解像度: 1.85→1.94 Å / 冗長度: 2.23 % / Rmerge(I) obs: 0.175 / Mean I/σ(I) obs: 3.9 / Num. unique all: 8471 / Rsym value: 0.175 / % possible all: 70.2
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解析
ソフトウェア
名称
バージョン
分類
PHASES
位相決定
CNS
1.1
精密化
MAR345
345DTB
データ収集
DENZO
データ削減
SCALEPACK
データスケーリング
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.85→8 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 208869.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / 交差検証法: THROUGHOUT / σ(F): 2 / σ(I): 1 詳細: THIS DEPOSITION UPDATES THE COORDINATES OF 1L8A AFTER VALIDATION THROUGH MOLPROBITY (I. W. DAVIS ET AL., NUCL. ACIDS RES. 32, W615-W619, 2004) AND MINIMIZATION WITH CNS (BRUNGER ET AL. ACTA ...詳細: THIS DEPOSITION UPDATES THE COORDINATES OF 1L8A AFTER VALIDATION THROUGH MOLPROBITY (I. W. DAVIS ET AL., NUCL. ACIDS RES. 32, W615-W619, 2004) AND MINIMIZATION WITH CNS (BRUNGER ET AL. ACTA CRYST. D54, 905-921, 1998). THE MAIN DIFFERENCE BETWEEN THIS DEPOSITION AND THE ORIGINAL ONE IS THE INTERCHANGE OF NITROGEN AND OXYGEN ATOMS IN SOME AMIDE SIDE CHAINS, AND INTERCHANGE OF NITROGEN AND CARBON ATOMS IN SOME HISTIDINE SIDE CHAINS. THIS DEPOSITION IS BETTER SUITED FOR DETAILED COMPARISONS WITH THE APO AND INHIBITED STRUCTURES 2G67, 1RP7, 2G25 AND 2G28 AS THOSE SUBSEQUENTLY DETERMINED STRUCTURES WERE ALSO TREATED IN THE SAME MANNER. KEY STRUCTURAL DETAILS AND INTERACTIONS DESCRIBED IN OUR 2002 PAPER IN 'BIOCHEMISTRY' HOWEVER, REMAIN UNCHANGED.