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FOR THE RECORD

Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings

¹ Institut für Biophysik und physikalische Biochemie, Universität Regensburg, Postfach, D-93040 Regensburg, Federal Republic of Germany
² Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, D-44227 Dortmund, Federal Republic of Germany

Reprint requests to: Professor Dr. Dr. Hans Robert Kalbitzer, Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Postfach, D-93040 Regensburg, Federal Republic of Germany; e-mail: Hans-Robert.Kalbitzer{at}biologie.uni-regensburg.de; fax: 49-941-943-2479.

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 ¹H–¹⁵N 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.

Keywords: Byr2; residual dipolar couplings; structure calculation; NMR

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