Crystal structure of putative nucleic acid-binding lipoprotein (YP_001337197.1) from Klebsiella pneumoniae subsp. pneumoniae MGH 78578 at 2.46 A resolution
要素
putative nucleic acid-binding lipoprotein
キーワード
DNA BINDING PROTEIN / YP_001337197.1 / putative nucleic acid-binding lipoprotein / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2 / Unknown function
機能・相同性
Protein of unknown function, OB-fold-containing / tRNA_anti-like / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Mainly Beta / DI(HYDROXYETHYL)ETHER / Uncharacterized protein
AUTHORS STATE THAT THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 10 CHAINS FORMING A DIMER OF STACKED PENTAMERIC RINGS. HOWEVER, QUATERNARY STRUCTURE ANALYSIS USING THE PISA SERVER AND ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORT THE ASSIGNMENT OF A MONOMER AS THE LIKELY STABLE FORM.
THIS CONSTRUCT IS COMPRISED OF RESIDUES 23-154 OF THE FULL-LENGTH PROTEIN 1-154. IT WAS EXPRESSED ...THIS CONSTRUCT IS COMPRISED OF RESIDUES 23-154 OF THE FULL-LENGTH PROTEIN 1-154. IT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
モノクロメーター: Double crystal monochromator / プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.9792 Å / 相対比: 1
反射
解像度: 2.46→29.881 Å / Num. obs: 68362 / % possible obs: 99.8 % / 冗長度: 7.5 % / Biso Wilson estimate: 50.365 Å2 / Rmerge(I) obs: 0.111 / Rsym value: 0.111 / Net I/σ(I): 4.443
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
2.46-2.52
7.6
0.696
1.1
37475
4955
0.696
99.7
2.52-2.59
7.6
0.551
1.4
36830
4870
0.551
99.8
2.59-2.67
7.6
0.482
1.4
35803
4742
0.482
99.9
2.67-2.75
7.5
0.372
2
34809
4619
0.372
99.9
2.75-2.84
7.6
0.302
2.5
33735
4465
0.302
99.9
2.84-2.94
7.5
0.249
3.1
32710
4333
0.249
100
2.94-3.05
7.5
0.202
3.8
31592
4188
0.202
100
3.05-3.18
7.5
0.156
4.8
30439
4039
0.156
100
3.18-3.32
7.5
0.121
6.1
29123
3868
0.121
100
3.32-3.48
7.5
0.109
3.1
27873
3723
0.109
100
3.48-3.67
7.5
0.095
3
26529
3538
0.095
100
3.67-3.89
7.5
0.082
4.1
25103
3363
0.082
100
3.89-4.16
7.4
0.076
7.7
23373
3147
0.076
100
4.16-4.49
7.4
0.071
8.9
21882
2956
0.071
100
4.49-4.92
7.4
0.068
9.4
20286
2747
0.068
100
4.92-5.5
7.3
0.065
10.3
18059
2463
0.065
100
5.5-6.35
7.2
0.075
8.8
15824
2190
0.075
99.7
6.35-7.78
7.1
0.07
9.1
13310
1877
0.07
99.6
7.78-11
6.9
0.058
10.3
10277
1481
0.058
99.2
11-29.881
6.2
0.06
9.4
4964
798
0.06
93
-
位相決定
位相決定
手法: 単波長異常分散
-
解析
ソフトウェア
名称
バージョン
分類
NB
REFMAC
5.2.0019
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: 単波長異常分散 / 解像度: 2.46→29.881 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.927 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 12.325 / SU ML: 0.142 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.287 / ESU R Free: 0.218 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.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...詳細: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.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. 4.PEG (PEG600 FRAGMENTS) FROM THE CRYSTALLIZATION CONDITION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE.
Rfactor
反射数
%反射
Selection details
Rfree
0.228
3458
5.1 %
RANDOM
Rwork
0.192
-
-
-
obs
0.194
68310
99.71 %
-
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: 1.5 Å / 溶媒モデル: MASK