解像度: 1.7→58.222 Å / Num. obs: 40912 / % possible obs: 95 % / 冗長度: 2 % / Biso Wilson estimate: 14.781 Å2 / Rmerge(I) obs: 0.074 / Rsym value: 0.074 / Net I/σ(I): 8.3
反射 シェル
Diffraction-ID: 1 / 冗長度: 2 %
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.7-1.79
0.265
2.5
10182
5141
0.265
81.9
1.79-1.9
0.192
3.6
11375
5728
0.192
96.1
1.9-2.03
0.132
4.6
10744
5408
0.132
96.3
2.03-2.19
0.085
8.4
9966
5018
0.085
96.8
2.19-2.4
0.073
9.6
9277
4673
0.073
97.3
2.4-2.69
0.063
11.3
8355
4206
0.063
97.5
2.69-3.1
0.051
13.7
7472
3763
0.051
98
3.1-3.8
0.039
16.4
6287
3168
0.039
98.3
3.8-5.38
0.037
17.2
4886
2458
0.037
98.6
5.38-58.22
0.035
18.5
2672
1349
0.035
98.9
-
位相決定
位相決定
手法: 多波長異常分散
-
解析
ソフトウェア
名称
バージョン
分類
NB
REFMAC
5.2.0019
精密化
PHENIX
精密化
SOLVE
位相決定
MolProbity
3beta29
モデル構築
SCALA
データスケーリング
PDB_EXTRACT
3.004
データ抽出
MOSFLM
データ削減
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.7→58.222 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.936 / SU B: 3.962 / SU ML: 0.072 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.115 / ESU R Free: 0.111 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...詳細: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. NADP (NAP) AND ACETATE (ACT) MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.199
2002
4.9 %
RANDOM
Rwork
0.16
-
-
-
obs
0.162
40802
94.71 %
-
溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: BABINET MODEL WITH MASK