- phenixbb - phenix-online.org

Immediately available: Postdoctoral position in Computational Structural Biology
by David Sivak 17 Sep '14

17 Sep '14

Dear colleagues, This fall I start my own research group in the Physics Department at Simon Fraser University in Vancouver, British Columbia. In the near future, I hope to hire an exceptional, highly-motivated postdoctoral fellow to work on computational structural biology. Please forward this announcement to any interested parties. My group combines approaches from physics, information theory, and statistics to study the fundamental principles of biomolecular function under strong fluctuations. The postdoctoral position will focus on the development of model comparison methods to understand the conformational heterogeneity revealed by structural biology experiments, especially X-ray crystallography. Within this broad research thrust there is ample freedom to pursue particular areas of personal scientific interest. Our theoretical flights of fancy are tethered to reality through a close collaboration with the experimental group of Jaime Fraser at UC San Francisco. Postdoctoral fellows in my group will work in the intellectually-stimulating and interactive biophysics community within SFU Physics, with close ties to the Molecular Biology/Biochemistry department, home to several top-notch structural biology groups. In my own (possibly biased) opinion, the endless all-season outdoors opportunities, mind-blowing food from all ethnicities, and mild weather make Vancouver an enviable place to call home; slightly more objectively, it makes every official top 5 list of most livable cities in the world. The ideal candidate would have experience with computer programming, biomolecular modeling and statistics, and a PhD in a relevant field (broadly construed: physics, biophysics, chemistry, bio- or chemical-engineering, molecular biology, or relevant areas of statistics, computer science, applied math, etc). But most important is intellectual curiosity, enthusiasm for research in this area, and an excellent track record in whatever field they have pursued. Interested candidates should send me a cover letter and CV (including publication list and contact information for 2-3 references). Further information is available at: http://davidsivak.com/ Thank you in advance! David -- David Sivak Asst. Prof., Dept. of Physics, Simon Fraser U david.sivak(a)gmail.com davidsivak.com 778-928-7995

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phenix.merging_statistics and resolution shells
by Murpholino Peligro 17 Sep '14

17 Sep '14

can I specify the ranges of the resolution shells in phenix.merging_statistics? (something like "XSCALE-word" RESOLUTION_SHELLS=) and how many resolution shells are ok? 10, 15, 20?

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LABELIT and MOSFLM version
by Ngoc Anh Thu Ho 16 Sep '14

16 Sep '14

Hello, labelit.index command cannot start Mosflm and gives an error, which reads: "MosflmVersionError: mosflm versions after 7.0.9 not supported” Other than that, indexing seems to be working fine. Can this be fixed or updated somehow? I’m using the latest Phenix 1.9-1692 and Mosflm 7.1.0 (with iMosflm 7.1.1). Best regards, Thu

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calculate CC*
by wei xia 15 Sep '14

15 Sep '14

Hi all:I have a set of data indexed with XDS (space group P222). When I use phaser, the MR solution was in space group P212121.I then changed the space group of mtz file to P212121 using phenix Reflection file editor and did the refinement. Now I use phenix to calculate CC*, in which I input unmerged data (from xds, P222) and merged data (mtz file, P212121) and final pdb file.It turned out to be "incompatible symmetry" error. Are there any easy ways to get the calculate CC* running?Thanks! Wei Xia

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Re: [phenixbb] [ccp4bb] Autobuild in specific area
by Terwilliger, Thomas Charles 14 Sep '14

