Dear Sparky and Cyana users,

This is an observation regarding backbone conformation in structures generated by CYANA using peak volumes/peak heights from SPARKY-

Although, CYANA generates structures with correct folds corresponding to the pattern of NOE connectivities, the conformation of the peptide backbone in regions of secondary structures does not perfectly resemble the secondary structure. For instance, in case of an anti-parallel beta sheet, although the conformation of the peptide backbone is extended, it is not perfectly extended as observed in antiparallel betasheets of published NMR structures in PDB data base. This is observed even after energy minimization of the final structures generated by CYANA. Do you’ll encounter these problems and how to correct it?

Thanks,

Betty