- phenixbb - phenix-online.org

R factor
by zhangh1＠umbc.edu 19 Sep '10

19 Sep '10

Hi, I want to calculate Fc based on the PDB file and reproduce the R factor in it. I first tried phenix.model_vs_data. It optimized ksol bsol and b_cart, and the output R factor (0.2143) is close enough to that in PDB (0.215). However, it didn't generate mtz files containing the calculated Fc. Then, I take the optimized ksol bsol and b_cart as the input and tried phenix.fmodel. I wrote my own code to calcuate the R factor. However, I got a lower R factor (0.2078). I think the reason might be my R calculation formula (sigma(fo-fc)/sigma(fo)) is wrong; or model_vs_data did more than just did flat solvent correction and anisotropic scaling. So, I am wondering whether phenix can: (1) Do the similar thing as model_vs_data (hope can be somehow faster:), but generate Fc-containing mtz file; (2) Do a simple R factor calculate to see whether my code is wrong (maybe answered already:) Thanks! Best Regards, Hailiang

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generate Rfree flag for twinned crystals with 3 twin fractions
by Zheng Zhou 19 Sep '10

19 Sep '10

Dear all After reading the informative posts in mailing list, I started to deal with my first twinning dataset. The space group is P3. Xtriage found 3 twin laws. R vs R statistics indicated perfect twinning for two twin laws and one is twin with RPS. I realize that twin-related reflections should be in the same work or free group. Could phenix handle the Rfree flag correctly for me when there are more than one twin fraction identified? By applying one twin law, the Rfree dropped from 37% to 28% using phenix. When I use Refmac, the twin fractions are refined and the Rfree is down to 26%. I copied the Rfree flag from phenix to the ccp4 in this case. When I let ccp4 generate Rfree flag automatically, the Rfree is refined to 26% too. Should I label the Rfree at a higher space group? Thanks for your advice Best, Zheng (Joe) Zhou

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Resolve NCS masks
by Florian Schmitzberger 18 Sep '10

18 Sep '10

Dear All, I would have a question regarding the use of masks in Resolve in Phenix for density modification: Is it possible to output the NCS and/or solvent masks Resolve is using during the Autosol run (similar as the options from the stand alone Resolve version) such as: mask_as_mtz ncs_mask_file mask.mtz protein_mask_file What are the best criteria (other than the final maps of course) within the output from Phenix.resolve to judge if the NCS (and/or solvent) mask was chosen adequately? (NCS_overlap?) I am mostly concerned if the masks chosen do include some of the more peripheral parts of my protein molecule and do not flatten these regions. Secondly, it is possible within Phenix Autosol wizard to supply a pdb file (with dummy atoms) for the mask for Resolve to construct the NCS mask? i.e. similar to set mask_pdb file= dummyatom.pdb Regards, Florian ----------------------------------------------------------- Florian Schmitzberger Biological Chemistry and Molecular Pharmacology Harvard Medical School 250 Longwood Avenue, SGM 130 Boston, MA 02115, US Tel: 001 617 432 5602

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Ligand restraints editing with REEL
by Joseph Brock 18 Sep '10

18 Sep '10

Hi all, I'm working on a 1.5A structure that contains a novel ligand within the active site, which is an Arsenic derivative of Glutathione, using the Phenix GUI, version 1.6.4-486. I have been using the 'Molinspiration' webpage (http://www.molinspiration.com/docu/webme/) to generate a smiles string, which I then feed into ELBOW. Although the structure/chemical restraints of Glutathione should be unchanged by the covalent linkage to arsenic through the cysteinyl sulfur, the resulting restraints file consistently restricts one of the dihedrals to a value that is incompatible with the (quite clear) electron density. This occurs regardless of wether i use AM1 optimization, and is unresponsive to using native Glutathione (which refines into the corresponding density extremely well) as an input geometry file with any of the available 'Use geometry for' options (final geometry, initial geometry, etc). I then tried opening the output file in REEL and manually changing the corresponding dihedrals to those of glutathione, however after running simple optimization, the resulting restraints file has the same problem, and upon choosing the 'transer geometry and restraints' option (or any option) midway through running the 'eLBOW optimization' or 'AM1 optimization' options, Phenix consistently crashes. Any advice on how to transfer the origional geometry of native Glutathione to my new ligand effectively would be greatly appreciated. I'm a little confused as to the abilities of REEL, and how to affect them. Thanks so much in advance. Cheers, -Joe.

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autobuild : MSE's keep coming back
by Lepore, Bryan 17 Sep '10

17 Sep '10

i used "semet=False" the .pdb has MET the .seq has M the output models, however, keep getting MSE's in them, complete with selenium. am i missing something? -bryan

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Re: [phenixbb] Something that came up on the CCP4 list...
by Simon Kolstoe 16 Sep '10

16 Sep '10

Just for the record I've had it make a big difference a number of times as well with both refmac & shelx. I was under the impression that phenix.refine was "cleverly" allowing me to use that trick by just starring the add riding hydrogens in the def file however it seems not - something worth knowing! Simon On 16 Sep 2010, at 20:01, Phil Jeffrey wrote: > I've had it make a big difference in certain circumstances. And in > other circumstances not so much. Definitely worth a try. I do not > use the technique routinely. > > Phil Jeffrey > Princeton > > > > On 9/16/10 11:49 AM, Simon Kolstoe wrote: >> So just to clarify further - if i am having problems with the final >> geometry of a model (eg clashscore as reported by molprobity), is >> it an >> appropriate trick to add hydrogens and then refine in phenix.refine >> using the riding hydrogens option, or does this not really change >> anything? >> >> Simon >> >> On 16 Sep 2010, at 14:26, Pavel Afonine wrote: >> >>> Hi Simon, >>> >>>> Could I just seek some clarification? I was under the impression >>>> that >>>> phenix.refine calculated riding hydrogens by default and took these >>>> into account as a restraint on the geometry? >>> >>> if you want hydrogen atoms to be used in refinement (as "riding >>> model" >>> or explicit) your need to make sure the PDB file that you give to >>> phenix.refine contains H atoms. That is you need to add them using >>> programs like phenix.reduce or phenix.ready_set or using >>> corresponding >>> functionality in the GUI. >>> >>> phenix.refine will not add them internally as part of refinement IF >>> hydrogen atoms are NOT present in input PDB file. >>> >>> Adding hydrogen atoms as 'riding model' does not add any refinable >>> parameters, but the scattering contribution from them is included >>> most >>> of the time. This is why we do not use H atoms silently but require >>> them to be in input PDB file - simply to make sure the reported >>> statistics (such as R-factors) is easily reproducible. >>> >>> All the best! >>> Pavel. >>> _______________________________________________ >>> phenixbb mailing list >>> phenixbb(a)phenix-online.org >>> http://phenix-online.org/mailman/listinfo/phenixbb >> >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >

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LABIN labels for Autosol/resolve NCS scores
by Florian Schmitzberger 16 Sep '10

