+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2nef | |||||||||
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タイトル | HIV-1 NEF (REGULATORY FACTOR), NMR, 40 STRUCTURES | |||||||||
要素 | NEGATIVE FACTOR (F-PROTEIN) | |||||||||
キーワード | REGULATORY FACTOR / AIDS / MYRISTYLATION / GTP-BINDING | |||||||||
機能・相同性 | 機能・相同性情報 symbiont-mediated suppression of host T-cell mediated immune response / symbiont-mediated suppression of host adaptive immune response / negative regulation of CD4 production / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / virion component => GO:0044423 / suppression by virus of host autophagy / CD4 receptor binding / thioesterase binding / host cell Golgi membrane ...symbiont-mediated suppression of host T-cell mediated immune response / symbiont-mediated suppression of host adaptive immune response / negative regulation of CD4 production / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / virion component => GO:0044423 / suppression by virus of host autophagy / CD4 receptor binding / thioesterase binding / host cell Golgi membrane / MHC class I protein binding / : / regulation of calcium-mediated signaling / viral life cycle / SH3 domain binding / ATPase binding / signaling receptor binding / GTP binding / protein kinase binding / host cell plasma membrane / extracellular region / membrane 類似検索 - 分子機能 | |||||||||
生物種 | Human immunodeficiency virus type 1 (ヒト免疫不全ウイルス) | |||||||||
手法 | 溶液NMR | |||||||||
データ登録者 | Grzesiek, S. / Bax, A. / Clore, G.M. / Gronenborn, A.M. / Hu, J.S. / Kaufman, J. / Palmer, I. / Stahl, S.J. / Tjandra, N. / Wingfield, P.T. | |||||||||
引用 | ジャーナル: Protein Sci. / 年: 1997 タイトル: Refined solution structure and backbone dynamics of HIV-1 Nef. 著者: Grzesiek, S. / Bax, A. / Hu, J.S. / Kaufman, J. / Palmer, I. / Stahl, S.J. / Tjandra, N. / Wingfield, P.T. #1: ジャーナル: Nat.Struct.Biol. / 年: 1996 タイトル: The Solution Structure of HIV-1 Nef Reveals an Unexpected Fold and Permits Delineation of the Binding Surface for the SH3 Domain of HCK Tyrosine Protein Kinase 著者: Grzesiek, S. / Bax, A. / Clore, G.M. / Gronenborn, A.M. / Hu, J.S. / Kaufman, J. / Palmer, I. / Stahl, S.J. / Wingfield, P.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 | 2nef.cif.gz | 1.9 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2nef.ent.gz | 1.6 MB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2nef.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 | 2nef_validation.pdf.gz | 346.2 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 2nef_full_validation.pdf.gz | 680.5 KB | 表示 | |
XML形式データ | 2nef_validation.xml.gz | 124.1 KB | 表示 | |
CIF形式データ | 2nef_validation.cif.gz | 159.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ne/2nef ftp://data.pdbj.org/pub/pdb/validation_reports/ne/2nef | 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: 16148.163 Da / 分子数: 1 / 変異: DEL(2-39), DEL(159-173), C206A / 由来タイプ: 組換発現 由来: (組換発現) Human immunodeficiency virus type 1 (ヒト免疫不全ウイルス) 属: Lentivirus / 生物種: Human immunodeficiency virus 1 / 株: BH10 / 遺伝子: HIV-1 NEF / プラスミド: PET11A / 遺伝子 (発現宿主): HIV-1 NEF / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): DE3 / 参照: UniProt: Q70627 |
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配列の詳細 | THE MATERIAL USED WAS A DELETION MUTANT: DELTA 2 - 39 AND DELTA 159 - 173, WHICH REMOVES THE ...THE MATERIAL USED WAS A DELETION MUTANT: DELTA 2 - 39 AND DELTA 159 - 173, WHICH REMOVES THE DISORDERED |
-実験情報
-実験
実験 | 手法: 溶液NMR |
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NMR実験の詳細 | Text: THE 3D STRUCTURE OF THE HIV-1 NEF (DELTA2 - 39, DELTA 159 - 173) SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON 1250 EXPERIMENTAL RESTRAINTS: 338 SEQUENTIAL (|I- ...Text: THE 3D STRUCTURE OF THE HIV-1 NEF (DELTA2 - 39, DELTA 159 - 173) SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON 1250 EXPERIMENTAL RESTRAINTS: 338 SEQUENTIAL (|I-J|=1), 101 MEDIUM RANGE (1 < |I-J| <=5) AND 245 LONG RANGE (|I-J| >5) INTERRESIDUES AND 70 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 64 DISTANCE RESTRAINTS FOR 32 HYDROGEN BONDS; 157 TORSION ANGLE (78 PHI, 10 PSI, 55 CHI1 AND 14 CHI2) RESTRAINTS; 91 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 184 (93 CALPHA AND 91 CBETA) 13C SHIFT RESTRAINTS. |
-試料調製
結晶化 | *PLUS 手法: other / 詳細: NMR |
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-解析
ソフトウェア |
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NMR software | 名称: X-PLOR / バージョン: 3.1 / 開発者: BRUNGER / 分類: 精密化 | ||||||||||||
精密化 | ソフトェア番号: 1 詳細: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING ...詳細: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99 - 103) AND CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92 - 96) RESTRAINTS. THE COORDINATES OF THE 40 FINAL SIMULATED ANNEALING STRUCTURES ARE PRESENTED IN THIS ENTRY. THE B FACTOR FIELD PRESENTS THE AVERAGE RMS OF THE 40 INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS OBTAINED BY BEST FITTING RESIDUES 76 - 94, 97 - 102, 106 -147, 181 - 191, AND 194 -199. THESE RESIDUES CORRESPOND TO THE NON-MOBILE CORE OF THE PROTEIN AS EVIDENCED BY 15N RELAXATION DATA. | ||||||||||||
NMRアンサンブル | 登録したコンフォーマーの数: 40 |