SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
CONTRIBUTES TO THE HYDROLYSIS OF HEMICELLULOSE, WHICH IS THE MAJOR COMPONENT OF PLANT CELL-WALLS. ...CONTRIBUTES TO THE HYDROLYSIS OF HEMICELLULOSE, WHICH IS THE MAJOR COMPONENT OF PLANT CELL-WALLS. XLNA AND XLNB SEEM TO ACT SEQUENTIALLY ON THE SUBSTRATE TO YIELD XYLOBIOSE AND XYLOSE AS CARBON SOURCES.
配列の詳細
THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE ...THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE PDB FILE IS AFTER CLEAVAGE OF THE SIGNAL PEPTIDE. RESIDUE 1 AND THE LAST 11 RESIDUES ARE TOO DISORDERED TO BE BUILT IN DENSITY
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実験情報
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実験
実験
手法: X線回折 / 使用した結晶の数: 1
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試料調製
結晶
マシュー密度: 1.9 Å3/Da / 溶媒含有率: 35.3 % / 解説: STRUCTURE ISOMORPHOUS WITH STARTING MODEL
解像度: 1.03→27.15 Å / Cor.coef. Fo:Fc: 0.985 / Cor.coef. Fo:Fc free: 0.978 / SU B: 0.712 / SU ML: 0.016 / 交差検証法: THROUGHOUT / ESU R: 0.022 / ESU R Free: 0.024 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUE 1 AND THE LAST 11 RESIDUES ARE TOO DISORDERED TO BE BUILT IN DENSITY A CIS-PEPTIDE BOND BETWEEN RESIDUES 89 AND 90 IS MANIFESTED ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUE 1 AND THE LAST 11 RESIDUES ARE TOO DISORDERED TO BE BUILT IN DENSITY A CIS-PEPTIDE BOND BETWEEN RESIDUES 89 AND 90 IS MANIFESTED BECAUSE THE MAIN CHAIN IS BUILT IN DOUBLE CONFORMATION.
Rfactor
反射数
%反射
Selection details
Rfree
0.137
6421
5 %
RANDOM
Rwork
0.114
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obs
0.115
122389
96.9 %
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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: BABINET MODEL WITH MASK