分子量: 1333.604 Da / 分子数: 1 / 由来タイプ: 合成 詳細: The peptide was chemically synthesized. It is a novel sequence derived from phage-display selection.
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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
DQF-COSY
2
3
2
2D-ROESY
2
4
2
COSY-35
NMR実験の詳細
Text: This structure was determined using standard 2D homonuclear techniques.
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試料調製
詳細
Solution-ID
内容
溶媒系
1
8mMpeptide
90% H2O/10% D2O
2
8mMpeptide
100% D2O
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
0
5.1
ambient
290K
2
0
5.1
ambient
290K
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 AVANCE / 製造業者: Bruker / モデル: AVANCE / 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
TimothyHavel
構造決定
Discover
3.1
Accelrys
精密化
精密化
手法: distance geometry, restrained molecular dynamics / ソフトェア番号: 1 詳細: The structures are based on 70 NOE distance restraints, 8 phi and 3 chi-1 dihedral angle restraints. No hydrogen bond restraints were employed. Note that the Ha-Hb coupling constants indicate ...詳細: The structures are based on 70 NOE distance restraints, 8 phi and 3 chi-1 dihedral angle restraints. No hydrogen bond restraints were employed. Note that the Ha-Hb coupling constants indicate rotational averaging about the Phe4 chi-1 angle. Several NOEs to the aromatic ring of Phe4 were not used to generate restraints as they could be satisfied by a -60 or 180 degree rotamer, but not by both. The mean backbone atom RMSD to the mean structure within the disulfide cycle is 0.31 +/- 0.06 Angstoms.
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