On thus topic, I note that the "ModelCIF" format has been developed which 
allows inclusion of appropriate parameters associated with predicted models, 
such as those from AlphaFold (e.g. confidence values instead of B-values).  

Would it be too much to ask for fields associated with "modelled but not seen" 
parts of a model to be included in this expanded format (or even in the normal 
PDBx/mmcif dictionary)?

Harry
--
Dr Harry Powell

> On 10 Mar 2023, at 20:15, Dale Tronrud <[email protected]> wrote:
> 
> Hi
> 
>   As a frequent contributor to prior discussions on this same topic I would 
> like to broaden the discussion a bit.  I'm sorry to say that most of the 
> comments on this threat are exactly the same positions that have been 
> expressed many times over the years.  I don't want to spent time, again, 
> retyping my opinions on how I prefer to torment the parameters of my models 
> to express what I believe is going on inside my crystals.
> 
>   The fundamental problem is that the parameters we are forced to use, in our 
> PDB depositions and in the refinement and model building programs available 
> to us, are wholly inadequate.  We cannot accurately (or precisely) describe 
> what we are are envisioning for the surface side chains, and sometimes entire 
> stretches of main chain, in our proteins. We can continue to argue with each 
> other year after year, but there is no solution to this problem other than 
> changing the nature of PDB models and allowing a reasonable description of 
> multi-conformation models.
> 
>   I believe it is fair to say that the consensus after a previous round of 
> this discussion was that, at the very least, we need a flag for each atom 
> which indicates whether that atom was placed based on electron density or 
> simply to make a chemically complete set of atoms for that type of monomer.  
> I haven't looked but I think that was about five or ten years ago.  Since 
> then the PDB has made major changes to the structure of PDB entries that will 
> require most software for analysis of macromolecular models be rewritten and 
> right now that organization is making a major push to get us to virtually 
> attend a workshop to help us make this transition.  And yet I don't think 
> there is anything in this new data dictionary to help us with this important 
> but intractable problem.
> 
>   Unless the PDB gives us the parameters we need to properly describe a 
> macromolecular model, and the refinement/model building developers give us 
> the tools to make use of them, we will be back here again, every five years 
> or so, rehashing this debate over exactly the same, irreconcilably poor, 
> solutions to this problem.
> 
> Dale E. Tronrud
> 
> 
>> On 3/10/2023 1:05 AM, Julia Griese wrote:
>> Hi all,
>> My impression has been that the most common approach these days is to “let 
>> the B-factors take care of it”, but I might be wrong. Maybe it’s time to run 
>> another poll?
>> Personally, I call any other approach R-factor cosmetics. The goal in model 
>> building is not to achieve the lowest possible R-factors, it’s to build the 
>> most physically meaningful, most likely to be correct, model. So if you know 
>> that the side chain is part of the protein, you should model it the best way 
>> you can. If it’s there, just disordered, then the most correct way to model 
>> it is to let it have high B-factors. Most molecular graphics programs don’t 
>> flag zero-occupancy atoms, so the user might never notice. Truncation of a 
>> side chain, unless there is evidence that it really physically isn’t there, 
>> is also misleading, in my opinion. I don’t believe that it is more helpful 
>> to the non-expert user than high B-factors either.
>> If people who are not structural biologists themselves don’t know how to use 
>> a structure, then we need to educate them better. It is very straightforward 
>> these days to look at electron density in the PDB viewer. It used to be 
>> difficult, but nowadays there’s no excuse for not checking the electron 
>> density. The PDB validation flags RSRZ outliers. You can easily colour a 
>> structure by B-factors. It doesn’t take that much effort to teach students 
>> how to validate structures. The main point you need to get across is that it 
>> is necessary to do so. And this needs to be done not only in courses aimed 
>> at prospective experimental structural biologists, of course, but whenever 
>> students use structures in any way.
>> This is just the opinion of someone who feels very strongly about teaching 
>> structure validation and rejoices when students’ reply to the question “What 
>> was the most important thing you learned today?” is: “Don’t blindly trust 
>> anything.”
>> Cheers
>> /Julia
>> -- 
>> Dr. Julia Griese
>> Associate Professor (Docent)
>> Principal Investigator
>> Department of Cell and Molecular Biology
>> Uppsala University
>> BMC, Box 596
>> SE-75124 Uppsala
>> Sweden
>> email: [email protected]
>> phone: +46-(0)18-471 4982
