0.3 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O
90% H2O/10% D2O
試料
濃度 (mg/ml)
構成要素
Isotopic labeling
Solution-ID
0.3mM
entity-1
[U-100% 15N]
1
0.3mM
entity-2
[U-100% 13C; U-100% 15N]
2
試料状態
イオン強度: 0.11 / pH: 4.6 / 圧: ambient / 温度: 293 K
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NMR測定
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: 700 MHz
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解析
NMR software
名称
開発者
分類
CYANA
Guntert, MumenthalerandWuthrich
構造決定
CNS
Brunger, Adams, Clore, Gros, Nilges, andRead
精密化
精密化
手法: simulated annealing / ソフトェア番号: 1
NMR constraints
NOE constraints total: 1188 / NOE intraresidue total count: 240 / NOE long range total count: 380 / NOE medium range total count: 210 / NOE sequential total count: 358 / Protein chi angle constraints total count: 17 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 69 / Protein psi angle constraints total count: 66
代表構造
選択基準: closest to the average
NMRアンサンブル
Average torsion angle constraint violation: 2.209 ° / コンフォーマー選択の基準: target function / 計算したコンフォーマーの数: 200 / 登録したコンフォーマーの数: 15 / Maximum lower distance constraint violation: 0.2 Å / Maximum torsion angle constraint violation: 5 ° / Maximum upper distance constraint violation: 0.3 Å / Torsion angle constraint violation method: RECORD SCRIPTS
NMR ensemble rms
Distance rms dev: 0.0178 Å / Distance rms dev error: 0.012 Å