RT Journal Article
SR Electronic
T1 Methods for estimation of model accuracy in CASP12
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 143925
DO 10.1101/143925
A1 Arne Elofsson
A1 Keehyoung Joo
A1 Chen Keasar
A1 Jooyoung Lee
A1 Ali H. A. Maghrabi
A1 Balachandran Manavalan
A1 Liam J. McGuffin
A1 David Ménendez Hurtado
A1 Claudio Mirabello
A1 Robert Pilstål
A1 Tomer Sidi
A1 Karolis Uziela
A1 Björn Wallner
YR 2017
UL http://biorxiv.org/content/early/2017/05/30/143925.abstract
AB Methods for reliably estimating the quality of 3D models of proteins are essential drivers for the wide adoption and serious acceptance of protein structure predictions by life scientists. In this paper, the most successful groups in CASP12 describe their latest methods for Estimates of Model Accuracy (EMA). We show that pure single model accuracy estimation methods have shown clear progress since CASP11; the three top methods (MESHI, ProQ3, SVMQA) all perform better than the top method of CASP11 (ProQ2). The pure single model accuracy estimation methods outperform quasi-single (ModFOLD6 variations) and consensus methods (Pcons,ModFOLDclust2, Pcomb-domain and Wallner) in model selection, but are still not as good as those methods in absolute model quality estimation and predictions of local quality. Finally, we show that the correlation of the best consensus, combined and quasi-single methods with model quality measures is higher than between different model quality measures when it comes to global correlation. However, for local accuracy estimation there still room for improvement.