- phenixbb - phenix-online.org

Composite Omit Map Calculations - Batch Que
by Matthew J. Whitley 07 Feb '12

07 Feb '12

Hello all, I usually set up simulated annealing composite omit map calculations via the Phenix GUI and set the number of processors equal to 2 to take advantage of my Mac's dual core processor in order to shorten the calculation time somewhat. My department does have a high performance cluster, however, and I would like to start using that multi-node system to shorten the calculation time substantially. The problem for me is that the high performance cluster requires jobs to be submitted and managed via a PBS queue. I know how to specify in the PBS shell script the computing resources I want to use (say, for example, 8 dual core processors for a total of 16 nodes). My question is, do I need to specify any additional settings in the actual Phenix command line execution statement? For example, nproc = 16? Anything else? The entire shell script containing the PBS setup statements and the actual Phenix execution statements is submitted by the qsub command. In essence, I am wondering how to get Phenix to "play nicely" with the queueing system such that the composite omit calculations will be distributed box by box over the resources I reserve via the PBS statements. Thanks in advance for any advice. Also, if anybody has experience running Phenix jobs via a shell script submitted to a batch queueing system, I would very much appreciate the chance to look at the shell script. Thanks, Matthew --- Matthew J. Whitley, Ph.D. Postdoctoral Research Fellow Angela Gronenborn Lab Department of Structural Biology University of Pittsburgh School of Medicine

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Difference in water molecules count
by bsubedi＠btk.fi 07 Feb '12

07 Feb '12

Hi All, I have been refining the mutant structures and at the end while making the comparative study I found that there is a large difference (almost half) number of water molecules in the protein strucutre of same mutant from different crystal conditions. The resolution of the structure, space group and no.of molecules in a.s.u is same. Here is the data collection statistics and no.of water & protein atoms present. I could also not understand the difference of unique and measured reflections at same resolution. Could anyone please explain me? Resolution range (Å) 20-1.6 (1.64-1.60) 20-1.8 (1.85-1.80) 20-1.9 (1.99-1.94) 20-1.6 (1.63-1.59) 20-1.6 (1.64-1.60) Number of measured reflections 221864 (14118) 173933 (9556) 85976 (5129) 206723 (12667) 262291 (15803) Unique reflections 84896 (6139) 59955 (4010) 38628 (2777) 86161 (5992) 85305 (5803) Completeness (%) 98.7 (97.2) 95.9 (87.9) 77.6 (75.5) 93.9 (87.9) 97.8 (90.9) No of protein atoms 5101 5096 5076 5113 5120 No of waters 1103 528 453 585 1214 Thanx, World

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CASP Roll: Call for novel fold and membrane protein targets to help improve structure modeling methods
by Torsten Schwede 06 Feb '12

06 Feb '12

Dear colleagues, As many of you know, the CASP community experiments have been running once every two years since 1994, collecting information on soon to be solved structures from the experimental community, and passing on sequence data to the structure modeling community so that blind predictions of structure can be collected and assessed (1). Over that period CASP has seen enormous progress in the quality of modeled structures (2), but many problems remain. The regular CASP experiments collect target information for a three month season every two years, and in that period, thanks especially to the structural genomics community, can acquire over 100 targets, sufficient to evaluate the state of the art for most types of template based modeling. There are some classes of target, specifically proteins with novel folds and membrane proteins, where there are not enough structures solved in three months to provide sufficient information so the methods can be fully evaluated. As a consequence, progress is slowed. To address this problem, with the encouragement of the modeling community, CASP has launched a rolling mechanism, where we accept targets in these categories at any time. Of course for that to work we rely on you, the experimentalists, to provide suitable targets! So we are asking that you tell us about structures in these categories that are about to be solved whenever they come up. For those of you who have not provided targets to CASP before, the procedure is simple – there is a web page for submitting targets, and a very experienced staff to deal with any queries. We don’t need the structure in advance of its release by the PDB, and if we are notified early enough (a minimum of three weeks before release, more is better) there need be no delay in structure release. If you have a suitable target now, we are up and running with 50+ prediction teams already submitting models, and would love to have your targets. Most important, the modeling community is now in continuous need of your assistance, so please get in touch whenever an opportunity arises in the future, and help improve modeling methods. Thanks, CASP organizing committee John Moult, IBBR, University of Maryland, USA Krzysztof Fidelis, University of California, Davis, USA Andriy Kryshtafovych, University of California, Davis, USA Torsten Schwede, University of Basel & SIB, Switzerland Anna Tramontano, University of Rome, Italy Get in touch: casp(a)predictioncenter.org More information: http://www.predictioncenter.org/casprol/ CASP Roll targets so far: http://www.predictioncenter.org/casprol/targetlist.cgi Submit a target: http://www.predictioncenter.org/casprol/targets_submission.cgi 1. Critical assessment of methods of protein structure prediction (CASP)--round IX. Moult J, Fidelis K, Kryshtafovych A, Tramontano A. Proteins. 2011;79 Suppl 10:1-5. doi: 10.1002/prot.23200. Epub 2011 Oct 14. 2. CASP9 results compared to those of previous CASP experiments. Kryshtafovych A, Fidelis K, Moult J. Proteins. 2011;79 Suppl 10:196-207. doi: 10.1002/prot.23182. Epub 2011 Oct 14.

