解像度: 2.71→29.761 Å / Num. obs: 37210 / % possible obs: 99.9 % / 冗長度: 7.3 % / Biso Wilson estimate: 67.24 Å2 / Rmerge(I) obs: 0.171 / Rsym value: 0.171 / Net I/σ(I): 3.7
反射 シェル
Diffraction-ID: 1
解像度 (Å)
冗長度 (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
2.71-2.78
7.4
1.555
0.4
20159
2725
1.555
100
2.78-2.86
7.4
1.162
0.6
19548
2632
1.162
100
2.86-2.94
7.4
0.895
0.8
19045
2558
0.895
100
2.94-3.03
7.4
0.732
0.9
18477
2486
0.732
100
3.03-3.13
7.4
0.521
1.4
18006
2432
0.521
100
3.13-3.24
7.4
0.408
1.7
17345
2337
0.408
100
3.24-3.36
7.4
0.318
2.3
16803
2268
0.318
100
3.36-3.5
7.4
0.23
3
16172
2196
0.23
100
3.5-3.65
7.4
0.183
3.7
15369
2089
0.183
100
3.65-3.83
7.3
0.149
4.6
14717
2011
0.149
100
3.83-4.04
7.3
0.134
5
13993
1928
0.134
100
4.04-4.28
7.2
0.118
5.3
12999
1812
0.118
100
4.28-4.58
7.1
0.106
6
12353
1733
0.106
100
4.58-4.95
7.1
0.096
6.7
11380
1598
0.096
100
4.95-5.42
7.2
0.086
7.3
10710
1490
0.086
100
5.42-6.06
7.1
0.085
7.5
9694
1366
0.085
100
6.06-7
7
0.086
7.2
8517
1210
0.086
100
7-8.57
6.9
0.074
7.7
7133
1040
0.074
100
8.57-12.12
6.6
0.067
7.2
5533
833
0.067
100
12.12-29.761
5.9
0.075
5.5
2750
466
0.075
93.5
-
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
データ抽出
MAR345
CCD
データ収集
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: 2.71→29.761 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.935 / SU B: 15.515 / SU ML: 0.147 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.288 / ESU R Free: 0.216 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. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...詳細: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. 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. 3. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 4. PEG 400 (2PE) FRAGMENTS, ETHYLENE GLYCOL (EDO) AND SULFATE IONS ARE MODELED BASED ON CRYSTALLIZATION/CRYO CONDITIONS. 5. THE TWO PHOSPHATES MODELED IN THE ACTIVE SITE ARE LIKELY PART OF MONONUCLEOTIDE FMN (BY SIMILARITY TO 2GJN). HOWEVER, THE DENSITY FOR FULL FMN IS TOO WEAK TO ALLOW RELIABLE REFINEMENT.
Rfactor
反射数
%反射
Selection details
Rfree
0.211
1854
5 %
RANDOM
Rwork
0.189
-
-
-
obs
0.19
37145
99.88 %
-
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: MASK