- PDB-3ec4: Crystal structure of Putative Acetyltransferase from the GNAT fam... -
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基本情報
登録情報
データベース: PDB / ID: 3ec4
タイトル
Crystal structure of Putative Acetyltransferase from the GNAT family (YP_497011.1) from NOVOSPHINGOBIUM AROMATICIVORANS DSM 12444 at 1.80 A resolution
要素
Putative Acetyltransferase from the GNAT family
キーワード
TRANSFERASE / YP_497011.1 / Putative Acetyltransferase from the GNAT family / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2 / Acetyltransferase (GNAT) family
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.
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実験情報
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実験
実験
手法: X線回折 / 使用した結晶の数: 1
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試料調製
結晶
マシュー密度: 2.08 Å3/Da / 溶媒含有率: 40.86 %
結晶化
温度: 277 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 8.43 詳細: 33.8% polyethylene glycol 4000, 0.2M sodium acetate, 0.1M TRIS pH 8.43, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
モノクロメーター: Single crystal Si(111) bent monochromator (horizontal focusing) プロトコル: MAD / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
ID
波長 (Å)
相対比
1
0.91837
1
2
0.97837
1
反射
解像度: 1.8→29.21 Å / Num. obs: 38799 / % possible obs: 99.9 % / 冗長度: 3.6 % / Biso Wilson estimate: 17.581 Å2 / Rmerge(I) obs: 0.104 / Rsym value: 0.104 / Net I/σ(I): 5.628
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
1.8-1.85
3.7
0.505
1.5
10441
2849
0.505
100
1.85-1.9
3.7
0.433
1.8
10154
2746
0.433
99.7
1.9-1.95
3.7
0.343
2.2
9807
2664
0.343
99.7
1.95-2.01
3.7
0.276
2.8
9588
2603
0.276
99.9
2.01-2.08
3.7
0.233
3.3
9267
2509
0.233
99.7
2.08-2.15
3.7
0.204
3.7
8983
2449
0.204
99.9
2.15-2.23
3.7
0.178
4.2
8724
2373
0.178
99.8
2.23-2.32
3.7
0.163
4.5
8316
2252
0.163
99.9
2.32-2.43
3.7
0.146
5
8062
2201
0.146
100
2.43-2.55
3.7
0.132
5.4
7739
2102
0.132
100
2.55-2.68
3.7
0.113
6.3
7339
2009
0.113
99.9
2.68-2.85
3.7
0.099
7.1
6930
1893
0.099
99.9
2.85-3.04
3.6
0.088
7.7
6559
1808
0.088
100
3.04-3.29
3.6
0.075
8.7
6027
1660
0.075
100
3.29-3.6
3.6
0.065
9.9
5625
1557
0.065
100
3.6-4.02
3.5
0.061
10
5082
1433
0.061
100
4.02-4.65
3.6
0.057
10.9
4466
1247
0.057
99.9
4.65-5.69
3.5
0.064
9.2
3791
1085
0.064
99.9
5.69-8.05
3.4
0.072
7.8
2896
858
0.072
99.8
8.05-29.21
3.1
0.064
8.7
1539
501
0.064
97.2
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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
5.2.0019
精密化
PHENIX
精密化
SHELX
位相決定
MolProbity
3beta29
モデル構築
SCALA
3.2.5
データスケーリング
PDB_EXTRACT
3.006
データ抽出
MOSFLM
データ削減
SHELXD
位相決定
autoSHARP
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.8→29.21 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.931 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 5.232 / SU ML: 0.086 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.134 / ESU R Free: 0.128 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. ACETATE FROM THE CRYSTALLIZATION BUFFER IS MODELED INTO THE STRUCTURE. 4. ELECTRON DENSITY CORRESPONDING TO GLY 121 ON THE B-SUBUNIT IS DISORDERED; THEREFORE, THIS RESIDUE WAS NOT MODELED. 5. ELECTRON DENSITIES FOR GLY 0 MSE 1, SER 2, AND GLU 3 AT THE N-TERMINUS OF BOTH SUBUNITS IN THE ASYMMETRIC UNIT ARE DISORDERED; THERFORE THESE RESIDUES WERE NOT MODELED. 6.ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
Rfactor
反射数
%反射
Selection details
Rfree
0.215
1941
5 %
RANDOM
Rwork
0.171
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obs
0.173
38743
99.78 %
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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: MASK