Re: [ccp4bb] new PDB file format

2023-04-03 Thread Gerard Kleywegt

Hi Robbie,

Well, there is 1SRX (https://pdbe.org/1srx)) from 1976, CA-only, coordinate 
precision 0.05Å. The explanation is in the paper: "The maps were interpreted 
in terms of the known amino-acid sequence (2) and a skeletal model of one 
molecule was built with the Kendrew-type models using an optical 
comparator(13)." :-) (https://www.pnas.org/doi/epdf/10.1073/pnas.72.6.2305)


--Gerard





On Mon, 3 Apr 2023, Robbie Joosten wrote:


WHAT_CHECK has a check for suspiciously rounded coordinates. I have never seen 
it triggered.
Cheers,
Robbie

On 3 Apr 2023 10:11, James Holton  wrote:
  Thanks to everyone for being such good sports!

  It is good to know that there is still room for good-natured funny in 
what can be stressful times.

  Truth be told, I actually did do some experiments rounding off PDB 
coordinates to the nearest A.  You can try it with this
  one-line shell command:

cat refined.pdb |\
awk '! /^ATOM|^HETAT/{print;next}\
  {X=substr($0,31,8);Y=substr($0,39,8);Z=substr($0,47,8);\
   pre=substr($0,1,30);post=substr($0,55)}\
  {X=sprintf("%.0f",X);Y=sprintf("%.0f",Y);Z=sprintf("%.0f",Z)}\
  {printf("%s%8.3f%8.3f%8.3f%s\n",pre,X,Y,Z,post)}' |\
cat > roundoff.pdb

    These rounded-off structures look ... weird. And yes they really do 
crash validation programs.  Food for thought perhaps
  on what "resolution", rmsd, and especially GDT_TS really mean?

  -James Holton
  MAD Scientist


  On 4/1/2023 1:28 PM, Sweet, Robert wrote:

Knowing the author as I do, I checked the date and time, and wasn't fooled.


From: CCP4 bulletin board  on behalf of Carter, Charlie 

Sent: Saturday, April 1, 2023 4:06 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] new PDB file format

I fell for this momentarily, hence compliments to James. I was fooled by the 
absolutely sensible intro.

Charlie

On Apr 1, 2023, at 12:34 AM, James Holton  wrote:

Anyone who has ever had to lecture a student for writing their unit cell lengths to dozens of decimal places is going to love the new 
PDB format.  It is more compact, more realistic, and less misleading to the poor, downstream consumers of structural data.


Only a few structures in the PDB are better than 1.0 A, and none come even close to 0.1 A.  Nevertheless, the classic PDB file format 
always listed atomic coordinates to three decimal places!  That's implying a precision of 0.001 A, which is not supported by the resol

ution of the data.  At long last, this age-old error is being corrected.  From 
now on, coordinates will be listed to the nearest Angst
rom only.

An unexpected consequence of this is that R-free of a typical structure is 
going to rise from the current ~20% to well into the 40%s.
 This is, however, more consistent with high-impact structures published in 
big-named journals using modern, better data collection me
thods like XFELs and CryoEM, so we are going to call this an improvement.  
Besides, R factors are just cosmetic anyway.

Updated molprobity scores are not yet available while the authors fix bugs in their programs.  Right now, they return errors with the 
new, improved coordinates, such as:

line 272: 57012 Segmentation fault  (core dumped)

So, just as we all must adapt to Python 3 this new standard I'm sure will earn 
us all the thanks of future generations. They will no d
oubt be very grateful that we took these pains to protect them from the dangers 
of too many decimal places.

-James Holton
MAD Scientist



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Re: [ccp4bb] Future Diffraction Methods

2023-01-30 Thread Gerard Kleywegt

Hi all,

I'm a big believer in cross-pollination between disciplines. I think there 
could be room for a multidisciplinary methods meeting (MMM) provided the right 
topics are chosen. If these are things that concern NMR-ists, X-ray-ans and 
cryo-EM-ers equally you might get the right mix of people in the room and 
exchange of ideas and experiences with it. For example, all three use Maximum 
Likelihood (ML) methods. All three are or possibly will be interested in 
applying Machine Learning (e, ML) methods (e.g., in cryo-EM these have 
already been used for automatic particle picking and map improvement). And 
they all need to worry about validating models based on predicted models.


