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.
解像度: 1.76→30.429 Å / Num. obs: 26997 / % possible obs: 99.1 % / 冗長度: 7 % / Biso Wilson estimate: 18.647 Å2 / Rmerge(I) obs: 0.117 / Rsym value: 0.117 / Net I/σ(I): 4.323
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
1.73-1.77
3.6
0.441
1.7
7152
1973
0.441
97.6
1.77-1.82
6.2
0.469
1.5
11804
1911
0.469
98.9
1.82-1.88
7.4
0.41
1.8
13865
1872
0.41
98.9
1.88-1.93
7.5
0.318
2.2
13406
1796
0.318
98.2
1.93-2
7.5
0.274
2.4
13232
1775
0.274
98.6
2-2.07
7.5
0.23
3
12726
1708
0.23
99.2
2.07-2.15
7.4
0.205
3.3
12360
1662
0.205
99.4
2.15-2.23
7.4
0.188
3.7
11821
1589
0.188
99
2.23-2.33
7.4
0.167
4
11333
1528
0.167
99
2.33-2.45
7.4
0.157
4.3
10850
1467
0.157
99.3
2.45-2.58
7.4
0.133
5.1
10351
1401
0.133
99.5
2.58-2.74
7.4
0.12
5.4
9793
1321
0.12
99.5
2.74-2.92
7.3
0.109
5.9
9257
1261
0.109
99.8
2.92-3.16
7.3
0.095
6.4
8651
1183
0.095
99.9
3.16-3.46
7.3
0.084
7.2
7796
1065
0.084
99.7
3.46-3.87
7.3
0.074
7.7
7178
980
0.074
99.9
3.87-4.47
7.3
0.074
7.8
6201
853
0.074
99.9
4.47-5.47
7.2
0.078
7.3
5340
744
0.078
99.9
5.47-7.74
7
0.082
7.4
4087
580
0.082
100
7.74-30.429
6.4
0.08
6
2107
328
0.08
98.4
-
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
MOSFLM
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: 1.76→30.429 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.936 / Occupancy max: 1 / Occupancy min: 0.38 / SU B: 4.858 / SU ML: 0.081 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.128 / ESU R Free: 0.12 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. GOL MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE MODELED IN THE PUTATIVE ACTIVE SITE OF THE PROTEIN AND IT MAY REPRESENT THE SUBSTRATE OF THE PROTEIN. 5. THE N-TERMINUS OF CHAIN B SHOWS MULTIPLE ORDER. THIS HAS BEEN MODELED AS TWO CONFORMERS. FOR CONFORMER A, RESIDUES 3-6 HAVE BEEN MODELED WITH RESIDUES 0-2 OMITTED DUE TO DISORDER. FOR CONFORMER B, RESIDUES 1-6 HAVE BEEN MODELED WITH ONLY RESIDUE 0 OMITTED DUE TO DISORDER.
Rfactor
反射数
%反射
Selection details
Rfree
0.208
1358
5 %
RANDOM
Rwork
0.17
-
-
-
obs
0.172
26993
98.97 %
-
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: BABINET MODEL WITH MASK