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FW: Summer Internship at Merck for Ph.D. students
by Soisson, Stephen M 06 Feb '12

06 Feb '12

All, We have a summer internship opening at Merck (see below for the details) for graduate students in the Global Structural Chemistry/X-ray crystallography/Biomolecular NMR group at either its Kenilworth, NJ or West Point, PA sites. Internships will begin in early June 2012, and will run for 10-12 weeks. If you are interested please visit our career site at www.merck.com/careers<http://www.merck.com/careers> to create a profile and submit your resume for requisition #CHE003379. Sincerely, Steve Soisson -------------- Job Description X-ray Crystallography/BioNMR Summer Internship 2012 - PhD:CHE003379 Description Merck is a global health care leader with a diversified portfolio of prescription medicines, vaccines and consumer health products, as well as animal health products. Today, we are building a new kind of healthcare company - one that is ready to help create a healthier future for all of us. Our ability to excel depends on the integrity, knowledge, imagination, skill, diversity and teamwork of people like you. To this end, we strive to create an environment of mutual respect, encouragement and teamwork. As part of our global team, you'll have the opportunity to collaborate with talented and dedicated colleagues while developing and expanding your career. Merck Research Labs will be offering 2012 summer internships in the Global Structural Chemistry group (X-ray crystallography or Biomolecular NMR) at either its Kenilworth, NJ or West Point, PA sites. Internships will begin in early June 2012, and will run for 9-11 weeks. A suitable candidate has a science background with interest in the use of X-ray crystallography and/or Biomolecular NMR in drug discovery. Not required, but a plus, would be experience in one or more of the areas of protein crystallization, X-ray theory, X-ray crystallography or Biomolecular NMR. Preference will be given to candidates having a strong math and/or physical science background with expertise in computers and computer programming. Candidates will gain firsthand experience in modern drug discovery, and will also make valuable contacts within the industry. **Please note when applying for this position, the candidate MUST upload a cover letter or a personal statement letter and a copy of your unofficial transcript along with your resume. Qualifications Required: * Currently pursuing a Ph.D. in Biomolecular NMR, X-ray crystallography, Computational Chemistry, Biophysics or a related field * Applicants must be available for full-time employment for 9 - 11 weeks during the months of June - August 2012. Preferred: * Experience in one or more of the areas of protein crystallization, X-ray theory, X-ray crystallography or Biomolecular NMR * Strong math and/or physical science background with expertise in computers and computer programming * Science background with an interest in computers and drug discovery Our employees are the key to our company's success. We demonstrate our commitment to our employees by offering a competitive and valuable rewards program. Merck's benefits are designed to support the wide range of goals, needs and lifestyles of our employees, and many of the people that matter the most in their lives. To be considered for this position, please visit our career site at www.merck.com/careers<http://www.merck.com/careers> to create a profile and submit your resume for requisition #CHE003379. Merck is an equal opportunity employer, M/F/D/V - proudly embracing diversity in all of its manifestations. Notice: This e-mail message, together with any attachments, contains information of Merck & Co., Inc. (One Merck Drive, Whitehouse Station, New Jersey, USA 08889), and/or its affiliates Direct contact information for affiliates is available at http://www.merck.com/contact/contacts.html) that may be confidential, proprietary copyrighted and/or legally privileged. It is intended solely for the use of the individual or entity named on this message. If you are not the intended recipient, and have received this message in error, please notify us immediately by reply e-mail and then delete it from your system.

