Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2.
Edith BuchingerSiv Å WiikAnna KusnierczykRenana RabePer A AasBodil KavliGeir SlupphaugFinn Lillelund AachmannPublished in: Biomolecular NMR assignments (2017)
Human uracil N-glycosylase isoform 2-UNG2 consists of an N-terminal intrinsically disordered regulatory domain (UNG2 residues 1-92, 9.3 kDa) and a C-terminal structured catalytic domain (UNG2 residues 93-313, 25.1 kDa). Here, we report the backbone 1H, 13C, and 15N chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.