Abstract:   A computer program has been developed to accurately and automatically  predict the ¹H and ¹³C chemical shifts of unassigned proteins on the basis of sequence homology. The program (called SHIFTY) uses standard sequence alignment techniques to compare the sequence of an unassigned
protein against the BioMagResBank  a public database containing sequences and NMR chemical shifts of nearly 200 assigned proteins [Seavey et al. (1991) J. Biomol. NMR, 1, 217-236 PubMed PMID: 1841696]. From this initial sequence alignment, the program uses a simple set of rules to directly assign or transfer
a complete set of ¹H or ¹³C chemical shifts (from the previously assigned homologues) to the unassigned protein. This " homologous assignment"
protocol takes advantage of the simple fact that homologous proteins tend to share both structural similarity and chemical shift similarity. SHIFTY has been
extensively tested on more than 25 medium-sized proteins. Under favorable circumstances, this program can predict the ¹H or ¹³C chemical shifts of
proteins with an accuracy far exceeding any other method published to date.  With the exponential growth in the number of assigned proteins appearing in
the literature (now at a rate of more than 150 per year), we believe that SHIFTY may have widespread utility in assigning individual members in
families of related proteins, an endeavor that accounts for a growing portion of the protein NMR work being done today.

J Biomol NMR 1997 Dec;10(4):329-336
[PubMed PMID: 9460240]
 

Listed here are the proteins used for this article.  Information in the table includes chemical shifts,  X-ray structure, the accession codes for data deposited in the BMRB and PDB databases, the resolution at which the crystal structure was solved, the sequence homologues that were used, the correlation coefficients for the different NMR specs, and the assignment prediction accuracy.