Journal
NUCLEIC ACIDS RESEARCH
Volume 39, Issue -, Pages D465-D474Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq1091
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Categories
Funding
- National Institutes of Health [R01 GM54762, U54 GM074945, U54 GM074929, U01 GM61390, P01 GM71790, F32 GM088991, P41 RR001081]
- National Science Foundation [0732065]
- Department of Energy [DE-SC0004916]
- Sandler Family Supporting Foundation
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR001081] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM071790, U54GM074945, F32GM088991, R01GM054762, U01GM061390, U54GM074929] Funding Source: NIH RePORTER
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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).
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