On 8/18/14, 9:41 AM, Natalie Stephenson wrote:
Hi all,

This probably seems a really obvious question, but I'm struggling to get my
head around it. I am performing simulations to determine the effect of
mutations on key regions of the protein. I have a crystal structure which I
am using as the WT construct, and have performed homology modelling to create
the point mutations of interest.

I have used g_rms using the Production MD .tpr as the reference to look at
the change in movement for key regions of the structure, comparing the degree
of movement with the WT and mutated construct. Unfortunately, this does not
necessarily tell me about changes occuring, for example, one key region is
showing no change in RMSD however is displaced compared to that in the WT.

Can you provide your exact command(s) and the groups chosen for fitting and output? The outcome is highly dependent upon proper choices being made.

Would it be better to use the WT EM.tpr as the reference structure for
everything (i.e. compare everything to the WT crystal structure)? Obviously
these topologies will have slightly different numbers of atoms etc. will this
be a problem?


This will be a problem. You can get around it, though, by using tpbconv (gmx convert-tpr in 5.0) to extract just backbone atoms from both .tpr files and trajectories. If you don't, g_rms will complain about mismatching atom numbers or you will be mapping the wrong atoms in the trajectory since the two proteins have different numbers of atoms.

Also note that g_rmsf is probably useful here, too, as you can get per-residue fluctuations and RMSD.

-Justin

--
==================================================

Justin A. Lemkul, Ph.D.
Ruth L. Kirschstein NRSA Postdoctoral Fellow

Department of Pharmaceutical Sciences
School of Pharmacy
Health Sciences Facility II, Room 601
University of Maryland, Baltimore
20 Penn St.
Baltimore, MD 21201

[email protected] | (410) 706-7441
http://mackerell.umaryland.edu/~jalemkul

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