MOLPROBITY STRUCTURE VALIDATION PROGRAMS : MOLPROBITY (KING, REDUCE, AND PROBE) AUTHORS : I.W. ...MOLPROBITY STRUCTURE VALIDATION PROGRAMS : MOLPROBITY (KING, REDUCE, AND PROBE) AUTHORS : I.W.DAVIS,J.M.WORD URL : HTTP://KINEMAGE.BIOCHEM.DUKE.EDU/MOLPROBITY/ AUTHORS : J.S.RICHARDSON,W.B.ARENDALL,D.C.RICHARDSON REFERENCE : NEW TOOLS AND DATA FOR IMPROVING : STRUCTURES, USING ALL-ATOM CONTACTS : METHODS IN ENZYMOLOGY. 2003;374:385-412. MOLPROBITY OUTPUT SCORES: ALL-ATOM CLASHSCORE : 15.09 (9.18 B<40) BAD ROTAMERS : 9.0% 25/277 (TARGET 0-1%) RAMACHANDRAN OUTLIERS : 4.4% 14/318 (TARGET 0.2%) RAMACHANDRAN FAVORED : 85.8% 273/318 (TARGET 98.0%)
Remark 999
SEQUENCE The sequence of myosin A tail domain interacting protein is not available at SWS and ...SEQUENCE The sequence of myosin A tail domain interacting protein is not available at SWS and Gebank databases at the time of processing.
解像度: 2.6→2.739 Å / 冗長度: 9.6 % / Mean I/σ(I) obs: 3.9 / Rsym value: 0.799 / % possible all: 100
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解析
ソフトウェア
名称
バージョン
分類
REFMAC
5.2.0005
精密化
MOSFLM
データ削減
XDS
データスケーリング
SHELXS
位相決定
精密化
構造決定の手法: 単波長異常分散 / 解像度: 2.6→20 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.868 / SU B: 29.053 / SU ML: 0.311 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / ESU R: 0.993 / ESU R Free: 0.359 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: RESIDUES 156 - 159, 183, 185, 188, 189 OF CHAIN B WERE MODELED WITHOUT SIDE CHAINS AS NO SIDE CHAIN DENSITY IS OBSERVABLE.
Rfactor
反射数
%反射
Selection details
Rfree
0.28326
693
5 %
RANDOM
Rwork
0.22658
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-
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obs
0.22938
13219
99.93 %
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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