14 Sep '14

Hi Foggy, This is a situation that autobuild does not address very well yet. Yes, you want rebuild_in_place=False. And yes, if you do that it will remove your model and rebuild it. It will also try to build into the remainder of the map. In practice, you already have pretty much the best that autobuild is going to produce. Delete the protein A chains that autobuild built, and put in your original protein A. Now you have your original model plus whatever autobuild was able to build. An alternative is: select "consider_main_chain_list=True" . This will take your input model A and at each step it will check to see if parts of that model are better than any other model that it has built. This can help for keeping the input model that you put in. All the best, Tom T ________________________________ From: CCP4 bulletin board [CCP4BB(a)JISCMAIL.AC.UK] on behalf of Zhang Foggy [foggyccp4(a)GMAIL.COM] Sent: Saturday, September 13, 2014 10:40 AM To: CCP4BB(a)JISCMAIL.AC.UK Subject: [ccp4bb] Autobuild in specific area Hi, All, I am trying to use Autobuild to build a protein-protein complex model. I obtained partial phase solution (protein-A) through MR, and can see some density of protein-B near protein-A. I would like to use Autobuild to build protein-B model into this area. I load data file, initial density map file, sequence file (both of protein A and B), and protein A model, and run Autobuild. However, The "rebuild-in-place" function confused me a lot, no matter I set it to True or False. When I set to True, it only rebuilt protein A model without adding any additional residues; while I set it to False, it deleted the input protein-A model, and rebuilt a new one... Could somebody tell me how to build the protein B model with keeping the input protein A model in Autobuild? Thanks. [https://ssl.gstatic.com/ui/v1/icons/mail/images/cleardot.gif] Foggy

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Autobuild in specific area
by Zhang Foggy 13 Sep '14

13 Sep '14

Hi, All, I am trying to use Autobuild to build a protein-protein complex model. I obtained partial phase solution (protein-A) through MR, and can see some density of protein-B near protein-A. I would like to use Autobuild to build protein-B model into this area. I load data file, initial density map file, sequence file (both of protein A and B), and protein A model, and run Autobuild. However, The "rebuild-in-place" function confused me a lot, no matter I set it to True or False. When I set to True, it only rebuilt protein A model without adding any additional residues; while I set it to False, it deleted the input protein-A model, and rebuilt a new one... Could somebody tell me how to build the protein B model with keeping the input protein A model in Autobuild? Thanks. Foggy

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phenix rosetta installation
by Dan Lin 12 Sep '14

12 Sep '14

Hi all: This is kind of a silly problem, but I'm trying to get phenix.rosetta_refine running on my computer and I am having some difficulty getting rosetta.build_phenix_interface to run. I'm getting a permission denied error in the os.symlink(python_lib, lib_link_name) line in rosetta_build_phenix_interface.py script and presumably I could fix this by changing the write permissions to wherever this points to, but I don't know where. Could anybody point me towards the folder that needs to fixed? Thanks, Dan

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restraints for dna planarity
by John Lee 12 Sep '14

12 Sep '14

Hi, I'm refining a low resolution structure of a dna-protein complex (3.7A) & wondering if someone could help me with setting restraints in Phenix to maintain the base-pair planarity of the dna? With the restraints I have, even with a reference model, I'm getting 'puckering' of the base-pairs. Although the h-bonding distances seem to hold over time, I can't seem to find a way to keep the planarity intact. Thanks in advance for your help. -John

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Phenix-Rosetta integration tests fail with Rosetta MPI on RHEL 6.3
by Sina Masoud-Ansari 12 Sep '14

12 Sep '14

Hi there, I'm wondering anyone has managed to successfully run Phenix with Rosetta MPI on Red Hat Enterprise Linux 6.3 or similar? I currently have a non-MPI build of Rosetta that passes all of the tests in phenix_regression.wizards.test_command_line_rosetta_quick However when running these tests with the MPI build of Rosetta the following tests fail: Running test_relax ------------------------------------------------------------ Numbers do not match: 6 1 Relaxed solutions 6 --- Relaxed solutions 1 ------------------------------------------------------------ FAILED See log files test_relax/test_relax.log test_relax/test_relax_current.log ================================================================= Running test_relax_double ------------------------------------------------------------ Numbers do not match: 6 1 Relaxed solutions 6 --- Relaxed solutions 1 ------------------------------------------------------------ ------------------------------------------------------------ Numbers do not match: 6 1 Relaxed solutions 6 --- Relaxed solutions 1 ------------------------------------------------------------ FAILED See log files test_relax_double/test_relax_double.log test_relax_double/test_relax_double_current.log ================================================================= Running test_relax_no_sol ------------------------------------------------------------ Numbers do not match: 6 1 Relaxed solutions 6 --- Relaxed solutions 1 ------------------------------------------------------------ FAILED See log files test_relax_no_sol/test_relax_no_sol.log test_relax_no_sol/test_relax_no_sol_current.log I have attempted to attach an archive of the logs. I'm working with Rosetta 3.5, more recent versions of Rosetta fail other tests in phenix_regression.wizards.test_command_line_rosetta_quick , please see https://www.rosettacommons.org/node/3721 for details. Rosetta 3.5 was compiled with GCC 4.4.6 using OpenMPI 1.6.4 Any help or advice is appreciated. -- Sina Masoud-Ansari Centre for eResearch 409.G21 24 Symonds Street University of Auckland e: s.ansari(a)auckland.ac.nz p: +64 9 3737599 ext 89369 w: http://www.eresearch.auckland.ac.nz

