#1: ジャーナル: J.Mol.Biol. / 年: 2004 タイトル: Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions. 著者: Li, H. / Byeon, I.-J.L. / Ju, Y. / Tsai, M.-D.
MKI67FHAdomaininteractingnucleolarphosphoprotein / Nucleolar protein interacting with the FHA domain of pKI-67 / hNIFK / Nucleolar phosphoprotein Nopp34
Text: The structure was determined using triple-resonance NMR spectroscopy
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試料調製
詳細
Solution-ID
内容
溶媒系
1
0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
93% H2O/7% D2O
2
0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
100% D2O
3
1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
93% H2O/7% D2O
4
1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4
100% D2O
試料状態
イオン強度: 150 mM NaCl / pH: 7.4 / 圧: ambient / 温度: 293 K
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NMR測定
NMRスペクトロメーター
タイプ
製造業者
モデル
磁場強度 (MHz)
Spectrometer-ID
Bruker AVANCE
Bruker
AVANCE
800
1
Bruker DMX
Bruker
DMX
750
2
Bruker AVANCE
Bruker
AVANCE
600
3
Bruker DMX
Bruker
DMX
500
4
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解析
NMR software
名称
バージョン
開発者
分類
X-PLOR
NIHversion
Brunger
構造決定
X-PLOR
NIHversion
Brunger
精密化
精密化
手法: simulated annealing / ソフトェア番号: 1 詳細: the structures are based on a total of 3476 constraints, 3141 are distance, 215 dihedral angle, and 120 N-H residual dipolar coupling constraints
代表構造
選択基準: closest to the average
NMRアンサンブル
コンフォーマー選択の基準: structures with the least restraint violations,structures with the lowest energy 計算したコンフォーマーの数: 512 / 登録したコンフォーマーの数: 100