[Date Prev][Date Next][Thread Prev][Thread Next][Date Index][Thread Index]

Re: [modeller_usage] special restrains for aromatic packing interactions



Is it possible to set the distance cutoff between a given atom of the protein and a subset of atoms in the ligand? E.g. in some crystal structures OG1 of a THR forms an H-bond with O1A of ATP, whereas in others with O2A. In that case can I force Modeller to keep (THR44:OG1 - ATP266:O1A <= 3.5+-0.1) OR (THR44:OG1 - ATP266:O2A <= 3.5+-0.1)  ?



2010/3/24 Modeller Caretaker <">>
On 03/23/2010 08:46 AM, Thomas Evangelidis wrote:
Since the phosphate groups of ATP are forced to lie within 3.5 A. from
the binding site residues, the Tyrosine ring will be in close proximity
to the Adenine ring. So I was thinking about adding a Coulomb or LJ or
SHPERE restraint including only the adenine and tyrosine rings.

Right, but all the restraints you mention are atomistic pairwise restraints. You can't restrain two rings, only two atoms.


If yes how can I measure the values (i.e. energy value
for LJ) from the templates?

You can measure the template distance in any reasonable PDB viewer, such as Chimera. Then I'd suggest you just use simple Modeller harmonic pairwise distance restraints with a mean corresponding to the measured distance, and tweak the standard deviation until things look right. The reason I suggest harmonic rather than Coulomb or LJ terms is that unless you're super-confident the form of the potential is inverse square or 6-12, those mathematical forms don't make sense. And there's no way you'd be able to accurately parameterize either interaction short of doing a lot of high basis set QM calculations. So you're probably better off with a simple harmonic.