分子量: 1867.177 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
2D-NOESY
1
3
1
DQF-COSY
2
4
2
COSY-35
2
5
2
2D-NOESY
2
6
2
2D-ROESY
NMR実験の詳細
Text: This structure was determined using standard 2D homonuclear techniques. The sample contains a mixture of cis and trans isomers about the Gly7-Pro8 peptide bond. Both sets of resonances were ...Text: This structure was determined using standard 2D homonuclear techniques. The sample contains a mixture of cis and trans isomers about the Gly7-Pro8 peptide bond. Both sets of resonances were assigned. The trans isoform is not well ordered in solution. The cis isoform is structured, especially within the disulfide cycle. Structures were calculated on the basis of restraints generated only from the cis isoform.
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試料調製
詳細
Solution-ID
内容
溶媒系
1
3mMpeptide
90% H2O, 10% D2O, pH5.1
2
3mMpeptide
100 % D2OpH5.1
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
0
5.1
ambient
303K
2
0
5.1
ambient
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 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 52 NOE distance restraints, 11 phi and 4 chi-1 dihedral angle restraints. No hydrogen bond restraints were employed. The mean backbone atom RMSD to the mean ...詳細: The structures are based on 52 NOE distance restraints, 11 phi and 4 chi-1 dihedral angle restraints. No hydrogen bond restraints were employed. The mean backbone atom RMSD to the mean structure within the disulfide cycle is 0.43 +/- 0.12 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