+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 1qtg | ||||||
---|---|---|---|---|---|---|---|
タイトル | AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR | ||||||
![]() | Transcriptional repressor arc | ||||||
![]() | GENE REGULATION / BETA-SHEET / RIGHT-HANDED HELIX / STRUCTURAL CHANGE | ||||||
機能・相同性 | ![]() | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
![]() | Cordes, M.H.J. / Walsh, N.P. / McKnight, C.J. / Sauer, R.T. | ||||||
![]() | ![]() タイトル: Evolution of a protein fold in vitro. 著者: Cordes, M.H. / Walsh, N.P. / McKnight, C.J. / Sauer, R.T. | ||||||
履歴 |
|
-
構造の表示
構造ビューア | 分子: ![]() ![]() |
---|
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 48.6 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 36.7 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
---|
-関連構造データ
関連構造データ | |
---|---|
類似構造データ |
-
リンク
-
集合体
登録構造単位 | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR アンサンブル |
|
-
要素
#1: タンパク質 | 分子量: 6238.272 Da / 分子数: 2 / 変異: N11L, L12N / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
---|
-実験情報
-実験
実験 | 手法: 溶液NMR |
---|
-
試料調製
結晶化 | *PLUS 手法: other / 詳細: NMR |
---|
-NMR測定
放射波長 | 相対比: 1 |
---|
-
解析
精密化 | 手法: simulated annealing / ソフトェア番号: 1 詳細: GENERATION OF THIS MODEL OF THE SWITCH ARC MUTANT INVOLVED A COMBINATION OF EXPERIMENTAL AND SIMU LATED DISTANCE RESTRAINTS. FOR RESIDUES 7-14, 81 NOE CROSSPEAKS WERE OBTAINED FROM A 50-MS 2D ...詳細: GENERATION OF THIS MODEL OF THE SWITCH ARC MUTANT INVOLVED A COMBINATION OF EXPERIMENTAL AND SIMU LATED DISTANCE RESTRAINTS. FOR RESIDUES 7-14, 81 NOE CROSSPEAKS WERE OBTAINED FROM A 50-MS 2D NOES Y SPECTRUM AND WERE TRANSLATED INTO STRONG (1.8-2.8 A), MEDIUM (1.8-3.3 A), MEDIUM-WEAK (1.8-3.8 A ) AND WEAK (1.8-4.3 A) DISTANCE RESTRAINTS.18 ADDITIONAL CROSSPEAKS WERE OBTAINED FROM A 150-MS 3D NOESY SPECTRUM AND WERE ASSIGNED LOOSER RESTRAINTS (1.8 TO 4.0 A OR 1.8 TO 6.0 A)BECAUSE OF THE L ONGER MIXING TIME USED IN THIS EXPERIMENT. TO SIMULATE THE STRUCTURE OF RESIDUES 14 TO 53 (RESIDUE 14 WAS DESCRIBED BY BOTH ACTUAL AND COMPUTED RESTRAINTS), A LIST OF 1635 DISTANCES WAS GENERATED BETWEEN PAIRS OF HEAVY ATOMS WITHIN 4 A OF EACH OTHER IN THE WILD-TYPE ARC CRYSTAL STRUCTURE, AND THE INTERATOMIC DISTANCES WERE CONSTRAINED TO BE WITHIN + OR - 1.0 A OF THIS VALUE. 28 INITIAL STR UCTURES WITH RANDOM CONFIGURATIONS FOR RESIDUES 1 TO 13 WERE GENERATED BY PERFORMING A SET OF CALC ULATIONS WITH ONLY THE SIMULATED RESTRAINTS FOR RESIDUES 14 TO 53. THEN, 28 MODEL STRUCTURES WERE GENERATED BY INCLUDING THE EXPERIMENTAL RESTRAINTS FOR RESIDUES 7 TO 14. NO RESTRAINTS WERE USED F OR RESIDUES 1 TO 6, WHICH APPEAR TO BE DISORDERED. AMBIGUITIES IN INTRA- AND INTERMOLECULAR NOE AS SIGNMENT RESULTING FROM ARC'S TWOFOLD SYMMETRY WERE RESOLVED COMPUTATIONALLY AS DESCRIBED (M. NILG ES, PROTEIN STRUCT. FUNCT. GENET. 17, 297 (1993).19 OF 28 STRUCTURES WERE ACCEPTED WITH NO NOE VIO LATIONS GREATER THAN 0.3 A. THE FIVE STRUCTURES WITH THE HIGHEST ENERGY, WHICH ALSO CONTAINED BACK BONE DIHEDRAL ANGLES IN DISALLOWED REGIONS OF RAMACHANDRAN SPACE, WERE DISCARDED. THE REMAINING 14 STRUCTURES, WHICH HAD PAIRWISE RMSD'S OF 0.6 A (BACKBONE) AND 1.6 A (HEAVY), WERE USED TO GENERAT E A MINIMIZED AVERAGE MODEL. |
---|---|
NMRアンサンブル | 登録したコンフォーマーの数: 1 |