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Problem with version 1.7.1-743 on OSX
by Miguel Ortiz Lombardía 06 Feb '12

06 Feb '12

Dear phenix developers, Last Friday (April 29) we upgraded phenix to its most recent version (1.7.1-743). Installation went smoothly on both Mac (10.6.7 64-bit) and Linux (Ubuntu 10.10 64-bit) machines. However, we observe that we cannot use phenix.refine (I don't know for the rest of the applications) from the GUI on the Macs. phenix.refine does work from the command line, though. So, whenever we try to add a pdb in the GUI, we get this error message: This application does not support the file type for /path/to/the/file.pdb (format: txt) If we try to open an mtz, it sometime works, but most often we get: PHENIX did not recognize the file type for /path/to/the/file.mtz! and on the terminal from where the GUI was started we can find: **SYMMETRY OPERATOR ERROR** Error in interpreting symop " X+2/3, Y+1/3, Z+1/3 " **SYMMETRY OPERATOR ERROR** Error in interpreting symop " -Y+2/3, X-Y+1/3, Z+1/3 " (and so on, so forth). Any clues ? Best regards, -- Miguel Architecture et Fonction des Macromolécules Biologiques (UMR6098) CNRS, Universités d'Aix-Marseille I & II Case 932, 163 Avenue de Luminy, 13288 Marseille cedex 9, France Tel: +33(0) 491 82 55 93 Fax: +33(0) 491 26 67 20 mailto:[email protected] http://www.afmb.univ-mrs.fr/Miguel-Ortiz-Lombardia -- This message has been scanned for viruses and dangerous content by MailScanner, and is believed to be clean.

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Illegal instruction (core dumped)
by Hasan Demirci 04 Feb '12

04 Feb '12

Hi Folks, I just finished updating phenix-dev-944 to phenix-dev-975 version on Fedora Core 16 OS intel quad-core machine. When I run phenix from terminal "phenix.refine" I am receiving the following error message "Illegal instruction (core dumped)". This is the first time I saw this error. All the other programs run fine except phenix. I downloaded and installed it twice to see if it was an error of download but it still gives the same message. Is it an installation error or is it a bug in this version? Thanks. -- Hasan DeMirci

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MAD from many crystal
by Theresa H 03 Feb '12

03 Feb '12

Hi everyone. Can I do 3 wavelength MAD phasing with AutoSol GUI with data from multiple crystals? Is there a reference/guide that I can use? Thank you. Theresa

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structure comparison
by Christian Roth 03 Feb '12

03 Feb '12

Hi all, I tried the structure comparison in phenix validation and loaded seveeral structures and a sequence file. I started and than this strange error appears Did I specified something wrong? Best Regards Christian AssertionError : Traceback: File "/userdata-2/christian/phenix- dev-968/cctbx_project/libtbx/thread_utils.py", line 229, in run return_value = self._target(self._args, self._kwargs, self._c) File "/userdata-2/christian/phenix- dev-968/cctbx_project/libtbx/runtime_utils.py", line 72, in __call__ result = self.target() File "/userdata-2/christian/phenix- dev-968/phenix/phenix/automation/structure_comparison/__init__.py", line 1041, in __call__ analyses = run(args=list(self.args), log=sys.stdout) File "/userdata-2/christian/phenix- dev-968/phenix/phenix/automation/structure_comparison/__init__.py", line 1006, in run analyses = manager(params.structure_comparison, log=log) File "/userdata-2/christian/phenix- dev-968/phenix/phenix/automation/structure_comparison/__init__.py", line 196, in __init__ self.run() File "/userdata-2/christian/phenix- dev-968/phenix/phenix/automation/structure_comparison/__init__.py", line 250, in run self.process_alignment() File "/userdata-2/christian/phenix- dev-968/phenix/phenix/automation/structure_comparison/__init__.py", line 370, in process_alignment log=self.log) File "/userdata-2/christian/phenix-dev-968/cctbx_project/mmtbx/msa.py", line 262, in align_pdb_hierarchies assert (reference_hierarchy is None)

