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Help with AutoBuild
by Parthasarathy Sampathkumar 15 Dec '18

15 Dec '18

Dear All, These days my research often involves structure determination of the Antigen:Fab complexes, wherein the antigen structure is already known. Given this: (1). I would like to run AutoBuild in such a way that the program does not to touch antigen model, but only Re-builds only the Fab molecule; and (2). in some cases, due to structural-symmetry within the variable and constant domains of heavy- and light- chains, AutoBuild is searching and applying NCS operator while it is not present, and would like to avoid the same. How could these be done either in GUI or in command-line?!! Many Thanks in advance, Best Wishes Partha PS: Of course, when the data is at "high-enough resolution", I build Fab model manually after MR and Refinement. But, in the above case, resolution is only 3-ish angstrom.

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speeding up effective resolution calculation
by Eric Williams 07 Dec '18

07 Dec '18

Greetings, all. I have what may be a naive question. :) I'm using phenix.resolution to calculate effective resolution, and I'm looking for ways to speed it up. I've tried a few different machine configurations, and it always takes around 20 minutes per structure. This is problematic for me, because I'm trying to collect data from the entire PDB. Does anyone here have experience using NumPy to optimize scripts and helpful suggestions for this case? Alternatively, how much speedup am I likely to get by rewriting the script in C and using it as a module? Thanks. :) Eric

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New PDB archive reference paper now in NAR 2019 Database issue
by John Berrisford 05 Dec '18

05 Dec '18

An important <https://doi.org/10.1093/nar/gky949> new publication describing the activities and development of the Protein Data Bank (PDB), and authored by the whole wwPDB consortium, has been recently released in the 2019 Database issue of Nucleic Acids Research. Please see the following news release from the <https://www.wwpdb.org/news/news?year=2018#5c05780d3675962a10fcf7a9> wwPDB website: " <https://doi.org/10.1093/nar/gky949> Protein Data Bank: the single global archive for 3D macromolecular structure data has been published in the 2019 Database issue of Nucleic Acids Research. The paper was authored by "wwPDB Consortium" to underscore the importance of the global wwPDB partnership in managing the PDB archive. This article describes the development of the PDB under the stewardship of wwPDB, such as new archival content, master format and dictionary and major remediation efforts. The publication also emphasizes the importance of continued community interactions, the scientific and technical challenges the PDB faces, and charts the road ahead." -- John Berrisford PDBe European Bioinformatics Institute (EMBL-EBI) European Molecular Biology Laboratory Wellcome Trust Genome Campus Hinxton Cambridge CB10 1SD UK Tel: +44 1223 492529 <http://www.pdbe.org/> http://www.pdbe.org <http://www.facebook.com/proteindatabank> http://www.facebook.com/proteindatabank <http://twitter.com/PDBeurope> http://twitter.com/PDBeurope

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Re: [phenixbb] Molprobity values on output pdb
by Christopher Williams 30 Nov '18

30 Nov '18

Hi Boaz, Is it possible for you to send me (and just me, not the bulletin board) your file for testing? Thank you, if so. Alternatively, you can try using our alternate site at http:// altmolprobity .biochem.duke.edu, where a bugfix that probably addresses this issue is currently under testing. Thanks and good luck, -Christopher Williams ---Richardson Lab, Duke University On Fri, Nov 30, 2018 at 11:57 AM Boaz Shaanan <bshaanan(a)bgu.ac.il> wrote: > Hi, > > > I noticed small differences between the molprobity > all-atoms clashscore reported in the output pdb file and the results > reported by the molprobity run (build 3318). > > > Cheers, > > > Boaz > > > > > > > > > > > > > *Boaz Shaanan, Ph.D. Dept. of Life > Sciences Ben-Gurion University of the > Negev Beer-Sheva > 84105 > Israel > E-mail: > bshaanan(a)bgu.ac.il <bshaanan(a)bgu.ac.il> Phone: 972-8-647-2220 > Fax: 972-8-647-2992 or 972-8-646-1710 * > > > > > > _______________________________________________ > phenixbb mailing list > phenixbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/phenixbb > Unsubscribe: phenixbb-leave(a)phenix-online.org

