+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1pul | ||||||
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タイトル | Solution structure for the 21KDa caenorhabditis elegans protein CE32E8.3. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET WR33 | ||||||
要素 | Hypothetical protein C32E8.3 in chromosome I | ||||||
キーワード | structural genomics / unknown function / ALPHA HELICAL / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / PSI / Protein Structure Initiative / NESG | ||||||
機能・相同性 | P25-alpha / p25-alpha / positive regulation of protein polymerization / EF-hand / Recoverin; domain 1 / EF-hand domain pair / Orthogonal Bundle / Mainly Alpha / Tubulin polymerization-promoting protein homolog 機能・相同性情報 | ||||||
生物種 | Caenorhabditis elegans (センチュウ) | ||||||
手法 | 溶液NMR / torsion angle dynamics | ||||||
データ登録者 | Tejero, R. / Aramini, J.M. / Swapna, G.V.T. / Monleon, D. / Chiang, Y. / Macapagal, D. / Gunsalus, K.C. / Kim, S. / Szyperski, T. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
引用 | ジャーナル: J.Biomol.Nmr / 年: 2004 タイトル: Backbone 1H, 15N and 13C assignments for the 21 kDa Caenorhabditis elegans homologue of "brain-specific" protein. 著者: Monleon, D. / Chiang, Y. / Aramini, J.M. / Swapna, G.V. / Macapagal, D. / Gunsalus, K.C. / Kim, S. / Szyperski, T. / Montelione, G.T. | ||||||
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 | 1pul.cif.gz | 323.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1pul.ent.gz | 266.9 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1pul.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 | 1pul_validation.pdf.gz | 345.1 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1pul_full_validation.pdf.gz | 425.2 KB | 表示 | |
XML形式データ | 1pul_validation.xml.gz | 19 KB | 表示 | |
CIF形式データ | 1pul_validation.cif.gz | 30.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/pu/1pul ftp://data.pdbj.org/pub/pdb/validation_reports/pu/1pul | HTTPS FTP |
-関連構造データ
類似構造データ | |
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その他のデータベース |
-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: 13747.630 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Caenorhabditis elegans (センチュウ) 遺伝子: C32E8.3 / Plasmid details: derivative of pET15b / プラスミド: pET15b-WR33 / 生物種 (発現宿主): Escherichia coli / 発現宿主: Escherichia coli BL21(DE3) (大腸菌) / 株 (発現宿主): BL21(DE3) / 参照: UniProt: P91127 |
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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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. AUTOMATIC BACKBONE ASSIGNMENTS WERE MADE USING AUTOASSIGN. MANUAL SIDE CHAIN ASSIGNMENTS. AUTOMATIC NOESY ASSIGNMENTS AS ...Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. AUTOMATIC BACKBONE ASSIGNMENTS WERE MADE USING AUTOASSIGN. MANUAL SIDE CHAIN ASSIGNMENTS. AUTOMATIC NOESY ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN BOND CONSTRAINTS WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL ANGLE CONSTRAINTS WERE DETERMINED USING HYPER AND TALOS. FINAL STRUCTURE QUALITY FACTORS FOR THE ENSEMBLE (RESIDUES 18 to 120), WHERE ORDERED RESIDUES [S(PHI) + S(PSI) > 1.8] COMPRISE 19-33,42-56,61-62,64-74,77-79,83-119: (A) RMSD FOR ORDERED RESIDUES: BB, 1.2; HEAVY ATOM, 1.7 (B) RAMACHANDRAN STATISTICS FOR ORDERED RESIDUES: MOST FAVORED: 93.0%; ADDITIONALLY ALLOWED: 5.7%; GENEROUSLY ALLOWED, 0.8%; DISALLOWED, 0.5% (C) PROCHECK SCORES FOR ORDERED RESIDUES (RAW/Z-): BB, 0.20/1.10; ALL, -0.02/-0.12. (D) MAGE MOLPROBITY CLASH SCORE (RAW/Z-): 33.54/-4.23. (E) RPF SCORES FOR GOODNESS OF FIT TO NOESY DATA: F-MEASURE, 0.834; RECALL, 0.900; PRECISION, 0.776; DP-SCORE, 0.606. |
-試料調製
詳細 | 内容: 1mM WR33 U-15N,13C; 20mM NaH2PO4, 50mM NaCl, 10mM DTT, 0.02% azide 溶媒系: 95% H20, 5% D2O, PH 6.5 |
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試料状態 | イオン強度: 50 mM NaCl / pH: 6.5 / 圧: ambient / 温度: 293 K |
-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: torsion angle dynamics / ソフトェア番号: 1 詳細: THE STRUCTURES ARE BASED ON A TOTAL 729 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE CONSTRAINTS, 260 DIHEDRAL ANGLE CONSTRAINTS, AND 50 HYDROGEN BOND CONSTRAINTS (9.3 CONSTRAINTS PER ...詳細: THE STRUCTURES ARE BASED ON A TOTAL 729 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE CONSTRAINTS, 260 DIHEDRAL ANGLE CONSTRAINTS, AND 50 HYDROGEN BOND CONSTRAINTS (9.3 CONSTRAINTS PER RESIDUE; 1.2 LONG-RANGE CONSTRAINTS PER RESIDUE). STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING AUTOSTRUCTURE (DYANA). THE 10 STRUCTURES WITH THE LOWEST TARGET FUNCTION WERE FURTHER REFINED BY RESTRAINED MOLECULAR DYNAMICS/ENERGY MINIMIZATION IN EXPLICIT WATER (CNS). THE UNSTRUCTURED N- (1 to 17) AND C- (121 to 125) TERMINAL REGIONS OF THE MOLECULE ARE OMITTED FROM THIS DEPOSITION. | ||||||||||||||||||||||||||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: target function / 計算したコンフォーマーの数: 56 / 登録したコンフォーマーの数: 10 |