BIOMOLECULE: 1 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM GENERATED ASSEMBLY INFORMATION ... BIOMOLECULE: 1 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON BURIED SURFACE AREA. THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 4 CHAINS. SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A TETRAMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
Remark 999
SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG.
モノクロメーター: Single crystal Si(111) bent (horizontal focusing) 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: 0.97916 Å / 相対比: 1
反射
解像度: 2.15→28.228 Å / Num. obs: 38522 / % possible obs: 100 % / 冗長度: 7.4 % / Rmerge(I) obs: 0.146 / Rsym value: 0.146 / Net I/σ(I): 4.2
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
2.15-2.21
7.4
1.024
0.7
21045
2832
1.024
100
2.21-2.27
7.4
0.9
0.8
20412
2740
0.9
100
2.27-2.33
7.4
0.818
0.9
19811
2668
0.818
100
2.33-2.4
7.4
0.756
1
19161
2573
0.756
100
2.4-2.48
7.5
0.678
1.1
18566
2492
0.678
100
2.48-2.57
7.5
0.483
1.6
18257
2447
0.483
100
2.57-2.67
7.4
0.391
1.9
17552
2363
0.391
100
2.67-2.78
7.5
0.34
2.2
16739
2245
0.34
100
2.78-2.9
7.4
0.268
2.8
16422
2212
0.268
100
2.9-3.04
7.5
0.214
3.5
15290
2051
0.214
100
3.04-3.21
7.4
0.152
4.9
14825
2003
0.152
100
3.21-3.4
7.4
0.118
6
14101
1902
0.118
100
3.4-3.63
7.4
0.1
7
12998
1761
0.1
100
3.63-3.93
7.3
0.087
7.4
12214
1666
0.087
100
3.93-4.3
7.3
0.077
8.5
11238
1531
0.077
100
4.3-4.81
7.3
0.066
8.9
10177
1403
0.066
100
4.81-5.55
7
0.086
7.4
8678
1235
0.086
100
5.55-6.8
6.8
0.086
7.4
7346
1079
0.086
100
6.8-9.62
6.7
0.065
7.5
5608
842
0.065
100
9.62-28.228
6.1
0.055
8
2929
477
0.055
96.2
-
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
データスケーリング
PDB_EXTRACT
2
データ抽出
MAR345
CCD
データ収集
MOSFLM
データ削減
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: 2.15→28.228 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.934 / SU B: 12.145 / SU ML: 0.153 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.209 / ESU R Free: 0.19 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 RECORD CONTAINS RESIDUAL B FACTORS ONLY. 4. ACETATE AND GLYCEROL ARE MODELED BASED ON CRYSTALLIZATION CONDITIONS.
Rfactor
反射数
%反射
Selection details
Rfree
0.252
1926
5 %
RANDOM
Rwork
0.2
-
-
-
all
0.203
-
-
-
obs
0.203
38482
100 %
-
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