SEQUENCE The sequence of this protein was published in a journal (Zamudio, F. Z., et al. 1997, FEBS ...SEQUENCE The sequence of this protein was published in a journal (Zamudio, F. Z., et al. 1997, FEBS Lett. 405, 385-389).
分子量: 3776.495 Da / 分子数: 1 / 由来タイプ: 合成 詳細: The peptide was chemically synthesized. This sequence occurs naturally in the venom of scorpion Pandinus imperator. 参照: UniProt: P59868
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実験情報
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実験
実験
手法: 溶液NMR
NMR実験
Conditions-ID
Experiment-ID
Solution-ID
タイプ
1
1
1
2D NOESY
1
2
1
DQF-COSY
1
3
1
E-COSY
NMR実験の詳細
Text: This structure was determined using standard 2D homonuclear techniques.
タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 600 MHz
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解析
NMR software
名称
バージョン
開発者
分類
XwinNMR
3
Bruker
collection
XwinNMR
3
Bruker
解析
X-PLOR
3.851
Brunger
構造決定
X-PLOR
3.851
Brunger
精密化
精密化
手法: distance geometry simulated annealing / ソフトェア番号: 1 詳細: The structures are based on a total of 519 restraints, 473 are NOE-derived distance constraints, 25 dihedral angle restraints, 12 distance restraints from hydrogen bonds, and 9 distance ...詳細: The structures are based on a total of 519 restraints, 473 are NOE-derived distance constraints, 25 dihedral angle restraints, 12 distance restraints from hydrogen bonds, and 9 distance restraints form disulfide bonds.
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: The submitted conformer models are those with the lowest energy and the least restraint violations. 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