Having said that, I think there is also a need for specialised, 
method-specific meetings, but the two types of meeting are not mutually 
exclusive.


My 2 öre,

--Gerard



On Mon, 30 Jan 2023, Alexandre Ourjoumtsev wrote:


Hi, everybody, hi, Nukri and Pavel !

I fully agree with Pavel that, if the speakers are not exceptional, if they are 
(as usually) concentrated on their specific and narrow problems, 
cross-discipline meetings make us lost quite fast, they are annoying and 
useless. Richard Feynmann had the same experience, according to his books :-)

At such meetings, people need to have a common point. However, it may be a 
point different from the SUBJECT of the research. This may be common TOOLS. And 
this indeed may lead to new ideas and results, maybe great ones.

There is a many-years positive experience of such meetings in Pushchino in 80ths (both of 
you know this place; for other readers of this post - this was indeed a great place !). 
Closer to our community, as I remember, Paul Adams and John Spence organized such kind of 
meetings about 20 years ago in US. I guess I know practical results from both these 
groups of meetings. Some Crystallographic Computing Schools also try to act a little bit 
"around the tools".

Why do not we think specifically in THIS direction (which is actually what 
Nukri said, right? and somehow not so far from the previous GRC?) ?
This is hard but feasible. But indeed hard :-(

Best regards to everybody,
and many thanks to James for raising the problem !

Sacha Urzhumtsev

- Le 30 Jan 23, à 2:38, Nukri Sanishvili  a écrit :


Hi Pavel,
Your description of the current status is exactly correct. And that's exactly
what I am proposing to change or, more accurately, try to change. By seeking
out and bringing together people who do complementary and collaborative work,
so they can set an example for others.
This, of course, isn't meant in place of more narrowly defined topical meetings
and conferences but to be in addition to those.
James asked the community if we had new ideas and this is a new-ish approach I
was suggesting.
Don't get me wrong - I myself will happily continue my efforts in more narrowly
defined meetings.
Best wishes,
Nukri



On Sun, Jan 29, 2023 at 6:44 PM Pavel Afonine < [ mailto:pafon...@gmail.com |
pafon...@gmail.com ] > wrote:



Nukri,



IMO, the idea of cross-discipline meetings is great conceptually, at least for
reasons you pointed out, but utopical in practice. When we attend our
field-specific meetings we meet colleagues we know, we talk to collaborators
from the past or find new ones, we have things in common that we can talk about
to forge something new, we meet authors of papers we were excited to read, and
so on, and so on.
I once attended a meeting of some chemistry society, well, which is not too far
from what we are doing, really, as interpreting atomic models is essentially
putting your chemistry knowledge into production. And, at that meeting I felt
like I'm alone in a dark forest.
Now, I imagine, if you bring two (or more) groups of people to your meeting from
two different domains, well, I guess you will end up having two bubbles of
people clustered by their field of interest.



Same disclaimer goes here as yours -- no offence to any one, just thinking out
loud...



All the best!
Pavel



On Sun, Jan 29, 2023 at 6:09 AM Nukri Sanishvili < [ mailto:sannu...@gmail.com |
sannu...@gmail.com ] > wrote:



Hi James,
This meeting has indeed been one of the best ones by its format, content, and
atmosphere. Many thanks to all the organizers and attendees of the past.
Nevertheless, it is not surprising that it was cancelled, given the trends in
structural biology research. Straightforward evolutionary pressure to adapt or
else...



Throughout my career I was always amazed (dare I say, annoyed?) how scientists
from different fields, or even the same field but different methods, speak
different languages. How little they understand each other, become entrenched
in their own methods and how much of the collaboration/cooperation
opportunities are wasted.



IMO, having a conference on "Complementary Methods in Structural Biology" with
the emphasis on complementarity and not on individual methods, would be a great
benefit in the long run. Hopefully 

[ccp4bb] Who will captain the good ship EMDB?