16 Sep '10

Dear All, I would have a number of Phenix related questions: Firstly, I used the anisotropy server ( to anisotropically truncate my mtz file with anomalous signal (SAD data). My question is if the labels (for F+/F- and SIGF+/SIGF- are correctly recognized by Phenix (Autosol). The columns labels are: F_ref for FP; QSIGF_ref for SIGFP; GF(+)pk for F(+); LSIGF(+)pk for SIGF(+), GF(-)pk for F(-); LSIGF(-)pk for SIGF(-). It seems QSIGF and GF(+)pk/LSIGF(+)pk etc. are , but I am uncertain if it recognizes F_ref, because for the LABIN INPUT LABELS it says "NONE" for"F". Phenix does not seem to detect the anistropy ("Not using aniso- corrected data files as the range of aniso b is only 19.52 and 'correct_aniso' is not set); so I suppose I should use the correct_aniso=True keyword. Secondly, what are good values for the evaluation of the NCS mask and NCS averaging Resolve is using in Phenix; NCS overlap values (e.g. in my case 1.1) and NCS_CORR (in my case 0.52) in the "resolve.scores" file. Does an NCS overlap value of greater than 1 make sense? I am working with a (anisotropic) dataset with 4.1/4.5 A resolution, 78 % solvent content, 2-fold NCS; Perhaps a naive question: It is not possible to use B-factor sharpened maps for autobuilding with Phenix Autobuild is it? Thank you for any comments! Regards, Florian ----------------------------------------------------------- Florian Schmitzberger Biological Chemistry and Molecular Pharmacology Harvard Medical School 250 Longwood Avenue, SGM 130 Boston, MA 02115, US Tel: 001 617 432 5602

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f', f'' of Bromide?
by Tri Ngo 16 Sep '10

16 Sep '10

Dear Phenix-BB members, I am trying to solve the MAD data of one bacteria protein. The crystal was soaked with 1M Sodium Bromide. The data were collected at three different wavelength. I intend to use Autosol to solve this structure, but I am not sure which parameter I should put in the field: f' and f''? I think there is a table in the synchrotron but maybe I didn't notice about that. So now what should I do? Thank you very much for your input! Best wishes, -- * TriNgo * Structural Biology Lab School of Medicine - Sungkyunkwan University Phone: 031-299-6150

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Intl Conf on Structural Genomics, Toronto, Canada, May 10-14, 2011
by Thomas C. Terwilliger 16 Sep '10

16 Sep '10

Dear Colleagues, We are pleased to let you know about the upcoming International Conference on Structural Genomics 2011, to be held in Toronto, Canada on May 10-14, 2011. This meeting is the 6th in this series of biennial meetings of the International Structural Genomics Organization. The meeting is designed to serve as a forum to discuss the most recent developments in structural genomics and structural/chemical biology, and their impact on research in biology, medicine and disease. A limited number of student travel fellowships will be available for travel to this meeting. A substantial number of short talks will be selected from poster abstracts. Please see http://www.icsg2011.org for further details. We hope to see you there! Best regards, Cheryl Arrowsmith ICSG 2011 Organizer Ted Baker Stephen Burley Dino Moras Joel Sussman Shigeyuki Yokoyama Tom Terwilliger ISGO Executive Committee

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64-bit Snow Leopard support
by Nathaniel Echols 16 Sep '10

16 Sep '10

Mac users-- The latest nightly version of Phenix (dev-532) is now capable of compiling 64-bit objects on Snow Leopard, which should help those of you working on very large and/or high-resolution structures. You will need to use the source installer for this; it will automatically recognize the machine type as "mac-intel-osx-x86_64" and use the correct sources. There are several things to be aware of before trying this: 1. I had to switch to the development version of wxPython to get the GUI working, and it's both inherently less stable and based on fundamentally different OS libraries, which may cause problems. I've fixed some of the most obvious issues and everything appears to run now, but I expect to find more glitches. (This shouldn't affect command-line users.) 2. We haven't extensively tested 64-bit Phenix on Mac; there may be undiagnosed low-level bugs, even for command-line-only use. This should change soon. 3. For the above reasons, and because source installation is generally difficult to support, we recommend that you continue to use the 32-bit binary installer if you are not experiencing memory problems. (It will figure out what you are trying to do and correct the machine type accordingly.) 4. One side effect of this change is that an installation made on Leopard will not work on Snow Leopard, and vice-versa. I may be able to fix this. Hopefully there will be a binary installer in the near future, if I can ever figure out how to fix NFS on my workstation. -Nat

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Something that came up on the CCP4 list...
by Simon Kolstoe 16 Sep '10

16 Sep '10

In the fascinating current discussion on the ccp4 list Pavel said: >Dear Ed, > >no, if you start with model that has no hydrogens, they will not be generated internally. > >Pavel. > On 9/15/10 2:58 PM, Ed Pozharski wrote: > Sure. But if I start with model that has no hydrogens, they will be > generated but not passed to the output, right. just like refmac. > > On Wed, 2010-09-15 at 14:52 -0700, Pavel Afonine wrote: >> Dear Ed, >> >> On 9/15/10 2:47 PM, Ed Pozharski wrote: >>> On Wed, 2010-09-15 at 16:26 -0400, Phil Jeffrey wrote: >>>> So the riding hydrogen model is imperfect. At least with >>>> phenix.refine >>>> you can measure it, unlike the default behavior of REFMAC. (But >>>> you >>>> can >>>> tell it to write hydrogens out, I believe). >>>> >>> My impression is that default behavior of phenix.refine is the >>> same - I >>> had to change parameters to include hydrogens in the output. >> No, if your input file contains H atoms, the output file will contain >> them too (in phenix.refine). You don't have to change any >> parameters for >> this. >> >> Pavel. Could I just seek some clarification? I was under the impression that phenix.refine calculated riding hydrogens by default and took these into account as a restraint on the geometry? Simon

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nqh-flip option
by Christian Roth 16 Sep '10

16 Sep '10

Dear all, I put manually in the parameterfile from the gui the option nqh_flips=True. After the run starts, a popup comes up claiming about an invalid unsupported option and the refinement stops without producing any file, even not a log-file. Does the nqh option not longer exists or what happend here? I use at the moment phenix 1.6-289. Thanks for your help. Christian

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Re: [phenixbb] autobuild : MSE's keep coming back
by Thomas C. Terwilliger 15 Sep '10

15 Sep '10

Hi Bryan, Hmmm...I can't seem to make it happen with my standard inputs. Can you possibly send me directly (terwilliger(a)lanl.gov) your AutoBuild_run_1_/autobuild.eff file or better yet that plus your input files and I'll try that out here? Thanks a lot, All the best, Tom T >>> are you using a recent version? >> >> v1.6.4 release tag 486 >> >>> is this rebuild_in_place or not? >> >> well, i did not specify rebuild_in_place, however, i poked around and can >> see that autobuild has switched on rebuild_in_place so i call that a >> "yes". >> >> -bryan >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >>

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Re: [phenixbb] autobuild : MSE's keep coming back
by Lepore, Bryan 15 Sep '10

15 Sep '10

> are you using a recent version? v1.6.4 release tag 486 > is this rebuild_in_place or not? well, i did not specify rebuild_in_place, however, i poked around and can see that autobuild has switched on rebuild_in_place so i call that a "yes". -bryan

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Re: [phenixbb] [ccp4bb] Deposition of riding H
by Dr. Mark Mayer 15 Sep '10

