SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
OUR SEQUENCE IS AN X-RAY SEQUENCE BASED ON THE ASSIGNMENT OF THE RESIDUES BY THEIR ELECTRON DENSITY. ...OUR SEQUENCE IS AN X-RAY SEQUENCE BASED ON THE ASSIGNMENT OF THE RESIDUES BY THEIR ELECTRON DENSITY. SOME AMBIGUITIES MAY EXIST. FURTHERMORE A DIFFERENT ISOFORM OF THE ENZYME MAY BE PRESENT IN THE CRYSTAL. THE SEQUENCE WAS ORIGINALLY IDENTIFIED DURING THE DETERMINATION OF THE STRUCTURE IN PDB ENTRY 1E4M.
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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: 3.2 Å3/Da / 溶媒含有率: 50 %
結晶化
手法: 蒸気拡散法, ハンギングドロップ法 / pH: 7 詳細: HANGING DROP METHOD, 12 MG/ML PROTEIN IN 30 MM HEPES, PH 6.5, 0.05 % NAN3, PRECIPITANT 66% SAT. AMMONIUM SULFATE, 100MM TRIS-HCL PH 7.0
解像度: 1.6→35 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 10000 / Isotropic thermal model: RESTRAINED / 交差検証法: THROUGHOUT / σ(F): 0 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: INHIBITOR TOPOLOGY AND PARAMETERS SAME AS IN ENTRY 1W9B, ONLY MOST OF THE ATOMS OF THE GLUCOSE GROUP HAVE BEEN DELETED. THE INHIBITOR HAS BEEN RENAMED FROM CGT TO SEH AFTER REFINEMENT