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Re: [phenixbb] [ccp4bb] Lysozyme/Xenon derivatives & Phenix.
by Randy Read 03 Feb '12

03 Feb '12

Hi, I'm cross-posting this to the Phenix-BB, because you did this calculation in Phenix, but since the site completion for SAD phasing would be done with Phaser, the answer is relevant to both packages. Basically, I think Jim Pflugrath's suggestion is correct. Comparing your Xe coordinates to S and Cl coordinates from one of our test SAD phasing datasets, the majority of your extra sites are in the positions of either intrinsic S anomalous scatterers or bound halides. The Phaser completion step found them, even though you only asked for 2 sites initially, because it continues adding new sites as long as there are significant peaks in the SAD LLG maps. The refined occupancies make sense, assuming you were collecting your data around 1A wavelength. At that wavelength f" is about 4-5e for Xe and about 0.25-0.3 for S or Cl, and multiplying (say) 4.5e by occupancies of 0.03-0.08 gives effective f" values of 0.14-0.36e. Of course, Phaser isn't just trying to fit the imaginary part of the scattering, so the occupancies could end up slightly higher because it's trying to account for atoms with 16-17 electrons using partially-occupied atoms with 54 electrons. Knowing that, once Phaser has found the Xe atoms, it will then find the weak anomalous scattering from S and Cl, you could tell Phaser to look in addition for S atoms. (At around 1A wavelength, there's not enough difference between S and Cl, in either their real or anomalous scattering, to matter, so you don't need to look for Cl in addition.) Phaser will reassign atom types based on refined occupancy, so it would likely get most of these right, which would very slightly improve your phasing model (because you would then have the right ratio of real to imaginary scattering). Another advantage to looking for both atom types is that, when you mix atoms with different ratios of real and imaginary scattering, Friedel's law is broken even for the substructure structure factors, which has two consequences. First, the likelihood score will probably be significantly better for the correct enantiomorph than the incorrect one; second, you're likely to end up with a slightly more complete substructure when working with the correct enantiomorph. Note that AutoSol also chose the correct enantiomorph after phasing, by looking at map quality indicators for the two hands. Regards, Randy Read On 2 Feb 2012, at 16:43, Brennan Bonnet wrote: > Hi all, > > I have a strange result using Phenix's AutoSol to look for xenon sites in lysozyme. > > For a few months now I have been trying to produce xenon derivatives of lysozyme using pressures in the range of 50-350psi and time ranges between 5-60min trying to find the "sweet spot" so that this technique can be applied to other proteins. > > For each dataset, I AutoSol using phenix and have it look for 2, 3, and 4 xenon sites. I haven't had much success though and typical values when asked to look