- PDB-4l1n: Crystal structure of a putative conserved lipoprotein (NT01CX_115... -
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データを開く
IDまたはキーワード:
読み込み中...
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基本情報
登録情報
データベース: PDB / ID: 4l1n
タイトル
Crystal structure of a putative conserved lipoprotein (NT01CX_1156) from Clostridium novyi NT at 2.70 A resolution
要素
Conserved lipoprotein, putative
キーワード
STRUCTURAL GENOMICS (構造ゲノミクス) / UNKNOWN FUNCTION / PF15525 family protein / DUF4652 / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
機能・相同性
Uncharacterised protein PF15525, DUF4652 / Protein of unknown function DUF4652 / Domain of unknown function (DUF4652) / Lipocalin / membrane => GO:0016020 / Βバレル / Mainly Beta / Conserved lipoprotein, putative
THE CONSTRUCT (36-240) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...THE CONSTRUCT (36-240) 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 Si(111) / 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: 0.9794 Å / 相対比: 1
反射
解像度: 2.7→44.915 Å / Num. obs: 14440 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 81.523 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 11.41
反射 シェル
Rmerge(I) obs: 0.011 / Diffraction-ID: 1
解像度 (Å)
最高解像度 (Å)
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
2.7-2.77
1.8
5580
1073
99.7
2.77-2.85
2
5259
1013
99.4
2.85-2.93
2.5
5216
1008
99.9
2.93-3.02
3.6
4929
961
99.4
3.02-3.12
4.8
4795
946
99.1
3.12-3.23
5.7
4198
910
99.3
3.23-3.35
8.5
4392
891
99.3
3.35-3.49
10.6
4550
846
100
3.49-3.64
12.4
4413
829
100
3.64-3.82
14.9
4067
772
100
3.82-4.03
16.1
3860
742
99.9
4.03-4.27
18.2
3664
717
99.7
4.27-4.56
20.6
3211
658
98.9
4.56-4.93
20.1
2740
622
99.5
4.93-5.4
21.2
3028
574
99.8
5.4-6.04
20.4
2703
527
100
6.04-6.97
21.5
2345
466
99.6
6.97-8.54
23.6
1856
395
99.5
8.54-12.08
27.1
1434
310
98.4
12.08
28.4
857
180
97.3
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位相決定
位相決定
手法: 単波長異常分散
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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
BUSTER-TNT
2.10.0
精密化
XDS
データ削減
SHELXD
位相決定
BUSTER
2.10.0
精密化
精密化
構造決定の手法: 単波長異常分散 / 解像度: 2.7→44.915 Å / Cor.coef. Fo:Fc: 0.9128 / Cor.coef. Fo:Fc free: 0.9078 / Occupancy max: 1 / Occupancy min: 0.75 / 交差検証法: THROUGHOUT / σ(F): 0 詳細: 1. 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 ...詳細: 1. 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. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 4. THE N-TERMINAL RESIDUES (36-79) ARE DISORDERED.