解像度: 1.55→1.57 Å / Rmerge(I) obs: 0.266 / Num. unique all: 664 / % possible all: 37.1
反射
*PLUS
Num. obs: 30523 / Rmerge(I) obs: 0.083
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解析
ソフトウェア
名称
バージョン
分類
bioteX
データ収集
bioteX
データ削減
X-PLOR
3.851
精密化
bioteX
データスケーリング
精密化
構造決定の手法: フーリエ合成 / 解像度: 1.5→7 Å / σ(F): 1.6 / 立体化学のターゲット値: X-PLOR force field 詳細: Residues simultaneously refined in two or more conformations are: Val53, Leu66, Ser86, Lys87, Ser110, Ser113, Ser130, Lys159, Asp165, Ser170, Gln175, Ser217, Lys230, Ser236, Ser244 Note that ...詳細: Residues simultaneously refined in two or more conformations are: Val53, Leu66, Ser86, Lys87, Ser110, Ser113, Ser130, Lys159, Asp165, Ser170, Gln175, Ser217, Lys230, Ser236, Ser244 Note that HOH383 makes short H-bonds to OgSer195 and O6' of the inhibitor Disordered waters are: HOH249 which is close to HOH250; HOH372 which is close to HOH373; HOH397 which is close to HOH398; HOH399 which is close to HOH400; sulfate_458 which is close to HOH459; HOH536 which is close to HOH537; HOH647 which is close to HOH648; HOH667 which is close to HOH668; HOH679 which is close to HOH680; HOH684 which is close to HOH685; HOH797 which is close to HOH798 which is close to HOH799; HOH902 which is close to HOH903; HOH947 which is close to HOH948; His40 and HIS91 are MONOPROTONATED ON THE EPSILON NITROGEN. His57 is doubly protonated.