+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1ncp | ||||||
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タイトル | STRUCTURAL CHARACTERIZATION OF A 39 RESIDUE SYNTHETIC PEPTIDE CONTAINING THE TWO ZINC BINDING DOMAINS FROM THE HIV-1 P7 NUCLEOCAPSID PROTEIN BY CD AND NMR SPECTROSCOPY | ||||||
要素 | (HIV-1 P7 NUCLEOCAPSID PROTEIN) x 2 | ||||||
キーワード | VIRAL PROTEIN / NUCLEOCAPSID PROTEIN | ||||||
機能・相同性 | 機能・相同性情報 integrase activity / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Minus-strand DNA synthesis / Plus-strand DNA synthesis / 2-LTR circle formation / Uncoating of the HIV Virion / Early Phase of HIV Life Cycle / Vpr-mediated nuclear import of PICs / Integration of provirus ...integrase activity / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Minus-strand DNA synthesis / Plus-strand DNA synthesis / 2-LTR circle formation / Uncoating of the HIV Virion / Early Phase of HIV Life Cycle / Vpr-mediated nuclear import of PICs / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / Binding and entry of HIV virion / viral life cycle / HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / Assembly Of The HIV Virion / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / Budding and maturation of HIV virion / host multivesicular body / protein processing / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / symbiont-mediated suppression of host gene expression / viral penetration into host nucleus / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / 転移酵素; リンを含む基を移すもの; 核酸を移すもの / host cell / peptidase activity / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / 加水分解酵素; エステル加水分解酵素 / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / viral translational frameshifting / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / DNA binding / zinc ion binding / identical protein binding / membrane 類似検索 - 分子機能 | ||||||
生物種 | Human immunodeficiency virus 1 (ヒト免疫不全ウイルス) | ||||||
手法 | 溶液NMR | ||||||
データ登録者 | Clore, G.M. / Omichinski, J.G. / Gronenborn, A.M. | ||||||
引用 | ジャーナル: FEBS Lett. / 年: 1991 タイトル: Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy. 著者: Omichinski, J.G. / Clore, G.M. / Sakaguchi, K. / Appella, E. / Gronenborn, A.M. | ||||||
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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 | 1ncp.cif.gz | 29.8 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1ncp.ent.gz | 13.3 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1ncp.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 | 1ncp_validation.pdf.gz | 347.2 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1ncp_full_validation.pdf.gz | 349.5 KB | 表示 | |
XML形式データ | 1ncp_validation.xml.gz | 2.8 KB | 表示 | |
CIF形式データ | 1ncp_validation.cif.gz | 3.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/nc/1ncp ftp://data.pdbj.org/pub/pdb/validation_reports/nc/1ncp | 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・ペプチド | 分子量: 1928.247 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Human immunodeficiency virus 1 (ヒト免疫不全ウイルス) 属: Lentivirus / 参照: UniProt: P04585 |
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#2: タンパク質・ペプチド | 分子量: 2073.419 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Human immunodeficiency virus 1 (ヒト免疫不全ウイルス) 属: Lentivirus / 参照: UniProt: P24740 |
#3: 化合物 |
-実験情報
-実験
実験 | 手法: 溶液NMR |
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-解析
精密化 | ソフトェア番号: 1 詳細: THIS ENTRY CONTAINS SOLUTION NMR STRUCTURE OF A 39 RESIDUE SYNTHETIC PEPTIDE CONTAINING THE TWO ZINC BINDING DOMAINS FROM THE HIV-1 P7 NUCLEOCAPSID PROTEIN. THE TWO DOMAINS ARE COMPLETELY ...詳細: THIS ENTRY CONTAINS SOLUTION NMR STRUCTURE OF A 39 RESIDUE SYNTHETIC PEPTIDE CONTAINING THE TWO ZINC BINDING DOMAINS FROM THE HIV-1 P7 NUCLEOCAPSID PROTEIN. THE TWO DOMAINS ARE COMPLETELY INDEPENDENT AND WERE SOLVED SEPARATELY. THE FIRST DOMAIN (CHAIN *N*, RESIDUES 1 - 17) WAS BASED ON 147 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS. THE SECOND DOMAIN (CHAIN *C*, RESIDUES 22 - 39) WAS BASED ON 148 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS. THE LINKER REGION IS HIGHLY FLEXIBLE AND CANNOT BE DEFINED FROM THE NMR DATA. THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD (NILGES, CLORE, AND GRONENBORN, FEBS LETT. 229, 317 (1988)). A TOTAL OF 15 SIMULATED ANNEALING STRUCTURES WAS CALCULATED FOR EACH DOMAIN. THE COORDINATES OF THE DOMAINS WERE THEN AVERAGED AND SUBJECTED TO RESTRAINED REGULARIZATION TO YIELD THE RESTRAINED MINIMIZED STRUCTURES. ONLY THESE COORDINATES ARE LISTED. THE FIRST CHAIN IS THE N-TERMINAL DOMAIN, AND THE SECOND IS THE C-TERMINAL DOMAIN. THE FIELD PRESENTED IN COLUMNS 61 - 66 IN THIS COORDINATE FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS FOR EACH DOMAIN. THE COORDINATES OF THE TWO DOMAINS HAVE BEEN BEST FITTED TO EACH OTHER. |
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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 |