>> http://www.icm.uu.se/structural-biology/griese-lab/ 
>> <http://www.icm.uu.se/structural-biology/griese-lab/>
>> *From: *CCP4 bulletin board <[email protected]> on behalf of Bernhard 
>> Lechtenberg <[email protected]>
>> *Reply-To: *Bernhard Lechtenberg <[email protected]>
>> *Date: *Friday, March 10, 2023 at 05:07
>> *To: *"[email protected]" <[email protected]>
>> *Subject: *Re: [ccp4bb] To Trim or Not to To Trim
>> I found the poll I wrote about earlier. This actually is way older than I 
>> had expected (2011). You can see the poll results (which was run by Ed 
>> Pozharski) and discussion at the time here in the CCP4BB archive:
>> https://www.mail-archive.com/[email protected]/msg20268.html 
>> <https://www.mail-archive.com/[email protected]/msg20268.html>
>> In brief, the results of 240 respondents were:
>> Delete the atoms                                         43%
>> Let refinement take care of it by inflating B-factors    41%
>> Set occupancy to zero                                    12%
>> Other                                                     4%
>> Bernhard
>> *From: *CCP4 bulletin board <[email protected]> on behalf of Debanu Das 
>> <[email protected]>
>> *Date: *Friday, 10 March 2023 at 2:56 pm
>> *To: *[email protected] <[email protected]>
>> *Subject: *Re: [ccp4bb] To Trim or Not to To Trim
>> We dealt with this in-depth during structural genomics days when we 
>> deposited over 1500 novel, high-quality, experimentally-phased structures 
>> into the PDB. Think it’s prudent to trim/truncate side chains without 
>> reliable density.
>> Non-structural biologists using PDB structures without expert help can err 
>> in any of these scenarios: misinterpreting most common/random rotamer, zero 
>> occupancy atoms, B-factors, etc.
>> What is the value of populating the PDB, which is a structural model 
>> repository, with such information that is not there, i.e., reliable 
>> structural model?
>> Any trained crystallographer/structural biologist can easily add in side 
>> chain information if needed for modeling/computational chemistry reasons.
>> Best regards,
>> Debanu
>> On Thu, Mar 9, 2023 at 6:50 PM Jurgen Bosch <[email protected] 
>> <mailto:[email protected]>> wrote:
>>    I’d say no trimming to side chains for the following reason: There
>>    are non-structural biologists using PDB files and if atoms are
>>    missing they don’t know what to do. A better approach is where no
>>    side chain density allows support of placement, pick the most common
>>    rotamer and set the occupancy to zero for those atoms lacking
>>    density support. More work for you but more accurate in my opinion.
>>    Jürgen
>>    _______________________________________________
>>    Jürgen Bosch, PhD, MBA
>>    Center for Global Health & Diseases
>>    Case Western Reserve University
>>    Cleveland, OH 44106
>>    https://www.linkedin.com/in/jubosch/
>>    <https://www.linkedin.com/in/jubosch/>
>>    CEO & Co-Founder at InterRayBio, LLC
>>        On Mar 9, 2023, at 9:45 PM, Bernhard Lechtenberg
>>        <[email protected]
>>        <mailto:[email protected]>> wrote:
>>        Hi Rhys,
>>        I am also all for leaving side chains and letting the B-factors
>>        deal with the weak/absent density.
>>        I don’t think there is a consensus, but I kind of remember that
>>        somebody did a poll a few years ago and if I remember correctly
>>        the main approaches were the one described above, or trimming
>>        the side-chains.
>>        Bernhard
>>        *Bernhard C. Lechtenberg* PhD
>>        NHMRC Emerging Leadership Fellow
>>        Laboratory Head
>>        Ubiquitin Signalling Division​​​​​​​​​​​​​​
>>        E [email protected] <mailto:[email protected]>
>>        T +61 3 9345 2217
>>        *From: *CCP4 bulletin board <[email protected]
>>        <mailto:[email protected]>> on behalf of Rhys Grinter
>>        <[email protected]
>>        <mailto:[email protected]>>
>>        *Date: *Friday, 10 March 2023 at 12:26 pm
>>        *To: *[email protected] <mailto:[email protected]>
>>        <[email protected] <mailto:[email protected]>>
>>        *Subject: *[ccp4bb] To Trim or Not to To Trim
>>        Hi All,
>>        I'm trying to crowdsource an opinion on how people deal with
>>        modelling side chains with poorly resolved electron or cryoEM
>>        density.
>>        My preference is to model the sidechain and allow the B-factors
>>        to go high in refinement to represent that the side chain is
>>        flexible. However, I'm aware that some people truncate
>>        sidechains if density is not present to justify modelling. I've
>>        also seen models where the sidechain is modelled but with zero
>>        occupancy if density isn't present.
>>        Is there a consensus and justifying arguments for why one
>>        approach is better?
>>        Cheers,
>>        Rhys
>>        
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>> LinkedIn: www.linkedin.com/in/debanudas 
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