Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.

@article{Kuszewski1996ImprovingTQ,
  title={Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.},
  author={John J Kuszewski and Angela M. Gronenborn and G Marius Clore},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 6},
  pages={
          1067-80
        }
}
A new conformational database potential involving dihedral angle relationships in databases of high-resolution highly refined protein crystal structures is presented as a method for improving the quality of structures generated from NMR data. The rationale for this procedure is based on the observation that uncertainties in the description of the nonbonded contacts present a key limiting factor in the attainable accuracy of protein NMR structures and that the nonbonded interaction terms… CONTINUE READING

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