_flat_file_name bmr15488.str _Entry_type original _Submission_date 2007-09-25 _Accession_date 2007-09-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vajpai Navratna . . 2 Strauss Andre . . 3 Fendrich Gabriele . . 4 Cowan-Jacob Sandra W. . 5 Manley Paul W. . 6 Jahnke Wolfgang . . 7 Grzesiek Stephan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 254 "13C chemical shifts" 516 "15N chemical shifts" 254 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-12 update BMRB 'added PubMed ID' 2008-06-05 update BMRB 'complete entry citation' 2008-03-31 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636920 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vajpai Navratna . . 2 Strauss Andre . . 3 Fendrich Gabriele . . 4 Cowan-Jacob Sandra W. . 5 Manley Paul W. . 6 Jahnke Wolfgang . . 7 Grzesiek Stephan . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 2 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 41 _Page_last 42 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ABL kinase domain with imatinib' _Enzyme_commission_number 'EC 2.7.1.112' loop_ _Mol_system_component_name _Mol_label 'ABL kinase domain' $ABL_kinase_domain_GAMDP-S229-S500 imatinib $entity_STI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'signal transdcution pathways, misregulation leads to Leukemia' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ABL_kinase_domain_GAMDP-S229-S500 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ABL_kinase_domain_GAMDP-S229-S500 _Molecular_mass 32014.7 _Mol_thiol_state 'not reported' loop_ _Biological_function 'kinase, signal transduction pathways' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 277 _Mol_residue_sequence ; GAMDPSPNYDKWEMERTDIT MKHKLGGGQYGEVYEGVWKK YSLTVAVKTLKEDTMEVEEF LKEAAVMKEIKHPNLVQLLG VCTREPPFYIITEFMTYGNL LDYLRECNRQEVNAVVLLYM ATQISSAMEYLEKKNFIHRD LAARNCLVGENHLVKVADFG LSRLMTGDTYTAHAGAKFPI KWTAPESLAYNKFSIKSDVW AFGVLLWEIATYGMSPYPGI DLSQVYELLEKDYRMERPEG CPEKVYELMRACWQWNPSDR PSFAEIHQAFETMFQES ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 224 GLY 2 225 ALA 3 226 MET 4 227 ASP 5 228 PRO 6 229 SER 7 230 PRO 8 231 ASN 9 232 TYR 10 233 ASP 11 234 LYS 12 235 TRP 13 236 GLU 14 237 MET 15 238 GLU 16 239 ARG 17 240 THR 18 241 ASP 19 242 ILE 20 243 THR 21 244 MET 22 245 LYS 23 246 HIS 24 247 LYS 25 248 LEU 26 249 GLY 27 250 GLY 28 251 GLY 29 252 GLN 30 253 TYR 31 254 GLY 32 255 GLU 33 256 VAL 34 257 TYR 35 258 GLU 36 259 GLY 37 260 VAL 38 261 TRP 39 262 LYS 40 263 LYS 41 264 TYR 42 265 SER 43 266 LEU 44 267 THR 45 268 VAL 46 269 ALA 47 270 VAL 48 271 LYS 49 272 THR 50 273 LEU 51 274 LYS 52 275 GLU 53 276 ASP 54 277 THR 55 278 MET 56 279 GLU 57 280 VAL 58 281 GLU 59 282 GLU 60 283 PHE 61 284 LEU 62 285 LYS 63 286 GLU 64 287 ALA 65 288 ALA 66 289 VAL 67 290 MET 68 291 LYS 69 292 GLU 70 293 ILE 71 294 LYS 72 295 HIS 73 296 PRO 74 297 ASN 75 298 LEU 76 299 VAL 77 300 GLN 78 301 LEU 79 302 LEU 80 303 GLY 81 304 VAL 82 305 CYS 83 306 THR 84 307 ARG 85 308 GLU 86 309 PRO 87 310 PRO 88 311 PHE 89 312 TYR 90 313 ILE 91 314 ILE 92 315 THR 93 316 GLU 94 317 PHE 95 318 MET 96 319 THR 97 320 TYR 98 321 GLY 99 322 ASN 100 323 LEU 101 324 LEU 102 325 ASP 103 326 TYR 104 327 LEU 105 328 ARG 106 329 GLU 107 330 CYS 108 331 ASN 109 332 ARG 110 333 GLN 111 334 GLU 112 335 VAL 113 336 ASN 114 337 ALA 115 338 VAL 116 339 VAL 117 340 LEU 118 341 LEU 119 342 TYR 120 343 MET 121 344 ALA 122 345 THR 123 346 GLN 124 347 ILE 125 348 SER 126 349 SER 127 350 ALA 128 351 MET 129 352 GLU 130 353 TYR 131 354 LEU 132 355 GLU 133 356 LYS 134 357 LYS 135 358 ASN 136 359 PHE 137 360 ILE 138 361 HIS 139 362 ARG 140 363 ASP 141 364 LEU 142 365 ALA 143 366 ALA 144 367 ARG 145 368 ASN 146 369 CYS 147 370 LEU 148 371 VAL 149 372 GLY 150 373 GLU 151 374 ASN 152 375 HIS 153 376 LEU 154 377 VAL 155 378 LYS 156 379 VAL 157 380 ALA 158 381 ASP 159 382 PHE 160 383 GLY 161 384 LEU 162 385 SER 163 386 ARG 164 387 LEU 165 388 MET 166 389 THR 167 390 GLY 168 391 ASP 169 392 THR 170 393 TYR 171 394 THR 172 395 ALA 173 396 HIS 174 397 ALA 175 398 GLY 176 399 ALA 177 400 LYS 178 401 PHE 179 402 PRO 180 403 ILE 181 404 LYS 182 405 TRP 183 406 THR 184 407 ALA 185 408 PRO 186 409 GLU 187 410 SER 188 411 LEU 189 412 ALA 190 413 TYR 191 414 ASN 192 415 LYS 193 416 PHE 194 417 SER 195 418 ILE 196 419 LYS 197 420 SER 198 421 ASP 199 422 VAL 200 423 TRP 201 424 ALA 202 425 PHE 203 426 GLY 204 427 VAL 205 428 LEU 206 429 LEU 207 430 TRP 208 431 GLU 209 432 ILE 210 433 ALA 211 434 THR 212 435 TYR 213 436 GLY 214 437 MET 215 438 SER 216 439 PRO 217 440 TYR 218 441 PRO 219 442 GLY 220 443 ILE 221 444 ASP 222 445 LEU 223 446 SER 224 447 GLN 225 448 VAL 226 449 TYR 227 450 GLU 228 451 LEU 229 452 LEU 230 453 GLU 231 454 LYS 232 455 ASP 233 456 TYR 234 457 ARG 235 458 MET 236 459 GLU 237 460 ARG 238 461 PRO 239 462 GLU 240 463 GLY 241 464 CYS 242 465 PRO 243 466 GLU 244 467 LYS 245 468 VAL 246 469 TYR 247 470 GLU 248 471 LEU 249 472 MET 250 473 ARG 251 474 ALA 252 475 CYS 253 476 TRP 254 477 GLN 255 478 TRP 256 479 ASN 257 480 PRO 258 481 SER 259 482 ASP 260 483 ARG 261 484 PRO 262 485 SER 263 486 PHE 264 487 ALA 265 488 GLU 266 489 ILE 267 490 HIS 268 491 GLN 269 492 ALA 270 493 PHE 271 494 GLU 272 495 THR 273 496 MET 274 497 PHE 275 498 GLN 276 499 GLU 277 500 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1FPU "Crystal Structure Of Abl Kinase Domain In Complex With A Small Molecule Inhibitor" 100.36 293 99.28 99.64 0.00e+00 PDB 1IEP "Crystal Structure Of The C-Abl Kinase Domain In Complex With Sti-571." 100.36 293 99.28 99.64 0.00e+00 PDB 1M52 "Crystal Structure Of The C-Abl Kinase Domain In Complex With Pd173955" 100.36 293 99.28 99.64 0.00e+00 PDB 1OPJ "Structural Basis For The Auto-Inhibition Of C-Abl Tyrosine Kinase" 100.36 293 99.28 99.64 0.00e+00 PDB 1OPK "Structural Basis For The Auto-Inhibition Of C-Abl Tyrosine Kinase" 98.19 495 99.26 100.00 0.00e+00 PDB 1OPL "Structural Basis For The Auto-Inhibition Of C-Abl Tyrosine Kinase" 98.19 537 99.63 100.00 0.00e+00 PDB 2E2B "Crystal Structure Of The C-Abl Kinase Domain In Complex With Inno-406" 100.36 293 99.64 99.64 0.00e+00 PDB 2F4J "Structure Of The Kinase Domain Of An Imatinib-Resistant Abl Mutant In Complex With The Aurora Kinase Inhibitor Vx-680" 98.19 287 99.63 99.63 0.00e+00 PDB 2FO0 "Organization Of The Sh3-Sh2 Unit In Active And Inactive Forms Of The C-Abl Tyrosine Kinase" 98.19 495 99.63 100.00 0.00e+00 PDB 2G1T "A Src-Like Inactive Conformation In The Abl Tyrosine Kinase Domain" 98.19 287 100.00 100.00 0.00e+00 PDB 2G2F "A Src-Like Inactive Conformation In The Abl Tyrosine Kinase Domain" 98.19 287 99.63 99.63 0.00e+00 PDB 2G2H "A Src-Like Inactive Conformation