data_15219 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N and 13C chemical shift assingments for human retinoid X receptor ligand-binding domain in complex with 9-cis retinoic acid and a glucocorticoid receptor interacting protein-1 peptide ; _BMRB_accession_number 15219 _BMRB_flat_file_name bmr15219.str _Entry_type original _Submission_date 2007-04-19 _Accession_date 2007-04-19 _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 Lu Jianyun . . 2 Chen Minghe . . 3 DeKoster Gregory T. . 4 Cistola David P. . 5 Li Ellen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 182 "13C chemical shifts" 578 "15N chemical shifts" 182 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-02-20 original author . stop_ _Original_release_date 2008-02-20 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'The RXRalpha C-terminus T462 is a NMR sensor for coactivator peptide binding' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18088598 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jianyun . . 2 Chen Minghe . . 3 DeKoster Gregory T. . 4 Cistola David P. . 5 Li Ellen . . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume 366 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 932 _Page_last 937 _Year 2008 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_2 _Saveframe_category citation _Citation_full . _Citation_title ; Analysis of Ligand Binding and Protein Dynamics of Human Retinoid X Receptor Alpha Ligand-Binding Domain by Nuclear Magnetic Resonance ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16460010 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jianyun . . 2 Cistola David P. . 3 Li Ellen . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full . _Journal_volume 45 _Journal_issue 6 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1629 _Page_last 1639 _Year 2006 _Details . loop_ _Keyword activation dynamics NMR RXRalpha structure stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'RXRalpha LBD ternary complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RXRalpha LBD' $RXRalpha_LBD 'GRIP1 NR Box 2' $GRIP1_NR_Box_2 '9-cis-retinoic acid' $REA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'RXRalpha LBD in complex with 9-cis-retinoic acid and GRIP1 NR box 2 peptide' save_ ######################## # Monomeric polymers # ######################## save_RXRalpha_LBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RXRalpha_LBD _Molecular_mass 27235.5 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 244 _Mol_residue_sequence ; GSHMTSSANEDMPVERILEA ELAVEPKTETYVEANMGLNP SSPNDPVTNICQAADKQLFT LVEWAKRIPHFSELPLDDQV ILLRAGWNELLIASFSHRSI AVKDGILLATGLHVHRNSAH SAGVGAIFDRVLTELVSKMR DMQMDKTELGCLRAIVLFNP DSKGLSNPAEVEALREKVYA SLEAYCKHKYPEQPGRFAKL LLRLPALRSIGLKCLEHLFF FKLIGDTPIDTFLMEMLEAP HQMT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -4 GLY 2 -3 SER 3 -2 HIS 4 -1 MET 5 223 THR 6 224 SER 7 225 SER 8 226 ALA 9 227 ASN 10 228 GLU 11 229 ASP 12 230 MET 13 231 PRO 14 232 VAL 15 233 GLU 16 234 ARG 17 235 ILE 18 236 LEU 19 237 GLU 20 238 ALA 21 239 GLU 22 240 LEU 23 241 ALA 24 242 VAL 25 243 GLU 26 244 PRO 27 245 LYS 28 246 THR 29 247 GLU 30 248 THR 31 249 TYR 32 250 VAL 33 251 GLU 34 252 ALA 35 253 ASN 36 254 MET 37 255 GLY 38 256 LEU 39 257 ASN 40 258 PRO 41 259 SER 42 260 SER 43 261 PRO 44 262 ASN 45 263 ASP 46 264 PRO 47 265 VAL 48 266 THR 49 267 ASN 50 268 ILE 51 269 CYS 52 270 GLN 53 271 ALA 54 272 ALA 55 273 ASP 56 274 LYS 57 275 GLN 58 276 LEU 59 277 PHE 60 278 THR 61 279 LEU 62 280 VAL 63 281 GLU 64 282 TRP 65 283 ALA 66 284 LYS 67 285 ARG 68 286 ILE 69 287 PRO 70 288 HIS 71 289 PHE 72 290 SER 73 291 GLU 74 292 LEU 75 293 PRO 76 294 LEU 77 295 ASP 78 296 ASP 79 297 GLN 80 298 VAL 81 299 ILE 82 300 LEU 83 301 LEU 84 302 ARG 85 303 ALA 86 304 GLY 87 305 TRP 88 306 ASN 89 307 GLU 90 308 LEU 91 309 LEU 92 310 ILE 93 311 ALA 94 312 SER 95 313 PHE 96 314 SER 97 315 HIS 98 316 ARG 99 317 SER 100 318 ILE 101 319 ALA 102 320 VAL 103 321 LYS 104 322 ASP 105 323 GLY 106 324 ILE 107 325 LEU 108 326 LEU 109 327 ALA 110 328 THR 111 329 GLY 112 330 LEU 113 331 HIS 114 332 VAL 115 333 HIS 116 334 ARG 117 335 ASN 118 336 SER 119 337 ALA 120 338 HIS 121 339 SER 122 340 ALA 123 341 GLY 124 342 VAL 125 343 GLY 126 344 ALA 127 345 ILE 128 346 PHE 129 347 ASP 130 348 ARG 131 349 VAL 132 350 LEU 133 351 THR 134 352 GLU 135 353 LEU 136 354 VAL 137 355 SER 138 356 LYS 139 357 MET 140 358 ARG 141 359 ASP 142 360 MET 143 361 GLN 144 362 MET 145 363 ASP 146 364 LYS 147 365 THR 148 366 GLU 149 367 LEU 150 368 GLY 151 369 CYS 152 370 LEU 153 371 ARG 154 372 ALA 155 373 ILE 156 374 VAL 157 375 LEU 158 376 PHE 159 377 ASN 160 378 PRO 161 379 ASP 162 380 SER 163 381 LYS 164 382 GLY 165 383 LEU 166 384 SER 167 385 ASN 168 386 PRO 169 387 ALA 170 388 GLU 171 389 VAL 172 390 GLU 173 391 ALA 174 392 LEU 175 393 ARG 176 394 GLU 177 395 LYS 178 396 VAL 179 397 TYR 180 398 ALA 181 399 SER 182 400 LEU 183 401 GLU 184 402 ALA 185 403 TYR 186 404 CYS 187 405 LYS 188 406 HIS 189 407 LYS 190 408 TYR 191 409 PRO 192 410 GLU 193 411 GLN 194 412 PRO 195 413 GLY 196 414 ARG 197 415 PHE 198 416 ALA 199 417 LYS 200 418 LEU 201 419 LEU 202 420 LEU 203 421 ARG 204 422 LEU 205 423 PRO 206 424 ALA 207 425 LEU 208 426 ARG 209 427 SER 210 428 ILE 211 429 GLY 212 430 LEU 213 431 LYS 214 432 CYS 215 433 LEU 216 434 GLU 217 435 HIS 218 436 LEU 219 437 PHE 220 438 PHE 221 439 PHE 222 440 LYS 223 441 LEU 224 442 ILE 225 443 GLY 226 444 ASP 227 445 THR 228 446 PRO 229 447 ILE 230 448 ASP 231 449 THR 232 450 PHE 233 451 LEU 234 452 MET 235 453 GLU 236 454 MET 237 455 LEU 238 456 GLU 239 457 ALA 240 458 PRO 241 459 HIS 242 460 GLN 243 461 MET 244 462 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 1DKF "Crystal Structure Of A Heterodimeric Complex Of Rar And Rxr Ligand-Binding Domains" 95.49 233 99.14 99.57 8.91e-168 PDB 1FBY "Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To 9-Cis Retinoic Acid" 97.95 239 100.00 100.00 4.82e-175 PDB 1FM6 "The 2.1 Angstrom Resolution Crystal Structure Of The Heterodimer Of The Human Rxralpha And Ppargamma Ligand Binding Domains Res" 97.54 238 100.00 100.00 5.11e-174 PDB 1FM9 "The 2.1 Angstrom Resolution Crystal Structure Of The Heterodimer Of The Human Rxralpha And Ppargamma Ligand Binding Domains Res" 97.54 238 100.00 100.00 5.11e-174 PDB 1G1U "The 2.5 Angstrom Resolution Crystal Structure Of The Rxralpha Ligand Binding Domain In