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Updated: Jun 15, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
CARON--average RMSD of NMR structure ensembles
Kresimir Sikic1, Oliviero Carugo
1Departement of Structural and Computational Biology, Max F. Perutz Laboratories, Vienna University, 1030 Vienna, Austria. kresimir.sikic@univie.ac.at
Abstract:
The NMR protein structures are often deposited in the Protein Data Bank as ensembles of models that agree with the experimental restraints. Information about stereochemical variability and the molecular flexibility can be obtained by systematic comparison of all models. Here we describe CARON, a software that allows the computation of the root-mean-square-distances between equivalent atoms and residues in all models and introduces these values into the occupancy and the B-factor fields of PDB-formatted files. This tool allows the user to both get a quantitative estimation of the conformational homogeneity of the models and to exploit this information in common computer graphics programs.
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