250 mM [U-99% 13C; U-99% 15N] SPRY, 93% H2O/7% D2O
93% H2O/7% D2O
3
250 mM [U-13C; U-15N; U-2H] SPRY, 93% H2O/7% D2O
93% H2O/7% D2O
試料
濃度 (mg/ml)
構成要素
Isotopic labeling
Solution-ID
250mM
SPRY-1
[U-98% 15N]
1
250mM
SPRY-2
[U-99% 13C; U-99% 15N]
2
250mM
SPRY-3
[U-13C; U-15N; U-2H]
3
試料状態
イオン強度: 0.05 / pH: 7.2 / 圧: ambient / 温度: 298 K
-
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 Avance
Bruker
AVANCE
700
1
Bruker Avance
Bruker
AVANCE
600
2
-
解析
NMR software
名称
開発者
分類
X-PLOR NIH
Schwieters, Kuszewski, TjandraandClore
構造決定
CARA
KellerandWuthrich
chemicalshiftassignment
CARA
KellerandWuthrich
peakpicking
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
解析
TopSpin
BrukerBiospin
collection
X-PLOR NIH
Schwieters, Kuszewski, TjandraandClore
精密化
精密化
手法: simulated annealing / ソフトェア番号: 1 詳細: THE WHOLE PROTEIN WAS ASSIGNED BY NMR. THE FINAL STRUCTURES OF THE PROTEIN WERE CALCULATED USING XPLOR-NIH. SIMULATED ANNEALING WITH NOE-DERIVED DISTANCE RESTRAINTS WAS APPLIED TO THE 325-349 ...詳細: THE WHOLE PROTEIN WAS ASSIGNED BY NMR. THE FINAL STRUCTURES OF THE PROTEIN WERE CALCULATED USING XPLOR-NIH. SIMULATED ANNEALING WITH NOE-DERIVED DISTANCE RESTRAINTS WAS APPLIED TO THE 325-349 LOOP ONLY WHEREAS RESIDUES 291-324 WERE HELD FIXED AT THE COORDINATES DETERMINED BY X-RAY CRYSTALLOGRAPHY FROM PDB ENTRY 3UV9.
NMR constraints
NOE constraints total: 259 / NOE intraresidue total count: 103 / NOE long range total count: 5 / NOE medium range total count: 49 / NOE sequential total count: 102
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: 500 / 登録したコンフォーマーの数: 10