[PyMOL] aa residues disconnected from 'fancy helices'?

[Michael Bovee]

Hi all,
I'm just starting to try out PyMOL (fink package 0.90-2, running 
through Apple's X11beta2, on a Lombard G3PB, MacOS 10.2.4).
Its much easier to learn that I thought it would be! Well done Warren, 
and codevelopers!  One puzzling thing I've noticed: when I build a 
model of my protein of interest using 'set cartoon_fancy_helices,1' and 
then show sidechains for several key catalytic residues, I find that 
the amino acids that reside along beta sheet or alpha helix regions 
appear properly connected to the alpha carbon backbone representation, 
but sidechains of amino acids that reside on 'strand' regions  appear 
to float in midair and do not connect to the strand backbone. Anyone 
else seen this behaviour?

Thanks!
--Michael Bovee
University of Vermont