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phenix refine geometry restraints
by George Devaniranjan 12 Sep '14

12 Sep '14

Hi, I was trying to restrain the N-CA-C angle to 110.0 I updated the .def file as follows: angle { action = *add atom_selection_1 = name N atom_selection_2 = name CA atom_selection_3 = name C angle_ideal = 110.0 sigma = 2 I got the following: Sorry: More than one atom selected: "name N" Number of selected atoms: 86 I tried using N in quotes and it doesn't work either but the example in the website had this(below), what am I doing wrong? resname ALA and (name ca or name c or name n or name o) Thank you

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refinement for non-standard DNA base
by John Cheong 11 Sep '14

11 Sep '14

Hi, I have 5-fluoro-Uracil in my DNA:protein complex. I modeled 5-F-dU into the map, ran eLBOW for geometry file and did refinement. After the refinement, 5-F-dU is not connected to the neighboring nucleotides and the phosphate oxygens are rotated to wrong positions. Can anyone teach me how to refine with non-standard DNA base ? Any help or advice would be appreciated. John

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Occupancy refinement of anomalous scatters
by Chen Zhao 09 Sep '14

09 Sep '14

Hi all, I have a question about the occupancy refinement of the anomalous scatters. This is because when I went through all the HA sites, I found that some of them has too high B factor and too high occ. I manually adjusted the occ and fed the model into refinement, but the B factor and occ came back to around their original level again. It seems that those have a stronger peak in the anomalous difference Fourier map has a higher occupancy after refinement, but this does not necessarily equals to a strong density peak in 2Fo-Fc map (some of them even disappear after refinement), and this might be related to their high B factor. Am I doing something wrong in the refinement? I am basically using phenix.refine default setting, but with TLS+isotropic B factor refinement and occupancy refinement of a small region (5-8 residues). The resolution is 3 A, and the refinement is already at the final stage. I am still at the learning stage and your input will be greatly appreciated. Thank you! Sincerely, Chen

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Refinement and Density modification
by Ashu S 09 Sep '14

09 Sep '14

Dear all, I am working on a 3.6A Se SAD data. Autosol followed by autobuild gave a decent map (as expected at this resolution) with a moderate trace. After building poly ala trace and assigning few resides in and around Se positions when I refine the model, all the sharp features of the electron density map are lost. For example, a nice looking helical density becomes a tube. I presume that this happens because wilson B is high (~110 A2) and the map requires modification, sharpening etc. Is there a way to get the map with similar sharp features after model building and refinement as auto build gives? How could I follow exactly the same steps of density modification etc which auto build does? Thanks, Ashu

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Refinement and Density Modification
by Ashu S 08 Sep '14

08 Sep '14

Dear all, I am working on a 3.6A Se SAD data. Autosol followed by autobuild gave a decent map (as expected at this resolution) with a moderate trace. After building poly ala trace and assigning few resides in and around Se positions when I refine the model, all the sharp features of the electron density map are lost. For example, a nice looking helical density becomes a tube. I presume that this happens because wilson B is high (~110 A2) and the map requires modification, sharpening etc. Is there a way to get the map with similar sharp features after model building and refinement as auto build gives? How could I follow exactly the same steps of density modification etc which auto build does? Thanks, Ashu

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refine anomalous
by Andreas Förster 08 Sep '14

