Hello,
I am currently equilibrating a system for MD like many times before. The problem
is that during the NTP pressure adjustment step my complex gets distorted. This
is due to the distance rescaling. It has not been a big deal for globular
proteins with the ligand rather close to the center of the solvent box since the
rearrangement of the complex was minimal.
But the system I want to study is rather elongated. I use a rectangular box
(~130x40x40A). Also the initial density is rather low after solvating with LEaP
(~0.8g/ml). The ligand resides at one end of the elongated protein.
This results in the ligand shifting significantly (>2A) with respect to the
protein during the density adjustment. Also the 2 parallel helices in the
dimeric protein shifts significantly. This happens depsite of using positional
restraints.
In general I think that only the water should adjust so that that solute stays
in its original configuration. But unfortunately the positions of all molecular
entities are rescaled.
Is there an easy way to prevent this?
Best regards,
Alexander
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Alexander Metz (PhD Student)
Heinrich Heine UniversitätDüsseldorf
InstitutfürPharmazeutischeundMedizinischeChemie
Computational Pharmaceutical Chemistry
Universitaetsstrasse 1
40225 Düsseldorf, Germany
Tel: +49 211 81 13854
++++++++++++++++++++++++++++++++++++++++++++++++++
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Received on Fri Sep 10 2010 - 04:00:03 PDT
