Dear users,

I am investigating protein crystal packing artifacts by doing equilibrium
simulations starting from a crystal structure. I would like to know if the
relaxations i see are reproducible, in the sense that many simulations with
independent velocities give the same general result.

My plans is to do only one set of (first NVT then NPT) equilibrations with
position restraints. Then, I thought I'd do a shorter NPT run with position
restraints, with more frequent output and using the trr snapshots as
starting points for production runs. 

The only question then is how far apart these snapshots need to be to
guarantee independent velocities. Attached is the velocity autocorrelation
for the Protein group. It seems to me that using snapshots 1ps apart would
do it, since the autocorrelation has decayed by then.

Is this a valid approach?



View this message in context:
Sent from the GROMACS Users Forum mailing list archive at
gmx-users mailing list
* Please search the archive at before posting!
* Please don't post (un)subscribe requests to the list. Use the 
www interface or send it to
* Can't post? Read

Reply via email to