In The Abl Tyrosine Kinase Domain" 98.19 287 99.63 99.63 0.00e+00 PDB 2G2I "A Src-Like Inactive Conformation In The Abl Tyrosine Kinase Domain" 98.19 287 99.63 99.63 0.00e+00 PDB 2GQG "X-Ray Crystal Structure Of Dasatinib (Bms-354825) Bound To Activated Abl Kinase Domain" 100.36 278 99.28 99.28 0.00e+00 PDB 2HIW "Crystal Structure Of Inactive Conformation Abl Kinase Catalytic Domain Complexed With Type Ii Inhibitor" 100.00 287 99.28 99.28 0.00e+00 PDB 2HYY "Human Abl Kinase Domain In Complex With Imatinib (Sti571, Glivec)" 98.19 273 100.00 100.00 0.00e+00 PDB 2HZ0 "Abl Kinase Domain In Complex With Nvp-Aeg082" 97.11 270 100.00 100.00 0.00e+00 PDB 2HZ4 "Abl Kinase Domain Unligated And In Complex With Tetrahydrostaurosporine" 98.19 273 100.00 100.00 0.00e+00 PDB 2HZI "Abl Kinase Domain In Complex With Pd180970" 100.00 277 100.00 100.00 0.00e+00 PDB 2HZN "Abl Kinase Domain In Complex With Nvp-Afg210" 100.36 293 99.28 99.64 0.00e+00 PDB 2QOH "Crystal Structure Of Abl Kinase Bound With Ppy-a" 98.19 288 99.63 100.00 0.00e+00 PDB 2V7A "Crystal Structure Of The T315i Abl Mutant In Complex With The Inhibitor Pha-739358" 98.56 286 99.27 99.27 0.00e+00 PDB 2Z60 "Crystal Structure Of The T315i Mutant Of Abl Kinase Bound With Ppy-A" 98.19 288 99.26 99.63 0.00e+00 PDB 3CS9 "Human Abl Kinase In Complex With Nilotinib" 100.00 277 100.00 100.00 0.00e+00 PDB 3DK3 "Crystal Structure Of Mutant Abl Kinase Domain In Complex With Small Molecule Fragment" 96.75 293 98.88 99.63 0.00e+00 PDB 3DK6 "Crystal Structure Of Mutant Abl Kinase Domain In Complex With Small Molecule Fragment" 96.75 293 98.51 99.25 0.00e+00 PDB 3DK7 "Crystal Structure Of Mutant Abl Kinase Domain In Complex With Small Molecule Fragment" 96.75 277 98.51 98.88 0.00e+00 PDB 3IK3 "Ap24534, A Pan-Bcr-Abl Inhibitor For Chronic Myeloid Leukemi Potently Inhibits The T315i Mutant And Overcomes Mutation-B Resist" 98.19 288 99.26 99.63 0.00e+00 PDB 3K5V "Structure Of Abl Kinase In Complex With Imatinib And Gnf-2" 100.36 293 99.28 99.64 0.00e+00 PDB 3KF4 "Structural Analysis Of Dfg-In And Dfg-Out Dual Src-Abl Inhibitors Sharing A Common Vinyl Purine Template" 98.19 288 99.63 100.00 0.00e+00 PDB 3KFA "Structural Analysis Of Dfg-In And Dfg-Out Dual Src-Abl Inhibitors Sharing A Common Vinyl Purine Template" 98.19 288 99.63 100.00 0.00e+00 PDB 3MS9 "Abl Kinase In Complex With Imatinib And A Fragment (Frag1) I Myristate Pocket" 100.36 293 99.28 99.64 0.00e+00 PDB 3MSS "Abl Kinase In Complex With Imatinib And Fragment (Frag2) In The Myristate Site" 100.36 293 99.28 99.64 0.00e+00 PDB 3OXZ "Crystal Structure Of Abl Kinase Domain Bound With A Dfg-Out Inhibitor Ap24534" 98.19 284 99.63 100.00 0.00e+00 PDB 3OY3 "Crystal Structure Of Abl T315i Mutant Kinase Domain Bound With A Dfg- Out Inhibitor Ap24589" 98.19 284 99.26 99.63 0.00e+00 PDB 3PYY "Discovery And Characterization Of A Cell-Permeable, Small-Molecule C- Abl Kinase Activator That Binds To The Myristoyl Binding " 98.19 298 100.00 100.00 0.00e+00 PDB 3QRI "The Crystal Structure Of Human Abl1 Kinase Domain In Complex With Dcc- 2036" 99.64 277 99.28 99.64 0.00e+00 PDB 3QRJ "The Crystal Structure Of Human Abl1 Kinase Domain T315i Mutant In Complex With Dcc-2036" 99.64 277 98.91 99.28 0.00e+00 PDB 3QRK "The Crystal Structure Of Human Abl1 Kinase Domain In Complex With Dp- 987" 99.64 277 99.28 99.64 0.00e+00 PDB 3UE4 "Structural And Spectroscopic Analysis Of The Kinase Inhibitor Bosutinib Binding To The Abl Tyrosine Kinase Domain" 98.19 287 100.00 100.00 0.00e+00 PDB 4TWP "The Crystal Structure Of Human Abl1 T315i Gatekeeper Mutant Kinase Domain In Complex With Axitinib" 96.75 271 99.63 99.63 0.00e+00 PDB 4WA9 "The Crystal Structure Of Human Abl1 Wild Type Kinase Domain In Complex With Axitinib" 98.19 286 100.00 100.00 0.00e+00 PDB 4XEY "Crystal Structure Of An Sh2-kinase Domain Construct Of C-abl Tyrosine Kinase" 98.19 408 100.00 100.00 0.00e+00 DBJ BAC41088 "unnamed protein product [Mus musculus]" 98.19 1123 99.63 100.00 0.00e+00 DBJ BAD92693 "v-abl Abelson murine leukemia viral oncogene homolog 1 isoform b variant [Homo sapiens]" 98.19 1167 100.00 100.00 0.00e+00 DBJ BAD92879 "Proto-oncogene tyrosine-protein kinase ABL1 variant [Homo sapiens]" 90.97 949 100.00 100.00 0.00e+00 DBJ BAE38629 "unnamed protein product [Mus musculus]" 95.31 368 99.24 99.62 0.00e+00 DBJ BAE43394 "unnamed protein product [Mus musculus]" 95.31 368 99.62 100.00 0.00e+00 EMBL CAA24781 "oncogene v-abl [Mus sp.]" 98.19 918 99.63 100.00 0.00e+00 EMBL CAA34438 "unnamed protein product [Homo sapiens]" 98.19 1130 100.00 100.00 0.00e+00 EMBL CAB56204 "unnamed protein product [Abelson murine leukemia virus]" 98.19 818 99.63 100.00 0.00e+00 EMBL CDQ98411 "unnamed protein product [Oncorhynchus mykiss]" 71.48 207 97.47 100.00 8.33e-141 GB AAA51561 "abl protein [Homo sapiens]" 98.19 1130 99.26 99.63 0.00e+00 GB AAA88241 "125 kDa c-abl protein [Mus musculus]" 98.19 1123 99.63 100.00 0.00e+00 GB AAB60393 "proto-oncogene tyrosine-protein kinase [Homo sapiens]" 98.19 1149 100.00 100.00 0.00e+00 GB AAB60394 "proto-oncogene tyrosine-protein kinase [Homo sapiens]" 98.19 1130 100.00 100.00 0.00e+00 GB AAC82569 "p120 polyprotein [Abelson murine leukemia virus]" 98.19 981 99.63 100.00 0.00e+00 REF NP_001094320 "tyrosine-protein kinase ABL1 [Rattus norvegicus]" 98.19 1143 99.63 100.00 0.00e+00 REF NP_001106174 "tyrosine-protein kinase ABL1 isoform a [Mus musculus]" 98.19 1142 99.63 100.00 0.00e+00 REF NP_001193789 "tyrosine-protein kinase ABL1 [Bos taurus]" 98.19 1151 99.26 100.00 0.00e+00 REF NP_001269974 "tyrosine-protein kinase ABL1 isoform c [Mus musculus]" 98.19 1118 99.63 100.00 0.00e+00 REF NP_001269975 "tyrosine-protein kinase ABL1 isoform d [Mus musculus]" 98.19 1117 99.63 100.00 0.00e+00 SP P00519 "RecName: Full=Tyrosine-protein kinase ABL1; AltName: Full=Abelson murine leukemia viral oncogene homolog 1; AltName: Full=Abels" 98.19 1130 100.00 100.00 0.00e+00 SP P00520 "RecName: Full=Tyrosine-protein kinase ABL1; AltName: Full=Abelson murine leukemia viral oncogene homolog 1; AltName: Full=Abels" 98.19 1123 99.63 100.00 0.00e+00 SP P00521 "RecName: Full=Tyrosine-protein kinase transforming protein Abl; AltName: Full=V-abl" 98.19 746 99.63 100.00 0.00e+00 SP P10447 "RecName: Full=Tyrosine-protein kinase transforming protein Abl; AltName: Full=V-abl" 94.58 439 99.24 99.62 0.00e+00 TPG DAA24240 "TPA: arg tyrosine kinase-like [Bos taurus]" 98.19 1151 99.26 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_STI _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE _BMRB_code STI _PDB_code STI _Molecular_mass 493.603 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? C18 C18 C . 