THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN FORMING A DIMER. CRYSTAL PACKING ANALYSIS SUGGESTS THAT A DIMER IS THE STABLE OLIGOMERIC FORM IN SOLUTION.
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 THE TARGET SEQUENCE.
解像度: 1.89→29.709 Å / Num. obs: 47086 / % possible obs: 99.9 % / 冗長度: 4.3 % / Rmerge(I) obs: 0.129 / Rsym value: 0.129 / Net I/σ(I): 5.451
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
1.89-1.95
3.6
0.845
0.9
12254
3423
0.845
100
1.95-2
4.4
0.627
1.2
14723
3355
0.627
100
2-2.06
4.4
0.533
1.4
14168
3231
0.533
100
2.06-2.12
4.4
0.441
1.7
13954
3174
0.441
100
2.12-2.19
4.4
0.356
2.2
13713
3107
0.356
100
2.19-2.27
4.4
0.312
2.5
12849
2938
0.312
100
2.27-2.36
4.4
0.283
2.7
12617
2888
0.283
100
2.36-2.45
4.4
0.254
3
12179
2755
0.254
100
2.45-2.56
4.4
0.21
3.7
11678
2665
0.21
100
2.56-2.69
4.4
0.185
4.1
11173
2564
0.185
100
2.69-2.83
4.4
0.16
4.8
10617
2425
0.16
100
2.83-3
4.4
0.133
5.6
10042
2303
0.133
100
3-3.21
4.4
0.098
7.3
9499
2182
0.098
100
3.21-3.47
4.3
0.08
8.8
8845
2038
0.08
100
3.47-3.8
4.3
0.061
11.2
8109
1877
0.061
100
3.8-4.25
4.3
0.053
12.5
7378
1714
0.053
99.9
4.25-4.91
4.3
0.051
12.3
6556
1529
0.051
99.8
4.91-6.01
4.2
0.059
11
5450
1294
0.059
99.7
6.01-8.5
4.2
0.054
12.2
4305
1036
0.054
99.4
8.5-29.709
3.8
0.042
14.8
2237
588
0.042
96.3
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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
SCALA
3.2.5
データスケーリング
PDB_EXTRACT
3.006
データ抽出
MAR345
CCD
データ収集
MOSFLM
データ削減
autoSHARP
位相決定
SHELXD
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.89→29.709 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.944 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 6.525 / SU ML: 0.098 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.14 / ESU R Free: 0.129 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. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3 .A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...詳細: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3 .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. 4. SULFATE (SO4) FROM THE CRYSTALLIZATION AND GLYCEROL (GOL) FROM THE CRYOPROTECTANT CONDITION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE. 5. AN UNIDENTIFIED LIGAND (UNL) HAS BEEN MODELED IN THE INTERFACE OF THE DIMER IN THE CRYSTAL STRUCTURE. THIS IS NOT THE PUTATIVE ACTIVE SITE OF THE PROTEIN.
Rfactor
反射数
%反射
Selection details
Rfree
0.207
2381
5.1 %
RANDOM
Rwork
0.171
-
-
-
obs
0.173
47036
99.47 %
-
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