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.
解像度: 2.1→27.308 Å / Num. obs: 13007 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 51.74 Å2 / Rmerge(I) obs: 0.038 / Net I/σ(I): 15.82
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
2.1-2.17
0.717
2
8271
2199
1
98.2
2.17-2.26
0.508
2.9
9601
2500
1
99.8
2.26-2.36
0.396
3.7
9048
2356
1
99.8
2.36-2.49
0.311
4.6
9632
2507
1
99.9
2.49-2.64
0.221
6.7
8893
2317
1
100
2.64-2.85
0.135
10.3
9426
2462
1
100
2.85-3.13
0.074
17
9047
2354
1
99.9
3.13-3.59
0.038
27.1
9296
2423
1
99.7
3.59-4.51
0.024
39
9004
2362
1
99.3
4.51-27.308
0.022
45.2
8880
2361
1
96.1
-
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
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
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: 2.1→27.308 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.943 / SU B: 9.222 / SU ML: 0.121 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.167 / ESU R Free: 0.168 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. RESIDUES 0 TO 2, 103 TO 115, 137 TO 145, 171 TO 193 ARE DISORDERED AND NOT MODELED IN THE STRUCTURE.
Rfactor
反射数
%反射
Selection details
Rfree
0.259
631
4.9 %
RANDOM
Rwork
0.204
-
-
-
obs
0.207
12970
99.46 %
-
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: 56.22 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-0.05 Å2
0 Å2
0 Å2
2-
-
-0.05 Å2
0 Å2
3-
-
-
0.09 Å2
精密化ステップ
サイクル: LAST / 解像度: 2.1→27.308 Å
タンパク質
核酸
リガンド
溶媒
全体
原子数
1076
0
0
42
1118
拘束条件
Refine-ID
タイプ
Dev ideal
Dev ideal target
数
X-RAY DIFFRACTION
r_bond_refined_d
0.017
0.022
1120
X-RAY DIFFRACTION
r_bond_other_d
0.001
0.02
755
X-RAY DIFFRACTION
r_angle_refined_deg
1.682
1.986
1519
X-RAY DIFFRACTION
r_angle_other_deg
0.925
3
1856
X-RAY DIFFRACTION
r_dihedral_angle_1_deg
4.527
5
150
X-RAY DIFFRACTION
r_dihedral_angle_2_deg
31.126
24.419
43
X-RAY DIFFRACTION
r_dihedral_angle_3_deg
13.745
15
189
X-RAY DIFFRACTION
r_dihedral_angle_4_deg
20.623
15
9
X-RAY DIFFRACTION
r_chiral_restr
0.093
0.2
178
X-RAY DIFFRACTION
r_gen_planes_refined
0.005
0.02
1262
X-RAY DIFFRACTION
r_gen_planes_other
0.001
0.02
202
X-RAY DIFFRACTION
r_nbd_refined
0.208
0.3
179
X-RAY DIFFRACTION
r_nbd_other
0.201
0.3
724
X-RAY DIFFRACTION
r_nbtor_refined
0.168
0.5
525
X-RAY DIFFRACTION
r_nbtor_other
0.094
0.5
603
X-RAY DIFFRACTION
r_xyhbond_nbd_refined
0.142
0.5
60
X-RAY DIFFRACTION
r_symmetry_vdw_refined
0.179
0.3
14
X-RAY DIFFRACTION
r_symmetry_vdw_other
0.359
0.3
29
X-RAY DIFFRACTION
r_symmetry_hbond_refined
0.295
0.5
8
X-RAY DIFFRACTION
r_mcbond_it
2.166
3
769
X-RAY DIFFRACTION
r_mcbond_other
0.489
3
303
X-RAY DIFFRACTION
r_mcangle_it
3.499
5
1195
X-RAY DIFFRACTION
r_scbond_it
6.29
8
388
X-RAY DIFFRACTION
r_scangle_it
8.888
11
324
LS精密化 シェル
解像度: 2.1→2.154 Å / Total num. of bins used: 20
Rfactor
反射数
%反射
Rfree
0.403
53
-
Rwork
0.293
882
-
obs
-
935
98.32 %
精密化 TLS
手法: refined / Origin x: 54.534 Å / Origin y: 23.346 Å / Origin z: 10.278 Å