0 . ? C19 C19 C . 0 . ? C2 C2 C . 0 . ? C20 C20 C . 0 . ? C22 C22 C . 0 . ? C23 C23 C . 0 . ? C25 C25 C . 0 . ? C26 C26 C . 0 . ? C27 C27 C . 0 . ? C28 C28 C . 0 . ? C29 C29 C . 0 . ? C4 C4 C . 0 . ? C46 C46 C . 0 . ? C49 C49 C . 0 . ? C5 C5 C . 0 . ? C50 C50 C . 0 . ? C52 C52 C . 0 . ? C53 C53 C . 0 . ? C54 C54 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C9 C9 C . 0 . ? H11 H11 H . 0 . ? H111 H111 H . 0 . ? H121 H121 H . 0 . ? H131 H131 H . 0 . ? H151 H151 H . 0 . ? H171 H171 H . 0 . ? H181 H181 H . 0 . ? H201 H201 H . 0 . ? H202 H202 H . 0 . ? H203 H203 H . 0 . ? H21 H21 H . 0 . ? H211 H211 H . 0 . ? H251 H251 H . 0 . ? H261 H261 H . 0 . ? H281 H281 H . 0 . ? H291 H291 H . 0 . ? H41 H41 H . 0 . ? H461 H461 H . 0 . ? H462 H462 H . 0 . ? H491 H491 H . 0 . ? H492 H492 H . 0 . ? H501 H501 H . 0 . ? H502 H502 H . 0 . ? H521 H521 H . 0 . ? H522 H522 H . 0 . ? H531 H531 H . 0 . ? H532 H532 H . 0 . ? H541 H541 H . 0 . ? H542 H542 H . 0 . ? H543 H543 H . 0 . ? H61 H61 H . 0 . ? N10 N10 N . 0 . ? N13 N13 N . 0 . ? N21 N21 N . 0 . ? N3 N3 N . 0 . ? N48 N48 N . 0 . ? N51 N51 N . 0 . ? N8 N8 N . 0 . ? O29 O29 O . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 C6 ? ? SING C1 C2 ? ? SING C1 H11 ? ? SING C6 C5 ? ? SING C6 H61 ? ? DOUB C5 C4 ? ? SING C5 C7 ? ? SING C4 N3 ? ? SING C4 H41 ? ? DOUB N3 C2 ? ? SING C2 H21 ? ? DOUB C7 C12 ? ? SING C7 N8 ? ? SING C12 C11 ? ? SING C12 H121 ? ? DOUB C11 N10 ? ? SING C11 H111 ? ? SING N10 C9 ? ? DOUB C9 N8 ? ? SING C9 N13 ? ? SING N13 C14 ? ? SING N13 H131 ? ? DOUB C14 C19 ? ? SING C14 C15 ? ? SING C19 C18 ? ? SING C19 C20 ? ? DOUB C18 C17 ? ? SING C18 H181 ? ? SING C17 C16 ? ? SING C17 H171 ? ? DOUB C16 C15 ? ? SING C16 N21 ? ? SING C15 H151 ? ? SING N21 C22 ? ? SING N21 H211 ? ? SING C22 C23 ? ? DOUB C22 O29 ? ? DOUB C23 C25 ? ? SING C23 C29 ? ? SING C25 C26 ? ? SING C25 H251 ? ? DOUB C26 C27 ? ? SING C26 H261 ? ? SING C27 C28 ? ? SING C27 C46 ? ? DOUB C28 C29 ? ? SING C28 H281 ? ? SING C29 H291 ? ? SING C46 N48 ? ? SING C46 H461 ? ? SING C46 H462 ? ? SING N48 C53 ? ? SING N48 C49 ? ? SING C53 C52 ? ? SING C53 H531 ? ? SING C53 H532 ? ? SING C52 N51 ? ? SING C52 H521 ? ? SING C52 H522 ? ? SING N51 C54 ? ? SING N51 C50 ? ? SING C54 H541 ? ? SING C54 H542 ? ? SING C54 H543 ? ? SING C50 C49 ? ? SING C50 H501 ? ? SING C50 H502 ? ? SING C49 H491 ? ? SING C49 H492 ? ? SING C20 H201 ? ? SING C20 H202 ? ? SING C20 H203 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $ABL_kinase_domain_GAMDP-S229-S500 Human 9606 Eukaryota Metazoa Homo sapiens BCR-ABL 'Fusion protein, present in patients suffering from Leukemia.' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $ABL_kinase_domain_GAMDP-S229-S500 'recombinant technology' . Baculovirus-infected "insect cells" . baculovirus Sf9 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ABL_kinase_domain_GAMDP-S229-S500 0.45 mM '[U-100% 13C; U-100% 15N]' BisTris 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 3 mM 'natural abundance' EDTA 2 mM 'natural abundance' $entity_STI 0.45 mM 'natural abundance' TCEP 3 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'Identical conditions were used in the preparation of selectively labeled ABL-imatinib samples.Following 15N labeled samples were produced: Ala, Gly, Ile, Leu, Met, Phe, Thr, Trp , Tyr , Val to overcome ambiguity.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ABL_kinase_domain_GAMDP-S229-S500 0.45 mM '[U-100% 15N]' BisTris 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 3 mM 'natural abundance' EDTA 2 mM 'natural abundance' TCEP 3 mM 'natural abundance' $entity_STI 0.45 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.2.2_01 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details ; Equipped with TCI cryoprobe triple resonance, tripe-axis pulsed field gradient probes ; save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'Equipped with triple resonance, tripe-axis pulsed field gradient probes' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_15N-edited_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited 1H-1H NOESY' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'Both Uniformly 13C,15N and uniformly 15N labeled samples are prepared at the same conditions' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 295.5 2.5 K pH 6.5 0.1 pH pressure 1 . atm 'ionic strength' 100 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '1H, 15N and 13C are referenced relative to the frequency of the 2H lock resonance of water' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water H 1 protons ppm 4.773 internal direct . other parallel 1 DSS C 13 'methyl protons' ppm 0.0 . indirect . other parallel 0.2514495 DSS N 15 'methyl protons' ppm 0.0 . indirect . other parallel 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HN(CO)CA' '3D HNCA' '3D 15N-edited 1H-1H NOESY' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'ABL kinase domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 224 1 GLY C C 179.98 0.040 1 2 224 1 GLY CA C 43.48 0.040 1 3 225 2 ALA H H 8.65 0.005 1 4 225 2 ALA C C 177.88 0.040 1 5 225 2 ALA CA C 53.34 0.040 1 6 225 2 ALA N N 123.26 0.040 1 7 226 3 MET H H 8.47 0.005 1 8 226 3 MET C C 175.72 0.040 1 9 226 3 MET CA C 55.09 0.040 1 10 226 3 MET N N 117.66 0.040 1 11 227 4 ASP H H 8.07 0.005 1 12 227 4 ASP CA C 52.78 0.040 1 13 227 4 ASP N N 122.57 0.040 1 14 228 5 PRO C C 176.76 0.040 1 15 228 5 PRO CA C 63.17 0.040 1 16 229 6 SER H H 8.39 0.005 1 17 229 6 SER CA C 56.55 0.040 1 18 229 6 SER N N 117.15 0.040 1 19 230 7 PRO C C 176.43 0.040 1 20 230 7 PRO CA C 63.44 0.040 1 21 231 8 ASN H H 8.29 0.005 1 22 231 8 ASN C C 174.56 0.040 1 23 231 8 ASN CA C 53.16 0.040 1 24 231 8 ASN N N 117.94 0.040 1 25 232 9 TYR H H 7.99 0.005 1 26 232 9 TYR C C 174.99 0.040 1 27 232 9 TYR CA C 58.06 0.040 1 28 232 9 TYR N N 120.55 0.040 1 29 233 10 ASP H H 8.17 0.005 1 30 233 10 ASP C C 177.05 0.040 1 31 233 10 ASP CA C 53.41 0.040 1 32 233 10 ASP N N 122.94 0.040 1 33 234 11 LYS H H 8.21 0.005 1 34 234 11 LYS C C 176.47 0.040 1 35 234 11 LYS CA C 57.65 0.040 1 36 234 11 LYS N N 119.96 0.040 1 37 235 12 TRP H H 8.12 0.005 1 38 235 12 TRP C C 176.56 0.040 1 39 235 12 TRP CA C 57.84 0.040 1 40 235 12 TRP N N 118.82 0.040 1 41 236 13 GLU H H 7.38 0.005 1 42 236 13 GLU C C 176.68 0.040 1 43 236 13 GLU CA C 56.62 0.040 1 44 236 13 GLU N N 119.39 0.040 1 45 237 14 MET H H 9.09 0.005 1 46 237 14 MET C C 175.60 0.040 1 47 237 14 MET CA C 54.68 0.040 1 48 237 14 MET N N 127.01 0.040 1 49 238 15 GLU H H 8.64 0.005 1 50 238 15 GLU C C 177.86 0.040 1 51 238 15 GLU CA C 55.44 0.040 1 52 238 15 GLU N N 121.95 0.040 1 53 239 16 ARG H H 8.99 