NMR studies of large proteins, over 100 kDa, in solution are technically challenging and thereby of considerable interest in the NMR field. This is primarily due to slowing of molecular tumbling in solution as molecular mass increases. Typical 1H-13C or 1H-15N correlation spectra using 13C- or 15N uniformly labeled proteins show severe line-broadening and signal overlap. It is well known that selective isotope labeling, often concomitant with deuteration, is a useful strategy to reduce signal overlap and line-broadening in biomolecular NMR. However, a reduction in the number of signals is, in turn, disadvantageous in characterization of the overall protein feature. Thus, inspection of solution state NMR data not only of 1H-13C correlation spectra recorded using the selectively-labeled proteins, but also of 1H-15N correlation spectra of uniformly 15N-labeled protein is still useful. We discuss consistency in NMR data recorded using different NMR nuclei for a 66 kDa protein, HIV-1 reverse transcriptase precursor, that forms a homodimer with micro-molar dissociation constant in solution, to understand the structural characteristics. This work is supported by NIH NIGMS and NIAID (GM105401 and GM082251).