手法: 溶液NMR 詳細: 1H, 15N, 13C chemical shift assignments and solution structure
NMR実験
Conditions-ID
Experiment-ID
Solution-ID
タイプ
1
1
1
2D 1H-15N HSQC
1
2
1
3D HNCA
1
3
1
3DHN(CO)CA
1
4
1
3D HNCO
1
5
1
3DHN(CA)CO
1
6
1
3D HN(CA)CB
1
7
1
3DCBCA(CO)NH
1
8
1
3D 1H-15N TOCSY
1
9
1
2D 1H-13C HSQC
1
10
1
3D (H)CCH-TOCSY
1
11
1
3D CCH-TOCSY
1
12
1
3D 1H-15N/13C NOESY aliphatic
1
13
1
2D 1H-13C HSQC aromatic
1
14
1
2DH(N)CO
-
試料調製
詳細
内容: 0.6 mM [U-100% 13C; U-100% 15N] lysm, 40 mM potassium phosphate, 90% H2O/10% D2O 溶媒系: 90% H2O/10% D2O
試料
濃度 (mg/ml)
構成要素
Isotopic labeling
Solution-ID
0.6mM
lysm-1
[U-100% 13C; U-100% 15N]
1
40mM
potassium phosphate-2
1
試料状態
イオン強度: 40 / pH: 6 / 圧: ambient / 温度: 298 K
-
NMR測定
NMRスペクトロメーター
タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 600 MHz
-
解析
NMR software
名称
バージョン
開発者
分類
Felix
2007
AccelrysSoftwareInc.
chemicalshiftassignment
Felix
2007
AccelrysSoftwareInc.
peakpicking
Felix
2007
AccelrysSoftwareInc.
解析
CNS
1.21
Brunger, Adams, Clore, Gros, NilgesandRead
精密化
CNS
1.21
Brunger, Adams, Clore, Gros, NilgesandRead
構造決定
TopSpin
1.3
BrukerBiospin
collection
精密化
手法: simulated annealing / ソフトェア番号: 1 / 詳細: in explicit waters using ARIA protocol
NMR constraints
NOE constraints total: 430 / NOE intraresidue total count: 14 / NOE long range total count: 142 / NOE medium range total count: 106 / NOE sequential total count: 168 / Hydrogen bond constraints total count: 32 / Protein chi angle constraints total count: 19 / Protein phi angle constraints total count: 41 / Protein psi angle constraints total count: 38
代表構造
選択基準: lowest energy
NMRアンサンブル
コンフォーマー選択の基準: structures with the 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: 10 / Maximum lower distance constraint violation: 0.1 Å / Maximum torsion angle constraint violation: 10.1 ° / Maximum upper distance constraint violation: 0.3 Å
NMR ensemble rms
Distance rms dev: 0.037 Å / Distance rms dev error: 0.001 Å