15 Sep '10

>However this thread appears to have reached the point where not much new >ground is being broken. As the person who started this thread I'll second Phil Jeffrey's comment. I chose to continue my depositions with riding H, and the rcsb agreed to accept the coordinates. Its been great hearing the experts weigh in on this. I've learned a lot, and clearly there is no consensus. As one of the vast majority of crystallographers dependent on all the hard work that program developers undertake to support structural biology, I'm happy to follow advice given by the developers of the various programs I use, and for Phenix the current advice is to deposit with riding H. -- Mark

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Re: [phenixbb] [ccp4bb] Deposition of riding H
by Felix Frolow 15 Sep '10

15 Sep '10

Pavel, Shelxl is working in correct coordinates - fractional... Many things are easier in fractional coordinates. Are you sure that Phenix does not go orthogonal -> fractional -> orthogonal in internal calculations? When fixing of parameter is made in fractional coordinates it does not produce confusion. Shelxl also make fractional -> orthogonal (AKA PDB) which is also correct. Constrain is not transferred there. BTW Shelxl knows symmetry very well and will constrain atoms that occupying symmetry elements. Shortly Shelxl knows crystallography best. When you will see number of lines in Shelxl Fortran code ( do not kill Fortran to early) you will be surprised. There are not so many of them. No graphical user interface yet, but COOT is of great help. Dr Felix Frolow Professor of Structural Biology and Biotechnology Department of Molecular Microbiology and Biotechnology Tel Aviv University 69978, Israel Acta Crystallographica F, co-editor e-mail: mbfrolow(a)post.tau.ac.il Tel: ++972-3640-8723 Fax: ++972-3640-9407 Cellular: 0547 459 608 On Sep 15, 2010, at 19:11 , Pavel Afonine wrote: > Hi Tim, > >> The pdbe.org, for example allows to upload auxiliary files and in my opinion the >> uploading of the final .ins-file (not the .res-file!) should be made mandatory >> in the case of shelxl refinement. >> >> Since coot has now become utterly convenient even for shelxl refinement, there >> is no reason one should not deposit the .ins-file ([flame] and the PDB-file >> probably for legacy reasons [/flame]). > > I was always wondering but never had a good occasion to ask (my Shelxl knowledge is limited and may be outdated so I apology in advance if my questions are too dummy; also I realize that I'm asking a non-CCP4 question on CCP4bb for which I apology again): > > - how .ins file encodes the information about NCS groups used in refinement (atom selection for NCS groups, restraint weights for different groups, etc? > > - how .ins file encodes the information about TLS (again, atom selections for TLS groups, TLS matrices, etc)? Related, does it have a concept of having TLS and other components to the total atomic displacement parameter (ADP)? > > - If I recall it correctly, to fix (=not refine) a certain parameter (say occupancy or B-factor) in Shelxl you need to add a number 10 to it. Is it true? IMHO, this might lead to confusion if such a file gets deposited to PDB. > > All the best! > Pavel.

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How does phenix.fmodel treat isotropic and anisotropic B?
by zhangh1＠umbc.edu 15 Sep '10

15 Sep '10

Hi, I am doing a phenix.fmodel calculation for a PDB structure containing anisotroipc B. If I understand it correctly, the B factor is composed of both the isotropic B for ATOM line (Biso) and the anisotropic B from ANISOU line (Uani): Fc=sigma ( fi * exp (-Biso*s*s) * exp (-st*Uani*s) * exp (i*r*s) ) Please correct me if the above equation is wrong. I also noticed that in PDB, the Uani (after scaling by 10^-4) is generally much smaller than Biso. So I assume that Biso has a much bigger contribution than Uani, the latter only implying the vibrational anisotropicity. However, I did a test calculation by setting all Bio to 0 whereas keeping Uani unchanged. Due to the above assumption, I expected the results should be very different from the native structure; however, coot told me they were just so close... Maybe I am wrong somewhere... Best Regards, Hailiang

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Sep 15, 2010 deadline- User proposal submission for Collaborative Crystallography at BCSB
by Banumathi Sankaran 14 Sep '10

14 Sep '10

Dear Users, The deadline for Nov/Dec 2010 Collaborative Crystallography proposals will be *Sep 15, 2010. * ---------------------------------------------------------------------------------------- Through the Collaborative Crystallography Program (CC) at the Advanced Light Source (ALS), scientists can send protein crystals to Berkeley Center for Structural Biology (BCSB) staff researchers for data collection and analysis. The CC Program can provide a number of benefits to researchers: * Obtain high quality data and analysis through collaborating with expert beamline researchers; * Rapid turn around on projects; and * Reduced travel costs. To apply, please submit a proposal through the ALS General User proposal review process for beamtime allocation. Proposals are reviewed and ranked by the Proposal Study Panel, and beamtime is allocated accordingly. BCSB staff schedule the CC projects on Beamlines 5.0.1 and 5.0.2 to fit into the available resources. Only non-proprietary projects will be accepted. As a condition of participation, BCSB staff researchers who participate in data collection and/or analysis must be appropriately acknowledged - typically being included as authors on publications and in PDB depositions. Please consult the website for additional information at: http://bcsb.als.lbl.gov/wiki/index.php/Collaborative_Crystallography ----------------------------------------------------------------------------------------- How To Apply: To learn more, go to: http://www.als.lbl.gov/als/quickguide/becomealsuser.html To submit a proposal, go to: http://alsusweb.lbl.gov/. Scroll down to "*Structural Biology beamlines (includes protein SAXS)*" and click on "New Proposal." Enter your proposal information, with attention to the following details: * For question 3/First choice, select "5.0.1 (Monochromatic);" for question 3/Second choice, select "5.0.2 (MAD)." * Check box (yes) in response to question (7) "Do you want collaborative crystallography (beamline 5.0.1 or 5.0.2 only) * In question 4, please describe a specific research project with a clear end point. In order to request CC time for Nov/Dec 2010 allocation period, proposals must be submitted by *Sep 15, 2010.* The deadline for CC proposals for the time period Jan/Feb 2010 will be Nov 15, 2010. Regards, Banumathi Sankaran

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Reproducibility of R-factors
by miket＠chem.ucla.edu 14 Sep '10

14 Sep '10

Hi All, I recently used phenix.model_vs_data to evaluate a structure that was refined using Refmac. The R_work and R_free calculated by refmac are 0.18 and 0.20, while model_vs_data calculates them as 0.20 and 0.22. Should I be concerned about this discrepancy? Is it typical for different programs to calculate different values for R-factors using the same data, and if so what is the source of this difference? Seems to me like there shouldn't be much of a difference (at least not 2%). Maybe I'm wrong. Any insight/advice would be appreciated. Thanks, Mike Thompson -- Michael C. Thompson Graduate Student Yeates Lab Biochemistry & Molecular Biology Division Department of Chemistry & Biochemistry University of California, Los Angeles miket(a)chem.ucla.edu

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Deposition of riding H
by Dr. Mark Mayer 14 Sep '10

14 Sep '10

Here's one for the community, which I'll post to both Phenix and CCP4 BBs. Where does the crystallographic community stand on deposition of coordinates with riding hydrogens? Explicit H are required for calculating all atom clash scores with Molprobity, and their use frequently gives better geometry (especially at low resolution). Phenix uses explicit riding H for refinement, and outputs these in the refined PDB. Refmac also uses riding H but does not output H coordinates. While depositing a series of structures refined at 1.4 - 2.75 A with Phenix got the following email from the RCSB, who asked I resupply coordinates without H for two of the structures. Since we can't see H even at 1.4 Å I don't understand why an arbitrary cut off of 1.5 Å was chosen, and also why explicit H atoms used in refinement and geometry validation should be stripped from the file. FROM RCSB We encourage depositors not to use hydrogens in the final PDB file for the low resolution structures (> 1.5 A). Please provide an updated PDB file. We request you to use processed PDB file as a starting point for making any corrections to the coordinates and/or re-refinement. -- Mark

