A statistical analysis of the atomic environments of arginine side cha
ins from 62 high resolution protein structures has been made. Using th
e definition of F. M. Richards (J. Mol. Biol., 82, 1-14, 1974), the pr
otein data set was subdivided into 19 different atom types and their p
ropensities to form atom contacts with the side chain atoms of arginin
e residues were calculated. For those arginine side chain - atom pairs
classed as interacting, a detailed analysis of their geometries was c
arried out. This has included the contact separation (R) and the spati
al distribution in terms of the spherical polar angles theta and phi.
The geometrical distributions of the 19 different atom types were comp
ared and contrasted to identify factors that are important for packing
. From the results we find that polarity, covalent constraints, volume
occlusion and solvent accessibility are the key determinants governin
g packing around arginine side chains.