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DRESS: a database of refined solution NMR structures

Authors :
Nabuurs, S.B.
Nederveen, A.J.
Vranken, W.
Doreleijers, J.F.
Bonvin, A.M.J.J.
Vuister, G.W.
Vriend, G.
Spronk, C.A.E.M.
NMR-spectroscopie
NMR Spectroscopy 1
Dep Scheikunde
NMR-spectroscopie
NMR Spectroscopy 1
Dep Scheikunde
Department of Bio-engineering Sciences
Other departments
Source :
Proteins, 55(3), 483-486. Wiley-Liss Inc., Proteins-Structure Function and Bioinformatics, 55, 483-6, Proteins-Structure Function and Bioinformatics, 55, 3, pp. 483-6, Proteins: Structure function and bioinformatics, 55(3), 483. Wiley-Liss Inc.
Publication Year :
2004

Abstract

Contains fulltext : 57416.pdf (Publisher’s version ) (Closed access) Several studies have shown that biomolecular NMR structures are often of lower quality when compared to crystal structures, and consequently they are often excluded from structural analyses. We present a publicly available database of re-refined NMR structures, exhibiting significantly improved quality. This database (available at http://www.cmbi.kun.nl/dress/) presents a uniformly refined and validated set of structural models that improves the value of these NMR structures as input for experimental and theoretical studies in many fields of research.

Details

ISSN :
08873585
Database :
OpenAIRE
Journal :
Proteins, 55(3), 483-486. Wiley-Liss Inc., Proteins-Structure Function and Bioinformatics, 55, 483-6, Proteins-Structure Function and Bioinformatics, 55, 3, pp. 483-6, Proteins: Structure function and bioinformatics, 55(3), 483. Wiley-Liss Inc.
Accession number :
edsair.doi.dedup.....efe97c0e875f5d21538d96835de23700