0.005 1 54 239 16 ARG C C 178.45 0.040 1 55 239 16 ARG CA C 59.88 0.040 1 56 239 16 ARG N N 126.79 0.040 1 57 240 17 THR H H 7.73 0.005 1 58 240 17 THR C C 175.15 0.040 1 59 240 17 THR CA C 63.05 0.040 1 60 240 17 THR N N 105.65 0.040 1 61 241 18 ASP H H 7.97 0.005 1 62 241 18 ASP C C 175.52 0.040 1 63 241 18 ASP CA C 55.57 0.040 1 64 241 18 ASP N N 120.59 0.040 1 65 242 19 ILE H H 7.58 0.005 1 66 242 19 ILE C C 175.82 0.040 1 67 242 19 ILE CA C 58.17 0.040 1 68 242 19 ILE N N 119.41 0.040 1 69 243 20 THR H H 9.01 0.005 1 70 243 20 THR C C 173.96 0.040 1 71 243 20 THR CA C 61.45 0.040 1 72 243 20 THR N N 123.63 0.040 1 73 244 21 MET H H 8.87 0.005 1 74 244 21 MET C C 176.24 0.040 1 75 244 21 MET CA C 55.19 0.040 1 76 244 21 MET N N 126.71 0.040 1 77 245 22 LYS H H 8.84 0.005 1 78 245 22 LYS C C 175.03 0.040 1 79 245 22 LYS CA C 56.10 0.040 1 80 245 22 LYS N N 123.72 0.040 1 81 246 23 HIS H H 7.37 0.005 1 82 246 23 HIS C C 174.42 0.040 1 83 246 23 HIS CA C 55.04 0.040 1 84 246 23 HIS N N 113.62 0.040 1 85 247 24 LYS H H 8.87 0.005 1 86 247 24 LYS C C 177.30 0.040 1 87 247 24 LYS CA C 57.84 0.040 1 88 247 24 LYS N N 121.94 0.040 1 89 248 25 LEU H H 9.09 0.005 1 90 248 25 LEU C C 179.37 0.040 1 91 248 25 LEU CA C 55.48 0.040 1 92 248 25 LEU N N 127.44 0.040 1 93 249 26 GLY H H 9.48 0.005 1 94 249 26 GLY C C 176.38 0.040 1 95 249 26 GLY CA C 47.58 0.040 1 96 249 26 GLY N N 112.07 0.040 1 97 250 27 GLY H H 8.64 0.005 1 98 250 27 GLY C C 174.79 0.040 1 99 250 27 GLY CA C 46.60 0.040 1 100 250 27 GLY N N 107.77 0.040 1 101 251 28 GLY H H 7.55 0.005 1 102 251 28 GLY C C 177.06 0.040 1 103 251 28 GLY CA C 45.65 0.040 1 104 251 28 GLY N N 103.76 0.040 1 105 252 29 GLN H H 7.52 0.005 1 106 252 29 GLN C C 174.49 0.040 1 107 252 29 GLN CA C 58.04 0.040 1 108 252 29 GLN N N 119.35 0.040 1 109 253 30 TYR H H 8.24 0.005 1 110 253 30 TYR C C 175.23 0.040 1 111 253 30 TYR CA C 56.36 0.040 1 112 253 30 TYR N N 114.53 0.040 1 113 254 31 GLY H H 7.67 0.005 1 114 254 31 GLY C C 176.09 0.040 1 115 254 31 GLY CA C 45.55 0.040 1 116 254 31 GLY N N 107.15 0.040 1 117 255 32 GLU H H 9.04 0.005 1 118 255 32 GLU C C 174.12 0.040 1 119 255 32 GLU CA C 55.06 0.040 1 120 255 32 GLU N N 128.50 0.040 1 121 256 33 VAL H H 7.62 0.005 1 122 256 33 VAL C C 174.43 0.040 1 123 256 33 VAL CA C 60.51 0.040 1 124 256 33 VAL N N 121.08 0.040 1 125 257 34 TYR H H 9.41 0.005 1 126 257 34 TYR C C 175.24 0.040 1 127 257 34 TYR CA C 56.98 0.040 1 128 257 34 TYR N N 125.98 0.040 1 129 258 35 GLU H H 8.39 0.005 1 130 258 35 GLU C C 174.66 0.040 1 131 258 35 GLU CA C 56.20 0.040 1 132 258 35 GLU N N 122.15 0.040 1 133 259 36 GLY H H 8.78 0.005 1 134 259 36 GLY C C 172.185 0.040 1 135 259 36 GLY CA C 44.11 0.040 1 136 259 36 GLY N N 113.21 0.040 1 137 260 37 VAL H H 8.67 0.005 1 138 260 37 VAL C C 175.28 0.040 1 139 260 37 VAL CA C 60.85 0.040 1 140 260 37 VAL N N 117.38 0.040 1 141 261 38 TRP H H 9.68 0.005 1 142 261 38 TRP C C 177.12 0.040 1 143 261 38 TRP CA C 53.72 0.040 1 144 261 38 TRP N N 129.29 0.040 1 145 262 39 LYS H H 8.86 0.005 1 146 262 39 LYS C C 178.50 0.040 1 147 262 39 LYS CA C 60.76 0.040 1 148 262 39 LYS N N 128.64 0.040 1 149 263 40 LYS H H 7.84 0.005 1 150 263 40 LYS C C 175.72 0.040 1 151 263 40 LYS CA C 58.78 0.040 1 152 263 40 LYS N N 117.43 0.040 1 153 264 41 TYR H H 5.99 0.005 1 154 264 41 TYR C C 173.92 0.040 1 155 264 41 TYR CA C 56.34 0.040 1 156 264 41 TYR N N 111.62 0.040 1 157 265 42 SER H H 7.77 0.005 1 158 265 42 SER C C 173.30 0.040 1 159 265 42 SER CA C 58.88 0.040 1 160 265 42 SER N N 114.91 0.040 1 161 266 43 LEU H H 7.12 0.005 1 162 266 43 LEU C C 175.93 0.040 1 163 266 43 LEU CA C 53.34 0.040 1 164 266 43 LEU N N 119.22 0.040 1 165 267 44 THR H H 8.96 0.005 1 166 267 44 THR C C 172.76 0.040 1 167 267 44 THR CA C 64.23 0.040 1 168 267 44 THR N N 125.55 0.040 1 169 268 45 VAL H H 8.60 0.005 1 170 268 45 VAL C C 173.00 0.040 1 171 268 45 VAL CA C 59.80 0.040 1 172 268 45 VAL N N 118.57 0.040 1 173 269 46 ALA H H 8.44 0.005 1 174 269 46 ALA C C 175.59 0.040 1 175 269 46 ALA CA C 50.41 0.040 1 176 269 46 ALA N N 122.83 0.040 1 177 270 47 VAL H H 8.95 0.005 1 178 270 47 VAL C C 174.85 0.040 1 179 270 47 VAL CA C 60.95 0.040 1 180 270 47 VAL N N 119.89 0.040 1 181 271 48 LYS H H 9.69 0.005 1 182 271 48 LYS CA C 55.66 0.040 1 183 271 48 LYS N N 111.82 0.040 1 184 272 49 THR H H 8.69 0.005 1 185 272 49 THR C C 172.56 0.040 1 186 272 49 THR CA C 58.97 0.040 1 187 272 49 THR N N 118.91 0.040 1 188 273 50 LEU H H 8.13 0.005 1 189 273 50 LEU C C 176.07 0.040 1 190 273 50 LEU CA C 54.11 0.040 1 191 273 50 LEU N N 123.51 0.040 1 192 274 51 LYS H H 8.47 0.005 1 193 274 51 LYS C C 176.36 0.040 1 194 274 51 LYS CA C 56.93 0.040 1 195 274 51 LYS N N 125.66 0.040 1 196 275 52 GLU H H 8.61 0.005 1 197 275 52 GLU C C 175.79 0.040 1 198 275 52 GLU CA C 57.82 0.040 1 199 275 52 GLU N N 120.91 0.040 1 200 276 53 ASP H H 8.44 0.005 1 201 276 53 ASP C C 176.33 0.040 1 202 276 53 ASP CA C 54.56 0.040 1 203 276 53 ASP N N 117.08 0.040 1 204 277 54 THR H H 7.62 0.005 1 205 277 54 THR C C 174.78 0.040 1 206 277 54 THR CA C 62.16 0.040 1 207 277 54 THR N N 111.38 0.040 1 208 278 55 MET H H 8.26 0.005 1 209 278 55 MET C C 176.09 0.040 1 210 278 55 MET CA C 56.03 0.040 1 211 278 55 MET N N 121.13 0.040 1 212 279 56 GLU H H 8.43 0.005 1 213 279 56 GLU C C 177.25 0.040 1 214 279 56 GLU CA C 56.68 0.040 1 215 279 56 GLU N N 120.15 0.040 1 216 280 57 VAL H H 8.22 0.005 1 217 280 57 VAL C C 177.05 0.040 1 218 280 57 VAL CA C 65.75 0.040 1 219 280 57 VAL N N 121.81 0.040 1 220 281 58 GLU H H 8.60 0.005 1 221 281 58 GLU C C 179.61 0.040 1 222 281 58 GLU CA C 60.45 0.040 1 223 281 58 GLU N N 119.16 0.040 1 224 282 59 GLU H H 7.92 0.005 1 225 282 59 GLU C C 173.58 0.040 1 226 282 59 GLU CA C 59.27 0.040 1 227 282 59 GLU N N 117.85 0.040 1 228 283 60 PHE H H 8.03 0.005 1 229 283 60 PHE C C 177.27 0.040 1 230 283 60 PHE CA C 61.80 0.040 1 231 283 60 PHE N N 124.23 0.040 1 232 284 61 LEU H H 8.51 0.005 1 233 284 61 LEU C C 180.84 0.040 1 234 284 61 LEU CA C 57.44 0.040 1 235 284 61 LEU N N 116.63 0.040 1 236 285 62 LYS H H 8.11 0.005 1 237 285 62 LYS C C 178.33 0.040 1 238 285 62 LYS CA C 59.60 0.040 1 239 285 62 LYS N N 121.75 0.040 1 240 286 63 GLU H H 7.77 0.005 1 241 286 63 GLU C C 177.96 0.040 1 242 286 63 GLU CA C 59.48 0.040 1 243 286 63 GLU N N 121.75 0.040 1 244 287 64 ALA H H 7.71 0.005 1 245 287 64 ALA C C 177.64 0.040 1 246 287 64 ALA CA C 55.28 0.040 1 247 287 64 ALA N N 119.48 0.040 1 248 288 65 ALA H H 7.55 0.005 1 249 288 65 ALA C C 181.20 0.040 1 250 288 65 ALA CA C 55.36 0.040 1 251 288 65 ALA N N 115.74 0.040 1 252 289 66 VAL H H 7.94 0.005 1 253 