caa a22 4500 477136044 CHVBK 20180405111718.0 cr unu---uuuuu 170330e19971201xx s 000 0 eng 10.1023/A:1018373822088 doi (NATIONALLICENCE)springer-10.1023/A:1018373822088 Automated 1H and 13C chemical shift prediction using the BioMagResBank [Elektronische Daten] [David Wishart, M. Watson, Robert Boyko, Brian Sykes] 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]. 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 expo- nential 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. Kluwer Academic Publishers, 1997 Chemical shift nationallicence Homology nationallicence Prediction nationallicence BioMagResBank nationallicence Wishart David Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, T6G 2N8, Edmonton, AB, Canada aut Watson M. Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, T6G 2N8, Edmonton, AB, Canada aut Boyko Robert Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut Sykes Brian Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut Journal of Biomolecular NMR Kluwer Academic Publishers 10/4(1997-12-01), 329-336 0925-2738 10:4<329 1997 10 10858 https://doi.org/10.1023/A:1018373822088 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018373822088 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Wishart David Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, T6G 2N8, Edmonton, AB, Canada aut NATIONALLICENCE 700 1- Watson M. Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, T6G 2N8, Edmonton, AB, Canada aut NATIONALLICENCE 700 1- Boyko Robert Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut NATIONALLICENCE 700 1- Sykes Brian Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 10/4(1997-12-01), 329-336 0925-2738 10:4<329 1997 10 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer