分子量: 1277.470 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
2D ROESY
1
2
1
2D TOCSY
1
3
1
DQF-COSY
2
4
2
2D ROESY
2
5
2
2D COSY-35
2
6
2
2D 13C-HMQC
NMR実験の詳細
Text: This structure was determined using standard 2D homonuclear techniques augmented by loose phi and psi restraints generated from TALOS. MODEL 21 is the average minimized structure.
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試料調製
詳細
Solution-ID
内容
溶媒系
1
8mMpeptide, nobuffer
90% H2O/10% D2O
2
8mMpeptide, nobuffer
100% D2O
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
0
5.0
1atm
303K
2
0
5.0
1atm
303K
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
DGII
98
TimHavel
構造決定
Discover
3
Accelrys
精密化
NMRPipe
2001
FrankDelaglio
データ解析
Felix
98
Accelrys
データ解析
XwinNMR
3.1
Bruker
collection
精密化
手法: distance geometry, restrained molecular dynamics / ソフトェア番号: 1 詳細: 100 distance geometry structures were calculated. The 80 structures of lowest penalty function were further refined using restrained molecular dynamics. The 20 structures of lowest restraint ...詳細: 100 distance geometry structures were calculated. The 80 structures of lowest penalty function were further refined using restrained molecular dynamics. The 20 structures of lowest restraint violation energy were used to describe the structure. 61 distance and 21 dihedral angle restraints were used. The final ensemble has no distance violations greater than 0.1 A and no dihedral angle vioaltions greater than 1 degree. 95% of the residues are in the most favourable region of the Ramachandran plot. The mean backbone atom rmsd to 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: 21