[PyMOL] Mysterious crash bug

2006-05-24 Thread Jacob Corn

Hi everyone,
On a few structures (some partially-built) I have run into an odd 
barely-reproducible crash bug with PyMOL 0.99rc6 (once on windows and once on 
linux). When a "problem" molecule is loaded (sometimes this is a specific 
combination of molecules, and not a single molecule), mousing-over any file in 
the File->Open dialog causes pymol to instantly crash. Altering the problem 
molecule's coordinates (either by rotation/translation in PyMOL or with 
subsequent rounds of building into density) often causes this problem to go away 
for that molecule.


This issue has bitten me on two occasions, but before I spend time trying to 
track down a reproducible case, I would like to find out if anyone else has 
noticed it, or if it's an isolated problem.


Jacob

--
Jacob Corn
The Berger Lab
UC Berkeley - Molecular and Cell Biology
jc...@uclink.berkeley.edu
phone: 510-643-8893
fax: 510-643-9290



Re: [PyMOL] loosen secondary structure

2006-05-24 Thread Robert Campbell
Hi,

* O. J. Ganesh  [2006-05-18 16:09] wrote:
>  
> Hey PyMOL gurus:
>  
> I have a 'perfect' helix. Is there some way to 'loosen' all of the
> angles in the helix so instead of 3.6 residues per turn, I could
> have, say, 8 residues per turn. My goal is to make the helix more
> 'coil-like'. Is this possible?

Well, if you know the phi/psi angles you like, then you could just build
it and specify those angles with my build_seq.py script:

http://adelie.biochem.queensu.ca/~rlc/work/pymol/build_seq.py

You can specify the phi, psi angles on the command line. Alternatively,
you can create a file of resname, phi, psi and build it with:

http://adelie.biochem.queensu.ca/~rlc/work/pymol/build_seq_phi_psi.py

if you don't want the phi/psi angles to be the same for every residue.

Cheers,
Rob
-- 
Robert L. Campbell, Ph.D. 
Senior Research Associatephone: 613-533-6821
Dept. of Biochemistry, Queen's University, fax: 613-533-2497
Kingston, ON K7L 3N6  Canada   http://adelie.biochem.queensu.ca/~rlc
PGP Fingerprint: 9B49 3D3F A489 05DC B35C  8E33 F238 A8F5 F635 C0E2



Re: [PyMOL] "unset" surface colors

2006-05-24 Thread Tsjerk Wassenaar

Hi Natasja,

That should be done with (IIRC)

set surface_color,-1

Tsjerk

On 5/24/06, Natasja Brooijmans  wrote:


 I accidently used the "set surface_color, x" command, and then unset. Now
the full surface is colored white. Rather, I want the surface to be colored
by the color of the underlying residues, but it looks like I can't get it to
do that after having used the set command. Any way of resetting the surface
settings back to the default? I tried deleting the object I created for the
surface and remaking it, but the settings are "stuck".

Thanks,

Natasja





--

Tsjerk A. Wassenaar, M.Sc.
Groningen Biomolecular Sciences and Biotechnology Institute (GBB)
Dept. of Biophysical Chemistry
University of Groningen
Nijenborgh 4
9747AG Groningen, The Netherlands
+31 50 363 4336


[PyMOL] "unset" surface colors

2006-05-24 Thread Natasja Brooijmans
I accidently used the "set surface_color, x" command, and then unset. Now the 
full surface is colored white. Rather, I want the surface to be colored by the 
color of the underlying residues, but it looks like I can't get it to do that 
after having used the set command. Any way of resetting the surface settings 
back to the default? I tried deleting the object I created for the surface and 
remaking it, but the settings are "stuck".
 
Thanks,

Natasja