SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF GAMMA DELTA RESOLVASE
Solution structure of the catalytic domain of gammadelta resolvase. Implications for the mechanism of catalysis.
1H, 15N and 13C Resonance Assignments for the Catalytic Core of Gamma Delta Resolvase
MRLFGYARVSTSQQSLDIQVRALKDAGVKANRIFTDKASGSSSDRKGLDLLRMKVEEGDVILVKKLDRLGRDTADMIQLI KEFDAQGVSIRFIDDGISTDGEMGK
4269 is the 1H, 15N and 13C Chemical Shift Assignments for the Catalytic Core of gamma delta Resolvase
The structure was determined using triple-resonance 3D NMR spectroscopy for resonance assignments and double-resonance 3D NMR spectroscopy for obtaining NOESY data.
lowest energy and agreement with experimental NOESY
The NMR restraints included 2109 useful NOE determined upper distance restraints, 35 hydrogen bonds, and 297 torsion angle restraints. Structures were calculated in the DYANA using torsion angle dynamics. The calculation started with 200 randomized structures. The 19 structures with the lowest target function were refined within XPLOR using simulated annealing. The 19 refined structural conformers displayed no NOE violations >0.3 angstroms and no dihedral angle violations >3 degrees.
torsion angle dynamics and simulated annealing
0.002 M gamma delta resolvase (1-105) U-15N; 0.020 M phosphate buffer, pH 6.5; 90% H2O, 10% D2O
0.002 M gamma delta resolvase (1-105) U-15N,13C; 0.020 M phosphate buffer, pH 6.5; 90% H2O, 10% D2O
0.002 M gamma delta resolvase (1-105) U-15N,13C; 0.020 M phosphate buffer, pH 6.5; 99% D2O
recombinase, catalytic domain, mixed alpha beta, monomer, DNA BINDING PROTEIN