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ModBase, a database of annotated comparative protein structure models, and associated resources
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://...
Autores principales: | , , , , , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013688/ https://www.ncbi.nlm.nih.gov/pubmed/21097780 http://dx.doi.org/10.1093/nar/gkq1091 |
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author | 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. Sjölander, Kimmen Ferrin, Thomas E. Burley, Stephen K. Sali, Andrej |
author_facet | 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. Sjölander, Kimmen Ferrin, Thomas E. Burley, Stephen K. Sali, Andrej |
author_sort | Pieper, Ursula |
collection | PubMed |
description | 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). |
format | Text |
id | pubmed-3013688 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-30136882011-01-03 ModBase, a database of annotated comparative protein structure models, and associated resources 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. Sjölander, Kimmen Ferrin, Thomas E. Burley, Stephen K. Sali, Andrej Nucleic Acids Res Articles 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). Oxford University Press 2011-01 2010-11-19 /pmc/articles/PMC3013688/ /pubmed/21097780 http://dx.doi.org/10.1093/nar/gkq1091 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles 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. Sjölander, Kimmen Ferrin, Thomas E. Burley, Stephen K. Sali, Andrej ModBase, a database of annotated comparative protein structure models, and associated resources |
title | ModBase, a database of annotated comparative protein structure models, and associated resources |
title_full | ModBase, a database of annotated comparative protein structure models, and associated resources |
title_fullStr | ModBase, a database of annotated comparative protein structure models, and associated resources |
title_full_unstemmed | ModBase, a database of annotated comparative protein structure models, and associated resources |
title_short | ModBase, a database of annotated comparative protein structure models, and associated resources |
title_sort | modbase, a database of annotated comparative protein structure models, and associated resources |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013688/ https://www.ncbi.nlm.nih.gov/pubmed/21097780 http://dx.doi.org/10.1093/nar/gkq1091 |
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