Tetramer In The Absence Of Ligand" 97.54 238 100.00 100.00 5.11e-174 PDB 1G5Y "The 2.0 Angstrom Resolution Crystal Structure Of The Rxralpha Ligand Binding Domain Tetramer In The Presence Of A Non-Activatin" 97.54 238 100.00 100.00 5.11e-174 PDB 1K74 "The 2.3 Angstrom Resolution Crystal Structure Of The Heterodimer Of The Human Ppargamma And Rxralpha Ligand Binding Domains Res" 97.54 238 100.00 100.00 5.11e-174 PDB 1LBD "Ligand-Binding Domain Of The Human Nuclear Receptor Rxr-Alpha" 98.36 282 100.00 100.00 3.96e-175 PDB 1MV9 "Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To The Eicosanoid Dha (Docosa Hexaenoic Acid) And A Coacti" 98.36 240 100.00 100.00 9.90e-176 PDB 1MVC "Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic Agonist Compound Bms 649 And A Coactivato" 98.36 240 100.00 100.00 9.90e-176 PDB 1MZN "Crystal Structure At 1.9 Angstroems Resolution Of The Homodimer Of Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic" 98.36 240 100.00 100.00 9.90e-176 PDB 1RDT "Crystal Structure Of A New Rexinoid Bound To The Rxralpha Ligand Binding Doamin In The RxralphaPPARGAMMA HETERODIMER" 97.95 242 99.58 99.58 3.20e-174 PDB 1XDK "Crystal Structure Of The RarbetaRXRALPHA LIGAND BINDING Domain Heterodimer In Complex With 9-Cis Retinoic Acid And A Fragment O" 97.54 238 99.16 99.58 1.17e-172 PDB 1XLS "Crystal Structure Of The Mouse CarRXR LBD HETERODIMER Bound To Tcpobop And 9cra And A Tif2 Peptide Containg The Third Lxxll Mot" 95.08 232 100.00 100.00 3.64e-169 PDB 1XV9 "Crystal Structure Of CarRXR HETERODIMER BOUND WITH SRC1 Peptide, Fatty Acid, And 5b-Pregnane-3,20-Dione." 96.72 236 100.00 100.00 1.12e-172 PDB 1XVP "Crystal Structure Of CarRXR HETERODIMER BOUND WITH SRC1 Peptide, Fatty Acid And Citco" 96.72 236 100.00 100.00 1.12e-172 PDB 2ACL "Liver X-Receptor Alpha Ligand Binding Domain With Sb313987" 97.54 238 100.00 100.00 5.11e-174 PDB 2P1T "Crystal Structure Of The Ligand Binding Domain Of The Retinoid X Receptor Alpha In Complex With 3-(2'-Methoxy)- Tetrahydronapht" 98.36 240 100.00 100.00 9.90e-176 PDB 2P1U "Crystal Structure Of The Ligand Binding Domain Of The Retinoid X Receptor Alpha In Complex With 3-(2'-Ethoxy)- Tetrahydronaphty" 98.36 240 100.00 100.00 9.90e-176 PDB 2P1V "Crystal Structure Of The Ligand Binding Domain Of The Retinoid X Receptor Alpha In Complex With 3-(2'-Propoxy)- Tetrahydronapht" 98.36 240 100.00 100.00 9.90e-176 PDB 2ZXZ "Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To A Synthetic Agonist Compound And A Coactivator Peptide" 98.36 240 100.00 100.00 9.90e-176 PDB 2ZY0 "Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To A Synthetic Agonist Compound And A Coactivator Peptide" 98.36 240 100.00 100.00 9.90e-176 PDB 3A9E "Crystal Structure Of A Mixed Agonist-bound Rar-alpha And Antagonist- Bound Rxr-alpha Heterodimer Ligand Binding Domains" 98.36 240 99.17 99.58 3.47e-174 PDB 3DZU "Intact Ppar Gamma - Rxr Alpha Nuclear Receptor Complex On Dna Bound With Bvt.13, 9-Cis Retinoic Acid And Ncoa2 Peptide" 98.36 467 100.00 100.00 3.90e-172 PDB 3DZY "Intact Ppar Gamma - Rxr Alpha Nuclear Receptor Complex On Dna Bound With Rosiglitazone, 9-Cis Retinoic Acid And Ncoa2 Peptide" 98.36 467 100.00 100.00 3.90e-172 PDB 3E00 "Intact Ppar Gamma - Rxr Alpha Nuclear Receptor Complex On Dna Bound With Gw9662, 9-Cis Retinoic Acid And Ncoa2 Peptide" 98.36 467 100.00 100.00 3.90e-172 PDB 3E94 "Crystal Structure Of Rxralpha Ligand Binding Domain In Complex With Tributyltin And A Coactivator Fragment" 100.00 244 100.00 100.00 3.97e-179 PDB 3FAL "Humanrxr Alpha & Mouse Lxr Alpha Complexed With Retenoic Acid And Gsk2186" 97.95 242 99.58 99.58 3.20e-174 PDB 3FC6 "Hrxralpha & Mlxralpha With An Indole Pharmacophore, Sb786875" 97.95 242 99.58 99.58 3.20e-174 PDB 3FUG "Crystal Structure Of The Retinoid X Receptor Ligand Binding Domain Bound To The Synthetic Agonist 3-[4-Hydroxy-3-(3,5, 5,8,8-Pe" 98.36 240 100.00 100.00 9.90e-176 PDB 3H0A "Crystal Structure Of Peroxisome Proliferator-activated Receptor Gamma (pparg) And Retinoic Acid Receptor Alpha (rxra) In Comple" 93.44 228 100.00 100.00 6.90e-166 PDB 3KWY "Crystal Structure Of Rxralpha Ligand Binding Domain In Complex With Triphenyltin And A Coactivator Fragment" 100.00 244 100.00 100.00 3.97e-179 PDB 3NSP "Crystal Structure Of Tetrameric Rxralpha-Lbd" 98.36 240 100.00 100.00 9.90e-176 PDB 3NSQ "Crystal Structure Of Tetrameric Rxralpha-Lbd Complexed With Antagonist Danthron" 98.36 240 100.00 100.00 9.90e-176 PDB 3OAP "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 9-cis Retinoic Acid And The Coactivator" 94.67 231 100.00 100.00 3.10e-168 PDB 3OZJ "Crystal Structure Of Human Retinoic X Receptor Alpha Complexed With Bigelovin And Coactivator Src-1" 97.54 238 100.00 100.00 5.11e-174 PDB 3PCU "Crystal Structure Of Human Retinoic X Receptor Alpha Ligand-Binding Domain Complexed With Lx0278 And Src1 Peptide" 94.26 230 100.00 100.00 1.82e-167 PDB 3R29 "Crystal Structure Of Rxralpha Ligand-Binding Domain Complexed With Corepressor Smrt2" 98.36 240 100.00 100.00 9.90e-176 PDB 3R2A "Crystal Structure Of Rxralpha Ligand-Binding Domain Complexed With Corepressor Smrt2 And Antagonist Rhein" 98.36 240 100.00 100.00 9.90e-176 PDB 3R5M "Crystal Structure Of Rxralphalbd Complexed With The Agonist Magnolol" 98.36 240 100.00 100.00 9.90e-176 PDB 3UVV "Crystal Structure Of The Ligand Binding Domains Of The Thyroid Receptor:retinoid X Receptor Complexed With 3,3',5 Triiodo-L- Th" 97.95 244 99.58 99.58 3.22e-174 PDB 4J5W "Crystal Structure Of The Apo-pxr/rxralpha Lbd Heterotetramer Complex" 96.72 264 100.00 100.00 1.52e-172 PDB 4J5X "Crystal Structure Of The Sr12813-bound Pxr/rxralpha Lbd Heterotetramer Complex" 96.72 264 100.00 100.00 1.52e-172 PDB 4K4J "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 9cuab30 And The Coactivator Peptide Gri" 94.67 231 100.00 100.00 3.10e-168 PDB 4K6I "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With Targretin And The Coactivator Peptide G" 94.67 231 100.00 100.00 3.10e-168 PDB 4M8E "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With (s) 4-methyl 9cuab30 Coactivator Peptid" 94.67 231 100.00 100.00 3.10e-168 PDB 4M8H "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With (r)4-methyl 9cuab30 And Coactivator Pep" 94.67 231 100.00 100.00 3.10e-168 PDB 4N5G "Crystal Structure Of Rxra Lbd Complexed With A Synthetic Modulator K8012" 100.00 244 100.00 100.00 3.97e-179 