SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ... SEQUENCE 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.
REMARK 999 SEQUENCE: THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION REMARK 999 TAG ...REMARK 999 SEQUENCE: THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. REMARK 999
解像度: 1.55→29.975 Å / Num. obs: 64534 / % possible obs: 100 % / 冗長度: 10.1 % / Biso Wilson estimate: 19.3 Å2 / Rmerge(I) obs: 0.083 / Rsym value: 0.083 / Net I/σ(I): 5.4
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
1.55-1.59
9.2
0.913
0.9
43050
4687
0.913
100
1.59-1.63
9.6
0.748
1
44104
4600
0.748
100
1.63-1.68
9.9
0.618
1.3
43612
4413
0.618
100
1.68-1.73
10.1
0.504
1.6
43920
4339
0.504
100
1.73-1.79
10.3
0.377
2.1
43196
4200
0.377
100
1.79-1.85
10.4
0.277
2.8
42534
4076
0.277
100
1.85-1.92
10.5
0.212
3.6
41002
3914
0.212
100
1.92-2
10.5
0.16
4.6
39966
3808
0.16
100
2-2.09
10.5
0.129
5.6
38425
3667
0.129
100
2.09-2.19
10.5
0.104
6.7
36260
3459
0.104
100
2.19-2.31
10.4
0.089
7.7
34692
3330
0.089
100
2.31-2.45
10.4
0.08
8.4
32908
3159
0.08
100
2.45-2.62
10.3
0.079
8.1
30757
2980
0.079
100
2.62-2.83
10.3
0.08
7.6
28637
2786
0.08
100
2.83-3.1
10.1
0.078
7.4
26109
2583
0.078
100
3.1-3.47
9.8
0.066
8.9
22862
2344
0.066
100
3.47-4
9.2
0.048
11.3
19274
2096
0.048
100
4-4.9
10.3
0.044
11
18595
1802
0.044
100
4.9-6.93
10.2
0.042
11.4
14693
1435
0.042
100
6.93-29.975
9.3
0.039
12.9
7962
856
0.039
98.8
-
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
5.3.0040
精密化
PHENIX
精密化
SOLVE
位相決定
MolProbity
3beta29
モデル構築
SCALA
データスケーリング
PDB_EXTRACT
3
データ抽出
ADSC
Quantum
データ収集
MOSFLM
データ削減
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.55→29.975 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.958 / SU B: 2.192 / SU ML: 0.042 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.064 / ESU R Free: 0.066 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 RECORD CONTAINS 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 RECORD CONTAINS 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. SULFATE ION FROM THE CRYSTALLIZATION CONDITIONS AND ETHYLENE GLYCOL FROM THE CRYO CONDITIONS ARE MODELED IN THE STRUCTURE. 5. UNKNOWN ELECTRON DENSITY NEAR RESIDUE 18 IN SUBUNIT A AND RESIDUE 14 IN SUBUNIT B IS NOT MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.196
3263
5.1 %
RANDOM
Rwork
0.17
-
-
-
obs
0.171
64447
99.97 %
-
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