2023-01-11 Thread Gerard Kleywegt

Dear colleagues,

We are living through unprecedented, exciting times for the cryo-EM field. For 
EMDB, the past decade has been challenging with sustained exponential(!) growth 
of the archive, and rapid methodological changes in the field that need to be 
supported (deposition requirements, metadata, validation).


With continuing major advances in the field (such as in-situ structural 
biology) and progress in other relevant fields (such as accurate 
protein-structure prediction methods), the years ahead promise to be equally 
exciting and challenging for EMDB.


To steer EMDB through the high seas of science, we are looking to recruit a new 
captain, er, Team Leader (an EMBL Faculty position). Are you (or do you know 
someone who is) an ambitious, mid-career scientist who has the skills, drive 
and vision to manage this journey, with the help of an enthusiastic team of 
scientists and software developers?


If you are (or you do), please set sail to: 
https://www.embl.org/jobs/position/EBI02047 for more information.


---

The Electron Microscopy Data Bank (EMDB; emdb-empiar.org) is one of the three 
core archives of the Worldwide Protein Data Bank organisation (wwPDB; 
wwpdb.org). The activities of the EMDB team at EMBL-EBI include archival, 
curation, integration, visualisation, validation and dissemination of cryo-EM 
data, weekly production processes, planning, coordinating and working with our 
wwPDB partners, and outreach, training and public engagement.


We expect the successful candidate to have ample experience with, and a good 
practical and theoretical understanding of cryo-EM/ET, to have experience 
carrying out scientific software development, as well as an ability to write 
successful grants, to manage projects, and to lead a highly skilled team.


The vacancy will close on 23 February 2023 and (virtual) interviews will take 
place on Monday 13 March 2023.


Please feel free to bring this position to the attention of anyone with the 
right skillset who might be interested.


Best wishes,

Gerard Kleywegt & Ardan Patwardhan

---
Gerard J. Kleywegt, EMBL-EBI, Hinxton, UK
Head of Molecular and  Cellular Structure
ger...@ebi.ac.uk pdbe.org emdb-empiar.org
PA: Roisin Dunloppdbe_ad...@ebi.ac.uk



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Re: [ccp4bb] ChEBI and SMILES

2022-10-07 Thread Gerard Kleywegt

Hi Harry,

On the ChEBI website, if I type a simple SMILES string into the search box 
(c1c1) it takes me to the corresponding entity page. I don't know if they 
have an API that supports this but I'm sure the friendly folks of the ChEBI 
helpdesk (https://www.ebi.ac.uk/chebi/emailChebiForward.do) can tell you.


Another resource that may be of use in this context is UniChem 
(https://www.ebi.ac.uk/unichem/). You provide an InChI (not SMILES 
unfortunately) and it will then return a list of the identifiers of the 
compound in bunch of resources (incl. ChEMBL, ChEBI, PDB, PubChem, Zinc, etc.) 
- if they exist in that resource of course. (It offers an API so is good for 
programmatic access - https://www.ebi.ac.uk/unichem/api/docs )


You can also provide a compound ID from any of those resources to find out 
what it is called in the other resources (if it exists there), e.g. 
https://www.ebi.ac.uk/unichem/compoundsources?type=sourceID=BNZ=3 
searches for the compound we know as BNZ in the PDB.


Hope this helps,

--Gerard




On Fri, 7 Oct 2022, Harry Powell wrote:


Hi Jeet

This is very useful - many thanks.

I was hoping there might be some kind of API for searching the ChEBI database 
online, but there we go…

It looks like downloading the ChEBI database is the first step here, since many 
entries appear to have SMILES information.

But (important to note) ChEBI ≠ ChEMBL, although there is an overlap (a 
considerable ione…).

