SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
解像度: 2→22.95 Å / Num. obs: 36411 / % possible obs: 98 % / 冗長度: 3.9 % / Rmerge(I) obs: 0.061 / Rsym value: 0.061 / Net I/σ(I): 8.1
反射 シェル
Diffraction-ID: 1
解像度 (Å)
% possible obs (%)
冗長度 (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Rsym value
% possible all
2-2.05
97
3.8
0.418
1.8
2658
0.418
97
2.05-2.11
96.9
3.9
0.398
1.1
2560
0.398
2.11-2.17
97.3
4
0.297
2.5
2526
0.297
2.17-2.24
97.5
4
0.23
3.2
2416
0.23
2.24-2.31
97.5
4
0.22
1.4
2366
0.22
2.31-2.39
97.7
4
0.16
4.6
2319
0.16
2.39-2.48
97.8
4
0.14
5.2
2226
0.14
2.48-2.58
97.9
4
0.116
6.3
2163
0.116
2.58-2.7
98.2
3.9
0.105
5.3
2079
0.105
2.7-2.83
98.2
4
0.074
9.5
1963
0.074
2.83-2.98
98.5
4
0.065
10.5
1880
0.065
2.98-3.16
98.5
4
0.054
12.6
1800
0.054
3.16-3.38
98.9
4
0.046
14.2
1684
0.046
3.38-3.65
98.9
3.9
0.043
13.3
1600
0.043
3.65-4
98.9
3.8
0.041
11.1
1440
0.041
4-4.47
99
3.9
0.035
17.5
1324
0.035
4.47-5.16
99.2
3.9
0.035
17.5
1188
0.035
5.16-6.32
99.4
3.8
0.037
16.2
998
0.037
6.32-8.94
99.3
3.7
0.035
16
797
0.035
8.94-22.95
93
3.3
0.029
21.3
424
0.029
-
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
5.2.0005
精密化
SCALA
データスケーリング
PDB_EXTRACT
1.601
データ抽出
MOSFLM
データ削減
CCP4
(SCALA)
データスケーリング
SOLVE
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2→22.95 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.942 / SU B: 8.124 / SU ML: 0.116 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / ESU R: 0.154 / ESU R Free: 0.152 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 0.7 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. METAL SITES: TWO METAL SITES WERE IDENTIFIED IN EACH MONOMER. MAGNESIUM, LOCATED AT THE ACTIVE SITE, WAS MODELLED BASED ON STRUCTURAL HOMOLOGS; THE OTHER METAL SITE IS COORDINATED BY FOUR CYSTEINES: 139,143,147,150. IT WAS TENTATIVELY ASSIGNED AS ZINC.
Rfactor
反射数
%反射
Selection details
Rfree
0.217
1810
5 %
RANDOM
Rwork
0.16
-
-
-
all
0.163
-
-
-
obs
0.16289
34588
97.55 %
-
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