Text: This structure was determined using standard 2D homonuclear techniques, in conjunction with a semi-automated assignment protocol.
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試料調製
詳細
Solution-ID
内容
溶媒系
1
1 mM ASIP(80-132: Q115Y, S124Y), 100 mM d3-acetic acid/d3-sodium acetate, 90% H2O 10% D2O
100 mM d3-acetic acid/d3-sodium acetate, 90% H2O 10% D2O
2
1 mM ASIP(80-132: Q115Y, S124Y), 100 mM d3-acetic acid/d3-sodium acetate, 100% D2O
100 mM d3-acetic acid/d3-sodium acetate, 100% D2O
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
100 mM d3-acetic acid/sodium acetate
5.0
ambient
288K
2
100 mM d3-acetic acid/sodium acetate
4.0
ambient
288K
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NMR測定
NMRスペクトロメーター
タイプ
製造業者
モデル
磁場強度 (MHz)
Spectrometer-ID
Varian UNITYPLUS
Varian
UNITYPLUS
800
1
Varian UNITYPLUS
Varian
UNITYPLUS
800
2
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解析
NMR software
名称
バージョン
開発者
分類
CYANA
1.0.6
Guentert, Herrmann, Mumenthaler, Wuthrich
構造決定
NMRPipe
2.3
Delaglio
解析
VNMR
6.1C
collection
CYANA
1.0.6
Guentert, Herrmann, Mumenthaler, Wuthrich
精密化
精密化
手法: simulated annealing, torsion angle dynamics / ソフトェア番号: 1 詳細: This structure family represents one of two major conformers present in solution. The two conformers arise from the cis-trans proline isomerization of the Ala104-Pro105 peptide bond.
代表構造
選択基準: minimized average structure
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: 1000 / 登録したコンフォーマーの数: 21 Distance constraint violation method: From the original family of twenty, the representative conformer had the lowest target function and was subjected to further minimization in water. The remaining ...Distance constraint violation method: From the original family of twenty, the representative conformer had the lowest target function and was subjected to further minimization in water. The remaining structures were obtained without explicit inclusion of solvent.