Harry


On 7 Oct 2022, at 10:29, jeet balraj  wrote:

Hi Harry
To search the ligand of interest in the ChEMBL database, you can follow these 
simple steps:
1. download the ChEMBL database and extract all its SMILES.
2. calculate the MorganFingerprint of each of the SMILES in the database.
3. calculate the MorganFingerprint of your ligand.
4. use the FPSim2 package from ChEMBL for the Tanimoto similarity search.
you can use RDKit to calculate the morgan fingerprints of each SMILES string.
Note: you have to first convert each SMILES in the database to canonical form.
I hope this helps.
Thanks
Jitendra Kuldeep
Postdoc researcher
Machine learning and precision oncology group
Cancer research center of marseille, INSERM
France 13009


On Fri, Oct 7, 2022 at 11:13 AM Harry Powell 
<193323b1e616-dmarc-requ...@jiscmail.ac.uk> wrote:
Hi

Probably a silly question, but I was wondering how to search for a ligand in 
ChEBI with a SMILES string? It’s not immediately obvious to my Friday-morning 
mind ...

Harry


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Best wishes,

--Gerard

**
   Gerard J. Kleywegt

  http://xray.bmc.uu.se/gerard   mailto:ger...@xray.bmc.uu.se
**
   The opinions in this message are fictional.  Any similarity
   to actual opinions, living or dead, is purely coincidental.
**
   Little known gastromathematical curiosity: let "z" be the
   radius and "a" the thickness of a pizza. Then the volume
of that pizza is equal to pi*z*z*a !
**



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[ccp4bb] Vacancy for a Scientific Programmer at EMDB (EMBL-EBI, Cambridge, UK)

2022-09-14 Thread Gerard Kleywegt

Dear colleagues,

EMBL-EBI is looking to recruit a Scientific Programmer to work on the Electron
Microscopy Data Bank (EMDB; emdb-empiar.org), one of the three core archives of
the Worldwide Protein Data Bank organisation (wwPDB; wwpdb.org).

The Scientific Programmer will work in a small but tight international team
focusing on managing the flow of data into the archive (data-in; deposition,
validation and curation) and the public release of the data (production). In the
past two years, EMDB has doubled in size to over 20,000 entries and the archive
is set to continue to grow very rapidly in the years to come, so this is a very
exciting time to join the effort.

More information can be found in the vacancy notice at
https://www.embl.org/jobs/position/EBI02066

A detailed description of the role and its requirements is available from
https://oc.ebi.ac.uk/s/j1g7grHEJoeO9BJ

The application period for this post will close on 23 October 2022 and (virtual)
interviews will take place on 17 or 18 November.

Please feel free to bring this position to the attention of anyone with the
right skillset who might be interested.

Best wishes,

Gerard Kleywegt

---
Gerard J. Kleywegt, EMBL-EBI, Hinxton, UK
Head of Molecular and  Cellular Structure
ger...@ebi.ac.uk pdbe.org emdb-empiar.org
PA: Roisin Dunloppdbe_ad...@ebi.ac.uk



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[ccp4bb] Yes, there are now 214 *million* structures in the AlphaFold Protein Structure Database

2022-07-28 Thread Gerard Kleywegt

Hi all,

I thought Sameer was burying the lead a tad in his message... :-) So, for 
those of you who -like me- are not on social media:


==> As of today, the AlphaFold Protein Structure Database contains 214 million 
models predicted with AlphaFold, covering almost all of UniProt. <==


So, if your favourite protein was not available in the database before today, 
it's worth checking in again at https://www.alphafold.ebi.ac.uk/ now.


See also:

- EMBL-EBI press release: 
https://www.ebi.ac.uk/about/news/technology-and-innovation/alphafold-200-million/

- Nature news: https://www.nature.com/articles/d41586-022-02083-2

- IUCr J guest editorial about the potential impact of all this on structural 
biologists (shameless plug): https://journals.iucr.org/m/issues/2022/04/00/me6185/index.html



Best wishes,

--Gerard





On Thu, 28 Jul 2022, Sameer Velankar wrote:


Dear All,

You may have seen our announcement today about expanding the AlphaFold Protein 
Structure Database to 214M predicted models. To enable this expansion, we’ve 
updated the Predicted Aligned Error (PAE) JSON format to make it compact (about 
4x smaller):

The PAE JSON numbers are now rounded to the closest integer, giving ~75% 
compressed size reduction. The integer resolution is sufficient for analytical 
purposes.
The indices are not stored anymore since we store the full 2D PAE matrix rather 
than a sparse one, giving ~4% compressed size reduction.
The “distances” field has been renamed to “predicted_aligned_error” and is now 
stored as a 2D array of shape (num_res, num_res) rather than a 1D array. We 
renamed the field on purpose so that existing code breaks rather than 
potentially silently returning wrong values.

