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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 1h8b | ||||||
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タイトル | EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin | ||||||
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機能・相同性 | ![]() actin filament uncapping / FATZ binding / titin Z domain binding / phospholipase C-activating angiotensin-activated signaling pathway / positive regulation of endocytic recycling / positive regulation of potassium ion transmembrane transporter activity / negative regulation of potassium ion transmembrane transporter activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() ![]() ![]() ![]() | ||||||
手法 | ![]() | ||||||
![]() | Atkinson, R.A. / Joseph, C. / Kelly, G. / Muskett, F.W. / Frenkiel, T.A. / Nietlispach, D. / Pastore, A. | ||||||
![]() | ![]() タイトル: Ca2+-Independent Binding of an EF-Hand Domain to a Novel Motif in the Alpha-Actinin-Titin Complex 著者: Atkinson, R.A. / Joseph, C. / Kelly, G. / Muskett, F.W. / Frenkiel, T.A. / Nietlispach, D. / Pastore, A. #1: ジャーナル: Biochemistry / 年: 2000 タイトル: The Binding of Alpha-Actinin to Titin: Implications for Z-Disk Assembly 著者: Atkinson, R.A. / Joseph, C. / Piaz, F.D. / Birolo, L. / Stier, G. / Pucci, P. / Pastore, A. | ||||||
履歴 |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 845.8 KB | 表示 | ![]() |
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PDB形式 | ![]() | 713.1 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 |
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-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: 8077.011 Da / 分子数: 1 / 断片: EF-HANDS 3&4 RESIDUE 822-894 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: タンパク質 | ![]() 分子量: 5667.321 Da / 分子数: 1 / 断片: Z-REPEAT 7 RESIDUES 648-698 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
構成要素の詳細 | CHAIN A ENGINEERED MUTATION THR822MET, MODIFIED FOR EXPRESSION F-ACTIN CROSS-LINKING PROTEIN IS ...CHAIN A ENGINEERED |
-実験情報
-実験
実験 | 手法: ![]() |
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NMR実験 | タイプ![]() |
NMR実験の詳細 | Text: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ...Text: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ONLY ONE OF THE TWO COMPONENTS WAS LABELLED |
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試料調製
詳細 | 内容: 0.7 MM COMPLEX |
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試料状態 | イオン強度: 20 mM / pH: 6.6 / 圧: 1 atm / 温度: 300 K |
結晶化![]() | *PLUS 手法: その他 / 詳細: NMR |
-NMR測定
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: TORSION ANGLE DYNAMICS, CARTESIAN DYANMICS / ソフトェア番号: 1 詳細: REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. ...詳細: REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THESE TWO RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF TITIN ZR7 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THE N-TERMINAL 8 RESIDUES AND THE C-TERMINAL 22 RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. | ||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: LOWEST ENERGIES / 計算したコンフォーマーの数: 50 / 登録したコンフォーマーの数: 30 |