08 Sep '14

Dear all, I've solved a structure from a SAD dataset collected at 1.54 Å. The structure contains a good number of sulfurs and also what I think is a potassium ion. To verify, I chose a refinement strategy including "Anomalous groups". This worked well in an important way - R values down by 2 percentage points - but the refined f' and f" values are way off. I start out with these parameters in *.eff: anomalous_scatterers { group { selection = (name SD or name SG) f_prime = 0.319342 f_double_prime = 0.557592 refine = *f_prime *f_double_prime } group { selection = name K f_prime = 0.365562 f_double_prime = 1.06736 refine = *f_prime *f_double_prime } } What I get back is: Anomalous scatterer group: Selection: "(name SD or name SG)" Number of selected scatterers: 15 f_prime: -1.15797 f_double_prime: 0.00577091 refine: f_prime f_double_prime Anomalous scatterer group: Selection: "name K" Number of selected scatterers: 1 f_prime: -4.41689 f_double_prime: 0.00271946 refine: f_prime f_double_prime I thought I'd get close to the book values for S and would be able to identify the other anomalous scatterer by the refined f'/f" values. Naiveté or stupidity? Thank you. Andreas -- Andreas Förster Crystallization and X-ray Facility Manager Centre for Structural Biology Imperial College London

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Fwd: Re: Sculptor
by Gabor Bunkoczi 08 Sep '14

08 Sep '14

Apologies, this was meant for the BB. -------- Original Message -------- Subject: Re: [phenixbb] Sculptor Date: 2014-09-08 10:41 From: Gabor Bunkoczi <gb360(a)cam.ac.uk> To: Marie Elizabeth Fraser <frasm(a)ucalgary.ca> Hi Marie, please check the extension of your alignment. If it is .pir, the second line is supposed to be a comment line, and it is therefore ignored. You can either change the extension to .ali, or insert an empty line after the ones starting with ">". If this is not the problem, then this is not supposed to happen. Please send me the logfile in the first instance, although I may need the actual alignment and the PDB file as well (you can delete the target sequence if you wish, an alignment with a single sequence is perfectly valid). BW, Gabor On 2014-09-08 01:22, Marie Elizabeth Fraser wrote: > Hello, > I'm running Sculptor from the Phenix GUI, trying to improve a > molecular replacement model. I've given the pdb file and a sequence > alignment. Sculptor does not appear to accept the first residues > aligned in the sequence alignment. In the alignment, these residues > are residue numbers 42 to 60, so they are on the second line of the > fasta file (the first line after the title) and Sculptor starts at > residue 61 (the subsequent line). Residues 42 to 60 of the target are > to match the first residues of the pdb model, so in the alignment, > there are 41 dashes before the beginning of the sequence for the pdb > file. Am I giving an incorrectly formatted sequence alignment, > misinterpreting what Sculptor does or is Sculptor supposed to do this? > Thank you, Marie > > _______________________________________________ > phenixbb mailing list > phenixbb(a)phenix-online.org > http://phenix-online.org/mailman/listinfo/phenixbb

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Sculptor
by Marie Elizabeth Fraser 08 Sep '14

08 Sep '14

Hello, I'm running Sculptor from the Phenix GUI, trying to improve a molecular replacement model. I've given the pdb file and a sequence alignment. Sculptor does not appear to accept the first residues aligned in the sequence alignment. In the alignment, these residues are residue numbers 42 to 60, so they are on the second line of the fasta file (the first line after the title) and Sculptor starts at residue 61 (the subsequent line). Residues 42 to 60 of the target are to match the first residues of the pdb model, so in the alignment, there are 41 dashes before the beginning of the sequence for the pdb file. Am I giving an incorrectly formatted sequence alignment, misinterpreting what Sculptor does or is Sculptor supposed to do this? Thank you, Marie

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refine structure with mtz file in P212121 or P222?
by Wei Shi 05 Sep '14

