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Hello Isabell--

You actually wrote to the list administrator email address. I'm replying
to the full Xplor-NIH list.

> 
> we are currently using XPLOR-NIH to determine NMR-constrained protein
> structures. I have modified one such protein to incorporate two
> fluroescent dye molecules (attached to a glutamine and cysteine side
> chain) and performed FRET experiments. I am now attempting to
> incorporate these modified amino acids in XPLOR.
> 
> The Dundee PRODRG server (davapc1.bioch.dundee.ac.uk/prodrg) provided
> me with paramter and topology file for the dye molecules attached to
> their respective amino acid built using a molecular mechanics program
> with ab initio minimization. Unfortunately, although I can generate a
> .psf file with these modified residues, I am unable to produce an
> extended protein structure, .pdb file.

what exactly is the problem you are facing?

> 
> The fluorescent dyes are based upon AlexaFluor 555 maleimide and
> AlexaFluor 647 cadaverine (both with a rhodamine-like core) and
> therefore contain fused aromatic ring systems. We suspect that some of
> the errors might be due to lack of planarity terms in our topology and
> parameter files.

possible. Sometimes, you have to change dihedrals into impropers to get
desired geometries. 

> 
> We would be grateful if you could provide us with any information on
> how we might define these correctly and if you have any additional
> information on topology files developed for fluorescent dyes or
> modified amino acids this would be extremely useful for us.
> 
> We have attached the topology and parameter file we are using. The
> modified amino acids are labelled DRG and DRE, respectively.
> 

One suggestion: use XPLOR atom naming for the backbone and
non-modified portions of the sidechains. It may take a bit of fiddling,
but it allows more use of built-in Xplor-NIH functionality.

best regards--
Charles
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