The 'Helical wheel and net' colour diagrams illustrate the arrangement of the residues in each helix. The residues are colour coded for hydrophobic (green), polar (blue) and charged (red) amino acid types. The wheels and nets assume the ideal helical value of 3.6 residues per turn.

A PostScript or PDF version of the plots (showing 8 helices per page) can be generated by clicking on the appropriate icon below the Table.


The data displayed in the table for each helix includes the helix number (assigned sequentially starting with 1 at the N-terminus of the protein), the residue numbers corresponding to the start and end of the helices, the helix type (H (alpha helix) or G (3,10) helix. This is followed by the number of residues in the helix and information about the geometry of the helix as follows: length and unit rise (both in Angstroms), the number of residues per turn (ideaally 3.6) for alpha helices), the helix pitch in Angstroms and a measure of the deviation of the helix geometry from an ideal helix (in degrees). This latter value should be 0 for a perfect helix. The geometrical parameters are not calculated for helices with fewer than four residues. The final column in the table gives the helix's amino acid sequence.


Gail Hutchinson 22nd May, 1996 spacer