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Validation Completeness Issue
by Antoine Koehl 29 Nov '18

29 Nov '18

Hi, I’m in the process of uploading data to the PDB. While AIMLESS had estimated my completeness at 94% (similar to the XTriage value of 93.2%), the internal PDB validation through EDS estimates my completeness to be closer to 83.5%. This is a rather large difference. Both are using the exact same resolution range (49.57-4.00). Is there something that EDS does differently for estimating completeness? Please advise, Antoine

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Test message
by Billy Poon 27 Nov '18

27 Nov '18

This is just a test. -- Billy K. Poon Research Scientist, Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory 1 Cyclotron Road, M/S 33R0345 Berkeley, CA 94720 Tel: (510) 486-5709 Fax: (510) 486-5909 Web: https://phenix-online.org

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Alternate conformer clash problem in phenix.refine
by Aaron Oakley 19 Nov '18

19 Nov '18

Salve! I am refining a protein/ligand complex where the ligand is bound with two conformers. Conformer A is covalently bound to a cysteine residue. Conformer B is free. I have prepared an appropriate cif dictionary for the ligand including info on handling the link. The problem is that during refinement, non-bonded interactions between the two conformers appear to not be switched off and their geometry becomes distorted. Is this diagnosis correct? If so, is there a way to manually switch off interactions? With thanks, a++ Aaron Oakley Associate Professor School of Chemistry and Molecular Bioscience | Molecular Horizons | Faculty of Science, Medicine and Health University of Wollongong NSW 2522 Australia T +61 2 4221 4347 | F +61 2 4221 4287 [cid:[email protected]]

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exclude clashes for non-symmetry contacts
by Edwin Pozharski 16 Nov '18

16 Nov '18

Is there some way to make phenix.refine to ignore clashes for specific pair(s) of chains? I am dealing with a rare case of twinning where same protein molecule exists in two orientations in the same unit cell. I tried just to duplicate the molecule and set initial occupancy to 0.5, but refinement fails (as I expected) saying that there are too many close contacts. Ideally, I would like to proceed with ignoring close contacts between, say, chains A/B. I am aware that one can exclude groups of residues from symmetry clashes, but these two copies are in the same cell. I guess I could try shifting one into the next unit cell and then excluding symmetry clashes, but even assuming that will work it is a rather ugly hack. The alternative is probably to define the second orientation as an alternative conformation. Aside from aesthetic objections, I don't want to lose the ability to restrain NCS - I need two orientations to be identical structures, and I am not sure yet whether I can use NCS groups defined via alternative conformers. Cheers, Ed.

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Normalized B-factor
by Mehmet Sen 16 Nov '18

16 Nov '18

Hello, I used the Structural Comparison tool to obtain normalized B- factor values for a couple of models, each with multiple chains. Is there an efficient way to visualize the normalized B-factor values (by writing over the old B-factor values) for the models, preferably in PyMOL? Thanks, Joyce V.

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Protonation of a symmetry-related His in Zn coordination sphere
by Priit Eek 16 Nov '18

16 Nov '18

Hi, I have a structure in which one of the His-residues of a Zn coordination sphere is from a symmetry-related protein chain. I specified the symmetry in an edits file so the coordination sphere is nice and plays well in refinement. I now added hydrogens to the model, but the His from the other chain does not get protonated correctly. I assume reduce doesn’t detect the presence of the symmetry-related Zn. It protonates NE, while that is the atom that interacts with Zn, but ND should be protonated instead. What would be the best way to fix this? And another question on the same matter: is it possible to specify a LINK in PDB between these atoms? Best regards, Priit ——— Priit Eek, PhD Researcher Department of Chemistry and Biotechnology Tallinn University of Technology Tel. +372 620 4387 priit.eek(a)taltech.ee

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