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Re: [phenixbb] Deposition of riding H
by Jeff Headd 14 Sep '10

14 Sep '10

Hi Mark, If hydrogens are used to arrive at a final refined model (whether riding or not) it is essential for the reproducibility of results that the H atom records be included in the deposited model. How B-factors are specified and some final atomic positions (such as rotatable methyl groups) are difficult or impossible to predict once removed, so without their deposition this information would be lost and any published statistics would not be reproducible as published. This point is illustrated in one of our recent papers: Afonine PV, Grosse-Kunstleve RW, Chen VB, Headd JJ, Moriarty NW, Richardson JS, Richardson DC, Urzhumtsev A, Zwart PH, Adams PD: phenix.model_vs_data: a high-level tool for the calculation of crystallographic model and data statistics. J. Appl. Cryst. 2010, 43, 669-67. Further, there is no universal standard currently in use that specifies H bond-lengths (some use electron cloud distances, others neutron distances, some a mixture of both), meaning that without inclusion of H atom records (or at least a reference to which library was used) it is very difficult to know where the H atoms were placed. Thanks, Jeff On Tue, Sep 14, 2010 at 10:32 AM, Dr. Mark Mayer <mayerm(a)mail.nih.gov> wrote: > Here's one for the community, which I'll post to both Phenix and CCP4 BBs. > > Where does the crystallographic community stand on deposition of coordinates > with riding hydrogens? > Explicit H are required for calculating all atom clash scores with > Molprobity, and their use frequently gives better geometry (especially at > low resolution). Phenix uses explicit riding H for refinement, and outputs > these in the refined PDB. Refmac also uses riding H but does not output H > coordinates. > > While depositing a series of structures refined at 1.4 - 2.75 A with Phenix > got the following email from the RCSB, who asked I resupply coordinates > without H for two of the structures. Since we can't see H even at 1.4 Å I > don't understand why an arbitrary cut off of 1.5 Å was chosen, and also why > explicit H atoms used in refinement and geometry validation should be > stripped from the file. > > FROM RCSB > > We encourage depositors not to use hydrogens in the final PDB file for > the low resolution structures (> 1.5 A). Please provide an updated PDB > file. We request you to use processed PDB file as a starting point for > making any corrections to the coordinates and/or re-refinement. > -- > > Mark > _______________________________________________ > phenixbb mailing list > phenixbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/phenixbb >

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Re: [phenixbb] autobuild : change reflection file mid-job?
by Thomas C. Terwilliger 14 Sep '10

14 Sep '10

Hi Bryan, Yes, I think to change the reflections file you will have to rerun the job as the reflections are read once in autobuild and propagated from there out. All the best, Tom T >> [it was inevitable..] >> >> if i swap the reflection file mid-job - THAT sounds like catastrophe : >> >> so does autobuild determine the format *only* from the .sca, .mtz affix? >> >> and it looks like reflections are read once at startup, and propagated >> from there out? >> >> -bryan >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >>

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autobuild : change reflection file mid-job?
by Lepore, Bryan 14 Sep '10

14 Sep '10

[it was inevitable..] if i swap the reflection file mid-job - THAT sounds like catastrophe : so does autobuild determine the format *only* from the .sca, .mtz affix? and it looks like reflections are read once at startup, and propagated from there out? -bryan

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Palestrant, Deborah is out of the office.
by deborah.palestrant＠novartis.com 13 Sep '10

13 Sep '10

I will be out of the office starting 09/13/2010 and will not return until 09/15/2010. I have limited access to email and will respond to your message when I return.

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Re: [phenixbb] autobuild : change .seq mid-job?
by Thomas C. Terwilliger 13 Sep '10

13 Sep '10

Hi Bryan, I think that you can do this, though I have not tried it. You need to replace two files: 1. your original sequence file wherever it is "/wherever/.../myseq.dat 2 a file with the same name "myseq.dat" or whatever, in the directory AutoBuild_run_1_/TEMP0 I would expect all model-building after that to have the new sequence. (Note that runs that are already going as sub-processes will keep their sequences). Now if this is rebuild_in_place, this would not be a good idea. I am assuming it is rebuild_in_place=False, and so it should work... Let me know how it turns out, -Tom T >> i have a long autobuild job going. i'd like to change the .seq files as >> its going - if i keep residue 1 numbered, could this still be a >> catastrophe? >> >> -bryan >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >>

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autobuild : change .seq mid-job?
by Lepore, Bryan 13 Sep '10

13 Sep '10

i have a long autobuild job going. i'd like to change the .seq files as its going - if i keep residue 1 numbered, could this still be a catastrophe? -bryan

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debugger pdb
by Krista Joosten 10 Sep '10

10 Sep '10

Hi all, I'm working with Tom Burnley on the development of time_averaging.py. I would like to use the debugger pdb, but am not sure how to do this and whether it's possible. After some googling, I tried to hack into phenix.time_averaging adding -m pdb when the variable DEBUG==1, but I got the error message 'no module called pdb'. Bye Krista

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Beamtime at the ALS-BCSB beamlines
by Peter Zwart 09 Sep '10

