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 SUPPORTS THE ASSIGNMENT OF A DIMER AS A 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
0.91837
1
2
0.97928
1
3
0.97895
1
反射
解像度: 1.3→24.268 Å / Num. obs: 69476 / % possible obs: 94.5 % / 冗長度: 3.9 % / Rmerge(I) obs: 0.055 / Rsym value: 0.055 / Net I/σ(I): 7.2
反射 シェル
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
1.3-1.33
3.9
0.524
1.4
19923
5045
0.524
92.3
1.33-1.37
3.9
0.449
1.7
19343
4898
0.449
92.6
1.37-1.41
3.9
0.386
2
18968
4803
0.386
92.9
1.41-1.45
4
0.302
2.5
18369
4645
0.302
93.2
1.45-1.5
3.9
0.243
3.1
17911
4535
0.243
93.5
1.5-1.55
3.9
0.195
3.9
17354
4401
0.195
93.7
1.55-1.61
3.9
0.154
4.9
16729
4247
0.154
94.2
1.61-1.68
3.9
0.135
5.5
16312
4136
0.135
94.5
1.68-1.75
3.9
0.105
6.8
15640
3961
0.105
94.7
1.75-1.84
3.9
0.088
8.1
14885
3773
0.088
95.1
1.84-1.94
3.9
0.071
9.5
14342
3643
0.071
95.5
1.94-2.06
3.9
0.058
11.1
13600
3448
0.058
95.9
2.06-2.2
3.9
0.05
12.5
12660
3212
0.05
96.1
2.2-2.37
3.9
0.046
13.1
12005
3054
0.046
96.3
2.37-2.6
3.9
0.042
14.7
10946
2779
0.042
96.8
2.6-2.91
3.9
0.042
13.5
9943
2532
0.042
97.1
2.91-3.36
3.9
0.039
14.5
8825
2251
0.039
97.2
3.36-4.11
3.9
0.035
16.9
7468
1910
0.035
97.5
4.11-5.81
3.9
0.037
15.8
5599
1441
0.037
96.4
5.81-24.39
3.8
0.045
13.7
2897
762
0.045
92.9
-
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
SCALA
データスケーリング
PDB_EXTRACT
2
データ抽出
MAR345
CCD
データ収集
MOSFLM
データ削減
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: 1.3→24.268 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.968 / SU B: 1.985 / SU ML: 0.036 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.049 / ESU R Free: 0.05 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: 1. HYDROGENS HAVE BEEN ADDED IN 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 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 (SO4) AND ETHYLENE GLYCOL (EDO) MOLECULES FROM THE CRYSTALLIZATION BUFFER WERE MODELED INTO THE STRUCTURE. 5. UNEXPLAINED ELECTRON DENSITY NEAR RESIDUES MSE105 AND TRP150 IN SUBUNIT A WERE NOT MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.175
3498
5 %
RANDOM
Rwork
0.135
-
-
-
all
0.137
-
-
-
obs
0.137
69476
94.54 %
-
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