DRESS: a database of REfined solution NMR structures
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 qual...
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Published in | Proteins, structure, function, and bioinformatics Vol. 55; no. 3; pp. 483 - 486 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
15.05.2004
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Subjects | |
Online Access | Get full text |
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Summary: | 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. Proteins 2004. © 2004 Wiley‐Liss, Inc. |
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Bibliography: | ark:/67375/WNG-K3P9FB8Q-Z ArticleID:PROT20118 istex:387741F6E3098D1CD2455AC26871A199ABDF1A6D European Community program NMRQUAL - No. QLG2-CT-2000-0313 National Institute of General Medical Sciences Netherlands Foundation for Chemical Research (NWO/CW) National Institutes of Health - No. P50-GM64598 |
ISSN: | 0887-3585 1097-0134 |
DOI: | 10.1002/prot.20118 |