IF your MR solution is correct ( ie r factor falls on refinement to 40%
say) and your protein A is roughly 50% of the complex, and IF your data is
good to 1.9A (assumed SG correct etc) I would do my best to correct any
obvious rebuilding needed for protein A, ( r factor should fall further if
this is done well) , then as others suggest fit an idealised  alpha helix
or two, then try rebuilding again with the best sequence you can derive fir
B. Once r factors in the 30-40% range you can often fit a “ val leu phe “
type sequence. I personally find this sort of challenge fun ! But maybe
others don’t...
Eleanor


On Sat, 4 Nov 2023 at 19:55, Randy John Read <[email protected]> wrote:

> Hi,
>
> At 1.9A resolution there should be lots of possibilities, depending on the
> details.
>
> You imply you have partial sequence information for chain B. Is there a
> genome for your plant or a relative of it? You could search for possible
> matches to your sequence, and then test all the AlphaFold models for the
> sequences that come up.
>
> When you say chain A has known homologues, what was the sequence identity
> of the homologue you used as a model? If it wasn’t pretty high, you may
> well be better off using an AlphaFold model of the correct sequence for A.
>
> Do you expect chain B to have helices or do you see helices in the map?
> Just adding some poly-Ala helices (which will tend to be locally very
> accurate if incomplete) will help to improve your phases. Arcimboldo would
> be a good tool for this, and you should also try it for completing from
> chain A.
>
> Do you have any anomalous scattering signal in your data? Even if it’s not
> enough to solve the structure, any signal can be exploited, using MR-SAD,
> to improve your phases and in particular reduce model bias in your map.
>
> Of course, other people have pointed out that you should make sure you can
> be confident in the MR solution. Also, you didn’t mentione whether there
> might be any issues in the data, like twinning. Presumably you would have
> mentioned if there was more than one copy of each protein in the a.u.
>
> Best wishes,
>
> Randy Read
>
> > On 4 Nov 2023, at 14:04, Sam Tang <[email protected]> wrote:
> >
> > Dear community,
> >
> > I am solving the structure of a complex between proteins A and B, where
> A is a protein with known homologs and B is a novel protein isolated from
> plant. The diffraction data was at 1.9 Ang collected in-house, indexed to
> P321. Using A as the search model, we have got a reasonable solution where,
> after one round of refinement, the A chain fits the map pretty well. What's
> left was to extend the termini and fit a few rotamers.
> >
> > For protein B (B chain) I have tried the web version of ARP/wARP but the
> outcome was not really good. The model was not successfully built as
> indicated by low model completeness and score. The tricky thing may be that
> we do not have the complete sequence information of this protein B in-hand.
> (The other way round, we more or less wish to rely on the high resolution
> data to confirm its sequence.) What approach would you then recommend to
> build the B chain in this scenario?
> >
> > Thanks in advance and best regards,
> >
> > Sam
> >
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>
> -----
> Randy J. Read
> Department of Haematology, University of Cambridge
> Cambridge Institute for Medical Research     Tel: +44 1223 336500
> The Keith Peters Building
> Hills Road                                                       E-mail:
> [email protected]
> Cambridge CB2 0XY, U.K.
> www-structmed.cimr.cam.ac.uk
>
>
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