for 2 sites have been Rwork/Rfree = 0.5585/0.5892, CC=0.14, Bayes-CC=6.5 and with xenon sites: > > (a, b, c, alpha, beta, gamma, space group) > CRYST1 78.870 78.870 36.940 90.00 90.00 90.00 P 41 21 2 > > (columns after numbering are a, b, c, occ, B factor) > HETATM 1 XE XE Z 1 48.601 67.475 1.088 0.06 6.58 XE > HETATM 2 XE XE Z 2 54.986 76.636 2.746 0.11 7.49 XE > > which, to me, says that there is no binding (or at least nothing obvious). > > I finally got a good result though with 350psi and 5 minutes pressurization. After AutoSol, FOM=0.436, Bayes-CC=33.57, Model CC=0.83, Rwork/Rfree=0.2843/0.3023, 117/125 residues build and placed. And even though I told it to only look for 2 sites, Phenix went ahead and found 22 sites: > > (a, b, c, alpha, beta, gamma, space group) > CRYST1 79.130 79.130 36.920 90.00 90.00 90.00 P 43 21 2 > > (colums after numbering are a, b, c, occ, B factor) > HETATM 1 XE XE Z 1 -36.117 -56.764 -1.825 0.18 9.43 XE > HETATM 2 XE XE Z 2 -54.805 -54.805 0.000 0.14 6.44 XE > HETATM 3 XE XE Z 3 -8.337 -31.695 -16.766 0.08 8.26 XE > HETATM 4 XE XE Z 4 -5.702 -64.959 -35.134 0.05 5.21 XE > HETATM 5 XE XE Z 5 -9.535 -22.397 -31.839 0.06 14.33 XE > HETATM 6 XE XE Z 6 -7.319 -66.343 -35.123 0.05 6.02 XE > HETATM 7 XE XE Z 7 -8.580 -21.153 -30.274 0.05 7.43 XE > HETATM 8 XE XE Z 8 -1.494 -29.583 -2.339 0.06 7.36 XE > HETATM 9 XE XE Z 9 -0.518 -16.483 -16.776 0.05 6.56 XE > HETATM 10 XE XE Z 10 -0.464 -29.847 -4.386 0.06 6.04 XE > HETATM 11 XE XE Z 11 -1.222 -16.234 -18.952 0.04 6.51 XE > HETATM 12 XE XE Z 12 -6.001 -20.380 -4.532 0.05 7.22 XE > HETATM 13 XE XE Z 13 -5.169 -27.522 -10.128 0.05 3.54 XE > HETATM 14 XE XE Z 14 -11.931 -67.039 -4.699 0.05 7.96 XE > HETATM 15 XE XE Z 15 -6.538 -10.408 -3.761 0.04 10.22 XE > HETATM 16 XE XE Z 16 -0.458 -23.897 -31.221 0.05 6.85 XE > HETATM 17 XE XE Z 17 -3.308 -65.181 -8.754 0.03 8.08 XE > HETATM 18 XE XE Z 18 -11.080 -29.129 -2.144 0.04 5.61 XE > HETATM 19 XE XE Z 19 -5.720 -73.029 -2.035 0.04 11.24 XE > HETATM 20 XE XE Z 20 10.236 60.097 33.822 0.03 5.38 XE > HETATM 21 XE XE Z 21 5.980 68.581 3.532 0.03 7.49 XE > HETATM 22 XE XE Z 22 11.107 13.277 27.334 0.03 7.10 XE > > I'm pretty sure there aren't 22 sites for xenon to bind in lysozyme but it looks to me like the top 2 (maybe top 3) are actual sites which is great. > The strange part is that when I use the same data and have Phenix look for 3 or 4 sites it then only finds 3 or 4 very low occupancy sites and the CC's/R's are again all very poor. > Has anyone had this problem or does anyone know what's going on? This is the first success that I'm having with xenon derivatization and it seems to me that if Phenix can find 22 sites when asked to find 2 it should have no problem when asked to find 3 or 4. > > Thanks in advance, > ~Brennan~ ------ Randy J. Read Department of Haematology, University of Cambridge Cambridge Institute for Medical Research Tel: + 44 1223 336500 Wellcome Trust/MRC Building Fax: + 44 1223 336827 Hills Road E-mail: rjr27(a)cam.ac.uk Cambridge CB2 0XY, U.K. www-structmed.cimr.cam.ac.uk

