Water plays a major structural and functional role around proteins. In an attempt to explore this mechanistic structural aspect of proteins, we present site-specific interaction of hydration water with the major coat protein subunit of filamentous virus Pf1 by magic angle spinning (MAS) solid-state NMR. The interaction of surrounding water with 36 MDa Pf1 virion is investigated in uniformly C-13, N-15 isotopically labeled; polyethylene glycol precipitated fully hydrated samples, by solid-state nuclear magnetic resonance spectroscopy. Dipolar edited two-dimensional (2D) H-1-N-15 heteronuclear correlation (HETCOR) experiments lead to unambiguous assignments of cross-peaks originating exclusively from H-1 resonances of water molecules correlating to the protein amide nitrogen. An enhanced resolved H-1 chemical shift dimension in these experiments also precludes the need of perdeuteration. We report seven residues spanning the 40 residue continuous a-helical conformation assembly of Pf1 interacting with surrounding water. It shows a highly hydrated inner core inside this viral filamentous assembly. The results obtained also suggest the first evidence of a water mediated interface cluster formed at the site of Arg44 with the single stranded DNA genome of the filamentous phage supramolecular assembly.