ENGINEERED RESIDUE IN CHAIN A, MET 229 TO ILE ENGINEERED RESIDUE IN CHAIN B, MET 229 TO ILE
配列の詳細
SINGLE MUTATION M229I
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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: 2.7 Å3/Da / 溶媒含有率: 54 % 解説: THE STRUCTURE WAS DETERMINED BY SHARP USING MERCURY SITES IDENTIFIED BY SHELXD. THE ANOMALOUS DIFFERENCES ARE INCLUDED IN THE DEPOSITED STRUCTURE FACTORS.
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 1.009 Å / 相対比: 1
反射
解像度: 1.8→20 Å / Num. obs: 63551 / % possible obs: 98.7 % / Observed criterion σ(I): 0 / 冗長度: 8 % / Biso Wilson estimate: 18.6 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 18
反射 シェル
解像度: 1.8→1.9 Å / 冗長度: 7.6 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 3.5 / % possible all: 97.9
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解析
ソフトウェア
名称
バージョン
分類
REFMAC
5.2.0019
精密化
MOSFLM
データ削減
SCALA
データスケーリング
SHARP
位相決定
精密化
構造決定の手法: 単波長異常分散 / 解像度: 1.8→12 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.938 / SU B: 2.481 / SU ML: 0.078 / 交差検証法: THROUGHOUT / ESU R: 0.13 / ESU R Free: 0.124 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE TWO MOLECULES IN THE ASYMMETRIC UNIT ARE RELATED BY A PSEUDO-TRANSLATIONAL VECTOR 0.5,0.45,0.5, BUT HAVE BEEN REFINED INDIVDUALLY. ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE TWO MOLECULES IN THE ASYMMETRIC UNIT ARE RELATED BY A PSEUDO-TRANSLATIONAL VECTOR 0.5,0.45,0.5, BUT HAVE BEEN REFINED INDIVDUALLY. RESIDUES A291-A292 AND B290- B293 WERE DISORDERED. THE TWO PROTEIN MONOMERS IN THE ASYMMETRIC UNIT ARE RELATED BY A PSEUDO-TRANSLATIONAL VECTOR (0.5, 0.45, 0.5). THE TWO MONOMERS WERE REFINED INDIVIDUALLY.
Rfactor
反射数
%反射
Selection details
Rfree
0.223
3203
5.1 %
RANDOM
Rwork
0.185
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obs
0.187
60152
98.4 %
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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: 1.4 Å / 溶媒モデル: MASK