PDB 4N8R "Crystal Structure Of Rxra Lbd Complexed With A Synthetic Modulator K- 8008" 100.00 244 100.00 100.00 3.97e-179 PDB 4NQA "Crystal Structure Of Liganded Hrxr-alpha/hlxr-beta Heterodimer On Dna" 98.36 365 100.00 100.00 9.44e-174 PDB 4OC7 "Retinoic Acid Receptor Alpha In Complex With (e)-3-(3'-allyl-6- Hydroxy-[1,1'-biphenyl]-3-yl)acrylic Acid And A Fragment Of The" 100.00 254 100.00 100.00 2.43e-179 PDB 4POH "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 8-methyl Uab30 And The Coactivator Pept" 94.67 231 100.00 100.00 3.10e-168 PDB 4POJ "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 7-methyl Uab30 And The Coactivator Pept" 94.67 231 100.00 100.00 3.10e-168 PDB 4PP3 "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 6-methyl Uab30 And The Coactivator Pept" 94.67 231 100.00 100.00 3.10e-168 PDB 4PP5 "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 5-methyl Uab30 And The Coactivator Pept" 94.67 231 100.00 100.00 3.10e-168 PDB 4RFW "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 9cuab70 And The Coactivator Peptide Gri" 94.67 231 100.00 100.00 3.10e-168 PDB 4RMC "Crystal Structure Of Human Retinoid X Receptor Alpha-ligand Binding Domain Complex With 9cuab76 And The Coactivator Peptide Gri" 94.67 231 100.00 100.00 3.10e-168 PDB 4RMD "Crystal Structure Of Human Retinoid X Receptor Alpha Ligand Binding Domain Complex With 9cuab110 And Coactivator Peptide Grip-1" 96.31 235 100.00 100.00 1.08e-171 PDB 4RME "Crystal Structure Of Human Retinoid X Receptor Alpha Ligand Binding Domain Complex With 9cuab111 And Coactivator Peptide Grip-1" 96.31 235 100.00 100.00 1.08e-171 PDB 4ZO1 "Crystal Structure Of The T3-bound Tr-beta Ligand-binding Domain In Complex With Rxr-alpha" 92.21 225 100.00 100.00 2.62e-163 DBJ BAE26004 "unnamed protein product [Mus musculus]" 98.36 467 99.17 99.58 9.64e-171 DBJ BAE73032 "hypothetical protein [Macaca fascicularis]" 98.36 462 98.75 98.75 4.31e-170 DBJ BAG54745 "unnamed protein product [Homo sapiens]" 98.36 365 100.00 100.00 9.44e-174 DBJ BAG72733 "retinoid X receptor, alpha [synthetic construct]" 98.36 462 100.00 100.00 2.20e-172 DBJ BAH02296 "retinoid X receptor, alpha [Homo sapiens]" 98.36 462 100.00 100.00 2.20e-172 EMBL CAA36982 "unnamed protein product [Homo sapiens]" 98.36 462 100.00 100.00 2.20e-172 EMBL CAA46962 "retinoid X receptor-alpha [Mus musculus]" 98.36 467 99.17 99.58 1.09e-170 EMBL CAL25727 "retinoid X receptor alpha [Rattus norvegicus]" 98.36 467 99.17 99.58 7.42e-171 EMBL CAL25728 "retinoid X receptor alpha [Rattus norvegicus]" 98.36 467 99.17 99.58 7.42e-171 EMBL CAL36079 "retinoid X receptor alpha [Rattus norvegicus]" 98.36 467 99.17 99.58 7.42e-171 GB AAA40080 "retinoid X receptor alpha [Mus musculus]" 98.36 467 99.17 99.58 1.09e-170 GB AAA42093 "retinoid X receptor alpha [Rattus norvegicus]" 98.36 467 99.17 99.58 6.58e-171 GB AAB36777 "RXR alpha 2 [Mus musculus]" 98.36 439 99.17 99.58 9.07e-171 GB AAB36778 "RXR alpha 3 [Mus musculus]" 98.36 439 99.17 99.58 9.07e-171 GB AAC95154 "retinoic acid receptor RXR [Cloning vector pERV3]" 98.36 479 100.00 100.00 2.98e-172 PRF 1609194A "retinoic acid receptor RXRalpha" 98.36 462 100.00 100.00 2.20e-172 REF NP_001277410 "retinoic acid receptor RXR-alpha isoform 2 [Mus musculus]" 98.36 439 99.17 99.58 9.07e-171 REF NP_001277411 "retinoic acid receptor RXR-alpha isoform 2 [Mus musculus]" 98.36 439 99.17 99.58 9.07e-171 REF NP_001278849 "retinoic acid receptor RXR-alpha isoform b [Homo sapiens]" 98.36 435 100.00 100.00 2.13e-172 REF NP_001278850 "retinoic acid receptor RXR-alpha isoform c [Homo sapiens]" 98.36 365 100.00 100.00 9.44e-174 REF NP_001291272 "retinoid X receptor, alpha [Bos taurus]" 98.36 439 98.75 100.00 6.90e-171 SP P19793 "RecName: Full=Retinoic acid receptor RXR-alpha; AltName: Full=Nuclear receptor subfamily 2 group B member 1; AltName: Full=Reti" 98.36 462 100.00 100.00 2.20e-172 SP P28700 "RecName: Full=Retinoic acid receptor RXR-alpha; AltName: Full=Nuclear receptor subfamily 2 group B member 1; AltName: Full=Reti" 98.36 467 99.17 99.58 1.09e-170 SP Q05343 "RecName: Full=Retinoic acid receptor RXR-alpha; AltName: Full=Nuclear receptor subfamily 2 group B member 1; AltName: Full=Reti" 98.36 467 99.17 99.58 6.58e-171 TPG DAA24096 "TPA: retinoid X receptor, alpha [Bos taurus]" 99.18 404 97.93 99.17 2.49e-169 stop_ save_ save_GRIP1_NR_Box_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GRIP1_NR_Box_2 _Molecular_mass 1574.8 _Mol_thiol_state 'not present' _Details . _Residue_count 13 _Mol_residue_sequence KHKILHRLLQDSS loop_ _Residue_seq_code _Residue_label 1 LYS 2 HIS 3 LYS 4 ILE 5 LEU 6 HIS 7 ARG 8 LEU 9 LEU 10 GLN 11 ASP 12 SER 13 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_REA _Saveframe_category ligand _Mol_type non-polymer _Name_common "REA (RETINOIC ACID)" _BMRB_code . _PDB_code REA _Molecular_mass 300.435 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Dec 20 05:01:57 2006 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C N 0 . ? C10 C10 C N 0 . ? C11 C11 C N 0 . ? C12 C12 C N 0 . ? C13 C13 C N 0 . ? C14 C14 C N 0 . ? C15 C15 C N 0 . ? C16 C16 C N 0 . ? C17 C17 C N 0 . ? C18 C18 C N 0 . ? C19 C19 C N 0 . ? C2 C2 C N 0 . ? C20 C20 C N 0 . ? C3 C3 C N 0 . ? C4 C4 C N 0 . ? C5 C5 C N 0 . ? C6 C6 C N 0 . ? C7 C7 C N 0 . ? C8 C8 C N 0 . ? C9 C9 C N 0 . ? H10 H10 H N 0 . ? H11 H11 H N 0 . ? H12 H12 H N 0 . ? H14 H14 H N 0 . ? H161 H161 H N 0 . ? H162 H162 H N 0 . ? H163 H163 H N 0 . ? H171 H171 H N 0 . ? H172 H172 H N 0 . ? H173 H173 H N 0 . ? H181 H181 H N 0 . ? H182 H182 H N 0 . ? H183 H183 H N 0 . ? H191 H191 H N 0 . ? H192 H192 H N 0 . ? H193 H193 H N 0 . ? H201 H201 H N 0 . ? H202 H202 H N 0 . ? H203 H203 H N 0 . ? H21 H21 H N 0 . ? H22 H22 H N 0 . ? H31 H31 H N 0 . ? H32 H32 H N 0 . ? H41 H41 H N 0 . ? H42 H42 H N 0 . ? H7 H7 H N 0 . ? H8 H8 H N 0 . ? HO2 HO2 H N 0 . ? O1 O1 O N 0 . ? O2 O2 O N 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 SING C1 C2 ? ? SING C1 C6 ? ? SING C1 C16 ? ? SING C1 C17 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? DOUB C5 C6 ? ? SING C5 C18 ? ? SING C6 C7 ? ? DOUB C7 C8 ? ? SING C7 H7 ? ? SING C8 C9 ? ? SING C8 H8 ? ? DOUB C9 C10 ? ? SING C9 C19 ? ? SING C10 C11 ? ? SING C10 H10 ? ? DOUB C11 C12 ? ? SING C11 H11 ? ? SING C12 C13 ? ? SING C12 H12 ? ? DOUB C13 C14 ? ? SING C13 C20 ? ? SING C14 C15 ? ? SING C14 H14 ? ? DOUB C15 O1 ? ? SING C15 O2 ? ? SING C16 H161 ? ? SING C16 H162 ? ? SING C16 H163 ? ? SING C17 H171 ? ? SING C17 H172 ? ? SING C17 H173 ? ? SING C18 H181 ? ? SING C18 H182 ? ? SING C18 H183 ? ? SING C19 H191 ? ? SING C19 H192 ? ? SING C19 H193 ? ? SING C20 H201 ? ? SING C20 H202 ? ? SING C20 H203 ? ? SING O2 HO2 ? ? 