A: Protein of Unknown Function (DUF1696) with Pleckstrin-homology Domains B: Protein of Unknown Function (DUF1696) with Pleckstrin-homology Domains C: Protein of Unknown Function (DUF1696) with Pleckstrin-homology Domains D: Protein of Unknown Function (DUF1696) with Pleckstrin-homology Domains E: Protein of Unknown Function (DUF1696) with Pleckstrin-homology Domains ヘテロ分子
Component-ID: 1 / Ens-ID: 1 / End label comp-ID: LEU / Refine code: 4
Dom-ID
Beg label comp-ID
Auth asym-ID
Label asym-ID
Auth seq-ID
Label seq-ID
1
GLY
A
A
9 - 124
2 - 117
2
ALA
B
B
12 - 124
5 - 117
3
ASN
C
C
10 - 124
3 - 117
4
ALA
D
D
12 - 124
5 - 117
5
GLU
E
E
13 - 124
6 - 117
詳細
AUTHORS STATE THAT SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A PENTAMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
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. THE CLONED CONSTRUCT CONTAINS RESIDUES 9-124 OF THE FULL LENGTH PROTEIN.
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
0.97925
1
2
0.91837
1
3
0.97871
1
反射
解像度: 2→29.828 Å / Num. obs: 43831 / % possible obs: 97.9 % / Observed criterion σ(I): -3 / 冗長度: 4.05 % / Biso Wilson estimate: 31.07 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 11.19
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
2-2.07
0.638
1.5
16853
7885
1
95.9
2.07-2.15
0.469
2
17146
7960
1
97.2
2.15-2.25
0.346
2.8
18168
8425
1
98
2.25-2.37
0.268
3.5
17920
8315
1
97.9
2.37-2.52
0.213
4.3
18021
8341
1
98.2
2.52-2.71
0.146
6.2
17473
8085
1
98.3
2.71-2.99
0.092
9.6
18401
8508
1
98.4
2.99-3.42
0.048
16.5
17721
8189
1
98.5
3.42-4.3
0.026
27.7
17874
8232
1
98.5
4.3-29.83
0.019
37.1
18127
8307
1
97.9
-
位相決定
位相決定
手法: 多波長異常分散
-
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
XSCALE
データスケーリング
PDB_EXTRACT
3.004
データ抽出
XDS
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: 2→29.828 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.939 / SU B: 7.891 / SU ML: 0.113 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.176 / ESU R Free: 0.159 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. 4. MPD AND CL ARE PRESENT IN CRYSTALLIZATION CONDITION.
Rfactor
反射数
%反射
Selection details
Rfree
0.227
2200
5 %
RANDOM
Rwork
0.184
-
-
-
obs
0.186
43782
98.93 %
-
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