For a protein of length num_res, the PAE JSON file has now the following format:

[{
 "predicted_aligned_error": [[0, 1, 4, 7, 9, ...], ...],  # Shape: (num_res, 
num_res).
 "max_predicted_aligned_error": 31.75  # Scalar.
}]

The fields in the JSON file are:
predicted_aligned_error: The PAE value of the residue pair, rounded to the 
closest integer. For PAE value on position (i, j), i is the residue on which 
the structure is aligned for the predicted error, j is the residue on which the 
error is predicted.
max_predicted_aligned_error: A number that denotes the largest possible 
unrounded value of PAE that could occur in the PAE array. The smallest possible 
value of PAE is 0.

The updated PAE format is only available from the AlphaFold Protein Structure 
Database. The PAE format from the AlphaFold Colab notebook is not updated.

If you require support with this change, please email alphaf...@deepmind.com 
 and they may be able to assist.

Best Wishes,

Sameer Velankar


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Best wishes,

--Gerard

**
   Gerard J. Kleywegt

  http://xray.bmc.uu.se/gerard   mailto:ger...@xray.bmc.uu.se
**
   The opinions in this message are fictional.  Any similarity
   to actual opinions, living or dead, is purely coincidental.
**
   Little known gastromathematical curiosity: let "z" be the
   radius and "a" the thickness of a pizza. Then the volume
of that pizza is equal to pi*z*z*a !
**



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[ccp4bb] Vacancy for EMDB Team Leader (EMBL Faculty position)

2022-07-18 Thread Gerard Kleywegt

Dear colleagues,

EMBL-EBI is looking to recruit a new Team Leader (EMBL Faculty position) to 
take charge of the Electron Microscopy Data Bank (EMDB; emdb-empiar.org), one 
of the three core archives of the Worldwide Protein Data Bank organisation 
(wwPDB; wwpdb.org).


In the past two years, EMDB has doubled in size to over 20,000 entries and the 
archive is set to continue to grow very rapidly in the years to come. We are 
therefore looking for an ambitious, mid-career scientist who has the skills, 
drive and vision to manage this expansion, with the help of the extant EMDB 
team (7 staff members at present), in collaboration with our wwPDB colleagues, 
and in consultation with the cryo-EM community.


The activities of the EMDB team include archival, curation, integration, 
visualisation, validation and dissemination of cryo-EM data, weekly production 
processes, planning, coordinating and working with our wwPDB partners, and 
outreach, training and public engagement. We expect the successful candidate to 
have ample experience with, and a good practical and theoretical understanding 
of cryo-EM/ET; to have experience carrying out scientific software development; 
as well as an ability to write successful grants, to manage projects, and to 
lead a team of scientists and software developers.


More details can be found in the vacancy notice at 
https://www.embl.org/jobs/position/EBI02047


The vacancy will close on 18 September 2022 and (virtual) interviews will take 
place on Thursday 20 October.


Please feel free to bring this position to the attention of anyone with the 
right skillset who might be interested.


Best wishes,

Gerard Kleywegt

---
Gerard J. Kleywegt, EMBL-EBI, Hinxton, UK
Head of Molecular and  Cellular Structure
ger...@ebi.ac.uk pdbe.org emdb-empiar.org
PA: Roisin Dunloppdbe_ad...@ebi.ac.uk



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[ccp4bb] AlphaFold DB - free and open access to (millions of) protein structure predictions

2021-07-22 Thread Gerard Kleywegt

Dear colleagues and friends,

I would like to share some exciting news that has been announced today. 
EMBL-EBI and DeepMind have co-developed the AlphaFold Protein Structure 
Database (AlphaFold DB; https://alphafold.ebi.ac.uk), a joint project to 
openly and freely share millions of AlphaFold protein-structure predictions 
with the scientific community. The database launched officially at 4 pm UK 
time on 22 July. Today’s release contains approximately 365,000 structures 
(covering over 20 reference proteomes), which will increase to an estimated 
130 million (!) 3D models in the coming months (covering all UniProt sequence 
clusters with up to 90% mutual sequence identity, i.e. UniRef90). A Nature 
paper describing  the predictions for the human proteome and mentioning the 
new AlphaFold DB resource was made public today: 
https://www.nature.com/articles/s41586-021-03828-1


