Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings.
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.
Gronwald
W
W
Institut für Biophysik und physikalische Biochemie, Universität Regensburg, Postfach, D-93040 Regensburg, Federal Republic of Germany.
Brunner
E
E
Huber
F
F
Wenzler
M
M
Herrmann
C
C
Kalbitzer
H R
HR
D001671:Biochemistry / Q000379:methods*; D005656:Fungal Proteins / Q000737:chemistry*; D020930:MAP Kinase Kinase Kinases; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D020928:Mitogen-Activated Protein Kinases / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D012568:Schizosaccharomyces / Q000737:chemistry; D029702:Schizosaccharomyces pombe Proteins
D005656:Fungal Proteins; D029702:Schizosaccharomyces pombe Proteins; D020928:Mitogen-Activated Protein Kinases; C077892:BYR2 protein, S pombe; D020930:MAP Kinase Kinase Kinases