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Hello Benjamin--

Sorry for the long delay- I've been busy helping with a course here at
NIH. 

> 
> i want to work on two protein-ligand-complexes in the same instance of 
> xplor at the same time. in the segment section i called the protein part 
> of complex 1 PRO1, the ligand LIG1; and PRO2 and LIG2 accordingly (the 
> coordinates of the two proteins partially overlap). after hydrogen 
> adding i want to separate the respective complexes from each other using
> 
> 
> CONStraints
>   
>    INTEraction (segid PRO1) (segid PRO1)
> 
>  END
> 
> 
> then i perform energy minimization and short MD simulation (the random 
> seed i set same for each run).
> when i compared the coordinate output of this combined runs with two 
> separate runs of the single complexes, i noticed quite big rmsds between 
> the corresponding structures. this might be no surprise due to the fact 
> that i perform energy minimization of the two complexes simultaneously 
> and the way of minimizing the energy of the whole system might be 
> different from minimizing the single systems. i next tested the same 
> setup as described above with the second complex rotated or translated. 
> now the system is the same as above, and if the two complexes do not see 
> each other (as i want them to) the outcome should be the same, which it 
> is not. am i overlooking something really simple? the energy terms i use 
> in the minimization step are bond angle impr vdw elec, maybe there is a 
> term which is excluded from the interaction constraint? or might it be 
> some non-bonded interaction i do not capture with the constraint?
> 

Do note that the constraints interaction statement only affects a subset
of XPLOR potential terms. A description of these terms can be found here

http://nmr.cit.nih.gov/xplor-nih/doc/current/xplor/node132.html

I suspect this is your problem.

best regards--
Charles

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