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. THE CONSTRUCT CONTAINS RESIDUES 23-537 OF THE TARGET SEQUENCE.
解像度: 1.7→28.039 Å / Num. obs: 60062 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 15.794 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 10.61
反射 シェル
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
Diffraction-ID
% possible all
1.7-1.76
0.328
2.5
21187
11140
1
97.1
1.76-1.83
0.258
3.1
22031
11511
1
99.4
1.83-1.91
0.205
4
21462
11189
1
99.3
1.91-2.02
0.148
5.4
23980
12489
1
99.3
2.02-2.14
0.106
7.3
21043
10937
1
99.4
2.14-2.31
0.081
9.4
22875
11880
1
99.4
2.31-2.54
0.065
11.6
21982
11339
1
99.1
2.54-2.9
0.047
15
22053
11297
1
98.5
2.9-3.66
0.032
20.8
22647
11457
1
97.8
3.66-28.039
0.025
27.4
22465
11225
1
96
-
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
5.4.0067
精密化
PHENIX
精密化
SHELX
位相決定
MolProbity
3beta29
モデル構築
XSCALE
データスケーリング
PDB_EXTRACT
3
データ抽出
MAR345
CCD
データ収集
XDS
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: 1.7→28.039 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.96 / SU B: 2.99 / SU ML: 0.052 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.086 / ESU R Free: 0.083 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. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...詳細: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. 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. 3. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 4. ACT IS MODELED BASED ON CRYSTALLIZATION CONDITIONS. 5. ZN IS MODELED BASED ON AN X-RAY FLOURESCENCE SCAN, ANOMALOUS DIFFERENCE FOURIERS, AND COORDINATION GEOMETRY. 6. RESIDUE GLY 41 IS A RAMACHANDRAN OUTLIER, AND IS PRESENT IN POOR DENSITY.
Rfactor
反射数
%反射
Selection details
Rfree
0.166
3037
5.1 %
RANDOM
Rwork
0.14
-
-
-
obs
0.142
60025
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: MASK
原子変位パラメータ
Biso mean: 12.202 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-0.16 Å2
0 Å2
0 Å2
2-
-
0.65 Å2
0 Å2
3-
-
-
-0.49 Å2
精密化ステップ
サイクル: LAST / 解像度: 1.7→28.039 Å
タンパク質
核酸
リガンド
溶媒
全体
原子数
3943
0
5
704
4652
拘束条件
Refine-ID
タイプ
Dev ideal
Dev ideal target
数
X-RAY DIFFRACTION
r_bond_refined_d
0.016
0.022
4156
X-RAY DIFFRACTION
r_bond_other_d
0.001
0.02
2719
X-RAY DIFFRACTION
r_angle_refined_deg
1.521
1.933
5694
X-RAY DIFFRACTION
r_angle_other_deg
1.413
3
6655
X-RAY DIFFRACTION
r_dihedral_angle_1_deg
6.169
5
541
X-RAY DIFFRACTION
r_dihedral_angle_2_deg
40.212
25.268
205
X-RAY DIFFRACTION
r_dihedral_angle_3_deg
12.917
15
642
X-RAY DIFFRACTION
r_dihedral_angle_4_deg
18.925
15
17
X-RAY DIFFRACTION
r_chiral_restr
0.1
0.2
611
X-RAY DIFFRACTION
r_gen_planes_refined
0.009
0.021
4806
X-RAY DIFFRACTION
r_gen_planes_other
0.003
0.02
843
X-RAY DIFFRACTION
r_mcbond_it
0.774
1.5
2590
X-RAY DIFFRACTION
r_mcbond_other
0.268
1.5
1048
X-RAY DIFFRACTION
r_mcangle_it
1.289
2
4183
X-RAY DIFFRACTION
r_scbond_it
2.237
3
1566
X-RAY DIFFRACTION
r_scangle_it
3.597
4.5
1496
LS精密化 シェル
解像度: 1.7→1.744 Å / Total num. of bins used: 20
Rfactor
反射数
%反射
Rfree
0.212
228
-
Rwork
0.189
4096
-
all
-
4324
-
obs
-
-
97.61 %
精密化 TLS
手法: refined / Origin x: -19.915 Å / Origin y: -52.104 Å / Origin z: 20.37 Å