289 66 VAL C C 175.64 0.040 1 254 289 66 VAL CA C 65.64 0.040 1 255 289 66 VAL N N 118.58 0.040 1 256 290 67 MET H H 7.75 0.005 1 257 290 67 MET C C 177.50 0.040 1 258 290 67 MET CA C 59.33 0.040 1 259 290 67 MET N N 117.58 0.040 1 260 291 68 LYS H H 7.15 0.005 1 261 291 68 LYS C C 177.51 0.040 1 262 291 68 LYS CA C 58.91 0.040 1 263 291 68 LYS N N 116.21 0.040 1 264 292 69 GLU H H 7.31 0.005 1 265 292 69 GLU C C 176.26 0.040 1 266 292 69 GLU CA C 56.13 0.040 1 267 292 69 GLU N N 114.86 0.040 1 268 293 70 ILE H H 7.10 0.005 1 269 293 70 ILE C C 174.66 0.040 1 270 293 70 ILE CA C 60.93 0.040 1 271 293 70 ILE N N 117.02 0.040 1 272 294 71 LYS H H 8.22 0.005 1 273 294 71 LYS C C 172.90 0.040 1 274 294 71 LYS CA C 55.90 0.040 1 275 294 71 LYS N N 127.09 0.040 1 276 295 72 HIS H H 8.56 0.005 1 277 295 72 HIS CA C 56.11 0.040 1 278 295 72 HIS N N 126.29 0.040 1 279 296 73 PRO C C 176.93 0.040 1 280 296 73 PRO CA C 64.87 0.040 1 281 297 74 ASN H H 11.17 0.005 1 282 297 74 ASN C C 173.33 0.040 1 283 297 74 ASN CA C 53.97 0.040 1 284 297 74 ASN N N 115.89 0.040 1 285 298 75 LEU H H 7.79 0.005 1 286 298 75 LEU C C 175.94 0.040 1 287 298 75 LEU CA C 54.52 0.040 1 288 298 75 LEU N N 121.13 0.040 1 289 299 76 VAL H H 7.67 0.005 1 290 299 76 VAL C C 172.77 0.040 1 291 299 76 VAL CA C 63.32 0.040 1 292 299 76 VAL N N 122.51 0.040 1 293 300 77 GLN H H 9.24 0.005 1 294 300 77 GLN C C 175.75 0.040 1 295 300 77 GLN CA C 55.30 0.040 1 296 300 77 GLN N N 126.83 0.040 1 297 301 78 LEU H H 8.32 0.005 1 298 301 78 LEU C C 175.94 0.040 1 299 301 78 LEU CA C 55.84 0.040 1 300 301 78 LEU N N 127.52 0.040 1 301 302 79 LEU H H 9.45 0.005 1 302 302 79 LEU C C 177.00 0.040 1 303 302 79 LEU CA C 55.08 0.040 1 304 302 79 LEU N N 125.66 0.040 1 305 303 80 GLY H H 7.82 0.005 1 306 303 80 GLY C C 178.95 0.040 1 307 303 80 GLY CA C 46.34 0.040 1 308 303 80 GLY N N 103.80 0.040 1 309 304 81 VAL H H 8.51 0.005 1 310 304 81 VAL C C 174.23 0.040 1 311 304 81 VAL CA C 58.83 0.040 1 312 304 81 VAL N N 109.98 0.040 1 313 305 82 CYS H H 8.89 0.005 1 314 305 82 CYS C C 176.01 0.040 1 315 305 82 CYS CA C 58.66 0.040 1 316 305 82 CYS N N 118.42 0.040 1 317 306 83 THR H H 11.20 0.005 1 318 306 83 THR C C 173.97 0.040 1 319 306 83 THR CA C 60.81 0.040 1 320 306 83 THR N N 115.03 0.040 1 321 307 84 ARG H H 8.28 0.005 1 322 307 84 ARG C C 176.42 0.040 1 323 307 84 ARG CA C 58.65 0.040 1 324 307 84 ARG N N 121.95 0.040 1 325 308 85 GLU H H 7.52 0.005 1 326 308 85 GLU CA C 53.73 0.040 1 327 308 85 GLU N N 113.93 0.040 1 328 310 87 PRO C C 175.50 0.040 1 329 310 87 PRO CA C 61.28 0.040 1 330 311 88 PHE H H 8.34 0.005 1 331 311 88 PHE C C 176.22 0.040 1 332 311 88 PHE CA C 54.99 0.040 1 333 311 88 PHE N N 123.14 0.040 1 334 312 89 TYR H H 9.07 0.005 1 335 312 89 TYR C C 177.54 0.040 1 336 312 89 TYR CA C 53.45 0.040 1 337 312 89 TYR N N 117.37 0.040 1 338 313 90 ILE H H 9.12 0.005 1 339 313 90 ILE C C 174.06 0.040 1 340 313 90 ILE CA C 63.52 0.040 1 341 313 90 ILE N N 120.03 0.040 1 342 314 91 ILE H H 8.72 0.005 1 343 314 91 ILE C C 175.97 0.040 1 344 314 91 ILE CA C 61.06 0.040 1 345 314 91 ILE N N 126.99 0.040 1 346 315 92 THR H H 9.54 0.005 1 347 315 92 THR C C 173.51 0.040 1 348 315 92 THR CA C 59.80 0.040 1 349 315 92 THR N N 117.42 0.040 1 350 316 93 GLU H H 7.41 0.005 1 351 316 93 GLU C C 172.82 0.040 1 352 316 93 GLU CA C 55.84 0.040 1 353 316 93 GLU N N 115.12 0.040 1 354 317 94 PHE H H 8.81 0.005 1 355 317 94 PHE C C 175.46 0.040 1 356 317 94 PHE CA C 56.34 0.040 1 357 317 94 PHE N N 121.29 0.040 1 358 318 95 MET H H 10.12 0.005 1 359 318 95 MET C C 176.32 0.040 1 360 318 95 MET CA C 53.34 0.040 1 361 318 95 MET N N 129.88 0.040 1 362 319 96 THR H H 8.43 0.005 1 363 319 96 THR C C 174.82 0.040 1 364 319 96 THR CA C 66.38 0.040 1 365 319 96 THR N N 115.82 0.040 1 366 320 97 TYR H H 7.93 0.005 1 367 320 97 TYR C C 175.82 0.040 1 368 320 97 TYR CA C 58.74 0.040 1 369 320 97 TYR N N 115.29 0.040 1 370 321 98 GLY H H 7.47 0.005 1 371 321 98 GLY C C 172.34 0.040 1 372 321 98 GLY CA C 46.12 0.040 1 373 321 98 GLY N N 104.98 0.040 1 374 322 99 ASN H H 8.06 0.005 1 375 322 99 ASN C C 176.03 0.040 1 376 322 99 ASN CA C 53.79 0.040 1 377 322 99 ASN N N 117.27 0.040 1 378 323 100 LEU H H 8.57 0.005 1 379 323 100 LEU C C 176.22 0.040 1 380 323 100 LEU CA C 57.27 0.040 1 381 323 100 LEU N N 121.18 0.040 1 382 324 101 LEU H H 7.24 0.005 1 383 324 101 LEU C C 177.60 0.040 1 384 324 101 LEU CA C 58.59 0.040 1 385 324 101 LEU N N 119.94 0.040 1 386 325 102 ASP H H 7.99 0.005 1 387 325 102 ASP C C 176.17 0.040 1 388 325 102 ASP CA C 57.51 0.040 1 389 325 102 ASP N N 117.04 0.040 1 390 326 103 TYR H H 8.07 0.005 1 391 326 103 TYR C C 178.55 0.040 1 392 326 103 TYR CA C 61.97 0.040 1 393 326 103 TYR N N 119.21 0.040 1 394 327 104 LEU H H 8.72 0.005 1 395 327 104 LEU C C 178.66 0.040 1 396 327 104 LEU CA C 57.23 0.040 1 397 327 104 LEU N N 118.36 0.040 1 398 328 105 ARG H H 7.67 0.005 1 399 328 105 ARG C C 178.45 0.040 1 400 328 105 ARG CA C 59.34 0.040 1 401 328 105 ARG N N 115.26 0.040 1 402 329 106 GLU H H 7.39 0.005 1 403 329 106 GLU C C 177.11 0.040 1 404 329 106 GLU CA C 55.67 0.040 1 405 329 106 GLU N N 114.45 0.040 1 406 330 107 CYS H H 7.22 0.005 1 407 330 107 CYS C C 173.06 0.040 1 408 330 107 CYS CA C 58.21 0.040 1 409 330 107 CYS N N 116.74 0.040 1 410 331 108 ASN H H 8.54 0.005 1 411 331 108 ASN C C 176.66 0.040 1 412 331 108 ASN CA C 52.54 0.040 1 413 331 108 ASN N N 118.14 0.040 1 414 332 109 ARG H H 8.90 0.005 1 415 332 109 ARG C C 176.66 0.040 1 416 332 109 ARG CA C 58.43 0.040 1 417 332 109 ARG N N 127.12 0.040 1 418 333 110 GLN H H 8.01 0.005 1 419 333 110 GLN C C 177.48 0.040 1 420 333 110 GLN CA C 58.00 0.040 1 421 333 110 GLN N N 115.99 0.040 1 422 334 111 GLU H H 7.20 0.005 1 423 334 111 GLU C C 177.06 0.040 1 424 334 111 GLU CA C 57.66 0.040 1 425 334 111 GLU N N 118.48 0.040 1 426 335 112 VAL H H 8.43 0.005 1 427 335 112 VAL C C 173.01 0.040 1 428 335 112 VAL CA C 61.26 0.040 1 429 335 112 VAL N N 121.89 0.040 1 430 336 113 ASN H H 6.80 0.005 1 431 336 113 ASN C C 175.14 0.040 1 432 336 113 ASN CA C 51.27 0.040 1 433 336 113 ASN N N 119.74 0.040 1 434 337 114 ALA H H 8.38 0.005 1 435 337 114 ALA C C 179.92 0.040 1 436 337 114 ALA CA C 56.41 0.040 1 437 337 114 ALA N N 118.94 0.040 1 438 338 115 VAL H H 7.50 0.005 1 439 338 115 VAL C C 178.25 0.040 1 440 338 115 VAL CA C 66.33 0.040 1 441 338 115 VAL N N 116.27 0.040 1 442 339 116 VAL H H 7.43 0.005 1 443 339 116 VAL C C 178.64 0.040 1 444 339 116 VAL CA C 66.44 0.040 1 445 339 116 VAL N N 122.29 0.040 1 446 340 117 LEU H H 8.42 0.005 1 447 340 117 LEU C C 180.31 0.040 1 448 340 117 LEU CA C 58.80 0.040 1 