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.
解像度: 2.2→15.895 Å / Num. obs: 31068 / % possible obs: 95.6 % / 冗長度: 1.9 % / Biso Wilson estimate: 37.26 Å2 / Rmerge(I) obs: 0.066 / Rsym value: 0.066 / Net I/σ(I): 7.9
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
2.2-2.32
1.9
0.417
1.7
8679
4574
0.417
97.1
2.32-2.46
1.9
0.272
2.8
8233
4354
0.272
97
2.46-2.63
1.9
0.191
3.9
7727
4078
0.191
96.9
2.63-2.84
1.9
0.128
5.9
7214
3829
0.128
97.3
2.84-3.11
1.9
0.082
8.4
6596
3503
0.082
96.9
3.11-3.48
1.9
0.056
11.4
5922
3135
0.056
96
3.48-4.02
1.9
0.045
13.6
5178
2727
0.045
94.6
4.02-4.92
1.8
0.035
18.2
4129
2250
0.035
91.5
4.92-6.96
2
0.04
15.3
3561
1752
0.04
93
6.96-15.895
2.1
0.035
12.6
1826
872
0.035
82.5
-
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
SHELX
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
SHELXD
位相決定
SHARP
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.2→15.895 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.91 / SU B: 17.317 / SU ML: 0.223 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.329 / ESU R Free: 0.248 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. RESIDUES 0-1 IN CHAIN A, 0-1, 78-84 IN CHAIN B, 0-1 IN CHAIN C, AND 0-1, 78-85 IN CHAIN D ARE DISORDERED AND NOT INCLUDED IN THE MODEL. 5. GOL AND PO4 MOLECULES FROM THE CRYSTALLIZATION/CRYO SOLUTION ARE MODELED. 6. R-FACTORS ARE SLIGHTLY HIGH, ESPECIALLY NEAR 5.5 A RESOLUTION SHELL.
Rfactor
反射数
%反射
Selection details
Rfree
0.275
1581
5.1 %
RANDOM
Rwork
0.223
-
-
-
obs
0.225
31066
95.45 %
-
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: BABINET MODEL WITH MASK