back calculated data agree with experimental NOESY spectrum, structures with the least restraint violations, structures with the lowest energy
代表モデル
モデル #12
closest to the average
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要素
#1: タンパク質・ペプチド
PSI-CONOTOXINPIIIF
分子量: 2674.157 Da / 分子数: 1 / 由来タイプ: 合成 詳細: Solid phase chemical synthesis was used. One sample contained only natural isotopic abundance residues. Another peptide incorporated 3-13C-labeled cysteine at position 4. The third peptide ...詳細: Solid phase chemical synthesis was used. One sample contained only natural isotopic abundance residues. Another peptide incorporated 3-13C-labeled cysteine at position 4. The third peptide incorporated 3-13C-labeled cysteine at positions 5, 10, 16, 21, and 22. The sequence for all peptides is the same as the native peptide FROM CONUS PURPURASCENS (PURPLE CONE). 参照: UniProt: P60245
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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 NOESY
1
2
1
DQF-COSY
2
3
2
PE-COSY
1
4
3
13C-selected 2D NOESY
1
5
4
13C-selected 2D NOESY
1
6
4
Double half-filtered 2D NOESY
2
7
4
Double half-filtered 2D PE-COSY
2
8
4
13C-selected 1D 1H NMR
NMR実験の詳細
Text: This structure was determined using isotopic filtration and isotope-selected 1H observation in addition to standard homonuclear techniques.
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試料調製
詳細
Solution-ID
内容
溶媒系
1
12 mM psi-conotoxin PIIIF; TFA added to pH 3.5
90% H2O/10% D2O
2
12 mM psi-conotoxin PIIIF
100% D2O
3
14 mM of psi-conotoxin PIIIF [5,10,16,21,22] 3-13C-Cys; TFA added to pH 3.5
90% H2O/10% D2O
4
16 mM of psi-conotoxin PIIIF [4] 3-13C-Cys; TFA added to pH 3.5
90% H2O/10% D2O
5
16 mM of psi-conotoxin PIIIF [4] 3-13C-Cys
100% D2O
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
12 mM; tetra-TFA salt
3.5
ambient
277K
2
12 mM; tetra-TFA salt
3.5
ambient
295K
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
製造業者
モデル
磁場強度 (MHz)
Spectrometer-ID
Varian UNITY
Varian
UNITY
500
1
Varian INOVA
Varian
INOVA
600
2
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解析
NMR software
名称
バージョン
開発者
分類
VNMR
6.1B
Varian, Inc.
collection
Felix
97
MSI, Inc.
解析
IRMA
97
MSI, Inc.
iterativematrixrelaxation
DGII
97
MSI, Inc.
構造決定
Discover
2.98
MSI, Inc.
構造決定
Discover
2.98
MSI, Inc.
精密化
精密化
手法: distance geometry molecular dynamics relaxation matrix distance geometry simulated annealing ソフトェア番号: 1 詳細: These structures are based on 380 NOE-derived distance restraints, 7 restraints on phi derived from J-coupling, and 7 restraints on chi1 determined from J-coupling and NOE volumes.
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: back calculated data agree with experimental NOESY spectrum, structures with the least restraint violations, structures with the lowest energy 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: 17