The protein is a dimer and the coordinates provided are for two sets of dimers, each representing an alternative protein conformation. Each model has 4 chains A,B,C and D. Chains A and B form one dimer in WT conformation, chains C and D form a second dimer in the distorted conformation
タイプ: solution 内容: 0.5 mM [U-100% 13C; U-100% 15N] Tryptohan aporepressor, 10 mM Tris-HCl buffer pH 5.7, 100 mM NaCl, 5 mM DTT, 0.02 % sodium azide, 90% H2O/10% D2O 詳細: 10 mM Tris-HCl buffer pH 5.7, 100 mM NaCl, 5 mM DTT and 0.02 % NaN3 Label: apoTrpR / 溶媒系: 90% H2O/10% D2O
試料
濃度 (mg/ml)
構成要素
Isotopic labeling
Solution-ID
0.5mM
Tryptohanaporepressor
[U-100% 13C; U-100% 15N]
1
10mM
Tris-HCl buffer pH 5.7
naturalabundance
1
100mM
NaCl
naturalabundance
1
5mM
DTT
naturalabundance
1
0.02 %
sodiumazide
naturalabundance
1
試料状態
イオン強度: 100 mM / Label: [U-100% 13C; U-100% 15N] / pH: 5.7 / 圧: 1 atm / 温度: 313 K
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NMR測定
NMRスペクトロメーター
タイプ: Bruker AVANCE / 製造業者: Bruker / モデル: AVANCE / 磁場強度: 800 MHz / 詳細: Equipped with a 5mm cryoprobe
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解析
NMR software
名称
バージョン
開発者
分類
AutoAssign
2.1.1
Zimmerman, Moseley, KulikowskiandMontelione
chemicalshiftassignment
TopSpin
2.3
BrukerBiospin
collection
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
解析
Sparky
3
Goddard
peakpicking
GROMACS
4.6.5
BerendsenH, vanderSpoelD, vanDrunenR.
structurecalculation
GROMACS
4.6.5
BerendsenH, vanderSpoelD, vanDrunenR.
精密化
精密化
手法: molecular dynamics / ソフトェア番号: 5 詳細: The coordinates provided are for two sets of models, each representing an alternative protein conformation that differ particularly in the segment of the protein sequence corresponding to helix E.
代表構造
選択基準: fewest violations
NMRアンサンブル
コンフォーマー選択の基準: all calculated structures submitted 計算したコンフォーマーの数: 15 / 登録したコンフォーマーの数: 15