MODBASE, a database of annotated comparative protein structure models, and associated resources. Export

@article{citeulike:358632, abstract = {MODBASE (http://salilab.org/modbase) is a relational database of annotated comparative protein structure models for all available protein sequences matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on the MODELLER package for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE uses the MySQL relational database management system for flexible querying and CHIMERA for viewing the sequences and structures (http://www.cgl.ucsf.edu/chimera/). MODBASE is updated regularly to reflect the growth in protein sequence and structure databases, as well as improvements in the software for calculating the models. For ease of access, MODBASE is organized into different data sets. The largest data set contains 1,26,629 models for domains in 659,495 out of 1,182,126 unique protein sequences in the complete Swiss-Prot/TrEMBL database (August 25, 2003); only models based on alignments with significant similarity scores and models assessed to have the correct fold despite insignificant alignments are included. Another model data set supports target selection and structure-based annotation by the New York Structural Genomics Research Consortium; e.g. the 53 new structures produced by the consortium allowed us to characterize structurally 24,113 sequences. MODBASE also contains binding site predictions for small ligands and a set of predicted interactions between pairs of modeled sequences from the same genome. Our other resources associated with MODBASE include a comprehensive database of multiple protein structure alignments (DBALI, http://salilab.org/dbali) as well as web servers for automated comparative modeling with MODPIPE (MODWEB, http://salilab. org/modweb), modeling of loops in protein structures (MODLOOP, http://salilab.org/modloop) and predicting functional consequences of single nucleotide polymorphisms (SNPWEB, http://salilab. org/snpweb).}, address = {Department of Biopharmaceutical Sciences, and California Institute for Quantitative Biomedical Research, Mission Bay Genentech Hall, 600 16th Street, Suite N472D, University of California San Francisco, San Francisco, CA 94143-2240, USA.}, author = {Pieper, Ursula and Eswar, Narayanan and Braberg, Hannes and Madhusudhan, M. S. and Davis, Fred P. and Stuart, Ashley C. and Mirkovic, Nebojsa and Rossi, Andrea and Marti-Renom, Marc A. and Fiser, Andras and Webb, Ben and Greenblatt, Daniel and Huang, Conrad C. and Ferrin, Thomas E. and Sali, Andrej}, citeulike-article-id = {358632}, citeulike-linkout-0 = {http://dx.doi.org/10.1093/nar/gkh095}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/14681398}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=14681398}, day = {1}, doi = {10.1093/nar/gkh095}, issn = {1362-4962}, journal = {Nucleic acids research}, keywords = {comparative\_protein\_structure}, month = {January}, number = {Database issue}, posted-at = {2009-10-27 18:00:17}, priority = {2}, title = {MODBASE, a database of annotated comparative protein structure models, and associated resources.}, url = {http://dx.doi.org/10.1093/nar/gkh095}, volume = {32}, year = {2004} }

TY - JOUR ID - citeulike:358632 L3 - citeulike-article-id:358632 N2 - MODBASE (http://salilab.org/modbase) is a relational database of annotated comparative protein structure models for all available protein sequences matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on the MODELLER package for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE uses the MySQL relational database management system for flexible querying and CHIMERA for viewing the sequences and structures (http://www.cgl.ucsf.edu/chimera/). MODBASE is updated regularly to reflect the growth in protein sequence and structure databases, as well as improvements in the software for calculating the models. For ease of access, MODBASE is organized into different data sets. The largest data set contains 1,26,629 models for domains in 659,495 out of 1,182,126 unique protein sequences in the complete Swiss-Prot/TrEMBL database (August 25, 2003); only models based on alignments with significant similarity scores and models assessed to have the correct fold despite insignificant alignments are included. Another model data set supports target selection and structure-based annotation by the New York Structural Genomics Research Consortium; e.g. the 53 new structures produced by the consortium allowed us to characterize structurally 24,113 sequences. MODBASE also contains binding site predictions for small ligands and a set of predicted interactions between pairs of modeled sequences from the same genome. Our other resources associated with MODBASE include a comprehensive database of multiple protein structure alignments (DBALI, http://salilab.org/dbali) as well as web servers for automated comparative modeling with MODPIPE (MODWEB, http://salilab. org/modweb), modeling of loops in protein structures (MODLOOP, http://salilab.org/modloop) and predicting functional consequences of single nucleotide polymorphisms (SNPWEB, http://salilab. org/snpweb). IS - Database issue JF - Nucleic acids research SN - 1362-4962 AD - Department of Biopharmaceutical Sciences, and California Institute for Quantitative Biomedical Research, Mission Bay Genentech Hall, 600 16th Street, Suite N472D, University of California San Francisco, San Francisco, CA 94143-2240, USA. TI - MODBASE, a database of annotated comparative protein structure models, and associated resources. VL - 32 KW - comparative_protein_structure AU - Pieper, Ursula AU - Eswar, Narayanan AU - Braberg, Hannes AU - Madhusudhan, MS AU - Davis, Fred AU - Stuart, Ashley AU - Mirkovic, Nebojsa AU - Rossi, Andrea AU - Marti-Renom, Marc AU - Fiser, Andras AU - Webb, Ben AU - Greenblatt, Daniel AU - Huang, Conrad AU - Ferrin, Thomas AU - Sali, Andrej PY - 2004/01/01/ UR - http://dx.doi.org/10.1093/nar/gkh095 ER -