09 Sep '10

Dear All, July 15, 2010 is the deadline for the March/April 2010 Rapid Access Proposal cycle. All Berkeley Center for Structural Biology(BCSB) beamlines are equipped with ADSC Q315/Q315R detectors, automated sample changers and data collection software enabling high-throughput crystal screening and data collection. Remote data collection is available on all BCSB beamlines, providing the user with the full complement of sample visualization, sample manipulation, beamline control, data acquisition and data analysis tools exactly as they would see them if they were stationed at the beamline. The main difference between local operation and remote operation, is the length of the network cable! This enhanced remote operation capability is coupled with 22hr onsite support by BCSB staff who are able to assist immediately with loading additional samples for remote users or troubleshoot any issues that might arise. Remote users can furthermore be kept up-to-date on changes in ring status via an SMS service ( http://bcsb.als.lbl.gov/wiki/index.php/Ring_Status_Notifications_to_Cell_Ph…) or via twitter (@AlsRingStatus). Specific features are summarized below. Beamlines 5.0.1, 5.0.2, 5.0.3: -------------------------------------- Beamline 5.0.2 is equipped with a novel variable collimator allowing users to adjust the beamsize continuously and on the fly between 25 and 100 micron, both horizontally and vertically. With a collimator setting of 30x30 micron, typical exposures are around 1 to 2 second. The Berkeley Automounter sample handling system has a routine capacity of 96 samples (6 pucks). In a typical high-throughput screening mode, the mount-to-mount time is around 2.5 minutes per sample, allowing users to screen a full puck within 45 minutes. The sector 5 beamline user stations are equipped with fully high-adjustable, ergonomically friendly work stations. Beamlines 8.2.1 and 8.2.2: ----------------------------------- To facilitate studies on small crystals, a microdiffractometer was installed in the beamline 8.2.1 endstation. The new equipment allows precise sample positioning to within 2 microns, excellent sample viewing of very small crystals, and an off-axis crystal positioningstage. Both beamlines 8.2.1 and 8.2.2 feature a Rigaku sample changer (Actor), allowing remote operations to now be a routine mode of access for these beamlines. Data analyses in the BCSB is facilitated by software maintained by sbgrid ( http://www.sbgrid.org). A 16 core linux machine is available for our users to process their data and solve/refine their structure. An additional mode of access to the BCSB beamlines is through the Collaborative Crystallography (CC) Program. Users apply for beamtime via the general user program, and collaborate with an expert crystallographer who will conduct the experiments and data reduction on behalf of the researchers. Depending on the users, structure solution, model building and refinement can be carried out as well. Please contact BCSBBeamtime(a)lbl.govfor more information. Please visit http://bcsb.lbl.gov/ for more details about the Center and its beamlines. To find out more, click on: http://www.als.lbl.gov/als/quickguide/independinvest.html We invite you to submit a proposal at: http://alsusweb.lbl.gov/ Scroll down to "Structural Biology beamines (includes protein SAXS)." Click on "New Proposal." If you have any questions or would like to request open beamtime, please e-mail BCSBBeamtime(a)lbl.gov. Please note that executed user agreements must be received by LBNL prior to beamtime. Proprietary fees, if applicable, must be received by LBNL at least five working days prior to scheduled beamtime. -- ----------------------------------------------------------------- P.H. Zwart Research Scientist Berkeley Center for Structural Biology Lawrence Berkeley National Laboratories 1 Cyclotron Road, Berkeley, CA-94703, USA Cell: 510 289 9246 BCSB: http://bcsb.als.lbl.gov PHENIX: http://www.phenix-online.org SASTBX: http://sastbx.als.lbl.gov -----------------------------------------------------------------

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Help on multi-start-simulated-annealing sigmaA-weighted 2fofc map
by fn1＠rice.edu 09 Sep '10

09 Sep '10

Hi everyone, I read on the paper that they use CNS (model_map.inp) to calculate the avarage sigmaA-weighted 2fofc map. Right now I have set up the simulated annealing with different random seeds. I wonder whether phenix could calculate the average map with the multiple coordinates from different starts? Thanks! Fengyun

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Can phenix calculate R factor based on the only given mtz file containing Fo and Fc?
by zhangh1＠umbc.edu 07 Sep '10

07 Sep '10

Hi, I am wondering whether phenix can calculate R factor based on the only given mtz file containing Fo and Fc? Thanks! Hailiang

2 1

will phenix.fmodel automatically generates and takes into account the TLS B by reading the TLS REMARK from pdb?
by zhangh1＠umbc.edu 07 Sep '10

07 Sep '10

Hi, For the pdb file generated by refmac which contains only the residual-B, will phenix.fmodel automatically generates and takes into account the TLS B by reading the TLS REMARK from pdb? Thanks a lot! Best Regards, Hailiang

2 5

constrained occupancy groups in phenix.refine
by Lionel Costenaro 03 Sep '10

03 Sep '10

Hello, A portion of my structure have two conformations at an interface between two (NCS) protein chains -in addition to other alternates conformations elsewhere. In both chains, I defined alt_A as one conformation and alt_B as the second conformation, and also for the waters in this region. I would like to constrained the occupancy of these conformations. I though that the following selections would do the job: occupancies { constrained_group { selection = "(chain A or chain B) and (resseq 105 or resseq 110:112 or resseq 140:143) and altid A" After refinement, all alt_A selected residues do have the same occupancy, but not the same occupancies for alt_B and the sum for one residue (occu alt_A +occu alt_B) is not 1. Adding a second group with the same selection but "altid B", constrains also the alt_B occupancies but the sum is still not 1. How should I defined my group(s)? Is it possible to select several non continuous residues from one chain (that's for the waters) without repeating each time "or resseq" ? Best regards, Lionel

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Re: [phenixbb] Can we untoggle molecular weight mean deviation check on ensembles in autoMR?
by James Thompson 03 Sep '10

03 Sep '10

A postdoc in my lab with many more files inside his Phenix build directory just showed me that the Mwt mean deviation check on input ensembles is hard-coded in Phaser. A seemingly arbitrary value of 20% is set within the file emsembles.cc. So, the answer to my previous question is presently NO. We users cannot untoggle or alter this mean deviation value without some recompile of Phaser. I will play with my Sculpt'ed output from the Mustang server to reduce the Mwt deviations within the ensemble of coordinates that I want to feed to Phaser-MP to get by. James R. Thompson <thompson.james at mayo.edu> > Can folks untoggle the molecular weight mean deviation check in > phenix.autoMR on the ensembles input? > > I want to use an ensemble of coordinates generated by the Mustangs > server from a SSM alignment. Therefore, by design the 10 PDBs input to > phenix.autoMR vary greatly in molecular weight from their mean value, > but the whole is likely an excellent probe for molecular replacement. > However, I am stymied by phenix.autoMR: > > ------------------------------------------------------------------------------------- > FATAL RUNTIME ERROR: Molecular weight of > /home/jrt04/Desktop/GB1STAS/MUSTANGServer_10_1.6_0_sculpt-coot-0.pdb > (6610.56) deviates more than 20% from the mean (3977.08). This pdb file > may contain domains or water not present in the other files. > ------------------------------------------------------------------------------------- > > I understand why this check might be of utility to the unobservant. How > can I disable this test? > > Many thanks, > Jim > > -- > James R. Thompson <thompson.james at mayo.edu>

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can phenix.refine output mtz with structure factors not just coeficients?
by amadrona＠uci.edu 02 Sep '10

02 Sep '10

Hi, I am going to deposit a structurein the pdb but noticed that all of the mtz files from phenix.refine only contain coeficients and not reflection info. Is it as simple as running another refinement with write_maps = true instead of false? Will this right out an mtz with structure factors instead of just coeficients. I am a newbie at crystalagraphy so I appolgize if this obvious. Ideally, I would like to create an mtz with structure factors as well as a map for CNS. Is there a way to do this without runing another refinment maybe using "maps.params". Thank you very much for the help! -Yarrow output { prefix = "CIN4_refine" serial = 12 serial_format = "%03d" title = None write_eff_file = True write_geo_file = True write_final_geo_file = False write_def_file = True export_final_f_model = mtz cns write_maps = false write_map_coefficients = True pickle_fmodel = False

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atom selection in phenix.pdbtools
by Michael Hothorn 01 Sep '10

01 Sep '10

Hi, I want to calculate the mean b-value for all atoms of a specific ligand in my structure. I tried: phenix.pdbtools --show-adp-statistic model.pdb keep="chain A and residue 400" , but it still prints out all b-values including solvent etc. any ideas? thanks Michael

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Re: [phenixbb] question on bad geometry
by Thomas C. Terwilliger 01 Sep '10

