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DRESS: a database of refined solution NMR structures
- 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.
- Subjects :
- Models, Molecular
Database
Bioinformatics
Chemistry
Structure validation
Nuclear magnetic resonance crystallography
computer.software_genre
Biochemistry
proteins
Set (abstract data type)
Structural Biology
Taverne
Solvents
Biophysical Chemistry
Cellular energy metabolism [UMCN 5.3]
Databases, Protein
Molecular Biology
computer
Nuclear Magnetic Resonance, Biomolecular
Subjects
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