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Bioinformatics Advance Access published online on November 13, 2007
Bioinformatics, doi:10.1093/bioinformatics/btm564
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© The Author (2007). Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Fast protein fold estimation from NMR-derived distance restraints

Annamária F. Ángyán 1, András Perczel 1,2, Sándor Pongor 3 and Zoltán Gáspári 1,*

1Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/A, 1117 Budapest, Hungary
2MHAS-ELTE Protein Modelling Group, Pázmány Péter sétány 1/A, 1117 Budapest, Hungary
3Protein Structure and Bioinformatics Group, International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34012 Trieste, Italy and Bioinformatics Group, Biological Research Centre, Hungarian Academy of Sciences, Temesvári körút 62, 6701 Szeged, Hungary

*To whom correspondence should be addressed. Dr. Zoltán Gáspári, E-mail: szpari{at}chem.elte.hu, gaspari.zoltan{at}gmail.com


  Abstract

Summary: PRIDE-NMR is a fast novel method to relate known protein folds to NMR distance restraints. It can be used to obtain a first guess about a structure being determined, as well as to estimate the completeness or verify the correctness of NOE data.

Availability: The PRIDE-NMR server is available at http://www.icgeb.org/pride

Contact: szpari{at}chem.elte.hu

Supplementary information: Description of the server and details of the tests presented can be found at http://www.icgeb.org/pride

Associate Editor: Prof. Burkhard Rost

Received on August 23, 2007; accepted on November 6, 2007

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