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 $RXRalpha_LBD Human 9606 Eukaryota Metazoa Homo sapiens $GRIP1_NR_Box_2 Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $RXRalpha_LBD 'recombinant technology' . . . BL21 DE3 pET15b $GRIP1_NR_Box_2 'chemical synthesis' . . . . . . 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 $RXRalpha_LBD 1.0 mM '[U-13C; U-15N; U-2H]' $REA 1.0 mM 'natural abundance' $GRIP1_NR_Box_2 1.0 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' 'sodium azide' 0.05 % 'natural abundance' EDTA 0.5 mM 'natural abundance' beta-mercaptoethanol 8 mM 'natural abundance' D2O 5 % 'natural abundance' H2O 95 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 . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'triple resonance probe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 700 _Details 'triple resonance probe' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details cryoprobe save_ ############################# # NMR applied experiments # ############################# save_4D_TROSY-HNCOCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCOCA' _Sample_label $sample_1 save_ save_4D_TROSY-HNCOi-1CAi_2 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCOi-1CAi' _Sample_label $sample_1 save_ save_4D_TROSY-HNCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCACO' _Sample_label $sample_1 save_ save_4D_15N,15N-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 15N,15N-NOESY' _Sample_label $sample_1 save_ save_3D_TROSY-HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY-HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CO)CACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CACB' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY-HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.21 . M pH 7.4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 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 '4D TROSY-HNCOCA' '3D TROSY-HNCO' '3D TROSY-HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'RXRalpha LBD' _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 1 225 7 SER C C 174.8 0.1 1 2 225 7 SER CA C 58.1 0.2 1 3 225 7 SER CB C 63.2 0.2 1 4 226 8 ALA H H 8.30 0.01 1 5 226 8 ALA C C 178.2 0.1 1 6 226 8 ALA CA C 53.0 0.2 1 7 226 8 ALA CB C 18.1 0.2 1 8 226 8 ALA N N 126.1 0.1 1 9 227 9 ASN H H 8.25 0.01 1 10 227 9 ASN C C 175.9 0.1 1 11 227 9 ASN CA C 54.0 0.2 1 12 227 9 ASN CB C 38.7 0.2 1 13 227 9 ASN N N 117.1 0.1 1 14 228 10 GLU H H 7.99 0.01 1 15 228 10 GLU C C 176.8 0.1 1 16 228 10 GLU CA C 56.8 0.2 1 17 228 10 GLU CB C 29.3 0.2 1 18 228 10 GLU N N 119.4 0.1 1 19 229 11 ASP H H 8.01 0.01 1 20 229 11 ASP C C 176.0 0.1 1 21 229 11 ASP CA C 54.8 0.2 1 22 229 11 ASP CB C 40.9 0.2 1 23 229 11 ASP N N 119.6 0.1 1 24 230 12 MET H H 8.11 0.01 1 25 230 12 MET C C 180.8 0.1 1 26 230 12 MET CA C 51.4 0.2 1 27 230 12 MET CB C 30.7 0.2 1 28 230 12 MET N N 119.3 0.1 1 29 231 13 PRO C C 180.3 0.1 1 30 231 13 PRO CA C 62.1 0.2 1 31 231 13 PRO CB C 31.2 0.2 1 32 232 14 VAL H H 9.15 0.01 1 33 232 14 VAL C C 178.2 0.1 1 34 232 14 VAL CA C 64.8 0.2 1 35 232 14 VAL CB C 30.1 0.2 1 36 232 14 VAL N N 122.7 0.1 1 37 233 15 GLU H H 9.68 0.01 1 38 233 15 GLU C C 179.9 0.1 1 39 233 15 GLU CA C 59.9 0.2 1 40 233 15 GLU CB C 28.0 0.2 1 41 233 15 GLU N N 121.4 0.1 1 42 234 16 ARG H H 7.19 0.01 1 43 234 16 ARG C C 179.1 0.1 1 44 234 16 ARG CA C 57.0 0.2 1 45 234 16 ARG CB C 31.3 0.2 1 46 234 16 ARG N N 116.6 0.1 1 47 235 17 ILE H H 7.13 0.01 1 48 235 17 ILE C C 177.4 0.1 1 49 235 17 ILE CA C 64.9 0.2 1 50 235 17 ILE CB C 36.5 0.2 1 51 235 17 ILE N N 123.2 0.1 1 52 236 18 LEU H H 8.29 0.01 1 53 236 18 LEU C C 178.4 0.1 1 54 236 18 LEU CA C 57.7 0.2 1 55 236 18 LEU CB C 39.3 0.2 1 56 236 18 LEU N N 121.2 0.1 1 57 237 19 GLU H H 7.76 0.01 1 58 237 19 GLU C C 179.1 0.1 1 59 237 19 GLU CA C 59.1 0.2 1 60 237 19 GLU CB C 29.1 0.2 1 61 237 19 GLU N N 116.9 0.1 1 62 238 20 ALA H H 7.45 0.01 1 63 238 20 ALA C C 179.0 0.1 1 64 238 20 ALA CA C 55.3 0.2 1 65 238 20 ALA CB C 17.3 0.2 1 66 238 20 ALA N N 122.5 0.1 1 67 239 21 GLU H H 7.66 0.01 1 68 239 21 GLU C C 180.4 0.1 1 69 239 21 GLU CA C 58.5 0.2 1 70 239 21 GLU CB C 29.6 0.2 1 71 239 21 GLU N N 116.0 0.1 1 72 240 22 LEU H H 8.54 0.01 1 73 240 22 LEU C C 180.0 0.1 1 74 240 22 LEU CA C 56.8 0.2 1 75 240 22 LEU CB C 40.3 0.2 1 76 240 22 LEU N N 117.7 0.1 1 77 241 23 ALA H H 8.10 0.01 1 78 241 23 ALA C C 179.5 0.1 1 79 241 23 ALA CA C 54.2 0.2 1 80 241 23 ALA CB C 17.6 0.2 1 81 241 23 ALA N N 120.9 0.1 1 82 242 24 VAL H H 6.99 0.01 1 83 242 24 VAL C C 176.3 0.1 1 84 242 24 VAL CA C 60.2 0.2 1 85 242 24 VAL CB C 30.8 0.2 1 86 242 24 VAL N N 106.3 0.1 1 87 243 25 GLU H H 7.18 0.01 1 88 243 25 GLU C C 174.4 0.1 1 89 243 25 GLU CA C 54.5 0.2 1 90 243 25 GLU CB C 29.1 0.2 1 91 243 25 GLU N N 126.1 0.1 1 92 244 26 PRO C C 176.9 0.1 1 93 244 26 PRO CA C 62.6 0.2 1 94 244 26 PRO CB C 31.4 0.2 1 95 245 27 LYS H H 8.47 0.01 1 96 245 27 LYS C C 176.9 0.1 1 97 245 27 LYS CA C 55.4 0.2 1 98 245 27 LYS CB C 31.5 0.2 1 99 245 27 LYS N N 122.7 0.1 1 100 246 28 THR H H 8.01 0.01 1 101 246 28 THR C C 174.6 0.1 1 102 246 28 THR CA C 61.7 0.2 1 103 246 28 THR CB C 69.2 0.2 1 104 246 28 THR N N 117.0 0.1 1 105 247 29 GLU H H 8.60 0.01 1 106 247 29 GLU C C 176.5 0.1 1 107 247 29 GLU CA C 56.6 0.2 1 108 247 29 GLU CB C 29.4 0.2 1 109 247 29 GLU N N 124.1 0.1 1 110 248 30 THR H H 7.92 0.01 1 111 248 30 THR C C 174.1 0.1 1 112 248 30 THR CA C 61.6 0.2 1 113 248 30 THR CB C 69.4 0.2 1 114 248 30 THR N N 115.2 0.1 1 115 249 31 TYR H H 8.13 0.01 1 116 249 31 TYR C C 175.6 0.1 1 117 249 31 TYR CA C 57.4 0.2 1 118 249 31 TYR CB C 38.1 0.2 1 119 249 31 TYR N N 123.8 0.1 1 120 250 32 VAL H H 7.89 0.01 1 121 250 32 VAL C C 175.9 0.1 1 122 250 32 VAL CA C 61.6 0.2 1 123 250 32 VAL CB C 32.3 0.2 1 124 250 32 VAL N N 122.8 0.1 1 125 251 33 GLU H H 8.31 0.01 1 126 251 33 GLU C C 176.8 0.1 1 127 251 33 GLU CA C 56.6 0.2 1 128 251 33 GLU CB C 29.3 0.2 1 129 251 33 GLU N N 124.7 0.1 1 130 252 34 ALA H H 8.23 0.01 1 131 252 34 ALA C C 177.7 0.1 1 132 252 34 ALA CA C 52.6 0.2 1 133 252 34 ALA CB C 18.3 0.2 1 134 252 34 ALA N N 125.0 0.1 1 135 253 35 