+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2l08 | ||||||
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タイトル | Solution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B | ||||||
要素 | Regulator of nonsense transcripts 3A | ||||||
キーワード | TRANSPORT PROTEIN (運搬体タンパク質) / NESG / Nonsense regulator / Structural Genomics (構造ゲノミクス) / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium | ||||||
機能・相同性 | 機能・相同性情報 negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of mRNA cis splicing, via spliceosome / exon-exon junction complex / telomeric DNA binding / mRNA transport / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / positive regulation of translation / Regulation of expression of SLITs and ROBOs / 精子形成 / in utero embryonic development ...negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of mRNA cis splicing, via spliceosome / exon-exon junction complex / telomeric DNA binding / mRNA transport / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / positive regulation of translation / Regulation of expression of SLITs and ROBOs / 精子形成 / in utero embryonic development / neuron projection / intracellular membrane-bounded organelle / mRNA binding / 核小体 / 核質 / 細胞核 / 細胞質基質 / 細胞質 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
データ登録者 | Mani, R. / Mao, L. / Ciccosanti, C. / Shastry, R. / Acton, T.B. / Xiao, R. / Swapna, G.V.T. / Everett, J.K. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
引用 | ジャーナル: To be Published タイトル: Solution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B 著者: Mani, R. / Mao, L. / Ciccosanti, C. / Shastry, R. / Acton, T.B. / Xiao, R. / Swapna, G.V.T. / Everett, J.K. / 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 | 2l08.cif.gz | 694.9 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2l08.ent.gz | 590.3 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2l08.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
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/l0/2l08 ftp://data.pdbj.org/pub/pdb/validation_reports/l0/2l08 | HTTPS FTP |
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-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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NMR アンサンブル |
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-要素
#1: タンパク質 | 分子量: 11596.175 Da / 分子数: 1 / 断片: sequence database residues 70-155 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: UPF3A, RENT3A, UPF3 / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): BL21(DE3)+ magic / 参照: UniProt: Q9H1J1 |
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-実験情報
-実験
実験 | 手法: 溶液NMR 詳細: HR4714B is a 97 residue protein consisiting of a 10 residue N-terminal tag. N-HSQC spectrum shows only 71 peaks out of the 87 peaks (excluding tag) that are expected. The line broeadening of ...詳細: HR4714B is a 97 residue protein consisiting of a 10 residue N-terminal tag. N-HSQC spectrum shows only 71 peaks out of the 87 peaks (excluding tag) that are expected. The line broeadening of the peaks occur from residue D45 to S54. Also, M11, R16, S81 NH's are missing from N-HSQC spectrum. The reason for line broadening is not known. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR実験 |
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NMR実験の詳細 | Text: The Structure was obtained using triple resonance NMR spectroscopy for backbone and side chain assignments. Automated NOESY assignments were made using Autostructure and CYANA3.0. Dihedral ...Text: The Structure was obtained using triple resonance NMR spectroscopy for backbone and side chain assignments. Automated NOESY assignments were made using Autostructure and CYANA3.0. Dihedral angle constraints were obtained using TALOS. The structure calculation was done excluding the 10-residue N-terminal tag. Completeness of assignment excluding the tag: Backbone - 80%, Sidechain - 80%. Peaks for 13 residues in NHSQC spectra are missing due to line broadening. |
-試料調製
詳細 |
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試料 |
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試料状態 | イオン強度: 100mM NaCl, 10mM Tris-HCl / pH: 7.5 / 圧: ambient / 温度: 298 K |
-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: simulated annealing / ソフトェア番号: 1 詳細: Final structure quality (excluding 10 residue tag) determined using PSVS-v1.4: Ordered residues are defines as: 10-19,22-34,36-45,54-72,76-94. (a) RMSD (ordered residues) all backbone aroms: ...詳細: Final structure quality (excluding 10 residue tag) determined using PSVS-v1.4: Ordered residues are defines as: 10-19,22-34,36-45,54-72,76-94. (a) RMSD (ordered residues) all backbone aroms: 0.6A. and heavy atoms 1.0A. (b) Ramachandran statistics for ordered residues: Most favored region: 85.1% Additionally favored region: 14.8% Generaously allowed region: 0.1% Disallowed region: 0.1%. (c) Procheck scores for ordered residues (RAW/Z): Phi/psi -0.73/-2.56, all -0.65/-3.84, (d) Molprobity clashscores (RAW/Z)22.41/-2.32 (e) RPF scores for the goodness fit to NOESY data: Recall: 89, Precision: 94, F-measure: 92, final dp-score - (f) RMS deviation for bond angles - 6.15, RMS deviation for bond lengths 0.01A. | ||||||||||||||||||||
NMR constraints | NOE constraints total: 1729 / NOE intraresidue total count: 281 / NOE long range total count: 333 / NOE medium range total count: 536 / NOE sequential total count: 471 / Protein phi angle constraints total count: 108 / Protein psi angle constraints total count: 108 | ||||||||||||||||||||
代表構造 | 選択基準: lowest energy | ||||||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 200 / 登録したコンフォーマーの数: 20 / Maximum lower distance constraint violation: 0.25 Å / Maximum torsion angle constraint violation: 8.5 ° / Maximum upper distance constraint violation: 1.7 Å | ||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.01 Å |