01 Sep '10

Hi Fengyun, Just to emphasize what Ed points out here, an essential step in completing a structure is to compare it, one residue, solvent molecule, or ligand at a time, with your electron density map, fixing any inconsistencies between the model and the map. There are many wonderful tools in all the crystallographic graphics programs to help you do this. All the best, Tom T >> On Tue, 2010-08-31 at 20:37 -0500, fn1(a)rice.edu wrote: >>> Does >>> that mean I need to manually adjust the model? >> >> Autobuilder is a fantastic tool which greatly simplifies the model >> building process, but you always must validate your structure by >> inspecting the electron density. I fully understand that (hopefully) it >> is what you plan to do and this is more of a reaction to the alarming >> number of obvious and easily correctable systematic errors one finds in >> structures deposited in the PDB these days. >> >> Thanks to Pavel for providing an excellent example to illustrate the >> point. One only needs to take a look at the model in context of >> electron density maps to confirm that autobuilder will fix some errors >> but also sometimes introduce some that require manual correction. >> >> Cheers, >> >> Ed. >> >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >>

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question on bad geometry
by fn1＠rice.edu 01 Sep '10

01 Sep '10

Hi everyone, I have a structure at 2.3 A refined in phenix to R/Rfree=0.23/0.28. However, the geometry is not that good, the followings are the output from phenix.model_vs_data, Stereochemistry statistics (mean, max, count): bonds : 0.0080 0.0547 3244 angles : 1.1669 12.1085 4374 dihedrals : 15.7241 85.6280 1202 chirality : 0.0706 0.2831 536 planarity : 0.0036 0.0246 573 non-bonded (min) : 2.1217 Ramachandran plot, number of: outliers : 17 (4.02 %) allowed : 37 (8.75 %) favored : 369 (87.23 %) Rotamer outliers : 30 (8.62 %) goal: < 1% Cbeta deviations >0.25A : 0 All-atom clashscore : 40.51 (steric overlaps >0.4A per 1000 atoms) I tried to use fix_rotamer=True, but it doesn't help at all. As to the rotamer outliers, the value is far higher than the ideal one. Does that mean I need to manually adjust the model? Or will autobuild help improve the geometry? Thanks! Fengyun

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How to do a phenix.fmodel calculation incorporating the exponential scaling model only?
by zhangh1＠umbc.edu 31 Aug '10

31 Aug '10

Hi, I want to use phenix.fmodel to do a calculation incorporating the exponential scaling model only (Not the flat model). I am not sure whether I just need simply specify: mask { use_asu_masks = False } since the output maps are just identical no matter use_asu_masks = True or False. Should I do something else to enable exponential scaling model only? Thanks! Best Regards, Hailiang

2 2

0.00 Refined Isotropic ADPs
by Joseph Noel 31 Aug '10

31 Aug '10

Hi All. Me again! LOL I am sure this has come up and related to how the "B-factor" in the refined PDB's ADP column is calculated including the overall anisotropic B-factor, etc but is it unusual to have isotropic ADPs refine to 0.00? I have several nice structures with 0.00 isotropic ADPs. I am not refining TLS or anisotropic ADPs at all. Just the normal course of refinement. These are regions of a high degree of order and the maps are beautiful but just wandering what the 0.00 ultimately means particularly when I eventually submit to the Protein Data Bank. Joe P.S. Nat's tips on COOT and Phenix are working beautifully now! Thanks Nat! ___________________________________________________________ Joseph P. Noel, Ph.D. Investigator, Howard Hughes Medical Institute Professor, The Jack H. Skirball Center for Chemical Biology and Proteomics The Salk Institute for Biological Studies 10010 North Torrey Pines Road La Jolla, CA 92037 USA Phone: (858) 453-4100 extension 1442 Cell: (858) 349-4700 Fax: (858) 597-0855 E-mail: noel(a)salk.edu Web Site (Salk): http://www.salk.edu/faculty/faculty_details.php?id=37 Web Site (HHMI): http://hhmi.org/research/investigators/noel.html ___________________________________________________________

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Re: [phenixbb] Phenix and COOT Together on a Mac (and Probe too?)
by Joseph Noel 31 Aug '10

31 Aug '10

Nat, One thing that seemed to solve all the problems at once was to completely remove any reference to the COOT path in the Phenix preferences! Is that weird? When I removed it completely only leaving the path to PYMOL then COOT is working just fine in conjunction with Phenix and even the Probe issues have disappeared. Prior to this, I was tried two different paths to COOT. 1. /sw64/bin/coot 2. /Applications/coot.app/Contents/MacOS/coot Neither behaved but if I don't specify anything it works. Joe ___________________________________________________________ Joseph P. Noel, Ph.D. Investigator, Howard Hughes Medical Institute Professor, The Jack H. Skirball Center for Chemical Biology and Proteomics The Salk Institute for Biological Studies 10010 North Torrey Pines Road La Jolla, CA 92037 USA Phone: (858) 453-4100 extension 1442 Cell: (858) 349-4700 Fax: (858) 597-0855 E-mail: noel(a)salk.edu Web Site (Salk): http://www.salk.edu/faculty/faculty_details.php?id=37 Web Site (HHMI): http://hhmi.org/research/investigators/noel.html ___________________________________________________________

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Problem with low figure of merit
by sankaranarayanan srinivasan 31 Aug '10

31 Aug '10

Hi all, I am new to structure solving. I have a 2.9A dataset for a Seleno crystal of which i am trying to use Autosol to build an initial map. I used the settings for a thorough solution, instead of quick. All the other parameters were set to default settings. The solution that i got from autosol, gave me the following result Solution # 1 BAYES-CC: 23.7 +/- 30.9 Dataset #1 FOM: 0.27 Residues built: 238 Side-chains built: 139 Chains: 15 Overall model-map correlation: 0.65 R/R-free: 0.38/0.42. Score type: SKEW CORR_RMS Raw scores: 0.02 0.77 100x EST OF CC: 16.86 32.11 The density modification map matches, quite well with many of my side chains fitted. My question here is , IS THERE A WAY I CAN IMPROVE THE Figure Of Merit , BY CHANGING ANY PARAMETERS IN PHENIX-AUTOSOL. I HAVE A HIGH SOLVENT CONTENT IN MY CRYSTAL AND I DID NOT INPUT THAT IN MY INITIAL PARAMETERS. DOES PHENIX AUTOSOL CONSIDER SOLVENT FLATTENING FOR SUCH CRYSTALS? I would appreciate someone's help in this regard Thanks Shankar

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Phenix and COOT Together on a Mac (and Probe too?)
by Joseph Noel 30 Aug '10

30 Aug '10

Hi All, I am having trouble getting COOT to link up with Phenix. I know that Bill Scott's fink version of COOT breaks the link but I have also tried the stand alone latest version for Mac OSX without success. I suspect there may be something additional I need to set up to get the two programs to talk to one and other. I can open COOT with the GUI link in Phenix but that's it. The two do not communicate and the "Phenix button" does not appear. I am running everything on a Mac laptop with an Intel chip and the latest snow leopard operating system. I can also run probe independently in COOT using the script suggestion for the .coot file from the MOLPROBITY web site. However, after several checks of bad contacts the system freezes at the level of XQuartz and I have to kill X-Windows to start over. I don't know if this is in someway linked to the problem getting COOT and Phenix to talk to one and other but I thought I would throw it out there. Finally, if I do run COOT by starting it from the Phenix GUI it also freezes after several rounds of building, etc just like the probes to check for clashes. If anyone has observed this behavior and has some suggestions I would much appreciate it! Its not a big deal as I can run things separately and work from a print out of Molprobity outliers but it would be sure nice to just click and correct. Sorry to keep going but I should say I have Bill Scott's fink'ed version of coot installed in as directed in /sw64 and the stand alone version installed along with CCP4 and Phenix in my Mac's /Applications directory where all my standard Mac apps appear. Thanks! Joe ___________________________________________________________ Joseph P. Noel, Ph.D. Investigator, Howard Hughes Medical Institute Professor, The Jack H. Skirball Center for Chemical Biology and Proteomics The Salk Institute for Biological Studies 10010 North Torrey Pines Road La Jolla, CA 92037 USA Phone: (858) 453-4100 extension 1442 Cell: (858) 349-4700 Fax: (858) 597-0855 E-mail: noel(a)salk.edu Web Site (Salk): http://www.salk.edu/faculty/faculty_details.php?id=37 Web Site (HHMI): http://hhmi.org/research/investigators/noel.html ___________________________________________________________

