  Topological properties of native folds are obtained from statistical analysis
of 160 low homology proteins covering the four structural classes. This is done
analysing one, two and three-vertex joint distribution of quantities related to
the corresponding network of amino acid residues. Emphasis on the amino acid
residue hydrophobicity leads to the definition of their center of mass as
vertices in this contact network model with interactions represented by edges.
The network analysis helps us to interpret experimental results such as
hydrophobic scales and fraction of buried accessible surface area in terms of
the network connectivity. To explore the vertex type dependent correlations, we
build a network of hydrophobic and polar vertices. This procedure presents the
wiring diagram of the topological structure of globular proteins leading to the
following attachment probabilities between hydrophobic-hydrophobic 0.424(5),
hydrophobic-polar 0.419(2) and polar-polar 0.157(3) residues.