The AlphaFold DB resource has been the work, carried out over a period of 
about three months, of scientists, IT specialists, web designers, comms people 
etc. at both EMBL-EBI and DeepMind, with the PDBe-KB team 
(https://pdbe-kb.org/), led by Sameer Velankar, playing a major role.


Given the accuracy demonstrated by AlphaFold models to date, this resource is 
likely to have a major impact not only on structural biology but on many 
fields of science and biotechnology. Soon, for the first time in history, for 
every protein sequence known to science, there will be either an experimental 
structure in the PDB, or a 3D model in AlphaFold DB, or a structure for a 
protein within “homology-modelling distance” of a target protein. The source 
code of AlphaFold has been made open as well, so predictions for completely 
new and non-natural (designed) sequences can be generated by anybody who wants 
to.


Speaking from experience, it may take some time to wrap your head around the 
sheer scale of the new resource and to ponder its potential impact on science. 
A small group of leading structural biologists within EMBL have produced a 
briefing document 
(https://www.embl.org/news/science/alphafold-potential-impacts/) that 
describes the technical achievements, the current limitations of AlphaFold and 
some of the potential applications and opportunities for new research in a 
number of (mainly structure-related) fields.


I for one am immensely excited and I invite you all to check out the new 
resource.


Best wishes,

--Gerard

---
Gerard J. Kleywegt, EMBL-EBI, Hinxton, UK
Head of Molecular and  Cellular Structure
ger...@ebi.ac.uk pdbe.org emdb-empiar.org
PA: Roisin Dunloppdbe_ad...@ebi.ac.uk



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[ccp4bb] Changes to the EMDB and EMPIAR URLs and the EMDB website

2021-07-21 Thread Gerard Kleywegt

Dear colleagues,

We are writing to you about some changes to the EMDB and EMPIAR URLs and the 
EMDB website.


As of today, EMDB and EMPIAR have their own EMBL-EBI top-level URL at 
https://www.ebi.ac.uk/emdb and https://www.ebi.ac.uk/empiar, respectively.


We will continue to operate the old websites for another week or two and then 
shut these down. At that stage we will put (best-effort) redirects in place to 
the new websites so as to minimise disruption for our users.


We would appreciate it if you could update any bookmarks or links you may have 
to these resources. More information about the changes and how some important 
URLs (e.g., for EMDB and EMPIAR entry pages) have changed can be found at 
https://www.ebi.ac.uk/emdb/move


Perhaps somewhat burying the lead, EMDB also launched a completely new website 
today with much improved look-and-feel, more and better functionality, vastly 
improved search system and entry pages that now provide (access to) much more 
(meta)data than before, etc.


Please steer your browser to https://www.ebi.ac.uk/emdb to check it out! Over 
the next few days we will be releasing short videos to highlight various 
features (homepage, basic search, entry pages and advanced search). These will 
be available via the new homepage and also be advertised on our Twitter 
account, @EMDB_EMIAR


If you have any questions (or want to report any issues, or have any other 
feedback) regarding these changes, please contact the EMDB helpdesk 
(emdbh...@ebi.ac.uk) or the EMPIAR helpdesk (empiarh...@ebi.ac.uk).


--The EMDB and EMPIAR teams at EMBL-EBI

---
Gerard J. Kleywegt, EMBL-EBI, Hinxton, UK
Head of Molecular and  Cellular Structure
ger...@ebi.ac.uk pdbe.org emdb-empiar.org
PA: Roisin Dunloppdbe_ad...@ebi.ac.uk



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Re: [ccp4bb] Pymol Map range

2021-05-06 Thread Gerard Kleywegt

Hi all,

By popular demand (yeah, me too) the HTML versions of the old USF manuals have 
been kindly added to the GitHub site (link below) by Martyn Winn.