449 340 117 LEU N N 119.15 0.040 1 450 341 118 LEU H H 7.79 0.005 1 451 341 118 LEU C C 180.38 0.040 1 452 341 118 LEU CA C 58.02 0.040 1 453 341 118 LEU N N 118.89 0.040 1 454 342 119 TYR H H 8.45 0.005 1 455 342 119 TYR C C 179.09 0.040 1 456 342 119 TYR CA C 59.38 0.040 1 457 342 119 TYR N N 124.13 0.040 1 458 343 120 MET H H 8.88 0.005 1 459 343 120 MET C C 177.29 0.040 1 460 343 120 MET CA C 60.91 0.040 1 461 343 120 MET N N 120.12 0.040 1 462 344 121 ALA H H 7.96 0.005 1 463 344 121 ALA C C 179.57 0.040 1 464 344 121 ALA CA C 55.66 0.040 1 465 344 121 ALA N N 119.42 0.040 1 466 345 122 THR H H 8.22 0.005 1 467 345 122 THR C C 177.11 0.040 1 468 345 122 THR CA C 67.85 0.040 1 469 345 122 THR N N 116.26 0.040 1 470 346 123 GLN H H 7.66 0.005 1 471 346 123 GLN C C 178.03 0.040 1 472 346 123 GLN CA C 59.89 0.040 1 473 346 123 GLN N N 122.19 0.040 1 474 347 124 ILE H H 7.75 0.005 1 475 347 124 ILE C C 178.17 0.040 1 476 347 124 ILE CA C 65.58 0.040 1 477 347 124 ILE N N 117.63 0.040 1 478 348 125 SER H H 8.45 0.005 1 479 348 125 SER C C 175.18 0.040 1 480 348 125 SER CA C 62.80 0.040 1 481 348 125 SER N N 114.21 0.040 1 482 349 126 SER H H 7.62 0.005 1 483 349 126 SER C C 177.36 0.040 1 484 349 126 SER CA C 60.91 0.040 1 485 349 126 SER N N 118.56 0.040 1 486 350 127 ALA H H 7.40 0.005 1 487 350 127 ALA C C 179.13 0.040 1 488 350 127 ALA CA C 54.64 0.040 1 489 350 127 ALA N N 122.76 0.040 1 490 351 128 MET H H 7.54 0.005 1 491 351 128 MET C C 178.42 0.040 1 492 351 128 MET CA C 54.77 0.040 1 493 351 128 MET N N 112.53 0.040 1 494 352 129 GLU H H 8.28 0.005 1 495 352 129 GLU C C 177.98 0.040 1 496 352 129 GLU CA C 59.78 0.040 1 497 352 129 GLU N N 122.45 0.040 1 498 353 130 TYR H H 7.38 0.005 1 499 353 130 TYR C C 177.08 0.040 1 500 353 130 TYR CA C 61.66 0.040 1 501 353 130 TYR N N 121.36 0.040 1 502 354 131 LEU H H 7.96 0.005 1 503 354 131 LEU C C 178.59 0.040 1 504 354 131 LEU CA C 59.00 0.040 1 505 354 131 LEU N N 118.45 0.040 1 506 355 132 GLU H H 8.77 0.005 1 507 355 132 GLU C C 180.23 0.040 1 508 355 132 GLU CA C 59.80 0.040 1 509 355 132 GLU N N 119.58 0.040 1 510 356 133 LYS H H 8.23 0.005 1 511 356 133 LYS C C 178.07 0.040 1 512 356 133 LYS CA C 59.06 0.040 1 513 356 133 LYS N N 121.33 0.040 1 514 357 134 LYS H H 7.46 0.005 1 515 357 134 LYS C C 174.85 0.040 1 516 357 134 LYS CA C 55.14 0.040 1 517 357 134 LYS N N 117.35 0.040 1 518 358 135 ASN H H 7.83 0.005 1 519 358 135 ASN C C 174.52 0.040 1 520 358 135 ASN CA C 54.80 0.040 1 521 358 135 ASN N N 113.22 0.040 1 522 359 136 PHE H H 8.16 0.005 1 523 359 136 PHE C C 174.33 0.040 1 524 359 136 PHE CA C 55.44 0.040 1 525 359 136 PHE N N 116.92 0.040 1 526 360 137 ILE H H 8.01 0.005 1 527 360 137 ILE CA C 59.73 0.040 1 528 360 137 ILE N N 114.41 0.040 1 529 361 138 HIS C C 176.56 0.040 1 530 362 139 ARG H H 9.84 0.005 1 531 362 139 ARG C C 176.12 0.040 1 532 362 139 ARG CA C 59.51 0.040 1 533 362 139 ARG N N 113.24 0.040 1 534 363 140 ASP H H 10.83 0.005 1 535 363 140 ASP C C 174.03 0.040 1 536 363 140 ASP CA C 52.62 0.040 1 537 363 140 ASP N N 126.58 0.040 1 538 364 141 LEU H H 9.42 0.005 1 539 364 141 LEU C C 175.34 0.040 1 540 364 141 LEU CA C 56.92 0.040 1 541 364 141 LEU N N 125.06 0.040 1 542 365 142 ALA H H 6.59 0.005 1 543 365 142 ALA C C 177.61 0.040 1 544 365 142 ALA CA C 52.25 0.040 1 545 365 142 ALA N N 120.45 0.040 1 546 366 143 ALA H H 10.31 0.005 1 547 366 143 ALA C C 178.89 0.040 1 548 366 143 ALA CA C 57.10 0.040 1 549 366 143 ALA N N 129.22 0.040 1 550 367 144 ARG H H 9.53 0.005 1 551 367 144 ARG C C 174.83 0.040 1 552 367 144 ARG CA C 57.35 0.040 1 553 367 144 ARG N N 113.61 0.040 1 554 368 145 ASN H H 7.28 0.005 1 555 368 145 ASN C C 172.74 0.040 1 556 368 145 ASN CA C 53.25 0.040 1 557 368 145 ASN N N 117.28 0.040 1 558 369 146 CYS H H 7.46 0.005 1 559 369 146 CYS C C 173.86 0.040 1 560 369 146 CYS CA C 57.61 0.040 1 561 369 146 CYS N N 112.72 0.040 1 562 370 147 LEU H H 9.26 0.005 1 563 370 147 LEU C C 174.99 0.040 1 564 370 147 LEU CA C 53.02 0.040 1 565 370 147 LEU N N 122.19 0.040 1 566 371 148 VAL H H 8.31 0.005 1 567 371 148 VAL C C 174.85 0.040 1 568 371 148 VAL CA C 60.77 0.040 1 569 371 148 VAL N N 118.44 0.040 1 570 372 149 GLY H H 9.19 0.005 1 571 372 149 GLY C C 172.91 0.040 1 572 372 149 GLY CA C 43.42 0.040 1 573 372 149 GLY N N 114.78 0.040 1 574 373 150 GLU H H 8.69 0.005 1 575 373 150 GLU C C 177.70 0.040 1 576 373 150 GLU CA C 57.71 0.040 1 577 373 150 GLU N N 118.34 0.040 1 578 374 151 ASN H H 9.10 0.005 1 579 374 151 ASN C C 175.01 0.040 1 580 374 151 ASN CA C 54.34 0.040 1 581 374 151 ASN N N 117.39 0.040 1 582 375 152 HIS H H 8.54 0.005 1 583 375 152 HIS C C 171.98 0.040 1 584 375 152 HIS CA C 57.06 0.040 1 585 375 152 HIS N N 109.84 0.040 1 586 376 153 LEU H H 6.72 0.005 1 587 376 153 LEU C C 175.41 0.040 1 588 376 153 LEU CA C 54.90 0.040 1 589 376 153 LEU N N 120.67 0.040 1 590 377 154 VAL H H 8.40 0.005 1 591 377 154 VAL C C 174.51 0.040 1 592 377 154 VAL CA C 59.61 0.040 1 593 377 154 VAL N N 124.09 0.040 1 594 378 155 LYS H H 8.60 0.005 1 595 378 155 LYS C C 175.12 0.040 1 596 378 155 LYS CA C 53.35 0.040 1 597 378 155 LYS N N 119.76 0.040 1 598 379 156 VAL H H 8.78 0.005 1 599 379 156 VAL C C 172.55 0.040 1 600 379 156 VAL CA C 63.64 0.040 1 601 379 156 VAL N N 123.50 0.040 1 602 380 157 ALA H H 8.29 0.005 1 603 380 157 ALA C C 174.81 0.040 1 604 380 157 ALA CA C 50.54 0.040 1 605 380 157 ALA N N 112.01 0.040 1 606 381 158 ASP H H 7.42 0.005 1 607 381 158 ASP C C 175.14 0.040 1 608 381 158 ASP CA C 54.52 0.040 1 609 381 158 ASP N N 115.59 0.040 1 610 382 159 PHE H H 7.79 0.005 1 611 382 159 PHE C C 177.25 0.040 1 612 382 159 PHE CA C 55.26 0.040 1 613 382 159 PHE N N 122.41 0.040 1 614 383 160 GLY H H 8.32 0.005 1 615 383 160 GLY CA C 47.37 0.040 1 616 383 160 GLY N N 110.28 0.040 1 617 384 161 LEU C C 178.81 0.040 1 618 385 162 SER H H 8.12 0.005 1 619 385 162 SER CA C 60.21 0.040 1 620 385 162 SER N N 114.76 0.040 1 621 387 164 LEU C C 177.21 0.040 1 622 388 165 MET H H 8.09 0.005 1 623 388 165 MET C C 176.49 0.040 1 624 388 165 MET CA C 56.33 0.040 1 625 388 165 MET N N 118.81 0.040 1 626 389 166 THR H H 8.20 0.005 1 627 389 166 THR C C 175.15 0.040 1 628 389 166 THR CA C 61.53 0.040 1 629 389 166 THR N N 114.49 0.040 1 630 390 167 GLY H H 8.52 0.005 1 631 390 167 GLY C C 174.40 0.040 1 632 390 167 GLY CA C 45.70 0.040 1 633 390 167 GLY N N 110.73 0.040 1 634 391 168 ASP H H 8.30 0.005 1 635 391 168 ASP C C 176.64 0.040 1 636 391 168 ASP CA C 54.28 0.040 1 637 391 168 ASP N N 119.78 0.040 1 638 392 169 THR H H 8.02 0.005 1 639 392 169 THR CA C 58.07 0.040 1 640 392 169 THR N N 115.88 0.040 1 641 393 170 