分子量: 1214.440 Da / 分子数: 1 / 由来タイプ: 合成 / 詳細: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
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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
DQF-COSY
1
2
1
2D TOCSY
1
3
1
2D ROESY
2
4
2
2D ROESY
2
5
2
2D COSY-35
NMR実験の詳細
Text: Resonance assignments were made using standard 2D homonuclear techniques
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試料調製
詳細
Solution-ID
内容
溶媒系
1
5mMpeptide, unbuffered
90% H2O/10% D2O
2
5mMpeptide, unbuffered
100% D2O
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
0
5.0
1atm
293K
2
0
5.0
1atm
293K
結晶化
*PLUS
手法: other / 詳細: NMR
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NMR測定
放射
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M
放射波長
相対比: 1
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: 500 MHz
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解析
NMR software
名称
バージョン
開発者
分類
XwinNMR
3.1
bruker
collection
Felix
980
accelrys
データ解析
DGII
980
TimHavel
構造決定
Amber
6
Case, Kollmanetal.
精密化
Amber
6
構造決定
精密化
手法: Distance geometry, restrained molecular dynamics with chemical shift refinement ソフトェア番号: 1 詳細: 100 structures were calculated using distance geometry. The 80 structures of lowest penalty function were refined using the Sander module of AMBER (v6.0). The calculation employed 72 distance ...詳細: 100 structures were calculated using distance geometry. The 80 structures of lowest penalty function were refined using the Sander module of AMBER (v6.0). The calculation employed 72 distance restraints, 11 dihedral angle restraints and 8 chemical shift restraints. The 20 structures of lowest violation energy were chosen to represent the structure. There are no violations of the input restraints > 0.1 A or 2 degrees. The rms. difference between calculation and observed chemical shifts is 0.07 ppm. 78% of the backbone geometries are in the most favourable region ofthe Ramachandran plot. The backbone heavy atom rmsd from the mean structure is 0.29+/-0.05 A.
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: structures with the least restraint violations 計算したコンフォーマーの数: 80 / 登録したコンフォーマーの数: 20