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Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins

BACKGROUND: We describe Distill, a suite of servers for the prediction of protein structural features: secondary structure; relative solvent accessibility; contact density; backbone structural motifs; residue contact maps at 6, 8 and 12 Angstrom; coarse protein topology. The servers are based on lar...

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Detalles Bibliográficos
Autores principales: Baú, Davide, Martin, Alberto JM, Mooney, Catherine, Vullo, Alessandro, Walsh, Ian, Pollastri, Gianluca
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1574355/
https://www.ncbi.nlm.nih.gov/pubmed/16953874
http://dx.doi.org/10.1186/1471-2105-7-402
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author Baú, Davide
Martin, Alberto JM
Mooney, Catherine
Vullo, Alessandro
Walsh, Ian
Pollastri, Gianluca
author_facet Baú, Davide
Martin, Alberto JM
Mooney, Catherine
Vullo, Alessandro
Walsh, Ian
Pollastri, Gianluca
author_sort Baú, Davide
collection PubMed
description BACKGROUND: We describe Distill, a suite of servers for the prediction of protein structural features: secondary structure; relative solvent accessibility; contact density; backbone structural motifs; residue contact maps at 6, 8 and 12 Angstrom; coarse protein topology. The servers are based on large-scale ensembles of recursive neural networks and trained on large, up-to-date, non-redundant subsets of the Protein Data Bank. Together with structural feature predictions, Distill includes a server for prediction of C(α )traces for short proteins (up to 200 amino acids). RESULTS: The servers are state-of-the-art, with secondary structure predicted correctly for nearly 80% of residues (currently the top performance on EVA), 2-class solvent accessibility nearly 80% correct, and contact maps exceeding 50% precision on the top non-diagonal contacts. A preliminary implementation of the predictor of protein C(α )traces featured among the top 20 Novel Fold predictors at the last CASP6 experiment as group Distill (ID 0348). The majority of the servers, including the C(α )trace predictor, now take into account homology information from the PDB, when available, resulting in greatly improved reliability. CONCLUSION: All predictions are freely available through a simple joint web interface and the results are returned by email. In a single submission the user can send protein sequences for a total of up to 32k residues to all or a selection of the servers. Distill is accessible at the address: .
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spelling pubmed-15743552006-09-26 Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins Baú, Davide Martin, Alberto JM Mooney, Catherine Vullo, Alessandro Walsh, Ian Pollastri, Gianluca BMC Bioinformatics Software BACKGROUND: We describe Distill, a suite of servers for the prediction of protein structural features: secondary structure; relative solvent accessibility; contact density; backbone structural motifs; residue contact maps at 6, 8 and 12 Angstrom; coarse protein topology. The servers are based on large-scale ensembles of recursive neural networks and trained on large, up-to-date, non-redundant subsets of the Protein Data Bank. Together with structural feature predictions, Distill includes a server for prediction of C(α )traces for short proteins (up to 200 amino acids). RESULTS: The servers are state-of-the-art, with secondary structure predicted correctly for nearly 80% of residues (currently the top performance on EVA), 2-class solvent accessibility nearly 80% correct, and contact maps exceeding 50% precision on the top non-diagonal contacts. A preliminary implementation of the predictor of protein C(α )traces featured among the top 20 Novel Fold predictors at the last CASP6 experiment as group Distill (ID 0348). The majority of the servers, including the C(α )trace predictor, now take into account homology information from the PDB, when available, resulting in greatly improved reliability. CONCLUSION: All predictions are freely available through a simple joint web interface and the results are returned by email. In a single submission the user can send protein sequences for a total of up to 32k residues to all or a selection of the servers. Distill is accessible at the address: . BioMed Central 2006-09-05 /pmc/articles/PMC1574355/ /pubmed/16953874 http://dx.doi.org/10.1186/1471-2105-7-402 Text en Copyright © 2006 Baú et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Software
Baú, Davide
Martin, Alberto JM
Mooney, Catherine
Vullo, Alessandro
Walsh, Ian
Pollastri, Gianluca
Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
title Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
title_full Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
title_fullStr Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
title_full_unstemmed Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
title_short Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
title_sort distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
topic Software
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1574355/
https://www.ncbi.nlm.nih.gov/pubmed/16953874
http://dx.doi.org/10.1186/1471-2105-7-402
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