Also, the machine in Uppsala that used to serve them has finally given up the 
ghost so GitHub is now the only source of USF source code and documentation.


--Gerard

PS: I managed to mistype the word "GitHub" twice while composing this email, 
as GutHub and HitHub...



On Thu, 4 Mar 2021, Gerard DVD Kleywegt wrote:


Hi all,

Following up on this: some time ago, Martyn Winn was kind enough to put the 
source of a bunch of old Uppsala Software Factory programs in GitHub:


  https://github.com/martynwinn/Uppsala-Software-Factory

It's all unsupported now (I haven't compiled anything in 12 years...) but 
free to do with whatever you like.


(The website in Uppsala has unfortunately not been accessible for several 
months already. This means that the manuals are not online. If there is 
interest I could post a tgz file with -as far as I can determine- the latest 
version of all manuals in HTML format (0.8 MB total).)


--Gerard


On Wed, 3 Mar 2021, James Holton wrote:


Yes, I stand corrected. "mapmask" is the CCP4 program.

mapman is still around.  I even found a way to get it to work on 64-bit!
https://git.bl831.als.lbl.gov/jamesh/map-bender/-/blob/master/mapman_regression_test.csh

-James Holton
MAD Scientist


On 3/3/2021 9:10 AM, Jon Cooper wrote:

 For old-schoolers, mapmask (once known as extend) in ccp4 does this.
 Mapman was from the Upsala suite and became XDLmapman in ccp4, but then
 became unusable and disappeared. I liked the original mapman as you had 
to

 actually give a name for your map, like 'jim' or 'jon'.

 Best wishes, Jon Cooper


 Sent from ProtonMail mobile



  Original Message 
 On 1 Mar 2021, 21:19, James Holton < jmhol...@lbl.gov> wrote:


 The CCP4 program you are looking for is called "mapman", and the
 option you need is "border".

 -James Holton
 MAD Scientist


 On 2/26/2021 8:07 AM, Horrell, Sam (DLSLtd,RAL,LSCI) wrote:


 Hello BB,

 I’m trying to make an image of some electron density in pymol but
 am running into a problem, my atoms are half in and half out of
 the unit cell so I only get half the density.

 Has anyone ran into this problem previously, and if so, is there
 a way to shift the origin, extend the map, or something so
 everything is covered?

 I realise this is not a ccp4 problem exactly, so I am ready for
 the inevitable replies, but I imagine a program in ccp4 might be
 the answer.

 Cheers,

 Sam

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Best wishes,

--Gerard

**
  Gerard J. Kleywegt

 http://xray.bmc.uu.se/gerard   mailto:ger...@xray.bmc.uu.se
**
  The opinions in this message are fictional.  Any similarity

[ccp4bb] Vacancy for an EMDB Coordinator at EMBL-EBI

2021-01-19 Thread Gerard Kleywegt


Are you an experienced electron microscopist who is passionate about cryo-EM 
and cryo-ET? Would you like to influence the way the world archives its EM 
data, including annotation, validation, dissemination, visualisation, etc.? Are 
you enthusiastic about engaging with the global EM community?


We are looking to recruit a Coordinator to lead the EMDB resource and 
activities at EMBL-EBI. This is a senior position, reporting directly to Dr 
Ardan Patwardhan who has overall responsibility for EMBL-EBI’s EM-archiving 
activities. It provides a rare and exciting opportunity for a motivated 
scientist with experience in this rapidly expanding and developing field to 
have a huge impact on how the scientific community archives, validates and 
re-uses EM data.


More information about the role, the requirements, the benefits of working at 
EMBL-EBI and the application procedure can be found at:


   https://www.embl.org/jobs/position/EBI01761/

If you know of any suitable candidates who might be interested in this 
position, please forward this mail to them. Thanks!


--Gerard

---
Gerard J. Kleywegt, EMBL-EBI, Hinxton, UK
Head of Molecular and  Cellular Structure
ger...@ebi.ac.uk pdbe.org emdb-empiar.org
PA: Roisin Dunloppdbe_ad...@ebi.ac.uk



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