N-TERMINAL FRAMGENT (V10-K43). FIRST FIVE RESIDUES ARE ARTIFACTS FROM CLONING AND PROTEASE CLEAVAGE ...N-TERMINAL FRAMGENT (V10-K43). FIRST FIVE RESIDUES ARE ARTIFACTS FROM CLONING AND PROTEASE CLEAVAGE SITE. THEY ARE NOT PART OF NATIVE STRUCTURE.
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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
HNCA
1
2
1
HN(CA)CB
1
3
1
HN(CA)CO
1
4
1
HSQC
2
5
1
HSQC ANOESY
2
6
1
NOESYHSQC
3
7
1
H(CCO)NH
4
8
1
C(CO)NH
4
9
1
(H)CCHTOCSY
5
10
1
TOCSY 90MS
6
11
1
13CHSQCB900
6
12
1
CNOESY B900
7
13
1
NOESY 200MS
NMR実験の詳細
Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON THE DOUBLY LABELED PEPTIDE BOUND TO DPC MICELLES. HOMONOCULEAR NOESY AND TOCSY EXPERIMENTS ON A SHORTER UNLABELED PEPTIDE ...Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON THE DOUBLY LABELED PEPTIDE BOUND TO DPC MICELLES. HOMONOCULEAR NOESY AND TOCSY EXPERIMENTS ON A SHORTER UNLABELED PEPTIDE ALSO BOUND TO DPC MICELLES AND PARAMAGNETIC RELAXATION EXPERIMENTS TO ORIENT THE PEPTIDE WITH RESPECT TO THE MICELLE.
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試料調製
詳細
Solution-ID
内容
1
93% H2O/7% D2O
2
100% D2O
3
93% H2O/7% D2O
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
70
6
1.0atm
310.0K
2
70
6
1.0atm
310.0K
3
70
6
1.0atm
310.0K
4
70
6
1.0atm
310.0K
5
70
6
1.0atm
303.0K
6
70
6
1.0atm
310.0K
7
70
6
1.0atm
303.0K
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NMR測定
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
Bruker DD2
Bruker
DD2
600
1
Varian
700
2
Bruker
750
3
Varian
500
4
Bruker
900
5
Bruker
900
6
Bruker
900
7
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解析
NMR software
名称
バージョン
開発者
分類
CYANA
GUNTERT
精密化
NMRDraw
ANY
構造決定
NMRPipe
ANY
構造決定
CcpNmr Analysis
2.4
構造決定
TALOS
1
構造決定
精密化
手法: simulated annealing / ソフトェア番号: 1 詳細: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMRアンサンブル
コンフォーマー選択の基準: LOWEST ENERGY / 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 20