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, FOLLOWED BY THE TARGET SEQUENCE.
Remark 300
BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 ...BIOMOLECULE: 1, 2 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 WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
モノクロメーター: Single crystal Si(111) bent monochromator (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
0.91837
1
2
0.97932
1
3
0.9791
1
反射
解像度: 1.7→29.412 Å / Num. obs: 26996 / % possible obs: 98.2 % / Biso Wilson estimate: 30.103 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 19.02
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
1.7-1.76
0.628
3.1
33318
4479
90.9
1.76-1.83
0.507
4
37113
4885
98
1.83-1.91
0.424
4.9
35967
4733
98.1
1.91-2.02
0.286
7.2
40849
5375
98.3
2.02-2.14
0.188
10.7
35721
4699
99.2
2.14-2.31
0.128
15.4
38710
5087
99.4
2.31-2.54
0.087
20.9
37811
4931
99.6
2.54-2.9
0.066
27.8
37532
4900
99.6
2.9
0.042
41.3
38859
5061
99.7
-
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
XDS
データ削減
SHELXD
位相決定
SOLVE
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.7→29.412 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.931 / SU B: 3.327 / SU ML: 0.057 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.086 / ESU R Free: 0.09 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. CHLORIDE AND NO3 ARE MODELED BASED ON THE CRYSTALLIZATION CONDITIONS. 5. THERE ARE SOME UNINTERPRETED BLOBS OF DENSITY NEAR THE PROTEIN SURFACE. 6. A26,A30,A66 AND A/B70 SIDE CHAINS ARE MODELLED AS PARTIAL OCCUPANCY.
Rfactor
反射数
%反射
Selection details
Rfree
0.219
1351
5 %
RANDOM
Rwork
0.186
-
-
-
obs
0.188
26956
99.71 %
-
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