Fig. 1 Sequence alignment of AFP on 8 templates
Six cystein residues which form the three conserved disulfide bridges in all these peptides are in bold face. The paring pattern of the disulfide bridges is
indicated by lines at the top. Dashes denote amino acid residue deletion. The left most code in bold face at each line is the PDB code of the structure
templates for modeling, except for 1HWT (see table 1). 2AFP is the anti-fungal peptide to be modeled. Number of amino acid residues of each
peptide is shown at the right side of each line.
Fig. 2 The three-dimensional model of the anti-fungal peptide
The atoms in the constructed three-dimensional model
are presented as sticks with the following color code: green for carbon,
blue for nitrogen, red for oxygen, white for hydrogen and yellow for
sulfide. A gray coil shows the backbone and the beta-strands
are emphasized by red ribbons. The three disulfide bridges are in
thick sticks with the sulfide atoms shown as balls.
Fig. 3 Structural superimposition of AFP on 8 templates
Structural superimposition of the anti-fungal model
(2AFP) on 8 templates. C-alpha
traces of each peptide are drawn in sticks with different colors.
The side chains of disulfide bridges are shown as ball-stick in yellow.
The PDB code (see table 1) of each chain is indicated with an arrow