+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1.0E+76 | ||||||
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タイトル | NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT D5N | ||||||
要素 | ALPHA-CONOTOXIN IM1(D5N) | ||||||
キーワード | PEPTIDE TOXIN / NEUROTOXIN (神経毒) / NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR ANTAGONIST / ALPHA-CONOTOXIN / NMR SOLUTION STRUCTURE | ||||||
機能・相同性 | Conotoxin, alpha-type, conserved site / Alpha-conotoxin family signature. / host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / ion channel regulator activity / toxin activity / extracellular region / Alpha-conotoxin ImI 機能・相同性情報 | ||||||
生物種 | CONUS IMPERIALIS (ミカドミナシ) | ||||||
手法 | 溶液NMR / TORSION ANGLE DYNAMICS, RESTRAINED ENERGY MINIMISATION | ||||||
データ登録者 | Rogers, J.P. / Luginbuhl, P. / Pemberton, K. / Harty, P. / Wemmer, D.E. / Stevens, R.C. | ||||||
引用 | ジャーナル: J.Mol.Biol. / 年: 2000 タイトル: Structure-Activity Relationships in a Peptidic Alpha7 Nicotinic Acetylcholine Receptor Antagonist 著者: Rogers, J.P. / Luginbuhl, P. / Pemberton, K. / Harty, P. / Wemmer, D.E. / Stevens, R.C. #1: ジャーナル: Biochemistry / 年: 1999 タイトル: NMR Solution Structure of Alpha-Conotoxin Imi and Comparison to Other Conotoxins Specific for Neuronal Nicotinic Acetylcholine Receptors 著者: Rogers, J.P. / Luginbuhl, P. / Shen, G.S. / Mccabe, R.T. / Stevens, R.C. / Wemmer, D.E. #2: ジャーナル: Mol.Pharmacol. / 年: 1995 タイトル: Alpha-Conotoxin Imi Exhibits Subtype-Specific Nicotinic Acetylcholine Receptor Blockade: Preferential Inhibition of Homomeric Alpha7 and Alpha9 Receptors 著者: Johnson, D.S. / Martinez, J. / Elgoyhen, A.B. / Heinemann, S.F. / Mcintosh, J.M. #3: ジャーナル: J.Biol.Chem. / 年: 1994 タイトル: A Nicotinic Acetylcholine Receptor Ligand of Unique Specificity, Alpha-Conotoxin Imi 著者: Mcintosh, J.M. / Yoshikami, D. / Mahe, E. / Nielsen, D.B. / Rivier, J.E. / Gray, W.R. / Olivera, B.M. | ||||||
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 | 1e76.cif.gz | 64.8 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1e76.ent.gz | 45.9 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1e76.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/e7/1e76 ftp://data.pdbj.org/pub/pdb/validation_reports/e7/1e76 | HTTPS FTP |
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-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: 1355.616 Da / 分子数: 1 / 変異: YES / 由来タイプ: 合成 詳細: SYNTHESIZED USING STANDARD FMOC CHEMISTRY. IM1 SEQUENCE FOUND NATURALLY IN CONUS IMPERIALIS VENOM 由来: (合成) CONUS IMPERIALIS (ミカドミナシ) / 参照: UniProt: P50983 |
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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: DATA CONSIST OF 70 UPPER LIMITS ON DISTANCES OBTAINED FROM NOE MEASUREMENTS AND 34 ANGLE CONSTRAINTS OBTAINED FROM NOE MEASUREMENTS AND COUPLING CONSTANT MEASUREMENTS. THESE INPUT DATA ARE ALSO ...Text: DATA CONSIST OF 70 UPPER LIMITS ON DISTANCES OBTAINED FROM NOE MEASUREMENTS AND 34 ANGLE CONSTRAINTS OBTAINED FROM NOE MEASUREMENTS AND COUPLING CONSTANT MEASUREMENTS. THESE INPUT DATA ARE ALSO AVAILABLE FROM THE PROTEIN DATA BANK. FIVE STEREOSPECIFIC RESONANCE ASSIGNMENTS HAVE BEEN MADE. TORSION ANGLE DYNAMICS CALCULATIONS WERE PERFORMED WITH THE PROGRAM DYANA (P. GUNTERT, C. MUMENTHALER, K. WUTHRICH, J. MOL. BIOL. (1997) VOL. 273, 283-298). FOR THE RESTRAINED ENERGY MINIMIZATION THE PROGRAM OPAL (P. LUGINBUHL, P. GUNTERT, M. BILLETER, K. WUTHRICH, J. BIOMOL. NMR (1996) VOL. 8, 136-146) WAS USED. DEPOSITED COORDINATES ARE THOSE OF CONFORMERS 1-20 IN THE PAPER CITED ON *JRNL* RECORDS ABOVE. NO VIOLATIONS OF DISTANCE CONSTRAINTS FROM NOES EXCEED 0.10 ANGSTROMS, AND NO VIOLATIONS OF ANGLE CONSTRAINTS EXCEED 2.0 DEGREES. REPRESENTATIVE CONFORMER HAS THE SMALLEST RMSD TO THE MEAN STRUCTURE UPON SUPERPOSITION OF THE BACKBONE ATOMS N, CA, AND C' OF RESIDUES 2-11. |
-試料調製
試料状態 | pH: 4.1 / 温度: 298 K |
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結晶化 | *PLUS 手法: その他 / 詳細: NMR |
-NMR測定
NMRスペクトロメーター | タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 400 MHz |
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-解析
NMR software |
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精密化 | 手法: TORSION ANGLE DYNAMICS, RESTRAINED ENERGY MINIMISATION ソフトェア番号: 1 詳細: FOR THE PRESENT STRUCTURES THE NMR DISTANCE CONSTRAINTS WERE WEIGHTED SUCH THAT A VIOLATION OF AN UPPER DISTANCE LIMIT OF 0.1 ANGSTROM CORRESPONDS TO AN ENERGY OF KT/2. THE CONSTRAINTS ON ...詳細: FOR THE PRESENT STRUCTURES THE NMR DISTANCE CONSTRAINTS WERE WEIGHTED SUCH THAT A VIOLATION OF AN UPPER DISTANCE LIMIT OF 0.1 ANGSTROM CORRESPONDS TO AN ENERGY OF KT/2. THE CONSTRAINTS ON DIHEDRAL ANGLES RESULTING FROM MEASUREMENTS OF VICINAL COUPLING CONSTANTS WERE WEIGHTED SUCH THAT A VIOLATION OF 2.5 DEGREES CORRESPONDS TO AN ENERGY OF KT/2. | ||||||||||||
代表構造 | 選択基準: closest to the average | ||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: LOWEST RESIDUAL TARGET FUNCTION 計算したコンフォーマーの数: 40 / 登録したコンフォーマーの数: 20 |