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Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar
W Gronwald1, E Brunner, F Huber
1Institut für Biophysik und physikalische Biochemie, Universität Regensburg, Postfach, D-93040 Regensburg, Federal Republic of Germany.
Abstract:
For the Ras-binding domain of the protein kinase Byr2, only a limited number of NOE contacts could be initially assigned unambiguously, as the quality of the NOESY spectra was too poor. However, the use of residual (1)H-(15)N dipolar couplings in the beginning of the structure determination process allows to overcome this problem. We used a three-step recipe for this procedure. A previously unknown structure could be calculated reasonably well with only a limited number of unambiguously assigned NOE contacts.