ASN H H 8.27 0.01 1 136 253 35 ASN C C 175.5 0.1 1 137 253 35 ASN CA C 53.0 0.2 1 138 253 35 ASN CB C 38.1 0.2 1 139 253 35 ASN N N 117.4 0.1 1 140 254 36 MET H H 8.17 0.01 1 141 254 36 MET C C 176.8 0.1 1 142 254 36 MET CA C 55.6 0.2 1 143 254 36 MET CB C 31.8 0.2 1 144 254 36 MET N N 120.8 0.1 1 145 255 37 GLY H H 8.25 0.01 1 146 255 37 GLY C C 173.8 0.1 1 147 255 37 GLY CA C 44.9 0.2 1 148 255 37 GLY N N 109.6 0.1 1 149 256 38 LEU H H 7.76 0.01 1 150 256 38 LEU C C 176.1 0.1 1 151 256 38 LEU CA C 54.3 0.2 1 152 256 38 LEU CB C 41.6 0.2 1 153 256 38 LEU N N 121.9 0.1 1 154 257 39 ASN H H 8.06 0.01 1 155 257 39 ASN C C 173.3 0.1 1 156 257 39 ASN CA C 50.5 0.2 1 157 257 39 ASN CB C 40.0 0.2 1 158 257 39 ASN N N 119.6 0.1 1 159 258 40 PRO C C 177.2 0.1 1 160 258 40 PRO CA C 63.2 0.2 1 161 258 40 PRO CB C 31.2 0.2 1 162 259 41 SER H H 8.25 0.01 1 163 259 41 SER C C 174.3 0.1 1 164 259 41 SER CA C 58.1 0.2 1 165 259 41 SER CB C 63.0 0.2 1 166 259 41 SER N N 115.4 0.1 1 167 260 42 SER H H 8.00 0.01 1 168 260 42 SER C C 172.8 0.1 1 169 260 42 SER CA C 55.8 0.2 1 170 260 42 SER CB C 63.0 0.2 1 171 260 42 SER N N 118.6 0.1 1 172 261 43 PRO C C 177.4 0.1 1 173 261 43 PRO CA C 59.2 0.2 1 174 262 44 ASN H H 7.88 0.01 1 175 262 44 ASN C C 174.5 0.1 1 176 262 44 ASN CA C 52.3 0.2 1 177 262 44 ASN CB C 38.6 0.2 1 178 262 44 ASN N N 116.5 0.1 1 179 263 45 ASP H H 8.00 0.01 1 180 263 45 ASP C C 173.8 0.1 1 181 263 45 ASP CA C 52.2 0.2 1 182 263 45 ASP CB C 40.6 0.2 1 183 263 45 ASP N N 121.5 0.1 1 184 264 46 PRO C C 178.5 0.1 1 185 264 46 PRO CA C 65.0 0.2 1 186 265 47 VAL H H 7.83 0.01 1 187 265 47 VAL C C 177.2 0.1 1 188 265 47 VAL CA C 67.4 0.2 1 189 265 47 VAL CB C 30.0 0.2 1 190 265 47 VAL N N 117.9 0.1 1 191 266 48 THR H H 7.46 0.01 1 192 266 48 THR C C 176.8 0.1 1 193 266 48 THR CA C 65.6 0.2 1 194 266 48 THR CB C 67.1 0.2 1 195 266 48 THR N N 117.8 0.1 1 196 267 49 ASN H H 7.83 0.01 1 197 267 49 ASN C C 178.5 0.1 1 198 267 49 ASN CA C 56.2 0.2 1 199 267 49 ASN CB C 37.0 0.2 1 200 267 49 ASN N N 118.8 0.1 1 201 268 50 ILE H H 8.47 0.01 1 202 268 50 ILE C C 176.8 0.1 1 203 268 50 ILE CA C 65.9 0.2 1 204 268 50 ILE CB C 36.9 0.2 1 205 268 50 ILE N N 123.3 0.1 1 206 269 51 CYS H H 8.40 0.01 1 207 269 51 CYS C C 176.7 0.1 1 208 269 51 CYS CA C 57.7 0.2 1 209 269 51 CYS CB C 30.8 0.2 1 210 269 51 CYS N N 118.4 0.1 1 211 270 52 GLN H H 8.22 0.01 1 212 270 52 GLN C C 178.6 0.1 1 213 270 52 GLN CA C 59.2 0.2 1 214 270 52 GLN CB C 27.6 0.2 1 215 270 52 GLN N N 121.0 0.1 1 216 271 53 ALA H H 7.55 0.01 1 217 271 53 ALA C C 178.2 0.1 1 218 271 53 ALA CA C 54.9 0.2 1 219 271 53 ALA CB C 17.8 0.2 1 220 271 53 ALA N N 123.2 0.1 1 221 272 54 ALA H H 8.29 0.01 1 222 272 54 ALA C C 178.1 0.1 1 223 272 54 ALA CA C 55.2 0.2 1 224 272 54 ALA CB C 17.8 0.2 1 225 272 54 ALA N N 119.8 0.1 1 226 273 55 ASP H H 7.56 0.01 1 227 273 55 ASP C C 177.2 0.1 1 228 273 55 ASP CA C 58.5 0.2 1 229 273 55 ASP CB C 44.0 0.2 1 230 273 55 ASP N N 115.4 0.1 1 231 274 56 LYS H H 7.39 0.01 1 232 274 56 LYS C C 180.9 0.1 1 233 274 56 LYS CA C 59.1 0.2 1 234 274 56 LYS CB C 31.7 0.2 1 235 274 56 LYS N N 115.0 0.1 1 236 275 57 GLN H H 8.45 0.01 1 237 275 57 GLN C C 178.8 0.1 1 238 275 57 GLN CA C 55.7 0.2 1 239 275 57 GLN CB C 29.7 0.2 1 240 275 57 GLN N N 115.8 0.1 1 241 276 58 LEU H H 8.18 0.01 1 242 276 58 LEU C C 178.3 0.1 1 243 276 58 LEU CA C 57.7 0.2 1 244 276 58 LEU CB C 40.2 0.2 1 245 276 58 LEU N N 127.3 0.1 1 246 277 59 PHE H H 7.15 0.01 1 247 277 59 PHE C C 179.7 0.1 1 248 277 59 PHE CA C 62.5 0.2 1 249 277 59 PHE CB C 38.0 0.2 1 250 277 59 PHE N N 115.3 0.1 1 251 278 60 THR H H 7.15 0.01 1 252 278 60 THR C C 175.7 0.1 1 253 278 60 THR CA C 64.1 0.2 1 254 278 60 THR CB C 68.2 0.2 1 255 278 60 THR N N 112.7 0.1 1 256 279 61 LEU H H 8.26 0.01 1 257 279 61 LEU C C 178.3 0.1 1 258 279 61 LEU CA C 56.8 0.2 1 259 279 61 LEU CB C 40.6 0.2 1 260 279 61 LEU N N 125.6 0.1 1 261 280 62 VAL H H 7.27 0.01 1 262 280 62 VAL C C 176.7 0.1 1 263 280 62 VAL CA C 66.6 0.2 1 264 280 62 VAL CB C 30.8 0.2 1 265 280 62 VAL N N 117.5 0.1 1 266 281 63 GLU H H 6.79 0.01 1 267 281 63 GLU C C 178.7 0.1 1 268 281 63 GLU CA C 58.6 0.2 1 269 281 63 GLU CB C 28.2 0.2 1 270 281 63 GLU N N 117.3 0.1 1 271 282 64 TRP H H 8.38 0.01 1 272 282 64 TRP C C 176.7 0.1 1 273 282 64 TRP CA C 61.7 0.2 1 274 282 64 TRP CB C 27.9 0.2 1 275 282 64 TRP N N 120.3 0.1 1 276 283 65 ALA H H 8.30 0.01 1 277 283 65 ALA C C 179.0 0.1 1 278 283 65 ALA CA C 54.6 0.2 1 279 283 65 ALA CB C 16.3 0.2 1 280 283 65 ALA N N 121.0 0.1 1 281 284 66 LYS H H 7.45 0.01 1 282 284 66 LYS C C 178.8 0.1 1 283 284 66 LYS CA C 58.9 0.2 1 284 284 66 LYS CB C 31.9 0.2 1 285 284 66 LYS N N 111.7 0.1 1 286 285 67 ARG H H 7.33 0.01 1 287 285 67 ARG C C 176.4 0.1 1 288 285 67 ARG CA C 55.6 0.2 1 289 285 67 ARG CB C 29.7 0.2 1 290 285 67 ARG N N 118.5 0.1 1 291 286 68 ILE H H 7.36 0.01 1 292 286 68 ILE C C 174.9 0.1 1 293 286 68 ILE CA C 55.0 0.2 1 294 286 68 ILE CB C 33.4 0.2 1 295 286 68 ILE N N 126.8 0.1 1 296 287 69 PRO C C 174.8 0.1 1 297 287 69 PRO CA C 64.3 0.2 1 298 287 69 PRO CB C 31.0 0.2 1 299 288 70 HIS H H 7.96 0.01 1 300 288 70 HIS C C 176.1 0.1 1 301 288 70 HIS CA C 58.2 0.2 1 302 288 70 HIS CB C 27.4 0.2 1 303 288 70 HIS N N 111.3 0.1 1 304 289 71 PHE H H 8.05 0.01 1 305 289 71 PHE C C 177.0 0.1 1 306 289 71 PHE CA C 62.9 0.2 1 307 289 71 PHE CB C 38.6 0.2 1 308 289 71 PHE N N 125.1 0.1 1 309 290 72 SER H H 9.09 0.01 1 310 290 72 SER C C 174.2 0.1 1 311 290 72 SER CA C 60.2 0.2 1 312 290 72 SER CB C 62.7 0.2 1 313 290 72 SER N N 111.0 0.1 1 314 291 73 GLU H H 7.11 0.01 1 315 291 73 GLU C C 178.1 0.1 1 316 291 73 GLU CA C 55.8 0.2 1 317 291 73 GLU CB C 29.3 0.2 1 318 291 73 GLU N N 118.2 0.1 1 319 292 74 LEU H H 7.21 0.01 1 320 292 74 LEU C C 174.9 0.1 1 321 292 74 LEU CA C 53.2 0.2 1 322 292 74 LEU CB C 39.7 0.2 1 323 292 74 LEU N N 122.0 0.1 1 324 293 75 PRO C C 178.1 0.1 1 325 293 75 PRO CA C 62.9 0.2 1 326 293 75 PRO CB C 31.2 0.2 1 327 294 76 LEU H H 8.72 0.01 1 328 294 76 LEU C C 178.4 0.1 1 329 294 76 LEU CA C 58.4 0.2 1 330 294 76 LEU CB C 40.4 0.2 1 331 294 76 LEU N N 129.0 0.1 1 332 295 77 ASP H H 8.65 0.01 1 333 295 77 ASP C C 179.2 0.1 1 334 295 77 ASP CA C 57.1 0.2 1 335 295 77 ASP CB C 39.9 0.2 1 336 295 77 ASP N N 114.5 0.1 1 337 296 78 ASP H H 7.14 0.01 1 338 296 78 ASP C C 177.5 0.1 1 339 296 78 ASP CA C 56.6 0.2 1 340 296 78 ASP CB C 39.9 0.2 1 341 296 78 ASP N N 119.1 0.1 1 342 297 79 GLN H H 7.74 0.01 1 343 297 79 GLN C C 178.9 0.1 1 344 297 79 GLN CA C 59.3 0.2 1 345 297 79 GLN N N 121.5 0.1 1 346 298 80 VAL H H 7.78 0.01 1 347 298 80 VAL C C 177.9 0.1 1 348 298 80 VAL CA C 66.0 0.2 1 349 298 80 VAL CB C 29.1 0.2 1 350 298 80 VAL N N 116.9 0.1 1 351 299 81 ILE H H 7.48 0.01 1 352 299 81 ILE C C 179.1 0.1 1 353 299 81 ILE CA C 65.0 0.2 1 354 299 81 ILE CB C 37.6 0.2 1 355 299 81 ILE N N 120.1 0.1 1 356 300 82 LEU H H 8.62 0.01 1 357 300 82 LEU C C 181.7 0.1 1 358 300 82 LEU CA C 57.7 0.2 1 359 300 82 LEU CB C 39.6 0.2 1 360 300 82 LEU N N 118.8 0.1 1 361 301 83 LEU H H 8.03 0.01 1 362 301 83 LEU C C 179.2 0.1 1 363 301 83 LEU CA C 58.1 0.2 1 364 301 83 LEU CB C 41.6 0.2 1 365 301 83 LEU N N 120.3 0.1 1 366 302 84 ARG H H 8.78 0.01 1 367 302 84 ARG C C 178.3 0.1 1 368 302 84 ARG CA C 60.0 0.2 1 369 302 84 ARG CB C 30.9 0.2 1 370 302 84 ARG N N 119.5 0.1 1 371 303 85 ALA H H 8.44 0.01 1 372 303 85 ALA C C 180.2 0.1 1 373 303 85 ALA CA C 53.7 0.2 1 374 303 85 ALA CB C 18.1 0.2 1 375 303 85 ALA N N 118.7 0.1 1 376 304 86 GLY H H 7.66 0.01 1 377 304 86 GLY C C 175.8 0.1 1 378 304 86 GLY CA C 45.5 0.2 1 379 304 86 GLY N N 102.9 0.1 1 380 305 87 TRP H H 8.07 0.01 1 381 305 87 TRP C C 174.9 0.1 1 382 305 87 TRP CA C 60.3 0.2 1 383 305 87 TRP CB C 26.4 0.2 1 384 305 87 TRP N N 119.6 0.1 1 385 306 88 ASN H H 7.04 0.01 1 386 306 88 ASN C C 175.9 0.1 1 387 306 88 ASN CA C 56.9 0.2 1 388 306 88 ASN CB C 34.0 0.2 1 389 306 88 ASN N N 117.8 0.1 1 390 307 89 GLU H H 6.80 0.01 1 391 307 89 GLU C C 178.4 0.1 1 392 307 89 GLU CA C 59.8 0.2 1 393 307 89 GLU N N 121.2 0.1 1 394 308 90 LEU H H 8.20 0.01 1 395 308 90 LEU C C 180.6 0.1 1 396 308 90 LEU CA C 57.8 0.2 1 397 308 90 LEU N N 118.1 0.1 1 398 309 91 LEU H H 8.32 0.01 1 399 309 91 LEU C C 179.7 0.1 1 400 309 91 LEU CA C 57.2 0.2 1 401 309 91 LEU CB C 40.8 0.2 1 402 309 91 LEU N N 119.3 0.1 1 403 310 92 ILE H H 7.87 0.01 1 404 310 92 ILE C C 179.1 0.1 1 405 310 92 ILE CA C 63.0 0.2 1 406 310 92 ILE CB C 37.1 0.2 1 407 310 92 ILE N N 120.7 0.1 1 408 311 93 ALA H H 8.15 0.01 1 409 311 93 ALA C C 177.7 0.1 1 410 311 93 ALA CA C 55.2 0.2 1 411 311 93 ALA CB C 15.7 0.2 1 412 311 93 ALA N N 123.0 0.1 1 413 312 94 SER H H 6.60 0.01 1 414 312 94 SER C C 178.3 0.1 1 415 312 94 SER CA C 62.1 0.2 1 416 312 94 SER CB C 60.0 0.2 1 417 312 94 SER N N 109.4 0.1 1 418 313 95 PHE H H 8.13 0.01 1 419 313 95 PHE C C 179.1 0.1 1 420 313 95 PHE CA C 59.4 0.2 1 421 313 95 PHE CB C 35.8 0.2 1 422 313 95 PHE N N 119.2 0.1 1 423 314 96 SER H H 7.68 0.01 1 424 314 96 SER C C 174.1 0.1 1 425 314 96 SER CA C 63.3 0.2 1 426 314 96 SER CB C 61.1 0.2 1 427 314 96 SER N N 125.8 0.1 1 428 315 97 HIS H H 7.37 0.01 1 429 315 97 HIS C C 178.6 0.1 1 430 315 97 HIS CA C 61.6 0.2 1 431 315 97 HIS CB C 32.2 0.2 1 432 315 97 HIS N N 121.7 0.1 1 433 316 98 ARG H H 7.55 0.01 1 434 316 98 ARG C C 178.2 0.1 1 435 316 98 ARG CA C 57.7 0.2 1 436 316 98 ARG CB C 30.3 0.2 1 437 316 98 ARG N N 119.1 0.1 1 438 317 99 SER H H 7.33 0.01 1 439 317 99 SER C C 173.5 0.1 1 440 317 99 SER CA C 59.6 0.2 1 441 317 99 SER CB C 62.6 0.2 1 442 317 99 SER N N 111.1 0.1 1 443 318 100 ILE H H 7.14 0.01 1 444 318 100 ILE C C 176.8 0.1 1 445 318 100 ILE CA C 64.8 0.2 1 446 318 100 ILE CB C 38.0 0.2 1 447 318 100 ILE N N 118.2 0.1 1 448 319 101 ALA H H 7.47 0.01 1 449 319 101 ALA C C 177.1 0.1 1 450 319 101 ALA CA C 52.2 0.2 1 451 319 101 ALA CB C 18.9 0.2 1 452 319 101 ALA N N 120.1 0.1 1 453 320 102 VAL H H 7.59 0.01 1 454 320 102 VAL C C 175.1 0.1 1 455 320 102 VAL CA C 59.6 0.2 1 456 320 102 VAL CB C 32.9 0.2 1 457 320 102 VAL N N 116.1 0.1 1 458 321 103 LYS H H 8.52 0.01 1 459 321 103 LYS C C 176.7 0.1 1 460 321 103 LYS CA C 55.3 0.2 1 461 321 103 LYS CB C 32.5 0.2 1 462 321 103 LYS N N 124.4 0.1 1 463 322 104 ASP H H 8.84 0.01 1 464 322 104 ASP C C 174.0 0.1 1 465 322 104 ASP CA C 55.2 0.2 1 466 322 104 ASP CB C 39.6 0.2 1 467 322 104 ASP N N 121.9 0.1 1 468 323 105 GLY H H 7.46 0.01 1 469 323 105 GLY C C 180.9 0.1 1 470 323 105 GLY CA C 46.2 0.2 1 471 323 105 GLY N N 103.1 0.1 1 472 324 106 ILE H H 8.39 0.01 1 473 324 106 ILE C C 173.3 0.1 1 474 324 106 ILE CA C 57.7 0.2 1 475 324 106 ILE CB C 41.1 0.2 1 476 324 106 ILE N N 110.6 0.1 1 477 325 107 LEU H H 8.19 0.01 1 478 325 107 LEU C C 175.4 0.1 1 479 325 107 LEU CA C 52.5 0.2 1 480 325 107 LEU CB C 42.3 0.2 1 481 325 107 LEU N N 124.4 0.1 1 482 326 108 LEU H H 8.67 0.01 1 483 326 108 LEU C C 180.6 0.1 1 484 326 108 LEU CA C 52.9 0.2 1 485 326 108 LEU CB C 42.1 0.2 1 486 326 108 LEU N N 123.0 0.1 1 487 327 109 ALA H H 11.20 0.01 1 488 327 109 ALA C C 177.8 0.1 1 489 327 109 ALA CA C 54.2 0.2 1 490 327 109 ALA CB C 18.6 0.2 1 491 327 109 ALA N N 127.6 0.1 1 492 328 110 THR H H 6.97 0.01 1 493 328 110 THR C C 175.5 0.1 1 494 328 110 THR CA C 60.3 0.2 1 495 328 110 THR CB C 68.7 0.2 1 496 328 110 THR N N 102.1 0.1 1 497 329 111 GLY H H 8.00 0.01 1 498 329 111 GLY C C 172.9 0.1 1 499 329 111 GLY CA C 44.8 0.2 1 500 329 111 GLY N N 109.6 0.1 1 501 330 112 LEU H H 6.32 0.01 1 502 330 112 LEU C C 174.8 0.1 1 503 330 112 LEU CA C 53.8 0.2 1 504 330 112 LEU CB C 42.9 0.2 1 505 330 112 LEU N N 119.5 0.1 1 506 331 113 HIS H H 8.47 0.01 1 507 331 113 HIS C C 175.7 0.1 1 508 331 113 HIS CA C 54.4 0.2 1 509 331 113 HIS CB C 32.0 0.2 1 510 331 113 HIS N N 122.7 0.1 1 511 332 114 VAL H H 8.64 0.01 1 512 332 114 VAL C C 174.3 0.1 1 513 332 114 VAL CA C 61.0 0.2 1 514 332 114 VAL CB C 32.8 0.2 1 515 332 114 VAL N N 125.0 0.1 1 516 333 115 HIS H H 8.81 0.01 1 517 333 115 HIS C C 176.7 0.1 1 518 333 115 HIS CA C 56.7 0.2 1 519 333 115 HIS CB C 32.3 0.2 1 520 333 115 HIS N N 128.0 0.1 1 521 334 116 ARG H H 8.52 0.01 1 522 334 116 ARG C C 177.8 0.1 1 523 334 116 ARG CA C 59.6 0.2 1 524 334 116 ARG CB C 29.9 0.2 1 525 334 116 ARG N N 125.8 0.1 1 526 336 118 SER C C 176.6 0.1 1 527 336 118 SER CA C 60.2 0.2 1 528 336 118 SER CB C 61.4 0.2 1 529 337 119 ALA H H 7.22 0.01 1 530 337 119 ALA C C 179.3 0.1 1 531 337 119 ALA CA C 54.5 0.2 1 532 337 119 ALA CB C 16.5 0.2 1 533 337 119 ALA N N 123.9 0.1 1 534 338 120 HIS H H 8.22 0.01 1 535 338 120 HIS C C 180.2 0.1 1 536 338 120 HIS CA C 60.3 0.2 1 537 338 120 HIS CB C 30.4 0.2 1 538 338 120 HIS N N 117.0 0.1 1 539 339 121 SER H H 8.04 0.01 1 540 339 121 SER C C 174.7 0.1 1 541 339 121 SER CA C 61.1 0.2 1 542 339 121 SER CB C 62.2 0.2 1 543 339 121 SER N N 117.6 0.1 1 544 