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基本情報
登録情報 | データベース: PDB / ID: 2l56 | ||||||
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タイトル | NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations | ||||||
![]() | General control protein GCN4 | ||||||
![]() | TRANSCRIPTION / GCN4 / COILED-COIL / TRIGGER PEPTIDE / MOLECULAR DYNAMICS SIMULATIONS | ||||||
手法 | 溶液NMR / molecular dynamics | ||||||
Model details | occurrence frequencies, model 1 | ||||||
![]() | Missimer, J.H. / Dolenc, J. / Steinmetz, M.O. / van Gunsteren, W.F. | ||||||
![]() | ![]() タイトル: Molecular basis of coiled-coil formation 著者: Steinmetz, M.O. / Jelesarov, I. / Matousek, W.M. / Honnappa, S. / Jahnke, W. / Missimer, J.H. / Frank, S. / Alexandrescu, A.T. / Kammerer, R.A. | ||||||
履歴 |
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Remark 0 | THIS ENTRY 2L56 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA (2OVN.MR) ...THIS ENTRY 2L56 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA (2OVN.MR) DETERMINED BY AUTHORS OF THE PDB ENTRY 2OVN: M.O.STEINMETZ,I.JELESAROV,W.M.MATOUSEK,S.HONNAPPA,W.JAHNKE,J.H.MISSIMER,S.FRANK,A.T.ALEXANDRESCU,R.A.KAMMERER. HYDROGEN BOND DISTANCE RESTRAINTS IN 2OVN.MR WERE NOT USED IN THE NEW REFINEMENT PROCEDURE BECAUSE THEY ARE NOT BASED ON THE EXPERIMENTAL NMR DATA. |
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集合体
登録構造単位 | ![]()
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NMR アンサンブル |
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要素
#1: タンパク質・ペプチド | 分子量: 1911.232 Da / 分子数: 1 / 由来タイプ: 合成 / 詳細: FMOC synthesis |
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-実験情報
-実験
実験 | 手法: 溶液NMR |
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解析
NMR software | 名称: GROMOS / バージョン: 53A6 FORCE FIELD / 開発者: van Gunsteren and Berendsen / 分類: 精密化 |
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精密化 | 手法: molecular dynamics / ソフトェア番号: 1 詳細: molecular dynamics simulation with time-averaged NOE distance restraining and local elevation biased 3J-value restraining using 179 NOE distances and 15 3J-coupling constants; the 10 ...詳細: molecular dynamics simulation with time-averaged NOE distance restraining and local elevation biased 3J-value restraining using 179 NOE distances and 15 3J-coupling constants; the 10 deposited structures were selected from a set of 20000 trajectory configurations by conformational cluster analysis; the occurrence frequencies of the clusters that correspond to the deposited model structures are the following: cluster 1 32% cluster 2 14% cluster 3 6% cluster 4 6% cluster 5 6% cluster 6 3% cluster 7 3% cluster 8 2% cluster 9 2% cluster 10 2%. Authors state that The deviations of the deposited trajectory structures from the so-called "ideal" values for geometrical and stereochemical quantities are partially due to the biasing force derived from the NOE distance bounds and 3J-coupling constants, and partially due to the finite temperature (278K) of the simulations. The ideal geometric and stereochemical values of the GROMOS force field are close to those of Engh and Huber. |
代表構造 | 選択基準: occurrence frequencies |
NMRアンサンブル | コンフォーマー選択の基準: conformational cluster analysis 計算したコンフォーマーの数: 20000 / 登録したコンフォーマーの数: 10 / 代表コンフォーマー: 1 |