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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 2kqn | ||||||
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タイトル | Solution structure of the AL-09 H87Y immunoglobulin light chain variable domain | ||||||
![]() | Ig kappa chain V-I region AU | ||||||
![]() | IMMUNE SYSTEM / Amyloidosis / Immunoglobulin kappa light chain / homodimer / Bence-Jones protein / Disulfide bond / Immunoglobulin domain / Immunoglobulin V region | ||||||
機能・相同性 | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta![]() | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR / AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT, ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Volkman, B.F. / Peterson, F.C. / Ramirez-Alvarado, M. / Baden, E.M. | ||||||
![]() | ![]() タイトル: A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. 著者: Peterson, F.C. / Baden, E.M. / Owen, B.A. / Volkman, B.F. / Ramirez-Alvarado, M. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 1.4 MB | 表示 | ![]() |
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PDB形式 | ![]() | 1.2 MB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 353.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 575.1 KB | 表示 | |
XML形式データ | ![]() | 72 KB | 表示 | |
CIF形式データ | ![]() | 110.1 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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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: 抗体 | 分子量: 12154.369 Da / 分子数: 2 / 断片: Immunoglobulin kappa light chain / 変異: H87Y / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
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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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試料調製
詳細 | 内容: 0.8 mM [U-100% 13C; U-100% 15N] AL-09 H87Y-1, 10 mM [U-2H] MES-2, 0.02 % sodium azide-3, 95% H2O, 5% D2O 溶媒系: 95% H2O/5% D2O | ||||||||||||||||
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試料 |
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試料状態 | イオン強度: 8 / pH: 6.8 / 圧: AMBIENT / 温度: 298 K |
-NMR測定
NMRスペクトロメーター | タイプ: Bruker Avance III / 製造業者: Bruker / モデル: AVANCE III / 磁場強度: 500 MHz |
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解析
NMR software |
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精密化 | 手法: AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT, ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT ソフトェア番号: 1 詳細: HOMODIMER STRUCTURES ARE BASED ON A TOTAL OF 2104 NOE CONSTRAINTS (341 INTRA, 394 SEQUENTIAL, 265 MEDIUM, 1027 INTRAMONOMER LONG RANGE AND 77 INTERMONOMER NOE CONSTRAINTS) AND 149 PHI AND PSI ...詳細: HOMODIMER STRUCTURES ARE BASED ON A TOTAL OF 2104 NOE CONSTRAINTS (341 INTRA, 394 SEQUENTIAL, 265 MEDIUM, 1027 INTRAMONOMER LONG RANGE AND 77 INTERMONOMER NOE CONSTRAINTS) AND 149 PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS PER MONOMER. CONSTRAINTS WERE ASSIGNED AND VALIDATED IN ONE MONOMER AND THEN DUPLICATED TO GENERATE A SYMMETRY RELATED CONSTRAINTS IN THE SECOND MONOMER. | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2104 / NOE intraresidue total count: 341 / NOE long range total count: 1104 / NOE medium range total count: 265 / NOE sequential total count: 394 / Protein phi angle constraints total count: 74 / Protein psi angle constraints total count: 75 | ||||||||||||||||||||||||||||
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: target function / 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 20 |