- PDB-2glz: Crystal structure of a formylmethanofuran dehydrogenase subunit e... -
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基本情報
登録情報
データベース: PDB / ID: 2glz
タイトル
Crystal structure of a formylmethanofuran dehydrogenase subunit e-like protein (dhaf_2992) from desulfitobacterium hafniense dcb-2 at 1.45 A resolution
要素
similar to Formylmethanofuran dehydrogenase subunit E
キーワード
METAL BINDING PROTEIN / Structural genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2
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 GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
解像度: 1.45→29.894 Å / Num. obs: 71200 / % possible obs: 99.9 % / 冗長度: 7.4 % / Biso Wilson estimate: 18.1 Å2 / Rmerge(I) obs: 0.071 / Rsym value: 0.071 / Net I/σ(I): 5.8
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 obs
Rsym value
% possible all
1.45-1.49
4.6
0.729
1
24112
5186
0.729
99.9
1.49-1.53
7.4
0.63
1
37182
5034
0.63
99.9
1.53-1.57
7.6
0.493
1.5
37810
4965
0.493
100
1.57-1.62
7.6
0.374
2
36437
4772
0.374
100
1.62-1.67
7.6
0.298
2.5
35494
4652
0.298
100
1.67-1.73
7.6
0.257
2.9
34680
4545
0.257
100
1.73-1.8
7.7
0.201
3.7
33160
4329
0.201
100
1.8-1.87
7.7
0.161
4.5
32179
4192
0.161
100
1.87-1.96
7.6
0.145
4
30513
4026
0.145
100
1.96-2.05
7.7
0.111
6
29699
3877
0.111
100
2.05-2.16
7.6
0.102
6
27621
3656
0.102
100
2.16-2.29
7.5
0.09
6.5
26497
3516
0.09
100
2.29-2.45
7.7
0.074
8.1
25265
3291
0.074
100
2.45-2.65
7.7
0.066
8.8
23432
3059
0.066
100
2.65-2.9
7.6
0.058
10.4
21842
2856
0.058
100
2.9-3.24
7.6
0.052
11.5
19586
2574
0.052
100
3.24-3.74
7.5
0.05
11.6
17262
2287
0.05
100
3.74-4.59
7.5
0.047
12.9
14671
1968
0.047
99.8
4.59-6.48
7.3
0.045
12.9
11220
1545
0.045
99.8
6.48-29.89
6.5
0.045
12.2
5688
870
0.045
94.8
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位相決定
位相決定
手法: 多波長異常分散
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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
1.701
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: 1.45→27.2 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.96 / SU B: 2.688 / SU ML: 0.05 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.058 / ESU R Free: 0.061 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 ...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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3). X-RAY ANOMALOUS SCATTERING MEASUREMENTS INDICATE EITHER A ZINC OR A NICKEL CATION ION IS COORDINATED IN AN TETRAHEDERAL COMPLEX TO THE SIDECHAINS OF HIS-15, HIS-17, CYS-19, AND CYS-55. THE RELATIVE OCCUPANCIES OF THE THE METAL IONS WERE ESTIMATED FROM THE RATIO OF THEIR ANOMALOUS DIFFERENCE MAP PEAK HEIGHTS. THE TOTAL OCCUPANCY OF THE ZN AND NI CATIONS WAS REDUCED TO 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING OBSERVED AT THIS SITE. 4). SEVERAL MOLECULES OF THE CRYOPROTECTANT, ETHYLENE GLYCOL, WERE MODELED INTO THE STRUCTURE. 5). UNKNOWN DIFFERENCE DENSITY, BETWEEN THE SIDECHAINS OF ASN 64 AND PHE 87 ON BOTH SUBUNITS, IN THE ASYMMETRIC UNIT HAS NOT BEEN MODELED. 6). ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
Rfactor
反射数
%反射
Selection details
Rfree
0.198
3593
5.1 %
RANDOM
Rwork
0.171
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-
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obs
0.173
71126
99.86 %
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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