ModBase, a database of annotated comparative protein structure models, and associated resources

作者：Pieper Ursula; Webb Benjamin M; Barkan David T; Schneidman Duhovny Dina; Schlessinger Avner; Braberg Hannes; Yang Zheng; Meng Elaine C; Pettersen Eric F; Huang Conrad C; Datta Ruchira S; Sampathkumar Parthasarathy; Madhusudhan Mallur S; Sjoelander Kimmen; Ferrin Thomas E; Burley Stephen K; Sali Andrej^*

来源：Nucleic Acids Research, 2011, 39(Database): D465-D474.

DOI：10.1093/nar/gkq1091

ModBase (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by ModPipe, an automated modeling pipeline that relies primarily on Modeller for fold assignment, sequence-structure alignment, model building and model assessment (http://salilab.org/modeller/). ModBase currently contains 10 355 444 reliable models for domains in 2 421 920 unique protein sequences. ModBase allows users to update comparative models on demand, and request modeling of additional sequences through an interface to the ModWeb modeling server (http://salilab.org/modweb). ModBase models are available through the ModBase interface as well as the Protein Model Portal (http://www.proteinmodelportal.org/). Recently developed associated resources include the SALIGN server for multiple sequence and structure alignment (http://salilab.org/salign), the ModEval server for predicting the accuracy of protein structure models (http://salilab.org/modeval), the PCSS server for predicting which peptides bind to a given protein (http://salilab.org/pcss) and the FoXS server for calculating and fitting Small Angle X-ray Scattering profiles (http://salilab.org/foxs).

• 出版日期2011-1