2 1

Can we untoggle molecular weight mean deviation check on ensembles in autoMR?
by James R. Thompson 30 Aug '10

30 Aug '10

Can folks untoggle the molecular weight mean deviation check in phenix.autoMR on the ensembles input? I want to use an ensemble of coordinates generated by the Mustangs server from a SSM alignment. Therefore, by design the 10 PDBs input to phenix.autoMR vary greatly in molecular weight from their mean value, but the whole is likely an excellent probe for molecular replacement. However, I am stymied by phenix.autoMR: ------------------------------------------------------------------------------------- FATAL RUNTIME ERROR: Molecular weight of /home/jrt04/Desktop/GB1STAS/MUSTANGServer_10_1.6_0_sculpt-coot-0.pdb (6610.56) deviates more than 20% from the mean (3977.08). This pdb file may contain domains or water not present in the other files. ------------------------------------------------------------------------------------- I understand why this check might be of utility to the unobservant. How can I disable this test? Many thanks, Jim -- James R. Thompson <thompson.james(a)mayo.edu>

1 0

stuck with phenix refine
by intekhab alam 29 Aug '10

29 Aug '10

Hi I am working with a twinned data set having R32 space group. when i tried to refine with phenix refine using the twin option it got stuck after some time. There is no error message showing up and the refinemnet donot progresses further. I have used the twin law suggested by Xtriage program in Phenix. Kindly help me out. Regards -- INTEKHAB ALAM LABORATORY OF STRUCTURAL BIOINFORMATICS KOREA UNIVERSITY, SEOUL

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Re: [phenixbb] phenix.automr questions
by Kay Diederichs 29 Aug '10

29 Aug '10

Dear Randy, Nat, Tom, thank you for pointing out the existence of phenix.phaser to me, and sketching its usage. I think I'll make my way with that information; nevertheless it would be great if it were officially documented (Google returned nothing to me about phenix.phaser). BTW, I'm trying to put together some orthogonal Phenix documentation at http://strucbio.biologie.uni-konstanz.de/ccp4wiki/index.php/Phenix . I take the opportunity to state that although the URL refers to the CCP4 users' wiki, and obviously Phenix is not part of CCP4, the wiki covers a broad range of crystallographic information. Thus, I do think it is appropriate to collect Phenix-related information (from a user perspective) there, and would like to invite everybody to contribute to the Phenix entry (and others!). thanks, Kay

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Re: [phenixbb] phenix.automr questions
by Kay Diederichs 29 Aug '10

29 Aug '10

Hi Tom, thanks for answering my questions! Yes, it would be good to have a flag to turn off the inverse hand because a) having the possibility to look at each spacegroup offers a very effective way of parallelization b) if I "grep" the spacegroup name in the logfile I find: dikay@turn10:-2010/phenix.automr% grep "P 4" mf92.log Space group: P 41 21 2 (No. 92) LIST OF ALL PLAUSIBLE SG: ['P 4 2 2', 'P 4 21 2', 'P 41 2 2', 'P 41 21 2', 'P 42 2 2', 'P 42 21 2', 'P 43 2 2', 'P 43 21 2'] Space group: P 41 21 2 (No. 92) NEW dictDATA {'raw_data': [' P 4abw 2nw', (101.71700286865234, 101.71700286865234, 344.74798583984375, 90.0, 90.0, 90.0), <scitbx_array_family_flex_ext.double object at 0xe554a10>, <scitbx_array_family_flex_ext.double object at 0xe554bd0>, <cctbx_array_family_flex_ext.miller_index object at 0xe4716c0>]} space_group : P 41 21 2 all_plausible_sg_list : ['P 4 2 2', 'P 4 21 2', 'P 41 2 2', 'P 41 21 2', 'P 42 2 2', 'P 42 21 2', 'P 43 2 2', 'P 43 21 2'] dictDATA: {'raw_data': [' P 4abw 2nw', (101.71700286865234, 101.71700286865234, 344.74798583984375, 90.0, 90.0, 90.0), <scitbx_array_family_flex_ext.double object at 0xe554a10>, <scitbx_array_family_flex_ext.double object at 0xe554bd0>, <cctbx_array_family_flex_ext.miller_index object at 0xe4716c0>]} HALL: P 4abw 2nw P 43 21 2 P 41 21 2 Space-Group Name (Number): P 41 21 2 (92) Space-Group Name: P 41 21 2 Space-Group Name (Number): P 41 21 2 (92) P 43 21 2 * P 41 21 2 Space-Group Name (Number): P 43 21 2 (96) Fast Translation Function Table: Space Group P 43 21 2 Space Group Name (Number): P 43 21 2 (96) Packing Table: Space Group P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) Refinement Table (Unsorted): Space Group P 43 21 2 Refinement Table (Sorted): Space Group P 43 21 2 Best Space Group: P 43 21 2 P 43 21 2 P 41 21 2 * Space-Group Name (Number): P 41 21 2 (92) Fast Translation Function Table: Space Group P 41 21 2 Best Space Group so far: P 43 21 2 Space Group Name (Number): P 41 21 2 (92) Packing Table: Space Group P 41 21 2 Space-Group Name (Number): P 41 21 2 (92) Refinement Table (Unsorted): Space Group P 41 21 2 Refinement Table (Sorted): Space Group P 41 21 2 Space-Group Name (Number): P 43 21 2 (96) Best spacegroup from search with first component in permutation: P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) Fast Translation Function Table: Space Group P 43 21 2 Space Group Name (Number): P 43 21 2 (96) Packing Table: Space Group P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) Refinement Table (Unsorted): Space Group P 43 21 2 Refinement Table (Sorted): Space Group P 43 21 2 Best Space Group: P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) Best spacegroup from search with first component in permutation: P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) Fast Translation Function Table: Space Group P 43 21 2 Space Group Name (Number): P 43 21 2 (96) Packing Table: Space Group P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) Refinement Table (Unsorted): Space Group P 43 21 2 Refinement Table (Sorted): Space Group P 43 21 2 Best Space Group: P 43 21 2 Space-Group Name (Number): P 43 21 2 (96) which shows that at a certain point the MTZ file's spacegroup is abandoned and the calculation finishes in the enantiomorph spacegroup, which has the drawback that I cannot really compare the best (complete) results of both enantiomorphs. And with one good and three bad search models I don't know if abandoning the given spacegroup early is definitively the right decision (but it's hard for me to tell exactly what criterion the decision was based upon - it may have been after an exhaustive search in #92 in which case my worry would not be justified). thanks, Kay > Message: 2 > Date: Sat, 28 Aug 2010 09:07:08 -0600 (MDT) > From: "Thomas C. Terwilliger"<terwilliger(a)lanl.gov> > To: "PHENIX user mailing list"<phenixbb(a)phenix-online.org> > Subject: Re: [phenixbb] phenix.automr questions > Message-ID:<14563.128.165.0.81.1283008028.squirrel(a)webmail.lanl.gov> > Content-Type: text/plain;charset=iso-8859-1 > > Hi Kay, > > I'll answer what I can; perhaps Randy the others may have more comments. > >>> Dear developers, >>> >>> I have four questions concerning phenix.automr (I'm using version 1.6.4): >>> >>> a) is there a way to make the program try all permutations for the >>> search order of my four search molecules, or do I have to write a script ? > > It would be a good idea for me to put that in. For now, yes, you have to > make a script to do that. > >>> >>> b) how can I completely switch off the search in the alternative >>> spacegroups - I am under the impression that although the "effective >>> parameters" are >>> all_plausible_sg_list = None >>> use_all_plausible_sg = False >>> the search is not only done in the spacegroup I specified (#92=P41212) >>> but also in #96=P43212 . I believe so because the output says: >>> ... >>> 2 alternative spacegroups >>> SpaceGroup will be determined by highest LLG in search for FIRST >>> ensemble >>> Search order: >>> P 43 21 2 >>> P 41 21 2 >>> ... >>> (I would rather run a second search "manually" in the other spacegroup!) > > Yes, it runs the inverse hand even if you say > "use_all_plausible_sg=False". However it should not run all the other > space groups (all_plausible_sg_list : ['P 4 2 2', 'P 4 21 2', 'P 41 2 2', > 'P 41 21 2', 'P 42 2 2', 'P 42 21 2', 'P 43 2 2', 'P 43 21 2']). I'll see > if we can put in a flag so it doesn't run the inverse hand if you don't > want it to. > > >>> >>> c) I have two occurrences of seq_file ("all.seq" and "all.dat"; the >>> latter is symlinked to the former). Am I right that I could just leave >>> out one of them? I did this after looking at >>> http://www.phenix-online.org/documentation/automr.htm#anch70 but I >>> wonder which of the specifications of sequences and masses overrides the >>> other one? or is the first specification used for editing the search >>> models, and the second for getting the likelihood terms right? > > Looking at your parameters file, I see what you mean. If you supply two > different files, then yes, the one you specified at the top of your file > with "seq_file=all.dat" is going to be used for editing the file for > autobuild, and the one you specified in the scope "component" is going to > be used for getting the likelihood terms right. > > Normally (always?) these should be the same. So normally, just supply the > first one "input_seq_file=seq.dat") and it will be used for both purposes. > > Or if you have several components, only specify them in the "component" > scopes, and all of them will be put together into a single file and used > as the input to autobuild. > > >>> >>> d) what kind of editing is done? Is phenix.sculptor run internally? I >>> find {a,b,c,d}_edited.pdb but are they actually used? > > Only basic editing to make the model compatible with autobuild is done. No > sculpting is done inside automr for now. > > All the best, > Tom T

