- PDB-4h0a: Crystal structure of a cysteine-rich secretory protein (SAV1118) ... -
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基本情報
登録情報
データベース: PDB / ID: 4h0a
タイトル
Crystal structure of a cysteine-rich secretory protein (SAV1118) from Staphylococcus aureus subsp. aureus Mu50 at 1.90 A resolution
要素
Uncharacterized protein
キーワード
UNKNOWN FUNCTION / CAP protein family / cysteine-rich secretory proteins / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 24-345 OF THE TARGET SEQUENCE.
解像度: 1.9→29.181 Å / Num. obs: 52080 / % possible obs: 96.3 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 34.616 Å2 / Rmerge(I) obs: 0.036 / Net I/σ(I): 11.38
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
1.9-1.97
0.643
1.7
19008
10028
1
94.2
1.97-2.05
0.395
2.5
19688
10282
1
98
2.05-2.14
0.301
3.3
18340
9600
1
96.8
2.14-2.25
0.193
4.8
18899
9897
1
97.7
2.25-2.39
0.145
6.1
19021
9977
1
97.4
2.39-2.58
0.105
8
20011
10490
1
98
2.58-2.84
0.073
11.3
19135
10045
1
97
2.84-3.25
0.042
16.9
18809
9971
1
96.7
3.25-4.08
0.025
26.6
17843
9552
1
93.6
4.08-29.181
0.019
33.6
18960
9843
1
94
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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
December6, 2010
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: 多波長異常分散 / 解像度: 1.9→29.181 Å / Cor.coef. Fo:Fc: 0.9542 / Cor.coef. Fo:Fc free: 0.9374 / Occupancy max: 1 / Occupancy min: 0.4 / 交差検証法: THROUGHOUT / σ(F): 0 詳細: 1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF ...詳細: 1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS 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. NCS RESTRAINTS WERE APPLIED DURING REFINEMENT USING LSSR (-AUTONCS) IN BUSTER. 6. MAD PHASE RESTRAINTS WERE USED DURING REFINEMENT. 7. 1,2-ETHANEDIOL (EDO) MOLECULES FROM THE CRYOPROTECTION SOLUTION ARE MODELED. 8. THERE IS SOME UNMODELED ELECTRON DENSITY IN THE REGION NEAR PHE-87, VAL-304 AND GLN-227 IN BOTH CHAINS. 9. THE N-TERMINAL REGIONS (A29-A34 AND B25-B37) HAVE POOR ELECTRON DENSITY AND MAY CONTAIN REGISTER ERRORS.