内容: 1.2 mM [U-100% 13C; U-100% 15N] ZUOTIN, 20 mM potassium phosphate, 50 mM sodium chloride, 1 mM DTT, 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
1.2mM
ZUOTIN-1
[U-100% 13C; U-100% 15N]
1
20mM
potassium phosphate-2
1
50mM
sodium chloride-3
1
1mM
DTT-4
1
試料状態
イオン強度: 70 / pH: 6.5 / 圧: AMBIENT / 温度: 283 K
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NMR測定
NMRスペクトロメーター
タイプ: BRUKER AVANCE II / 製造業者: Bruker / モデル: AVANCE II / 磁場強度: 600 MHz
-
解析
NMR software
名称
バージョン
開発者
分類
XPLOR-NIH
2.9.3
SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJ
精密化
TopSpin
2.1
BrukerBiospin
collection
NMRPipe
2007
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
解析
XEASY
1.3
Bartelsetal.
データ解析
GARANT
2.1
Bartels, Guntert, BilleterandWuthrich
データ解析
CYANA
2.1
Guntert, MumenthalerandWuthrich
構造決定
CYANA
2.1
Guntert, MumenthalerandWuthrich
精密化
精密化
手法: torsion angle dynamics / ソフトェア番号: 1 詳細: AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT. STRUCTURES ARE BASED ...詳細: AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT. STRUCTURES ARE BASED ON A TOTAL OF 1471 NOE CONSTRAINTS (418 INTRA, 272 SEQUENTIAL, 463 MEDIUM, AND 318 LONG RANGE) AND 148 PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS.
NMR constraints
NOE constraints total: 1471 / NOE intraresidue total count: 418 / NOE long range total count: 318 / NOE medium range total count: 463 / NOE sequential total count: 272 / Protein phi angle constraints total count: 74 / Protein psi angle constraints total count: 74
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: target function / 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