1 0

phenix.automr questions
by Kay Diederichs 29 Aug '10

29 Aug '10

Dear developers, I have four questions concerning phenix.automr (I'm using version 1.6.4): a) is there a way to make the program try all permutations for the search order of my four search molecules, or do I have to write a script ? b) how can I completely switch off the search in the alternative spacegroups - I am under the impression that although the "effective parameters" are all_plausible_sg_list = None use_all_plausible_sg = False the search is not only done in the spacegroup I specified (#92=P41212) but also in #96=P43212 . I believe so because the output says: ... 2 alternative spacegroups SpaceGroup will be determined by highest LLG in search for FIRST ensemble Search order: P 43 21 2 P 41 21 2 ... (I would rather run a second search "manually" in the other spacegroup!) c) I have two occurrences of seq_file ("all.seq" and "all.dat"; the latter is symlinked to the former). Am I right that I could just leave out one of them? I did this after looking at http://www.phenix-online.org/documentation/automr.htm#anch70 but I wonder which of the specifications of sequences and masses overrides the other one? or is the first specification used for editing the search models, and the second for getting the likelihood terms right? d) what kind of editing is done? Is phenix.sculptor run internally? I find {a,b,c,d}_edited.pdb but are they actually used? thank you, Kay P.S. I run with "phenix.automr mr.eff" where mr.eff is automr { data = "m879_2_rg92.mtz" seq_file = all.dat ensemble { ensembleID = "mol1" copies_to_find = 1 coords = a.pdb identity = 80 } ensemble { ensembleID = "mol2" copies_to_find = 1 coords = b.pdb identity = 45 } ensemble { ensembleID = "mol3" copies_to_find = 1 coords = c.pdb identity = 45 } ensemble { ensembleID = "mol4" copies_to_find = 1 coords = d.pdb identity = 45 } component { component_type = *protein nucleic_acid seq_file = all.seq component_copies = 1 } autobuild_variables{ n_cycle_rebuild_max = 1 } }

4 3

Phenix error running MIR-example
by Shankar Prasad Kanaujia 29 Aug '10

29 Aug '10

Dear Developers/Users, I am getting an error while running "rh-dehalogenase-mir" example provided in the phenix example. I am using phenix 1.6.4 version. It runs properly using the command "phenix.run_example rh-dehalogenase-mir", whereas, it gives error in GUI mode. I am attaching the picture of my input and error (in the right-top corner). Please let me know the reason of this error. -- Yours Sincerely, Shankar Prasad Kanaujia Research Student C/O - Dr. K. Sekar Bioinformatics Centre, SERC Indian Institute of Science, Bangalore-12 Phone - 9480258032 Office - 080-2293-3059

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Postdoctoral position in Protein X-ray Crystallography
by cdas＠purdue.edu 29 Aug '10

29 Aug '10

Applications are invited for a postdoctoral research position in the Das Lab, Department of Chemistry, Purdue University, West Lafayette, IN, USA. The position requires the applicant to work on structural and biochemical characterization of ubiquitin hydrolases (deubiquitinases) and their complexes with substrates, cofactors and inhibitors (see Boudreaux et al, PNAS, 107, 9117 (2010)). The applicant is also expected to work on an ongoing collaborative project on method development related to imaging of protein crystals (of ubiquitin hydrolases and others) using second order non-linear optical methods. We are looking for highly motivated candidates with extensive experience in biochemical studies, crystallization and structure determination of proteins by x-ray crystallography. Specifically, the candidate is required to have hands-on experience with protein purification, crystallization, X-ray data collection, structure determination and structural analysis. Applicants should send their CV and the names and contact information of at least three references via email to: Chitta Das Assistant Professor Department of Chemistry Purdue University 560 Oval Drive West Lafayette IN, 47907 Email address: cdas(a)purdue.edu

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Can Phenix refine B factors for several residues only?
by zhangh1＠umbc.edu 29 Aug '10

29 Aug '10

Hi, I want to refine B factors for several residues only (all the other B factors and all coordinates fixed, I know it sounds weird but there is a reason to try that). Is there anyway Phenix can do this? Thanks for any suggestions! Best Regards, Hailiang

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