THIS CONSTRUCT (RESIDUES 18-228) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THIS CONSTRUCT (RESIDUES 18-228) 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: 1.37→29.552 Å / Num. all: 93097 / Num. obs: 93097 / % possible obs: 99.4 % / 冗長度: 3.5 % / Rsym value: 0.093 / Net I/σ(I): 7.2
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
1.37-1.41
3.5
0.88
0.8
23690
6832
0.88
99.5
1.41-1.44
3.5
0.702
1
23101
6664
0.702
99.8
1.44-1.49
3.5
0.516
1.4
22530
6476
0.516
99.8
1.49-1.53
3.5
0.396
1.8
22135
6301
0.396
99.8
1.53-1.58
3.5
0.333
2.1
21450
6075
0.333
99.6
1.58-1.64
3.5
0.264
2.7
20962
5914
0.264
99.5
1.64-1.7
3.6
0.221
3.3
20340
5694
0.221
99.3
1.7-1.77
3.6
0.175
4.1
19586
5461
0.175
99.1
1.77-1.85
3.6
0.143
5
18823
5246
0.143
99.1
1.85-1.94
3.6
0.119
5.9
18063
5045
0.119
99.1
1.94-2.04
3.6
0.101
6.7
17075
4784
0.101
99.3
2.04-2.17
3.5
0.091
7.4
16170
4573
0.091
99.5
2.17-2.32
3.5
0.086
7.6
15231
4307
0.086
99.6
2.32-2.5
3.5
0.083
7.8
13994
4023
0.083
99.7
2.5-2.74
3.4
0.081
7.8
12783
3723
0.081
99.7
2.74-3.06
3.3
0.072
9
11209
3353
0.072
98.7
3.06-3.54
3.3
0.061
10.5
9687
2963
0.061
99.3
3.54-4.33
3.6
0.05
12.9
9243
2544
0.05
99.4
4.33-6.13
3.6
0.046
13.8
7191
1998
0.046
98.8
6.13-29.552
3.4
0.042
15
3865
1121
0.042
95.8
-
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
MolProbity
3beta29
モデル構築
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
SCALA
3.3.20
データスケーリング
REFMAC
5.5.0110
精密化
MOSFLM
データ削減
SHELXD
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.37→29.552 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.964 / Occupancy max: 1 / Occupancy min: 0.33 / SU B: 1.766 / SU ML: 0.032 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.053 / ESU R Free: 0.052 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. CHLORIDE (CL) AND GLYCEROL (GOL) FROM THE CRYSTALLIZATION/CRYO CONDITIONS HAVE BEEN MODELED INTO THE STRUCTURE. 4.UNKNOWN LIGANDS (UNL) HAVE BEEN MODELED INTO THE PUTATIVE ACTIVE SITE.IDENTIFICATION OF THE PUTATIVE ACTIVE SITE IS BASED ON ElECTRON DENSITY AND STRUCTURAL COMPARISONS WITH SIMILAR PROTEINS OF KNOWN FUNCTION. 5.THE SIDECHAINS OF GLU B177,ASP B193,GLU A211, AND GLU B33 SHOW ELEVATED NEGATIVE DIFFERENCE DENSITY. THE OCCUPANCIES OF THE SIDECHAIN ATOMS WERE NOT ADJUSTED IN THESE REGIONS OF APPARENT RADIATION DAMAGE.
Rfactor
反射数
%反射
Selection details
Rfree
0.1732
4655
5 %
RANDOM
Rwork
0.1337
-
-
-
obs
0.1356
92858
99.03 %
-
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: 1.4 Å / 溶媒モデル: BABINET MODEL WITH MASK