The differentiation of the human rhinovirus into serotypes, all having very similar structures and the same architecture, is shown to be related to the packing of the viruses in the crystal and to its space-group symmetry. The molecular crystallographic properties (here described in terms of a molecular lattice Lambda(M) instead of the form lattice Lambda(F) considered in previous publications) appear to be compatible with the crystal structure and with the packing lattice Lambda(P), introduced in Part I [Janner (2010). Acta Cryst. A66, 301-311]. On the basis of the enclosing forms of the capsid, a sphere packing is considered, where the spheres touch at kissing points. Residues of each of the four coat proteins (VP1, VP2, VP3, VP4), having a minimal distance from the kissing points, define a set of kissing point related (KPR) residues. In this set only four different residues occur, one for each coat protein, ordered into symmetric clusters {already classified in a previous publication [Janner (2006). Acta Cryst. A62, 270-286]} and indexed by neighbouring lattice points of Lambda(P) (or equivalently of Lambda(M)). The indexed KPR residues allow a fingerprint characterization of the five rhinovirus serotypes whose structures are known (HRV16, HRV14, HRV3, HRV2 and HRV1A). In the fingerprint they occur as internal (if inside the given capsid), as external (if belonging to the neighbouring viruses) or as a contact residue (if at a kissing point position). The same fingerprint, periodically extended, permits a coarse-grained reconstruction of the essential properties of the crystal packing, invariant with respect to the space group of the serotype.