structures with acceptable covalent geometry,structures with the least restraint violations
代表モデル
モデル #1
closest to the average
-
要素
#1: タンパク質・ペプチド
e109zetapeptide
分子量: 2143.615 Da / 分子数: 1 / 由来タイプ: 合成 詳細: 'solid-phase peptide synthesis of a novel peptide based on a naive phage-peptide library that was sorted for binding to the high-affinity IGE receptor'
-
実験情報
-
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 NOESY
1
2
1
DQF-COSY
1
3
1
2D TOCSY
1
4
2
2D COSY-35
1
5
2
2D NOESY
1
6
1
2D ROESY
NMR実験の詳細
Text: This structure was determined using standard 2D homonuclear techniques. 3JHNHA WERE OBTAINED BY FITTING LORENTZIAN LINES TO THE ANTIPHASE DOUBLETS OF HN-HA PEAKS IN A 2QF-COSY SPECTRUM ...Text: This structure was determined using standard 2D homonuclear techniques. 3JHNHA WERE OBTAINED BY FITTING LORENTZIAN LINES TO THE ANTIPHASE DOUBLETS OF HN-HA PEAKS IN A 2QF-COSY SPECTRUM PROCESSED TO HIGH DIGITAL RESOLUTION IN F2. 3JHAHB WERE EXTRACTED FROM A COSY-35 SPECTRUM ACQUIRED IN D2O
タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 500 MHz
-
解析
NMR software
名称
バージョン
開発者
分類
XwinNMR
2.1
Bruker, Inc.
collection
Felix
98
MolecularSimulations, Inc.
データ解析
DGII
98
MolecularSimulations, Inc.
構造決定
Discover
98
MolecularSimulations, Inc.
精密化
精密化
手法: hybrid distance geometry, simulated annealing, then further refined by restrained molecular dynamics ソフトェア番号: 1 詳細: The structures are based on a total of 101 NOE-derived distance restraints, 18 dihedral angle restraints, and 12 distant restraints from 6 hydrogen bonds.
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 acceptable covalent geometry,structures with the least restraint violations 計算したコンフォーマーの数: 50 / 登録したコンフォーマーの数: 20