Abstract
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-refinedNMRstructures, 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 theseNMRstructures as input
for experimental and theoretical studies in many
fields of research. Proteins 2004;55:483–486.
| Original language | Undefined/Unknown |
|---|---|
| Pages (from-to) | 483-486 |
| Number of pages | 4 |
| Journal | Proteins: Structure function and bioinformatics |
| Volume | 55 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2004 |