- PDB-3bos: Crystal structure of a putative dna replication regulator HDA (SA... -
+
データを開く
IDまたはキーワード:
読み込み中...
-
基本情報
登録情報
データベース: PDB / ID: 3bos
タイトル
Crystal structure of a putative dna replication regulator HDA (SAMA_1916) from Shewanella amazonensis sb2b at 1.75 A resolution
要素
Putative DNA replication factor
キーワード
HYDROLASE REGULATOR / DNA BINDING PROTEIN / P-LOOP CONTAINING NUCLEOSIDE TRIPHOSPHATE HYDROLASES / STRUCTURAL GENOMICS / JOINT CENTER FOR STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI-2
機能・相同性
機能・相同性情報
DNA replication origin binding / DNA replication initiation / negative regulation of DNA-templated DNA replication initiation / nucleotide binding / metal ion binding / plasma membrane 類似検索 - 分子機能
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
0.97932
1
2
0.91837
1
反射
解像度: 1.75→29.553 Å / Num. obs: 55436 / % possible obs: 99.7 % / 冗長度: 3.7 % / Biso Wilson estimate: 19.79 Å2 / Rmerge(I) obs: 0.102 / Rsym value: 0.102 / Net I/σ(I): 5.2
反射 シェル
Diffraction-ID: 1
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
1.75-1.8
3.7
0.643
1.2
14990
4067
0.643
100
1.8-1.84
3.7
0.54
1.4
14585
3950
0.54
100
1.84-1.9
3.7
0.439
1.7
14304
3864
0.439
100
1.9-1.96
3.7
0.328
2.2
13806
3738
0.328
100
1.96-2.02
3.7
0.26
2.9
13380
3628
0.26
100
2.02-2.09
3.7
0.212
3.5
12948
3502
0.212
100
2.09-2.17
3.7
0.174
4.3
12673
3421
0.174
100
2.17-2.26
3.7
0.156
4.4
12019
3250
0.156
100
2.26-2.36
3.7
0.137
5.3
11765
3173
0.137
100
2.36-2.47
3.7
0.122
5.9
11174
3015
0.122
100
2.47-2.61
3.7
0.11
6.5
10633
2855
0.11
99.9
2.61-2.77
3.7
0.098
6.9
10146
2744
0.098
99.9
2.77-2.96
3.7
0.093
6.9
9375
2538
0.093
99.9
2.96-3.2
3.7
0.087
7.2
8864
2395
0.087
99.7
3.2-3.5
3.7
0.073
8.3
8185
2213
0.073
99.5
3.5-3.91
3.7
0.063
9.7
7377
1991
0.063
99.5
3.91-4.52
3.7
0.063
9.2
6477
1761
0.063
98.7
4.52-5.53
3.7
0.061
9.5
5494
1499
0.061
98.2
5.53-7.83
3.6
0.064
9.7
4174
1174
0.064
97.9
7.83-29.553
3.4
0.06
9.7
2221
658
0.06
94.1
-
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
SCALA
データスケーリング
PDB_EXTRACT
3
データ抽出
MAR345
CCD
データ収集
MOSFLM
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: 1.75→29.553 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.946 / SU B: 4.072 / SU ML: 0.072 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.104 / ESU R Free: 0.103 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. CDP AND MAGNESIUM ARE MODELED BASED ON ELECTRON DENSITY, HOMOLOGOUS STRUCTURES, COORDINATION AS WELL AS HYDROGEN BONDING. THE CDP DENSITY CAN ALSO FIT UDP, BUT WITH SLIGHTLY LESS FAVORABLE HYDROGEN BOND INTERACTIONS. 5. CHLORIDE, SODIUM, ETHYLENE GLYCOL (EDO) AND THIOCYNATE (SCN) ARE PRESENT IN THE CRYSTALLIZATION/CRYO CONDITIONS. 6. THE DENSITY FOR RESIDUES A32-33, B102-103 ARE POOR. THE MODEL WAS BUILT BASED ON THE OTHER WELL ORDERED SUBUNIT.
Rfactor
反射数
%反射
Selection details
Rfree
0.201
2813
5.1 %
RANDOM
Rwork
0.166
-
-
-
obs
0.168
55402
99.54 %
-
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