Michael,

That's because sheet's aren't flat -- cartoons aren't reality.

set cartoon_flat_sheets, off
set cartoon_smooth_loops, off

In order to force the cartoons to follow the true CA trace.

Cheers,
Warren



--
mailto:war...@delanoscientific.com
Warren L. DeLano, Ph.D.
Principal Scientist
DeLano Scientific LLC
Voice (650)-346-1154 
Fax   (650)-593-4020

> -----Original Message-----
> From: pymol-users-ad...@lists.sourceforge.net 
> [mailto:pymol-users-ad...@lists.sourceforge.net] On Behalf Of 
> Michael Bovee
> Sent: Friday, November 07, 2003 8:50 AM
> To: pymol-users@lists.sourceforge.net
> Subject: [PyMOL] aa residues disconnected from 'fancy helices'?
> 
> 
> 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
> 
> 
> 
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