340 122 ALA H H 7.31 0.01 1 545 340 122 ALA C C 177.4 0.1 1 546 340 122 ALA CA C 51.6 0.2 1 547 340 122 ALA CB C 19.4 0.2 1 548 340 122 ALA N N 121.2 0.1 1 549 341 123 GLY H H 7.49 0.01 1 550 341 123 GLY C C 175.6 0.1 1 551 341 123 GLY CA C 45.8 0.2 1 552 341 123 GLY N N 104.9 0.1 1 553 342 124 VAL H H 7.46 0.01 1 554 342 124 VAL C C 174.9 0.1 1 555 342 124 VAL CA C 58.6 0.2 1 556 342 124 VAL CB C 30.0 0.2 1 557 342 124 VAL N N 112.1 0.1 1 558 343 125 GLY H H 8.43 0.01 1 559 343 125 GLY C C 174.7 0.1 1 560 343 125 GLY CA C 45.2 0.2 1 561 343 125 GLY N N 110.2 0.1 1 562 345 127 ILE C C 175.8 0.1 1 563 345 127 ILE CA C 59.7 0.2 1 564 345 127 ILE CB C 43.7 0.2 1 565 346 128 PHE H H 7.60 0.01 1 566 346 128 PHE C C 177.3 0.1 1 567 346 128 PHE CA C 62.1 0.2 1 568 346 128 PHE CB C 38.1 0.2 1 569 346 128 PHE N N 126.5 0.1 1 570 347 129 ASP H H 8.79 0.01 1 571 347 129 ASP C C 180.0 0.1 1 572 347 129 ASP CA C 57.1 0.2 1 573 347 129 ASP CB C 39.2 0.2 1 574 347 129 ASP N N 118.4 0.1 1 575 348 130 ARG H H 7.72 0.01 1 576 348 130 ARG C C 178.8 0.1 1 577 348 130 ARG CA C 60.4 0.2 1 578 348 130 ARG CB C 28.7 0.2 1 579 348 130 ARG N N 121.1 0.1 1 580 349 131 VAL H H 7.79 0.01 1 581 349 131 VAL C C 179.1 0.1 1 582 349 131 VAL CA C 66.7 0.2 1 583 349 131 VAL CB C 29.6 0.2 1 584 349 131 VAL N N 120.2 0.1 1 585 350 132 LEU H H 7.94 0.01 1 586 350 132 LEU C C 179.3 0.1 1 587 350 132 LEU CA C 57.8 0.2 1 588 350 132 LEU CB C 40.0 0.2 1 589 350 132 LEU N N 118.5 0.1 1 590 351 133 THR H H 8.59 0.01 1 591 351 133 THR C C 175.9 0.1 1 592 351 133 THR CA C 65.4 0.2 1 593 351 133 THR CB C 69.1 0.2 1 594 351 133 THR N N 114.8 0.1 1 595 352 134 GLU H H 8.80 0.01 1 596 352 134 GLU C C 176.6 0.1 1 597 352 134 GLU CA C 57.4 0.2 1 598 352 134 GLU CB C 29.4 0.2 1 599 352 134 GLU N N 118.7 0.1 1 600 353 135 LEU H H 6.93 0.01 1 601 353 135 LEU C C 176.3 0.1 1 602 353 135 LEU CA C 55.1 0.2 1 603 353 135 LEU CB C 41.8 0.2 1 604 353 135 LEU N N 113.0 0.1 1 605 354 136 VAL H H 8.36 0.01 1 606 354 136 VAL C C 178.8 0.1 1 607 354 136 VAL CA C 67.3 0.2 1 608 354 136 VAL CB C 30.8 0.2 1 609 354 136 VAL N N 120.0 0.1 1 610 355 137 SER H H 8.60 0.01 1 611 355 137 SER C C 175.9 0.1 1 612 355 137 SER CA C 61.8 0.2 1 613 355 137 SER CB C 63.5 0.2 1 614 355 137 SER N N 111.5 0.1 1 615 356 138 LYS H H 6.08 0.01 1 616 356 138 LYS C C 179.5 0.1 1 617 356 138 LYS CA C 56.9 0.2 1 618 356 138 LYS CB C 30.1 0.2 1 619 356 138 LYS N N 117.6 0.1 1 620 357 139 MET H H 8.39 0.01 1 621 357 139 MET C C 177.6 0.1 1 622 357 139 MET CA C 60.1 0.2 1 623 357 139 MET CB C 31.6 0.2 1 624 357 139 MET N N 119.7 0.1 1 625 358 140 ARG H H 8.41 0.01 1 626 358 140 ARG C C 180.0 0.1 1 627 358 140 ARG CA C 58.7 0.2 1 628 358 140 ARG CB C 29.2 0.2 1 629 358 140 ARG N N 119.7 0.1 1 630 359 141 ASP H H 8.53 0.01 1 631 359 141 ASP C C 178.0 0.1 1 632 359 141 ASP CA C 57.1 0.2 1 633 359 141 ASP CB C 39.8 0.2 1 634 359 141 ASP N N 121.5 0.1 1 635 360 142 MET H H 7.45 0.01 1 636 360 142 MET C C 175.1 0.1 1 637 360 142 MET CA C 54.9 0.2 1 638 360 142 MET CB C 33.2 0.2 1 639 360 142 MET N N 113.9 0.1 1 640 361 143 GLN H H 7.84 0.01 1 641 361 143 GLN C C 176.1 0.1 1 642 361 143 GLN CA C 55.9 0.2 1 643 361 143 GLN CB C 25.5 0.2 1 644 361 143 GLN N N 120.0 0.1 1 645 362 144 MET H H 7.86 0.01 1 646 362 144 MET C C 177.0 0.1 1 647 362 144 MET CA C 56.4 0.2 1 648 362 144 MET CB C 34.1 0.2 1 649 362 144 MET N N 119.7 0.1 1 650 363 145 ASP H H 10.50 0.01 1 651 363 145 ASP C C 176.3 0.1 1 652 363 145 ASP CA C 52.6 0.2 1 653 363 145 ASP CB C 41.4 0.2 1 654 363 145 ASP N N 136.7 0.1 1 655 364 146 LYS H H 8.36 0.01 1 656 364 146 LYS C C 178.9 0.1 1 657 364 146 LYS CA C 59.1 0.2 1 658 364 146 LYS CB C 32.1 0.2 1 659 364 146 LYS N N 116.0 0.1 1 660 365 147 THR H H 8.08 0.01 1 661 365 147 THR C C 176.6 0.1 1 662 365 147 THR CA C 67.4 0.2 1 663 365 147 THR CB C 68.9 0.2 1 664 365 147 THR N N 120.2 0.1 1 665 366 148 GLU H H 8.80 0.01 1 666 366 148 GLU C C 178.6 0.1 1 667 366 148 GLU CA C 59.7 0.2 1 668 366 148 GLU CB C 29.6 0.2 1 669 366 148 GLU N N 124.7 0.1 1 670 367 149 LEU H H 8.13 0.01 1 671 367 149 LEU C C 178.7 0.1 1 672 367 149 LEU CA C 57.2 0.2 1 673 367 149 LEU CB C 39.7 0.2 1 674 367 149 LEU N N 118.6 0.1 1 675 368 150 GLY H H 8.14 0.01 1 676 368 150 GLY C C 176.4 0.1 1 677 368 150 GLY CA C 47.2 0.2 1 678 368 150 GLY N N 106.8 0.1 1 679 369 151 CYS H H 8.40 0.01 1 680 369 151 CYS C C 176.9 0.1 1 681 369 151 CYS CA C 63.6 0.2 1 682 369 151 CYS CB C 29.2 0.2 1 683 369 151 CYS N N 118.8 0.1 1 684 370 152 LEU H H 8.55 0.01 1 685 370 152 LEU C C 179.1 0.1 1 686 370 152 LEU CA C 58.4 0.2 1 687 370 152 LEU CB C 41.0 0.2 1 688 370 152 LEU N N 121.4 0.1 1 689 371 153 ARG H H 8.54 0.01 1 690 371 153 ARG C C 177.6 0.1 1 691 371 153 ARG CA C 60.7 0.2 1 692 371 153 ARG CB C 29.1 0.2 1 693 371 153 ARG N N 116.8 0.1 1 694 372 154 ALA H H 8.76 0.01 1 695 372 154 ALA C C 178.3 0.1 1 696 372 154 ALA CA C 54.9 0.2 1 697 372 154 ALA CB C 17.6 0.2 1 698 372 154 ALA N N 123.2 0.1 1 699 373 155 ILE H H 8.28 0.01 1 700 373 155 ILE C C 178.6 0.1 1 701 373 155 ILE CA C 66.5 0.2 1 702 373 155 ILE CB C 38.4 0.2 1 703 373 155 ILE N N 119.9 0.1 1 704 374 156 VAL H H 8.76 0.01 1 705 374 156 VAL C C 176.4 0.1 1 706 374 156 VAL CA C 65.3 0.2 1 707 374 156 VAL N N 109.8 0.1 1 708 375 157 LEU H H 7.95 0.01 1 709 375 157 LEU C C 178.5 0.1 1 710 375 157 LEU CA C 57.7 0.2 1 711 375 157 LEU CB C 41.1 0.2 1 712 375 157 LEU N N 123.8 0.1 1 713 376 158 PHE H H 7.23 0.01 1 714 376 158 PHE C C 181.3 0.1 1 715 376 158 PHE CA C 56.8 0.2 1 716 376 158 PHE CB C 39.8 0.2 1 717 376 158 PHE N N 115.3 0.1 1 718 377 159 ASN H H 8.22 0.01 1 719 377 159 ASN C C 177.4 0.1 1 720 377 159 ASN CA C 55.6 0.2 1 721 377 159 ASN CB C 39.3 0.2 1 722 377 159 ASN N N 119.1 0.1 1 723 378 160 PRO C C 175.6 0.1 1 724 378 160 PRO CA C 62.9 0.2 1 725 378 160 PRO CB C 31.6 0.2 1 726 379 161 ASP H H 7.80 0.01 1 727 379 161 ASP C C 176.6 0.1 1 728 379 161 ASP CA C 54.4 0.2 1 729 379 161 ASP CB C 40.7 0.2 1 730 379 161 ASP N N 119.2 0.1 1 731 380 162 SER H H 7.00 0.01 1 732 380 162 SER C C 174.0 0.1 1 733 380 162 SER CA C 59.6 0.2 1 734 380 162 SER CB C 62.6 0.2 1 735 380 162 SER N N 117.5 0.1 1 736 381 163 LYS H H 8.67 0.01 1 737 381 163 LYS C C 177.7 0.1 1 738 381 163 LYS CA C 57.1 0.2 1 739 381 163 LYS CB C 31.2 0.2 1 740 381 163 LYS N N 128.6 0.1 1 741 382 164 GLY H H 8.78 0.01 1 742 382 164 GLY C C 174.9 0.1 1 743 382 164 GLY CA C 44.5 