+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2bbm | ||||||
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タイトル | SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULTIDIMENSIONAL NMR | ||||||
要素 |
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キーワード | CALCIUM-BINDING PROTEIN | ||||||
機能・相同性 | 機能・相同性情報 negative regulation of phospholipase C-activating phototransduction signaling pathway / myosin VI complex / myosin VI head/neck binding / myosin VII complex / photoreceptor cell axon guidance / negative regulation of opsin-mediated signaling pathway / rhabdomere development / rhabdomere / regulation of muscle filament sliding / myosin-light-chain kinase ...negative regulation of phospholipase C-activating phototransduction signaling pathway / myosin VI complex / myosin VI head/neck binding / myosin VII complex / photoreceptor cell axon guidance / negative regulation of opsin-mediated signaling pathway / rhabdomere development / rhabdomere / regulation of muscle filament sliding / myosin-light-chain kinase / detection of chemical stimulus involved in sensory perception of smell / myosin light chain kinase activity / myosin V complex / kinetochore organization / autophagic cell death / myosin light chain binding / : / G protein-coupled opsin signaling pathway / actin filament-based movement / myosin V binding / cardiac muscle tissue morphogenesis / channel regulator activity / cellular response to ethanol / calcium/calmodulin-dependent protein kinase activity / muscle cell cellular homeostasis / mitotic spindle pole / myosin heavy chain binding / centriole replication / striated muscle contraction / enzyme regulator activity / centriole / sensory perception of sound / mitotic spindle / spindle / sensory perception of smell / cell cortex / midbody / calmodulin binding / phosphorylation / protein phosphorylation / centrosome / calcium ion binding / nucleoplasm / ATP binding / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | Drosophila melanogaster (キイロショウジョウバエ) | ||||||
手法 | 溶液NMR | ||||||
データ登録者 | Clore, G.M. / Bax, A. / Ikura, M. / Gronenborn, A.M. | ||||||
引用 | ジャーナル: Science / 年: 1992 タイトル: Solution structure of a calmodulin-target peptide complex by multidimensional NMR. 著者: Ikura, M. / Clore, G.M. / Gronenborn, A.M. / Zhu, G. / Klee, C.B. / Bax, A. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 2bbm.cif.gz | 73.2 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2bbm.ent.gz | 55.2 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2bbm.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 2bbm_validation.pdf.gz | 297.1 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 2bbm_full_validation.pdf.gz | 296.8 KB | 表示 | |
XML形式データ | 2bbm_validation.xml.gz | 5.8 KB | 表示 | |
CIF形式データ | 2bbm_validation.cif.gz | 7.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/bb/2bbm ftp://data.pdbj.org/pub/pdb/validation_reports/bb/2bbm | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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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: 16694.324 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Drosophila melanogaster (キイロショウジョウバエ) 器官: SKELETAL / 参照: UniProt: P62152 |
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#2: タンパク質・ペプチド | 分子量: 2972.538 Da / 分子数: 1 / 由来タイプ: 組換発現 / 参照: UniProt: P07313 |
#3: 化合物 | ChemComp-CA / |
-実験情報
-実験
実験 | 手法: 溶液NMR |
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-試料調製
結晶化 | *PLUS 手法: other / 詳細: NMR |
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-解析
精密化 | ソフトェア番号: 1 詳細: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM ...詳細: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES BETWEEN THE CALCULATED STRUCTURES). THE STRUCTURES ARE BASED ON 1827 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 148 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 74 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE CALCULATIONS; 24 RESTRAINTS FOR THE 4 CALCIUM IONS, AND 113 PHI TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING DATA, CONSTANTS, NOE AND 13C SECONDARY CHEMICAL SHIFTS. THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD [M.NILGES, G.M.CLORE, AND A.M.GRONENBORN, FEBS LETT. 229, 317-324 (1988)]. A TOTAL OF 21 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE PRESENTED IN THIS ENTRY. THIS WAS OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE COORDINATES OF THE 21 INDIVIDUAL SA STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK ENTRY 2BBN. THE LAST COLUMN IN THIS COORDINATE FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS. |
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NMRアンサンブル | 登録したコンフォーマーの数: 1 |