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基本情報
登録情報 | データベース: PDB / ID: 1jwd | ||||||
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タイトル | Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin. | ||||||
![]() | Calcyclin | ||||||
![]() | METAL BINDING PROTEIN / Ca(2+)-binding protein / S100 protein / EF-hand / S100A6 | ||||||
機能・相同性 | ![]() S100 protein binding / cytoplasmic side of plasma membrane / calcium-dependent protein binding / nuclear envelope / collagen-containing extracellular matrix / calcium ion binding / perinuclear region of cytoplasm / extracellular space / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | 溶液NMR / distance geometry, restrained molecular dynamics | ||||||
![]() | Maler, L. / Sastry, M. / Chazin, W.J. | ||||||
![]() | ![]() タイトル: A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin 著者: Maler, L. / Sastry, M. / Chazin, W.J. #1: ![]() タイトル: High Resolution Solution Structure of Apo Calcyclin and Structural Variations in the S100 Family of Calcium-binding Proteins. 著者: Maler, L. / Potts, B.C.M. / Chazin, W.J. #2: ![]() タイトル: The Three-dimenisonal Structure of Ca(2+)-bound Calcyclin: Implications for Ca(2+)-signal Transduction by S100 Proteins. 著者: Sastry, M. / Ketchem, R.R. / Crescenzi, O. / Weber, C. / Lubienski, M.J. / Hidaka, H. / Chazin, W.J. #3: ![]() タイトル: The Structure of Calcyclin Reveals a Novel Homodimeric Fold for S100 Ca(2+)-binding Proteins. 著者: Potts, B.C. / Smith, J. / Akke, M. / Macke, T.J. / Okazaki, K. / Hidaka, H. / Chase, D.A. / Chazin, W.J. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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-検証レポート
文書・要旨 | ![]() | 370.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 607.6 KB | 表示 | |
XML形式データ | ![]() | 61.3 KB | 表示 | |
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-関連構造データ
関連構造データ | |
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リンク
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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 | 分子量: 10167.729 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
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-実験情報
-実験
実験 | 手法: 溶液NMR | ||||||||||||||||||||||||||||||||
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NMR実験 |
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NMR実験の詳細 | Text: Dimer constraints were obtained from the 3D_13C-filter,13C-edited experiment in combination with 3D_13C-separated_NOESY |
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試料調製
詳細 |
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試料状態 | イオン強度: 30 mM CaCl2 / pH: 7.0 / 圧: ambient / 温度: 300 K | ||||||||||||||||||
結晶化 | *PLUS 手法: other / 詳細: NMR |
-NMR測定
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M | ||||||||||||||||||||
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放射波長 | 相対比: 1 | ||||||||||||||||||||
NMRスペクトロメーター |
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解析
NMR software |
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精密化 | 手法: distance geometry, restrained molecular dynamics / ソフトェア番号: 1 詳細: The calculations were carried out using a total of 3104 distance and 294 torsion angle constraints. Starting structures were generated as monomers (one chain) with no intersubunit constraints ...詳細: The calculations were carried out using a total of 3104 distance and 294 torsion angle constraints. Starting structures were generated as monomers (one chain) with no intersubunit constraints using distance geometry followed by restrained molecular dynamics (rMD). The dimer structures were generated by rMD docking driven by the intersubunit NOEs using two arbitrarily selected starting subunit structures. Each dimer was further refined by rMD with all 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: The program Findfam was used to establish that the number of structures required to accurately represent the ensemble was less than 22 (the number selected to ...コンフォーマー選択の基準: The program Findfam was used to establish that the number of structures required to accurately represent the ensemble was less than 22 (the number selected to represent previous S100A6 ensembles). Structures were ordered by lowest restraint violations, then accepted if total molecular energy and each contributing term was within two standard deviations of the mean. The 22 structures with least restraint violations (energy penalty and magnitude of largest violation) all met these criteria. 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 22 |