TYR H H 8.30 0.005 1 642 393 170 TYR CA C 57.41 0.040 1 643 393 170 TYR N N 118.75 0.040 1 644 396 173 HIS C C 175.55 0.040 1 645 396 173 HIS CA C 63.05 0.040 1 646 397 174 ALA H H 8.50 0.005 1 647 397 174 ALA C C 177.38 0.040 1 648 397 174 ALA CA C 53.14 0.040 1 649 397 174 ALA N N 119.16 0.040 1 650 398 175 GLY H H 8.46 0.005 1 651 398 175 GLY C C 178.71 0.040 1 652 398 175 GLY CA C 45.59 0.040 1 653 398 175 GLY N N 105.49 0.040 1 654 399 176 ALA H H 8.03 0.005 1 655 399 176 ALA C C 178.18 0.040 1 656 399 176 ALA CA C 51.16 0.040 1 657 399 176 ALA N N 124.26 0.040 1 658 400 177 LYS H H 8.07 0.005 1 659 400 177 LYS CA C 55.67 0.040 1 660 400 177 LYS N N 119.18 0.040 1 661 403 180 ILE H H 8.69 0.005 1 662 403 180 ILE N N 128.57 0.040 1 663 404 181 LYS C C 175.34 0.040 1 664 405 182 TRP H H 8.46 0.005 1 665 405 182 TRP C C 175.66 0.040 1 666 405 182 TRP CA C 61.15 0.040 1 667 405 182 TRP N N 120.15 0.040 1 668 406 183 THR H H 7.45 0.005 1 669 406 183 THR C C 171.77 0.040 1 670 406 183 THR CA C 64.28 0.040 1 671 406 183 THR N N 116.24 0.040 1 672 407 184 ALA H H 8.47 0.005 1 673 407 184 ALA CA C 50.00 0.040 1 674 407 184 ALA N N 128.98 0.040 1 675 408 185 PRO C C 177.28 0.040 1 676 408 185 PRO CA C 65.57 0.040 1 677 409 186 GLU H H 9.68 0.005 1 678 409 186 GLU C C 178.25 0.040 1 679 409 186 GLU CA C 58.70 0.040 1 680 409 186 GLU N N 116.53 0.040 1 681 410 187 SER H H 6.98 0.005 1 682 410 187 SER C C 175.49 0.040 1 683 410 187 SER CA C 60.57 0.040 1 684 410 187 SER N N 122.00 0.040 1 685 411 188 LEU H H 7.28 0.005 1 686 411 188 LEU C C 178.47 0.040 1 687 411 188 LEU CA C 57.28 0.040 1 688 411 188 LEU N N 120.59 0.040 1 689 412 189 ALA H H 8.04 0.005 1 690 412 189 ALA C C 179.39 0.040 1 691 412 189 ALA CA C 54.30 0.040 1 692 412 189 ALA N N 116.79 0.040 1 693 413 190 TYR H H 6.95 0.005 1 694 413 190 TYR CA C 56.21 0.040 1 695 413 190 TYR N N 111.02 0.040 1 696 414 191 ASN H H 7.75 0.005 1 697 414 191 ASN C C 173.90 0.040 1 698 414 191 ASN CA C 54.35 0.040 1 699 414 191 ASN N N 117.68 0.040 1 700 415 192 LYS H H 6.91 0.005 1 701 415 192 LYS C C 174.95 0.040 1 702 415 192 LYS CA C 55.17 0.040 1 703 415 192 LYS N N 116.60 0.040 1 704 416 193 PHE H H 8.75 0.005 1 705 416 193 PHE C C 175.05 0.040 1 706 416 193 PHE CA C 56.86 0.040 1 707 416 193 PHE N N 123.72 0.040 1 708 417 194 SER H H 9.79 0.005 1 709 417 194 SER C C 175.35 0.040 1 710 417 194 SER CA C 58.15 0.040 1 711 417 194 SER N N 117.31 0.040 1 712 418 195 ILE H H 9.55 0.005 1 713 418 195 ILE C C 177.72 0.040 1 714 418 195 ILE CA C 61.75 0.040 1 715 418 195 ILE N N 122.51 0.040 1 716 419 196 LYS H H 7.88 0.005 1 717 419 196 LYS C C 172.44 0.040 1 718 419 196 LYS CA C 56.48 0.040 1 719 419 196 LYS N N 114.84 0.040 1 720 420 197 SER H H 8.45 0.005 1 721 420 197 SER C C 178.91 0.040 1 722 420 197 SER CA C 62.33 0.040 1 723 420 197 SER N N 120.62 0.040 1 724 421 198 ASP H H 7.77 0.005 1 725 421 198 ASP C C 178.97 0.040 1 726 421 198 ASP CA C 58.14 0.040 1 727 421 198 ASP N N 126.98 0.040 1 728 422 199 VAL H H 8.15 0.005 1 729 422 199 VAL C C 177.50 0.040 1 730 422 199 VAL CA C 67.81 0.040 1 731 422 199 VAL N N 122.60 0.040 1 732 423 200 TRP H H 7.39 0.005 1 733 423 200 TRP C C 179.13 0.040 1 734 423 200 TRP CA C 61.98 0.040 1 735 423 200 TRP N N 119.47 0.040 1 736 424 201 ALA H H 8.00 0.005 1 737 424 201 ALA C C 180.42 0.040 1 738 424 201 ALA CA C 56.65 0.040 1 739 424 201 ALA N N 121.46 0.040 1 740 425 202 PHE H H 9.46 0.005 1 741 425 202 PHE C C 176.65 0.040 1 742 425 202 PHE CA C 61.86 0.040 1 743 425 202 PHE N N 119.52 0.040 1 744 426 203 GLY H H 8.30 0.005 1 745 426 203 GLY C C 175.43 0.040 1 746 426 203 GLY CA C 47.70 0.040 1 747 426 203 GLY N N 106.60 0.040 1 748 427 204 VAL H H 7.81 0.005 1 749 427 204 VAL C C 177.44 0.040 1 750 427 204 VAL CA C 68.06 0.040 1 751 427 204 VAL N N 119.57 0.040 1 752 428 205 LEU H H 9.19 0.005 1 753 428 205 LEU C C 179.04 0.040 1 754 428 205 LEU CA C 58.28 0.040 1 755 428 205 LEU N N 124.42 0.040 1 756 429 206 LEU H H 8.81 0.005 1 757 429 206 LEU C C 178.28 0.040 1 758 429 206 LEU CA C 57.62 0.040 1 759 429 206 LEU N N 119.32 0.040 1 760 430 207 TRP H H 7.84 0.005 1 761 430 207 TRP C C 178.93 0.040 1 762 430 207 TRP CA C 63.68 0.040 1 763 430 207 TRP N N 122.85 0.040 1 764 431 208 GLU H H 9.15 0.005 1 765 431 208 GLU C C 178.59 0.040 1 766 431 208 GLU CA C 61.85 0.040 1 767 431 208 GLU N N 119.92 0.040 1 768 432 209 ILE H H 8.56 0.005 1 769 432 209 ILE C C 176.93 0.040 1 770 432 209 ILE CA C 65.64 0.040 1 771 432 209 ILE N N 117.53 0.040 1 772 433 210 ALA H H 8.06 0.005 1 773 433 210 ALA C C 178.32 0.040 1 774 433 210 ALA CA C 53.90 0.040 1 775 433 210 ALA N N 116.94 0.040 1 776 434 211 THR H H 7.18 0.005 1 777 434 211 THR C C 174.60 0.040 1 778 434 211 THR CA C 60.73 0.040 1 779 434 211 THR N N 103.61 0.040 1 780 435 212 TYR H H 7.81 0.005 1 781 435 212 TYR C C 175.34 0.040 1 782 435 212 TYR CA C 61.56 0.040 1 783 435 212 TYR N N 116.52 0.040 1 784 436 213 GLY H H 9.50 0.005 1 785 436 213 GLY C C 175.79 0.040 1 786 436 213 GLY CA C 46.63 0.040 1 787 436 213 GLY N N 103.31 0.040 1 788 437 214 MET H H 7.47 0.005 1 789 437 214 MET C C 176.17 0.040 1 790 437 214 MET CA C 56.80 0.040 1 791 437 214 MET N N 119.81 0.040 1 792 438 215 SER H H 8.30 0.005 1 793 438 215 SER CA C 56.52 0.040 1 794 438 215 SER N N 116.86 0.040 1 795 439 216 PRO C C 173.73 0.040 1 796 439 216 PRO CA C 62.46 0.040 1 797 440 217 TYR H H 6.98 0.005 1 798 440 217 TYR CA C 58.19 0.040 1 799 440 217 TYR N N 114.16 0.040 1 800 441 218 PRO C C 179.22 0.040 1 801 441 218 PRO CA C 63.89 0.040 1 802 442 219 GLY H H 8.81 0.005 1 803 442 219 GLY C C 173.67 0.040 1 804 442 219 GLY CA C 45.79 0.040 1 805 442 219 GLY N N 110.84 0.040 1 806 443 220 ILE H H 7.37 0.005 1 807 443 220 ILE C C 175.47 0.040 1 808 443 220 ILE CA C 59.12 0.040 1 809 443 220 ILE N N 119.70 0.040 1 810 444 221 ASP H H 8.56 0.005 1 811 444 221 ASP C C 177.34 0.040 1 812 444 221 ASP CA C 54.27 0.040 1 813 444 221 ASP N N 127.34 0.040 1 814 445 222 LEU H H 8.57 0.005 1 815 445 222 LEU C C 178.46 0.040 1 816 445 222 LEU CA C 58.15 0.040 1 817 445 222 LEU N N 125.05 0.040 1 818 446 223 SER H H 8.48 0.005 1 819 446 223 SER C C 175.31 0.040 1 820 446 223 SER CA C 60.65 0.040 1 821 446 223 SER N N 112.06 0.040 1 822 447 224 GLN H H 7.87 0.005 1 823 447 224 GLN C C 175.82 0.040 1 824 447 224 GLN CA C 55.31 0.040 1 825 447 224 GLN N N 119.43 0.040 1 826 448 225 VAL H H 6.83 0.005 1 827 448 225 VAL C C 175.66 0.040 1 828 448 225 VAL CA C 67.67 0.040 1 829 448 225 VAL N N 118.50 0.040 1 830 449 226 TYR H H 8.68 0.005 1 831 449 226 TYR C C 176.21 0.040 1 832 449 226 TYR CA C 63.74 0.040 1 833 449 226 TYR N N 119.00 