The eukaryotic minichromsome maintenance (Mcm) proteins (Mcm2-7) are evolutionally conserved from yeast to human. These proteins are essential for DNA replication and Mcm6 is one subunit of Mcm2-7 complex that serves as the replicative helicase in DNA replication. Cdt1 is a critical member of pre-replicative complex (pre-RC), which directs the chromatin loading of Mcm2-7 complex. The Cdt1 binding domain (CBD) of human Mcm6 was found to directly interact with Cdt1 and this interaction may mediate the chromatin loading of Mcm2-7 complex. The structure of CBD exhibits a typical "winged-helix" fold which is generally involved in protein-nucleic acid interaction. Here we report the (1)H, (15)N and (13)C chemical shift assignments of human Mcm6 CBD determined by triple resonance experiments. The resonance assignments obtained in this work were required for the structure-function studies of CBD by NMR spectroscopy (BMRB deposits with accession number 16396).