Assignment of Backbone Resonances from Minimal NMR Data Using Connectivity, Torsion Angle Constraints, and Chemical Shifts
A program is presented which will return the most probable sequence location for a short connected set of residues in a protein given just 13Cα chemical shifts (δ(13Cα)) and data restricting the φ and ψ backbone angles. Data taken from both the BioMagResBank and the Protein Data Bank were used to create a probability density function (PDF) using a multivariate normal distribution in δ(13Cα), φ, and ψ space for each amino acid residue. Extracting and combining probabilities for particular amino acid residues in a short proposed sequence yields a score indicative of the correctness of the proposed assignment. The program is illustrated using several proteins for which structure and 13Cαchemical shift data are available.
Published in Journal of Biomolecular NMR, Volume 29, Issue 1, 2004, pages 1-9.
The final publication is available at Springer via http://dx.doi.org/10.1023/B:JNMR.0000019500.76436.31
L. C. Morris, Valafar H., Prestegard J. H., (2004). Assignment of Backbone Resonances from Minimal NMR Data Using Connectivity, Torsion Angle Constraints, and Chemical Shifts. Journal of Biomolecular NMR, 29(1): 1-9.