title: Fams-ace: a combined method to select the best model after remodeling all server models.
abstract: During Critical Assessment of Protein Structure Prediction (CASP7, Pacific Grove, CA, 2006), fams-ace was entered in the 3D coordinate prediction category as a human expert group. The procedure can be summarized by the following three steps. (1) All the server models were refined and rebuilt utilizing our homology modeling method. (2) Representative structures were selected from each server, according to a model quality evaluation, based on a 3D1D profile score (like Verify3D). (3) The top five models were selected and submitted in the order of the consensus-based score (like 3D-Jury). Fams-ace is a fully automated server and does not require human intervention. In this article, we introduce the methodology of fams-ace and discuss the successes and failures of this approach during CASP7. In addition, we discuss possible improvements for the next CASP.
authors: School of Pharmacy, Kitasato University, Tokyo, Japan.
authors: Genki
authors: G
authors: Terashi
authors: Mayuko
authors: M
authors: Takeda-Shitaka
authors: Kazuhiko
authors: K
authors: Kanou
authors: Mitsuo
authors: M
authors: Iwadate
authors: Daisuke
authors: D
authors: Takaya
authors: Akio
authors: A
authors: Hosoi
authors: Kazuhiro
authors: K
authors: Ohta
authors: Hideaki
authors: H
authors: Umeyama
mesh_terms: D000465:Algorithms; D019295:Computational Biology / Q000379:methods*; D008958:Models, Molecular; D008962:Models, Theoretical; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D040681:Structural Homology, Protein
chemical_list: D011506:Proteins