BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 ... BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). SIZE EXCLUSION CHROMATOGRAPHY AND STATIC LIGHT SCATTERING SUPPORT THE ASSIGNMENT OF A DIMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
Remark 999
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.
モノクロメーター: Single crystal Si(111) bent (horizontal focusing) プロトコル: MAD / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
ID
波長 (Å)
相対比
1
0.94642
1
2
0.97925
1
3
0.97902
1
反射
解像度: 2.2→28.341 Å / Num. obs: 22404 / % possible obs: 94.2 % / Biso Wilson estimate: 47.699 Å2 / Rmerge(I) obs: 0.035 / Net I/σ(I): 13.88
反射 シェル
Diffraction-ID: 1
解像度 (Å)
最高解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique all
% possible all
2.2-2.27
0.29
2.8
5582
3464
76.4
2.27-2.36
0.239
3.3
7255
4079
93.3
2.36-2.47
0.206
3.9
7675
4323
94.6
2.47-2.6
0.151
5.2
7496
4200
94.5
2.6-2.76
0.121
6.5
7441
4167
95.1
2.76-2.97
0.086
8.9
7645
4277
97
2.97-3.27
0.051
14
7888
4413
98.1
3.27-3.74
0.03
21.9
7864
4381
98.9
3.74
0.019
31.4
7961
4385
99
-
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
MolProbity
3beta29
モデル構築
SHELX
位相決定
REFMAC
5.2.0019
精密化
XSCALE
データスケーリング
PDB_EXTRACT
2
データ抽出
MAR345
CCD
データ収集
XDS
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→28.341 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.928 / SU B: 19.299 / SU ML: 0.226 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.324 / ESU R Free: 0.228 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. GOL AND CL ARE MODELED BASED ON CRYSTALLIZATION AND CRYO CONDITIONS. 5. THE FOLLOWING REGIONS HAVE VERY POOR DENSITIES: A51-A62, A190-A206, B39-B63 AND B192-B204. 6. THERE ARE SOME RESIDUAL DENSITIES IN THE PUTATIVE ACTIVE SITES NEAR RESIDUES 16, 18. THEY ARE NOT MODELED DUE TO THE POOR DENSITY.
Rfactor
反射数
%反射
Selection details
Rfree
0.247
1148
5.1 %
RANDOM
Rwork
0.201
-
-
-
all
0.203
-
-
-
obs
0.203
22404
99.2 %
-
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