- PDB-4q5t: Crystal structure of an atmB (putative membrane lipoprotein) from... -
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基本情報
登録情報
データベース: PDB / ID: 4q5t
タイトル
Crystal structure of an atmB (putative membrane lipoprotein) from Streptococcus mutans UA159 at 1.91 A resolution
要素
Lipoprotein
キーワード
TRANSPORT PROTEIN / methionine-binding / NLPA lipoprotein / PF03180 family / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
THIS CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...THIS CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 25-280 OF THE TARGET SEQUENCE.
解像度: 1.91→28.777 Å / Num. obs: 23167 / % possible obs: 98 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 23.682 Å2 / Rmerge(I) obs: 0.057 / Net I/σ(I): 11.11
反射 シェル
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
Diffraction-ID
% possible all
1.91-1.98
0.448
2
10172
4385
1
96.6
1.98-2.06
0.31
2.7
10262
4401
1
99
2.06-2.15
0.243
3.6
9478
4093
1
96.4
2.15-2.26
0.168
5.2
9817
4212
1
97.7
2.26-2.41
0.132
6.2
10937
4652
1
98.9
2.41-2.59
0.098
8
9984
4228
1
99.2
2.59-2.85
0.075
10.6
10243
4367
1
98.5
2.85-3.26
0.049
15.4
10277
4370
1
99.2
3.26-4.1
0.031
24.8
9897
4280
1
96.2
4.1-28.777
0.022
32.3
10512
4406
1
98.1
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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
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
XSCALE
March15, 2012
データスケーリング
PHENIX
1.8.2
精密化
XDS
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: 1.907→28.777 Å / Occupancy max: 1 / Occupancy min: 0.5 / SU ML: 0.21 / σ(F): 1.22 / 位相誤差: 23.87 / 立体化学のターゲット値: MLHL 詳細: 1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORDS CONTAIN SUM OF ...詳細: 1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U FACTORS. 4. 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. 5. LIGAND SELENOMETHIONINE HAS BEEN MODELED BASED ON DENSITY AND ANOMALOUS DIFFERENCE FOURIER MAP. 6. NONAETHYLENE GLYCOL (2PE) MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE MODELED.
Rfactor
反射数
%反射
Rfree
0.2302
1189
5.14 %
Rwork
0.1827
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-
obs
0.185
23128
99.24 %
溶媒の処理
減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å / 溶媒モデル: FLAT BULK SOLVENT MODEL