Hi

Actually, since Deep Mind is a commercial organization (funded by shareholders 
and people who buy their services), I don’t think they are subject to the same 
rules as academia as regards making their source code public. It would be very 
nice if they would (could?) make their code public, but I don’t see any 
obligation to do so. Their responsibility is primarily to their shareholders 
(you can argue the rights and wrongs of that until the cows come home).

Commercially, they can maintain an advantage through several routes - they can 
publish in patents (so people can see what they’ve done, but not legally 
implement it without a licence), they can keep it all confidential and hope 
that no-one manages to reverse engineer and implement it (at the risk of 
someone else publishing the details and removing their advantage), they can 
publish something that is honest but just misleading enough (or lacking in 
detail) to throw people off the scent, or…

If they can provoke other developers to work out where they have gone wrong and 
produce something that competes with AlphaFold2, that would be great. If they 
can provide something like a web service that allows users to run their method, 
that would be great too, but the important thing is (that unless they had prior 
knowledge of the structures in CASP14) they’ve done something that no-one else 
has managed to do as well in spite of years of trying.

Just my two ha’porth.

Harry

> On 9 Dec 2020, at 10:36, Hughes, Jonathan 
> <jon.hug...@bot3.bio.uni-giessen.de> wrote:
> 
> i think the answer to all these doubts and questions is quite simple: the 
> AlphaFold2 people must make all details of their methods public (source code) 
> and, as would probably be necessary, open their system for inspection and use 
> by independent experts. isn't that what peer review and reproducibility are 
> all about? those rules date from the time before every tom, dick and 
> henriette could publicize anything they like inside their own zuckerberg 
> bubble. my opinion is that this is a virtual infectious disease that will 
> cause humanity far bigger problems than corona ever will – i just hope i'm 
> wrong!
> 
> best
> 
> jon
> 
>  
> 
> Von: CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> Im Auftrag von Mark J van 
> Raaij
> Gesendet: Mittwoch, 9. Dezember 2020 11:14
> An: CCP4BB@JISCMAIL.AC.UK
> Betreff: Re: [ccp4bb] External: Re: [ccp4bb] AlphaFold: more thinking and 
> less pipetting (?)
> 
>  
> 
> on the day the news came out, I did wonder if the AlphaFold2 team somehow had 
> access to all the preliminary PDB files sent around via Gmail (which belongs 
> to the same company), but more as a joke/conspirational thought.
> 
> "our" target T1052, was also predicted very well by domains and as a monomer. 
> It will be interesting to see how well future iterations of the method can 
> assemble the complete protein chain and the complete protein chains into the 
> correct heteromer.
> 
>  
> 
> Mark J van Raaij
> Dpto de Estructura de Macromoleculas
> Centro Nacional de Biotecnologia - CSIC
> calle Darwin 3
> E-28049 Madrid, Spain
> tel. (+34) 91 585 4616
> 
> Section Editor Acta Crystallographica F
> https://journals.iucr.org/f/
> 
>  
> 
> On 9 Dec 2020, at 10:37, Cedric Govaerts <cedric.govae...@ulb.ac.be> wrote:
> 
>  
> 
> Dear All
> 
>  
> 
> After about 10 (!) years of (very) hard work we solved the structures of our 
> dearest membrane transporter.  Dataset at 2.9 And resolution, fairly 
> anisotropic, experimental phasing, and many looooong nights with Coot and 
> Buster to achieve model refinement. 
> 
>  
> 
> The experimental structure had a well defined ligand nicely coordinated but 
> also a lipid embedded inside the binding cavity (a complete surprise but 
> biologically relevant) and two detergent molecules well defined 
> (experimental/crystallisation artefact).
> 
>  
> 
> As our paper was accepted basically when CASP organisers were calling for 
> targets I offered my baby to the computing Gods. However we only provided the 
> sequence to CASP, no info regarding any ligand or lipid.
> 
>  
> 
> Less than a month after, the CASP team contacted us and send us the best 
> model.  In fact it was 2 half models as the transporter is a pseudo dimer, 
> with the N-lobe and C-lobe moving relative to each other during transport 
> cycle, thus divided as two domains in CASP.
> 
>  
> 
> The results were breathtaking. 0.7 And RSMD on one half, 0.6 on the other. 
> And yes, group 427 was the superpower (did not know at the time that it was 
> AlphaFold).
> 
>  
> 
> We had long discussions with the CASP team, as -for us- this almost exact 
> modelling was dream-like (or science fiction) and -at some point- we were 
> even suspecting fraud, as our coordinates had travelled over the internet a 
> few times around when interacting with colleagues.  The organisers reassured 
> us that we were not the only target that had been “nailed” so no reason to 
> suspect any wrongdoing.
> 
>  
> 
> To this day I am still baffled and I would be happy to hear from the 
> community, maybe from some of the CASP participants.
> 
>  
> 
> The target is T024, the “perfect" models are domain-split version (T024-D1 
> and T024-D2), as AlphaFold2 did not perform so well on the complete assembly.
> 
> Deposited PDB is 6T1Z
> 
>  
> 
> Cedric
> 
>  
> 
> PS: I should also note that many other groups performed very well, much 
> better than I would have dreamed, including on the full protein but just not 
> as crazy-good.
> 
> —
> 
> Prof. Cedric Govaerts, Ph.D.
> Universite Libre de Bruxelles
> Campus Plaine. Phone :+32 2 650 53 77
> Building BC, Room 1C4 203
> Boulevard du Triomphe, Acces 2
> 1050 Brussels
> Belgium
> http://govaertslab.ulb.ac.be/
> 
>  
> 
>  
> 
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