Characterization of Dimeric Interactions within Protrusion-Domain Interfaces of Parallel and X-Shaped Conformations of Macrobrachium rosenbergii Nodavirus: A Theoretical Study Using the DFT Method along with QTAIM and NBO Analyses

[Image: see text] The protrusion domain (P-domain; MrNVPd) of Macrobrachium rosenbergii nodavirus (MrNV) exists in two conformations, parallel and X-shaped. We have performed a theoretical study to gain insight into the nature of the dimeric interactions involving the dimeric interfaces within parallel and X-shaped conformations of MrNVPd by applying the quantum theory of atoms in molecules (QTAIM) and natural bond orbital (NBO) analyses in the framework of the density functional theory (DFT) approach. The results reveal that the dimer–dimer interfaces of MrNVPd have hydrogen bonds of common types. Leu255–Lys287, Tyr257–Lys287, Lys287–Ser253, Met294–Cys328, Asp295–Lys327, Ser298–Ser324, Ile326–Asp295, and Cys328–Met294 are the key residue pairs of the dimer–dimer interfaces to maintain the dimer–dimer structures of MrNVPd through charge–charge, charge–dipole, dipole–dipole, hydrophobic, and hydrogen bonding interactions. The strengths of these intermolecular dimer–dimer interactions in the parallel conformation are much greater than those in the X-shaped conformation. The parallel trimeric interface is held basically by electrostatic and hydrophobic interactions. The electrostatic interactions accompanying a strong hydrogen bond of Oγ1–Hγ1···Oγ1 in the Thr276 A–Thr276 D pair maintain the intermolecular interface of two X-shaped MrNVPd dimers.