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Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.
Kuszewski J, Gronenborn AM, Clore GM. Kuszewski J, et al. Among authors: clore gm. Protein Sci. 1996 Jun;5(6):1067-80. doi: 10.1002/pro.5560050609. Protein Sci. 1996. PMID: 8762138 Free PMC article.
We tested this approach with the experimental NMR data (comprising an average of about 30 restraints per residue and consisting of interproton distances, torsion angles, 3JHN alpha coupling constants, and 13C chemical shifts) used previously to calculate the solution structure of …
We tested this approach with the experimental NMR data (comprising an average of about 30 restraints per residue and consisting of interprot …
489 results