The solution structure of the BRCT domain from human polymerase reveals homology with the TdT BRCT domain
Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining.
GTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPAL LDISWLTESLGAGQPVPVECRHRLE
The initial structures were computed using the auto noeassign feature of CYANA 2.1; 1503 NOE distance restraints were assigned, and 147 dihedral angle restraints were used in the calculation. The 20 best CYANA structures were refined in explicit solvent using ARIA 2.0a with the 1506 NOE distance restraints, 147 dihedral angle restraints, 42 H-bond restraints, and 48 residual dipolar coupling restraints.
Torsion angle dynamics followed by molecular dynamics refinement in explicit water solvent
1mM polymerase mu BRCT domain, 25 mM d-Tris, 50 mM KCl, 0.02% NaN3, 5 mM DTT, pH 7.9, 90% H2O, 10% D2O
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, and Bax
Guentert, Mumenthaler, Herrmann, and Wuthrich
BRCT domain, alpha-beta-alpha sandwich, TRANSFERASE
STPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPAL LDISWLTESLGAGQPVPVECRHRLE