0.2 1 744 382 164 GLY N N 110.9 0.1 1 745 383 165 LEU H H 6.75 0.01 1 746 383 165 LEU C C 178.2 0.1 1 747 383 165 LEU CA C 54.5 0.2 1 748 383 165 LEU CB C 42.1 0.2 1 749 383 165 LEU N N 119.7 0.1 1 750 384 166 SER H H 10.85 0.01 1 751 384 166 SER C C 176.4 0.1 1 752 384 166 SER CA C 60.9 0.2 1 753 384 166 SER CB C 62.3 0.2 1 754 384 166 SER N N 123.4 0.1 1 755 385 167 ASN H H 8.35 0.01 1 756 385 167 ASN C C 173.3 0.1 1 757 385 167 ASN CA C 50.5 0.2 1 758 385 167 ASN CB C 37.2 0.2 1 759 385 167 ASN N N 118.7 0.1 1 760 386 168 PRO C C 177.7 0.1 1 761 386 168 PRO CA C 65.3 0.2 1 762 386 168 PRO CB C 31.0 0.2 1 763 387 169 ALA H H 7.97 0.01 1 764 387 169 ALA C C 181.1 0.1 1 765 387 169 ALA CA C 54.7 0.2 1 766 387 169 ALA CB C 17.3 0.2 1 767 387 169 ALA N N 119.9 0.1 1 768 388 170 GLU H H 7.48 0.01 1 769 388 170 GLU C C 178.7 0.1 1 770 388 170 GLU CA C 58.1 0.2 1 771 388 170 GLU CB C 28.9 0.2 1 772 388 170 GLU N N 120.4 0.1 1 773 389 171 VAL H H 6.94 0.01 1 774 389 171 VAL C C 177.3 0.1 1 775 389 171 VAL CA C 66.5 0.2 1 776 389 171 VAL CB C 30.7 0.2 1 777 389 171 VAL N N 119.7 0.1 1 778 390 172 GLU H H 8.50 0.01 1 779 390 172 GLU C C 177.8 0.1 1 780 390 172 GLU CA C 59.3 0.2 1 781 390 172 GLU CB C 28.8 0.2 1 782 390 172 GLU N N 121.8 0.1 1 783 391 173 ALA H H 7.72 0.01 1 784 391 173 ALA C C 180.6 0.1 1 785 391 173 ALA CA C 54.4 0.2 1 786 391 173 ALA CB C 17.2 0.2 1 787 391 173 ALA N N 121.1 0.1 1 788 392 174 LEU H H 7.36 0.01 1 789 392 174 LEU C C 178.3 0.1 1 790 392 174 LEU CA C 57.4 0.2 1 791 392 174 LEU CB C 38.7 0.2 1 792 392 174 LEU N N 120.1 0.1 1 793 393 175 ARG H H 8.03 0.01 1 794 393 175 ARG C C 177.1 0.1 1 795 393 175 ARG CA C 60.1 0.2 1 796 393 175 ARG CB C 29.7 0.2 1 797 393 175 ARG N N 120.5 0.1 1 798 394 176 GLU H H 7.97 0.01 1 799 394 176 GLU C C 178.5 0.1 1 800 394 176 GLU CA C 57.6 0.2 1 801 394 176 GLU CB C 27.9 0.2 1 802 394 176 GLU N N 118.0 0.1 1 803 395 177 LYS H H 7.52 0.01 1 804 395 177 LYS C C 180.1 0.1 1 805 395 177 LYS CA C 58.9 0.2 1 806 395 177 LYS CB C 31.7 0.2 1 807 395 177 LYS N N 119.0 0.1 1 808 396 178 VAL H H 7.87 0.01 1 809 396 178 VAL C C 178.7 0.1 1 810 396 178 VAL CA C 66.5 0.2 1 811 396 178 VAL CB C 31.9 0.2 1 812 396 178 VAL N N 118.1 0.1 1 813 397 179 TYR H H 8.78 0.01 1 814 397 179 TYR C C 178.1 0.1 1 815 397 179 TYR CA C 60.2 0.2 1 816 397 179 TYR CB C 36.4 0.2 1 817 397 179 TYR N N 117.4 0.1 1 818 398 180 ALA H H 8.51 0.01 1 819 398 180 ALA C C 181.6 0.1 1 820 398 180 ALA CA C 55.0 0.2 1 821 398 180 ALA CB C 17.5 0.2 1 822 398 180 ALA N N 127.6 0.1 1 823 399 181 SER H H 7.82 0.01 1 824 399 181 SER C C 177.5 0.1 1 825 399 181 SER CA C 61.3 0.2 1 826 399 181 SER CB C 62.5 0.2 1 827 399 181 SER N N 118.1 0.1 1 828 400 182 LEU H H 9.05 0.01 1 829 400 182 LEU C C 176.9 0.1 1 830 400 182 LEU CA C 57.7 0.2 1 831 400 182 LEU CB C 41.0 0.2 1 832 400 182 LEU N N 124.8 0.1 1 833 401 183 GLU H H 8.43 0.01 1 834 401 183 GLU C C 178.1 0.1 1 835 401 183 GLU CA C 60.4 0.2 1 836 401 183 GLU CB C 27.2 0.2 1 837 401 183 GLU N N 121.1 0.1 1 838 402 184 ALA H H 7.39 0.01 1 839 402 184 ALA C C 180.4 0.1 1 840 402 184 ALA CA C 54.5 0.2 1 841 402 184 ALA CB C 17.2 0.2 1 842 402 184 ALA N N 119.1 0.1 1 843 403 185 TYR H H 8.15 0.01 1 844 403 185 TYR C C 177.6 0.1 1 845 403 185 TYR CA C 61.5 0.2 1 846 403 185 TYR CB C 37.8 0.2 1 847 403 185 TYR N N 121.1 0.1 1 848 404 186 CYS H H 9.22 0.01 1 849 404 186 CYS C C 178.4 0.1 1 850 404 186 CYS CA C 64.7 0.2 1 851 404 186 CYS CB C 26.6 0.2 1 852 404 186 CYS N N 119.6 0.1 1 853 405 187 LYS H H 8.24 0.01 1 854 405 187 LYS C C 177.4 0.1 1 855 405 187 LYS CA C 58.8 0.2 1 856 405 187 LYS CB C 31.4 0.2 1 857 405 187 LYS N N 119.7 0.1 1 858 406 188 HIS H H 7.52 0.01 1 859 406 188 HIS C C 176.9 0.1 1 860 406 188 HIS CA C 57.7 0.2 1 861 406 188 HIS CB C 30.3 0.2 1 862 406 188 HIS N N 117.1 0.1 1 863 407 189 LYS H H 8.33 0.01 1 864 407 189 LYS C C 176.1 0.1 1 865 407 189 LYS CA C 56.1 0.2 1 866 407 189 LYS CB C 31.7 0.2 1 867 407 189 LYS N N 119.7 0.1 1 868 408 190 TYR H H 7.70 0.01 1 869 408 190 TYR C C 174.4 0.1 1 870 408 190 TYR CA C 53.8 0.2 1 871 408 190 TYR CB C 37.4 0.2 1 872 408 190 TYR N N 115.7 0.1 1 873 409 191 PRO C C 178.4 0.1 1 874 409 191 PRO CA C 64.6 0.2 1 875 409 191 PRO CB C 30.7 0.2 1 876 410 192 GLU H H 9.30 0.01 1 877 410 192 GLU C C 175.4 0.1 1 878 410 192 GLU CA C 55.9 0.2 1 879 410 192 GLU CB C 27.5 0.2 1 880 410 192 GLU N N 118.6 0.1 1 881 411 193 GLN H H 7.79 0.01 1 882 411 193 GLN C C 173.8 0.1 1 883 411 193 GLN CA C 52.4 0.2 1 884 411 193 GLN CB C 29.6 0.2 1 885 411 193 GLN N N 120.3 0.1 1 886 413 195 GLY C C 174.3 0.1 1 887 413 195 GLY CA C 45.5 0.2 1 888 414 196 ARG H H 7.67 0.01 1 889 414 196 ARG C C 176.7 0.1 1 890 414 196 ARG CA C 60.0 0.2 1 891 414 196 ARG CB C 30.5 0.2 1 892 414 196 ARG N N 124.1 0.1 1 893 415 197 PHE H H 8.93 0.01 1 894 415 197 PHE C C 176.2 0.1 1 895 415 197 PHE CA C 60.0 0.2 1 896 415 197 PHE CB C 38.4 0.2 1 897 415 197 PHE N N 118.7 0.1 1 898 416 198 ALA H H 7.98 0.01 1 899 416 198 ALA C C 178.4 0.1 1 900 416 198 ALA CA C 54.5 0.2 1 901 416 198 ALA CB C 17.3 0.2 1 902 416 198 ALA N N 120.2 0.1 1 903 417 199 LYS H H 7.69 0.01 1 904 417 199 LYS C C 180.2 0.1 1 905 417 199 LYS CA C 59.8 0.2 1 906 417 199 LYS CB C 31.5 0.2 1 907 417 199 LYS N N 117.5 0.1 1 908 418 200 LEU H H 8.00 0.01 1 909 418 200 LEU C C 178.4 0.1 1 910 418 200 LEU CA C 57.8 0.2 1 911 418 200 LEU CB C 41.3 0.2 1 912 418 200 LEU N N 118.7 0.1 1 913 423 205 PRO C C 177.6 0.1 1 914 423 205 PRO CA C 66.4 0.2 1 915 424 206 ALA H H 7.23 0.01 1 916 424 206 ALA C C 178.9 0.1 1 917 424 206 ALA CA C 54.9 0.2 1 918 424 206 ALA CB C 17.6 0.2 1 919 424 206 ALA N N 120.5 0.1 1 920 425 207 LEU H H 7.75 0.01 1 921 425 207 LEU C C 177.6 0.1 1 922 425 207 LEU CA C 57.7 0.2 1 923 425 207 LEU CB C 42.1 0.2 1 924 425 207 LEU N N 118.5 0.1 1 925 426 208 ARG H H 7.84 0.01 1 926 426 208 ARG C C 178.1 0.1 1 927 426 208 ARG CA C 56.1 0.2 1 928 426 208 ARG CB C 26.7 0.2 1 929 426 208 ARG N N 119.0 0.1 1 930 427 209 SER H H 8.10 0.01 1 931 427 209 SER C C 175.9 0.1 1 932 427 209 SER CA C 61.1 0.2 1 933 427 209 SER CB C 61.8 0.2 1 934 427 209 SER N N 113.8 0.1 1 935 461 243 MET C C 175.6 0.1 1 936 461 243 MET CA C 55.1 0.2 1 937 461 243 MET CB C 32.2 0.2 1 938 462 244 THR H H 7.61 0.01 1 939 462 244 THR C C 179.1 0.1 1 940 462 244 THR CA C 62.6 0.2 1 941 462 244 THR CB C 70.2 0.2 1 942 462 244 THR N N 120.3 0.1 1 stop_ save_