Use of multiple receivers has a great potential to revolutionize practice of protein NMR as this enables encoding of several nuclei at the same time. In the context of multidimensional NMR spectroscopy of labeled proteins, the possibilities for pulse sequence design grow several fold for extraction of information, which was either difficult to extract earlier or would have required a series of long experiments. In this background, we present here a novel pulse sequence which involves parallel acquisition of 1H and 13C detected multidimensional data sets on proteins in a single experiment. It provides two three dimensional data sets, 3D-HA(CA)NH||3D-HACACO acquired parallely, which display 1Hα, 15N, 1HN and 1Hα, 13Cα, 13CO chemical shifts along their F1, F2, F3 dimensions, respectively. While both the experiments display intra-residue correlations, the 3D-HA(CA)NH provides also sequential ‘i-1→ i’ correlation along the 1Hα dimension. The 3D-HACACO data set provides also side chain information of residues having H-C-CO network (i.e., 1Hβ, 13Cβ and 13COγ of Asp and Asn, and 1Hγ, 13Cγ and 13COγ of Glu and Gln). Moreover, in 3D-HACACO, information on prolines is also recorded which is generally absent in most conventional proton detected experiments. With the prospect of further development in the 13C detection methods and fast acquisition methods we expect such experiments to become routine in the near future.