0.040 1 834 450 227 GLU H H 8.24 0.005 1 835 450 227 GLU C C 179.27 0.040 1 836 450 227 GLU CA C 59.26 0.040 1 837 450 227 GLU N N 117.03 0.040 1 838 451 228 LEU H H 7.76 0.005 1 839 451 228 LEU C C 179.63 0.040 1 840 451 228 LEU CA C 58.04 0.040 1 841 451 228 LEU N N 118.77 0.040 1 842 452 229 LEU H H 8.47 0.005 1 843 452 229 LEU C C 172.59 0.040 1 844 452 229 LEU CA C 57.56 0.040 1 845 452 229 LEU N N 120.02 0.040 1 846 453 230 GLU H H 8.60 0.005 1 847 453 230 GLU C C 177.32 0.040 1 848 453 230 GLU CA C 58.87 0.040 1 849 453 230 GLU N N 122.33 0.040 1 850 454 231 LYS H H 7.19 0.005 1 851 454 231 LYS C C 175.38 0.040 1 852 454 231 LYS CA C 56.07 0.040 1 853 454 231 LYS N N 117.81 0.040 1 854 455 232 ASP H H 7.67 0.005 1 855 455 232 ASP C C 175.21 0.040 1 856 455 232 ASP CA C 56.52 0.040 1 857 455 232 ASP N N 112.13 0.040 1 858 456 233 TYR H H 8.07 0.005 1 859 456 233 TYR C C 176.26 0.040 1 860 456 233 TYR CA C 60.09 0.040 1 861 456 233 TYR N N 120.60 0.040 1 862 457 234 ARG H H 6.86 0.005 1 863 457 234 ARG C C 173.88 0.040 1 864 457 234 ARG CA C 52.23 0.040 1 865 457 234 ARG N N 124.99 0.040 1 866 458 235 MET H H 7.28 0.005 1 867 458 235 MET C C 175.83 0.040 1 868 458 235 MET CA C 58.13 0.040 1 869 458 235 MET N N 116.56 0.040 1 870 459 236 GLU H H 8.52 0.005 1 871 459 236 GLU C C 175.38 0.040 1 872 459 236 GLU CA C 55.68 0.040 1 873 459 236 GLU N N 120.09 0.040 1 874 460 237 ARG H H 8.27 0.005 1 875 460 237 ARG CA C 55.47 0.040 1 876 460 237 ARG N N 124.05 0.040 1 877 461 238 PRO C C 175.96 0.040 1 878 461 238 PRO CA C 62.18 0.040 1 879 462 239 GLU H H 8.57 0.005 1 880 462 239 GLU C C 178.05 0.040 1 881 462 239 GLU CA C 58.23 0.040 1 882 462 239 GLU N N 123.15 0.040 1 883 463 240 GLY H H 8.82 0.005 1 884 463 240 GLY C C 173.70 0.040 1 885 463 240 GLY CA C 45.32 0.040 1 886 463 240 GLY N N 113.14 0.040 1 887 464 241 CYS H H 7.77 0.005 1 888 464 241 CYS CA C 56.05 0.040 1 889 464 241 CYS N N 122.50 0.040 1 890 465 242 PRO C C 177.92 0.040 1 891 465 242 PRO CA C 63.39 0.040 1 892 466 243 GLU H H 9.45 0.005 1 893 466 243 GLU C C 179.07 0.040 1 894 466 243 GLU CA C 61.34 0.040 1 895 466 243 GLU N N 127.65 0.040 1 896 467 244 LYS H H 9.17 0.005 1 897 467 244 LYS C C 179.34 0.040 1 898 467 244 LYS CA C 59.24 0.040 1 899 467 244 LYS N N 116.33 0.040 1 900 468 245 VAL H H 6.88 0.005 1 901 468 245 VAL C C 177.15 0.040 1 902 468 245 VAL CA C 66.19 0.040 1 903 468 245 VAL N N 117.26 0.040 1 904 469 246 TYR H H 7.80 0.005 1 905 469 246 TYR C C 176.60 0.040 1 906 469 246 TYR CA C 61.23 0.040 1 907 469 246 TYR N N 120.90 0.040 1 908 470 247 GLU H H 8.41 0.005 1 909 470 247 GLU C C 179.39 0.040 1 910 470 247 GLU CA C 59.51 0.040 1 911 470 247 GLU N N 117.42 0.040 1 912 471 248 LEU H H 6.99 0.005 1 913 471 248 LEU C C 178.81 0.040 1 914 471 248 LEU CA C 57.87 0.040 1 915 471 248 LEU N N 120.60 0.040 1 916 472 249 MET H H 7.74 0.005 1 917 472 249 MET C C 176.06 0.040 1 918 472 249 MET CA C 60.67 0.040 1 919 472 249 MET N N 120.09 0.040 1 920 473 250 ARG H H 7.51 0.005 1 921 473 250 ARG C C 179.76 0.040 1 922 473 250 ARG CA C 57.24 0.040 1 923 473 250 ARG N N 111.56 0.040 1 924 474 251 ALA H H 7.52 0.005 1 925 474 251 ALA C C 179.80 0.040 1 926 474 251 ALA CA C 54.85 0.040 1 927 474 251 ALA N N 123.69 0.040 1 928 475 252 CYS H H 7.44 0.005 1 929 475 252 CYS C C 174.20 0.040 1 930 475 252 CYS CA C 63.65 0.040 1 931 475 252 CYS N N 115.62 0.040 1 932 476 253 TRP H H 6.72 0.005 1 933 476 253 TRP C C 176.87 0.040 1 934 476 253 TRP CA C 52.21 0.040 1 935 476 253 TRP N N 111.83 0.040 1 936 477 254 GLN H H 6.90 0.005 1 937 477 254 GLN C C 177.00 0.040 1 938 477 254 GLN CA C 56.66 0.040 1 939 477 254 GLN N N 118.69 0.040 1 940 478 255 TRP H H 9.54 0.005 1 941 478 255 TRP C C 176.54 0.040 1 942 478 255 TRP CA C 61.51 0.040 1 943 478 255 TRP N N 125.09 0.040 1 944 479 256 ASN H H 8.92 0.005 1 945 479 256 ASN CA C 50.35 0.040 1 946 479 256 ASN N N 116.03 0.040 1 947 480 257 PRO C C 178.06 0.040 1 948 480 257 PRO CA C 65.36 0.040 1 949 481 258 SER H H 7.81 0.005 1 950 481 258 SER C C 174.95 0.040 1 951 481 258 SER CA C 60.57 0.040 1 952 481 258 SER N N 108.08 0.040 1 953 482 259 ASP H H 7.76 0.005 1 954 482 259 ASP C C 176.12 0.040 1 955 482 259 ASP CA C 54.84 0.040 1 956 482 259 ASP N N 118.63 0.040 1 957 483 260 ARG H H 7.30 0.005 1 958 483 260 ARG CA C 54.39 0.040 1 959 483 260 ARG N N 120.07 0.040 1 960 484 261 PRO C C 174.15 0.040 1 961 484 261 PRO CA C 62.22 0.040 1 962 485 262 SER H H 7.97 0.005 1 963 485 262 SER C C 176.35 0.040 1 964 485 262 SER CA C 56.16 0.040 1 965 485 262 SER N N 109.93 0.040 1 966 486 263 PHE H H 11.30 0.005 1 967 486 263 PHE C C 179.40 0.040 1 968 486 263 PHE CA C 63.69 0.040 1 969 486 263 PHE N N 121.78 0.040 1 970 487 264 ALA H H 8.79 0.005 1 971 487 264 ALA C C 180.85 0.040 1 972 487 264 ALA CA C 55.83 0.040 1 973 487 264 ALA N N 123.48 0.040 1 974 488 265 GLU H H 7.85 0.005 1 975 488 265 GLU C C 180.01 0.040 1 976 488 265 GLU CA C 59.33 0.040 1 977 488 265 GLU N N 119.29 0.040 1 978 489 266 ILE H H 8.54 0.005 1 979 489 266 ILE C C 177.00 0.040 1 980 489 266 ILE CA C 65.94 0.040 1 981 489 266 ILE N N 122.50 0.040 1 982 490 267 HIS H H 9.27 0.005 1 983 490 267 HIS C C 176.96 0.040 1 984 490 267 HIS CA C 59.09 0.040 1 985 490 267 HIS N N 117.64 0.040 1 986 491 268 GLN H H 7.85 0.005 1 987 491 268 GLN C C 178.28 0.040 1 988 491 268 GLN CA C 58.99 0.040 1 989 491 268 GLN N N 117.76 0.040 1 990 492 269 ALA H H 7.97 0.005 1 991 492 269 ALA C C 181.07 0.040 1 992 492 269 ALA CA C 55.29 0.040 1 993 492 269 ALA N N 122.34 0.040 1 994 493 270 PHE H H 8.29 0.005 1 995 493 270 PHE C C 178.17 0.040 1 996 493 270 PHE CA C 63.42 0.040 1 997 493 270 PHE N N 117.45 0.040 1 998 494 271 GLU H H 8.62 0.005 1 999 494 271 GLU C C 179.37 0.040 1 1000 494 271 GLU CA C 60.08 0.040 1 1001 494 271 GLU N N 118.87 0.040 1 1002 495 272 THR H H 7.94 0.005 1 1003 495 272 THR C C 176.03 0.040 1 1004 495 272 THR CA C 65.77 0.040 1 1005 495 272 THR N N 112.84 0.040 1 1006 496 273 MET H H 7.76 0.005 1 1007 496 273 MET C C 178.00 0.040 1 1008 496 273 MET CA C 58.98 0.040 1 1009 496 273 MET N N 119.71 0.040 1 1010 497 274 PHE H H 8.68 0.005 1 1011 497 274 PHE C C 176.98 0.040 1 1012 497 274 PHE CA C 60.05 0.040 1 1013 497 274 PHE N N 118.94 0.040 1 1014 498 275 GLN H H 8.06 0.005 1 1015 498 275 GLN C C 176.49 0.040 1 1016 498 275 GLN CA C 57.12 0.040 1 1017 498 275 GLN N N 118.69 0.040 1 1018 499 276 GLU H H 7.83 0.005 1 1019 499 276 GLU C C 175.76 0.040 1 1020 499 276 GLU CA C 56.54 0.040 1 1021 499 276 GLU N N 119.26 0.040 1 1022 500 277 SER H H 7.58 0.005 1 1023 500 277 SER CA C 60.82 0.040 1 1024 500 277 SER N N 121.77 0.040 1 stop_ save_