signal peptidase I / thylakoid membrane organization / signal peptide processing / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / serine-type endopeptidase activity / plasma membrane 類似検索 - 分子機能
Peptidase S26A, signal peptidase I, lysine active site / Signal peptidases I lysine active site. / Peptidase S26A, signal peptidase I / Signal peptidase, peptidase S26 / Peptidase S26A, signal peptidase I, conserved site / Signal peptidases I signature 3. / Peptidase S26A, signal peptidase I, serine active site / Signal peptidases I serine active site. / Peptidase S26 / LexA/Signal peptidase-like superfamily ...Peptidase S26A, signal peptidase I, lysine active site / Signal peptidases I lysine active site. / Peptidase S26A, signal peptidase I / Signal peptidase, peptidase S26 / Peptidase S26A, signal peptidase I, conserved site / Signal peptidases I signature 3. / Peptidase S26A, signal peptidase I, serine active site / Signal peptidases I serine active site. / Peptidase S26 / LexA/Signal peptidase-like superfamily / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein 類似検索 - ドメイン・相同性
alpha-maltose / Maltose/maltodextrin-binding periplasmic protein / Signal peptidase IB 類似検索 - 構成要素
THESE MUTATIONS ARE CONSEQUENCE OF PCR REACTION. THE MUTATION R393N WAS INTRODUCED TO STABILIZE THE ...THESE MUTATIONS ARE CONSEQUENCE OF PCR REACTION. THE MUTATION R393N WAS INTRODUCED TO STABILIZE THE LINKER REGION
解像度: 1.9→19.78 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.937 / WRfactor Rfree: 0.1953 / WRfactor Rwork: 0.1637 / FOM work R set: 0.8302 / SU B: 3.701 / SU ML: 0.104 / SU R Cruickshank DPI: 0.143 / SU Rfree: 0.1312 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.143 / ESU R Free: 0.131 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
Rfactor
反射数
%反射
Selection details
Rfree
0.2194
2503
5.1 %
RANDOM
Rwork
0.1879
46809
-
-
obs
0.1895
46809
99.83 %
-
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