There is considerable interest in determining amide-(15)N chemical shift anisotropy (CSA) tensors from biomolecules and understanding their variation for structural and dynamics studies using solution and solid-state NMR spectroscopy and also by quantum chemical calculations. Due to the difficulties associated with the measurement of CSA tensors from membrane proteins, NMR-based structural studies heavily relied on the CSA tensors determined from model systems, typically single crystals of model peptides. In the present study, the principal components of backbone amide-(15)N CSA tensors have been determined using density functional theory for a 16.7 kDa membrane-bound paramagnetic heme containing protein, cytochrome-b(5) (cytb(5)). All the calculations were performed by taking residues within 5 Å distance from the backbone amide-(15)N nucleus of interest. The calculated amide-(15)N CSA spans agree less well with our solution NMR data determined for an effective internuclear distance r(N-H) = 1.023 Å and a constant angle β = 18° that the least shielded component (δ(11)) makes with the N-H bond. The variation of amide-(15)N CSA span obtained using quantum chemical calculations is found to be smaller than that obtained from solution NMR measurements, whereas the trends of the variations are found to be in close agreement. We believe that the results reported in this study will be useful in studying the structure and dynamics of membrane proteins and heme-containing proteins, and also membrane-bound protein-protein complexes such as cytochromes-b5-P450.