- PDB-3fcn: Crystal structure of an alpha-helical protein of unknown function... -
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IDまたはキーワード:
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基本情報
登録情報
データベース: PDB / ID: 3fcn
タイトル
Crystal structure of an alpha-helical protein of unknown function (rru_a3208) from rhodospirillum rubrum atcc 11170 at 1.45 A resolution
要素
an alpha-helical protein of unknown function (Pfam01724)
キーワード
UNKNOWN FUNCTION / Duf29 family protein / structural genomics (構造ゲノミクス) / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2
機能・相同性
Uncharcterised protein PF01724 / Protein from unkown function DUF29 / Domain of unknown function DUF29 / Malate Synthase G; Chain: A; Domain 4 / Up-down Bundle / Mainly Alpha / Uncharacterized protein
THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...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.
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
0.97882
1
3
0.97828
1
反射
解像度: 1.45→26.343 Å / Num. obs: 39973 / % possible obs: 100 % / 冗長度: 3.6 % / Biso Wilson estimate: 13.896 Å2 / Rmerge(I) obs: 0.082 / Rsym value: 0.082 / Net I/σ(I): 5.67
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
1.45-1.49
3.6
0.549
1.3
10528
2899
0.549
100
1.49-1.53
3.6
0.439
1.7
10350
2845
0.439
100
1.53-1.57
3.6
0.395
1.9
10045
2759
0.395
100
1.57-1.62
3.6
0.341
2.2
9833
2700
0.341
100
1.62-1.67
3.7
0.28
2.6
9478
2594
0.28
100
1.67-1.73
3.6
0.249
2.9
9278
2548
0.249
100
1.73-1.8
3.6
0.211
3.5
8863
2429
0.211
100
1.8-1.87
3.6
0.171
4.2
8586
2353
0.171
100
1.87-1.96
3.6
0.14
5.2
8242
2261
0.14
100
1.96-2.05
3.6
0.105
6.6
7839
2161
0.105
100
2.05-2.16
3.6
0.089
7.6
7513
2071
0.089
100
2.16-2.29
3.6
0.084
7.8
7117
1972
0.084
100
2.29-2.45
3.6
0.08
7.8
6610
1836
0.08
100
2.45-2.65
3.6
0.075
8.4
6251
1727
0.075
100
2.65-2.9
3.6
0.063
9.8
5774
1594
0.063
100
2.9-3.24
3.6
0.055
10.6
5266
1455
0.055
100
3.24-3.74
3.6
0.055
10.6
4636
1288
0.055
100
3.74-4.59
3.5
0.051
11.8
3937
1110
0.051
99.9
4.59-6.48
3.5
0.053
11.4
3042
872
0.053
99.4
6.48-29.67
3.2
0.047
12.2
1599
499
0.047
97.1
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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
REFMAC
5.5.0053
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: 1.45→26.343 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.961 / Occupancy max: 1 / Occupancy min: 0.18 / SU B: 2.235 / SU ML: 0.038 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.056 / ESU R Free: 0.058 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. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY.
Rfactor
反射数
%反射
Selection details
Rfree
0.184
2002
5 %
RANDOM
Rwork
0.161
-
-
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obs
0.162
39934
99.88 %
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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