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Re: [phenixbb] Lysozyme/Xenon derivatives & Phenix.
by Terwilliger, Thomas C 02 Feb '12

02 Feb '12

Hi Brennan, The number of sites that you ask for affects the HYSS heavy-atom search procedure, but not too much else. Once some sites are found by HYSS, then autosol uses phaser to identify additional sites (that's why you got 22 sites, not 2). I am a little surprised that changing the number of sites from 2 to 4 makes the difference between finding correct sites and not finding them at all, but it does seem possible. For your experiment, one thing you could do: once you figure out where the "standard" Xe sites are, just feed them in to autosol with a sites_file=xxx.pdb for all your datasets. Then they are all starting out with pretty much the same information. All the best, Tom T ________________________________________ From: CCP4 bulletin board [CCP4BB(a)JISCMAIL.AC.UK] on behalf of Brennan Bonnet [Brennan.Bonnet(a)LIGHTSOURCE.CA] Sent: Thursday, February 02, 2012 9:43 AM To: CCP4BB(a)JISCMAIL.AC.UK Subject: [ccp4bb] Lysozyme/Xenon derivatives & Phenix. Hi all, I have a strange result using Phenix's AutoSol to look for xenon sites in lysozyme. For a few months now I have been trying to produce xenon derivatives of lysozyme using pressures in the range of 50-350psi and time ranges between 5-60min trying to find the "sweet spot" so that this technique can be applied to other proteins. For each dataset, I AutoSol using phenix and have it look for 2, 3, and 4 xenon sites. I haven't had much success though and typical values when asked to look for 2 sites have been Rwork/Rfree = 0.5585/0.5892, CC=0.14, Bayes-CC=6.5 and with xenon sites: (a, b, c, alpha, beta, gamma, space group) CRYST1 78.870 78.870 36.940 90.00 90.00 90.00 P 41 21 2 (columns after numbering are a, b, c, occ, B factor) HETATM 1 XE XE Z 1 48.601 67.475 1.088 0.06 6.58 XE HETATM 2 XE XE Z 2 54.986 76.636 2.746 0.11 7.49 XE which, to me, says that there is no binding (or at least nothing obvious). I finally got a good result though with 350psi and 5 minutes pressurization. After AutoSol, FOM=0.436, Bayes-CC=33.57, Model CC=0.83, Rwork/Rfree=0.2843/0.3023, 117/125 residues build and placed. And even though I told it to only look for 2 sites, Phenix went ahead and found 22 sites: (a, b, c, alpha, beta, gamma, space group) CRYST1 79.130 79.130 36.920 90.00 90.00 90.00 P 43 21 2 (colums after numbering are a, b, c, occ, B factor) HETATM 1 XE XE Z 1 -36.117 -56.764 -1.825 0.18 9.43 XE HETATM 2 XE XE Z 2 -54.805 -54.805 0.000 0.14 6.44 XE HETATM 3 XE XE Z 3 -8.337 -31.695 -16.766 0.08 8.26 XE HETATM 4 XE XE Z 4 -5.702 -64.959 -35.134 0.05 5.21 XE HETATM 5 XE XE Z 5 -9.535 -22.397 -31.839 0.06 14.33 XE HETATM 6 XE XE Z 6 -7.319 -66.343 -35.123 0.05 6.02 XE HETATM 7 XE XE Z 7 -8.580 -21.153 -30.274 0.05 7.43 XE HETATM 8 XE XE Z 8 -1.494 -29.583 -2.339 0.06 7.36 XE HETATM 9 XE XE Z 9 -0.518 -16.483 -16.776 0.05 6.56 XE HETATM 10 XE XE Z 10 -0.464 -29.847 -4.386 0.06 6.04 XE HETATM 11 XE XE Z 11 -1.222 -16.234 -18.952 0.04 6.51 XE HETATM 12 XE XE Z 12 -6.001 -20.380 -4.532 0.05 7.22 XE HETATM 13 XE XE Z 13 -5.169 -27.522 -10.128 0.05 3.54 XE HETATM 14 XE XE Z 14 -11.931 -67.039 -4.699 0.05 7.96 XE HETATM 15 XE XE Z 15 -6.538 -10.408 -3.761 0.04 10.22 XE HETATM 16 XE XE Z 16 -0.458 -23.897 -31.221 0.05 6.85 XE HETATM 17 XE XE Z 17 -3.308 -65.181 -8.754 0.03 8.08 XE HETATM 18 XE XE Z 18 -11.080 -29.129 -2.144 0.04 5.61 XE HETATM 19 XE XE Z 19 -5.720 -73.029 -2.035 0.04 11.24 XE HETATM 20 XE XE Z 20 10.236 60.097 33.822 0.03 5.38 XE HETATM 21 XE XE Z 21 5.980 68.581 3.532 0.03 7.49 XE HETATM 22 XE XE Z 22 11.107 13.277 27.334 0.03 7.10 XE I'm pretty sure there aren't 22 sites for xenon to bind in lysozyme but it looks to me like the top 2 (maybe top 3) are actual sites which is great. The strange part is that when I use the same data and have Phenix look for 3 or 4 sites it then only finds 3 or 4 very low occupancy sites and the CC's/R's are again all very poor. Has anyone had this problem or does anyone know what's going on? This is the first success that I'm having with xenon derivatization and it seems to me that if Phenix can find 22 sites when asked to find 2 it should have no problem when asked to find 3 or 4. Thanks in advance, ~Brennan~

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