05 Sep '14

Hi all, I am working with a protein-ligand complex structure. The data was indexed with XDS and mtz file is generated using Phenix---Reflection tools---Reflection file editor. The space group used was P222. Then, I used the Phenix---Molecular replacement to find a solution (try all possible in same pointgroup), and the MR solution was in space group P212121. And then, I reindexed the data in XDS using space group P212121 and then generate the mtz file in space group P212121. So, I have two mtz file, in space group P212121 and P222. When I refine the MR solution with the different mtz files, the map generated is not same for the ligand. The statisitcs is better with P222 mtz file than P212121 mtz file. I am wondering why the density for the ligand and the statistics is different using mtz file in different space groups and which mtz file should I use to get the final structure model. Thank you so much! Best, Wei

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phenix.refine and R free values
by PC 03 Sep '14

03 Sep '14

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OMIT map
by abhishek jamwal 02 Sep '14

02 Sep '14

Dear phenixbb members, I want to build a SA-OMIT map for a ligand present in xtal structure of a protein. I am using "AutoBuild-create omit map" module of PHENIX ver. 1.8.4-1496 (graphical interface) for this purpose. However, when I run the program after adding requisite input files, it gives an error: " The map file parameter is not supported for omit map calculation" Q: What is this "file parameter" and way to fix this error/parameter ? waiting for answers many thanks in advance Abhishek Jamwal Structural Biology Group ICGEB, New Delhi

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Phasing using CryoEM Map
by Alexander Kintzer 02 Sep '14

02 Sep '14

Hello All, I trying to phase my 4Å data with low resolution cryoEM maps (various 12-18Å). There is some documentation, but not really for dealing with EM data. I am having trouble converting the EM data from mrc to suitable F's for phaser. One would want to try different density contours of the cryoEM map, but I haven't found a good way to accomplish this. I also have been unable to search for Ta6Br12 clusters using Autosol even though the documentation seems to suggest that it is possible using the "TX" or "XX" designation for heavy atom search. Any guidance would be extremely helpful. best, Alex

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Tau angles
by George Devaniranjan 02 Sep '14

02 Sep '14

Hi, Is there a way of extracting the tau (and omega) angles of residues in phenix ? Thank you

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Re: [phenixbb] following on the anomalous map
by Kay Diederichs 29 Aug '14

29 Aug '14

Hi Charles, > Date: Thu, 28 Aug 2014 09:59:30 -0400 > From: CPMAS Chen <cpmasmit(a)gmail.com> > To: Gabor Bunkoczi <gb360(a)cam.ac.uk> > Cc: "PHENIX user mailing list \(phenixbb(a)phenix-online.org\)" > <phenixbb(a)phenix-online.org> > Subject: Re: [phenixbb] following on the anomalous map > Message-ID: > <CAAU4GKbzA37j=51X4jMOJjq3t4rKW7Jz9+CQrPxO-HN1kFOOiQ(a)mail.gmail.com> > Content-Type: text/plain; charset="utf-8" > > HI, Gabor, > > Thanks for you suggestion. > > I tried this method, it did not give out NO sites for Br. > > why there is apparent anomalous signal and I cannot identify any Br sites? are you sure that your data processing used the correct parameters? E.g. in XDS you should definitively be using "FRIEDEL'S_LAW=FALSE". If you use XSCALE after XDS, it automagically picks up this setting from XDS_ASCII.HKL i.e. you don't have to specify this again. If you, by mistake, use FRIEDEL'S_LAW=TRUE, then the large intensity differences of Friedel pairs will be judged as outliers by XDS, and these reflections will be rejected - that might lead to featureless maps. If the anomalous signal is very strong, and the multiplicity is high, and the Chi^2 values are >1.5, you may also want to use (additionally) "STRICT_ABSORPTION_CORRECTION=TRUE" . But this is rarely necessary. There are similar options in other data processing programs. If you mix and match data processing programs (e.g. XDS integration and aimless scaling) you have to be careful to have the right settings in all programs. best, Kay > > As Nat pointed out, other atoms should have very weak anomalous signal > diffracted at Br absorption peak (3.8e- for Br, versus 0.2e- for the > sulfurs). In the difference map, I can clearly see some peaks at high sigma > (> 6), but the anomalous difference map(they are all generated by > phenix.refine or phenix.maps) is almost featureless, or the peaks has > no overlaps. The anomalous difference gives the possible place of Br while > the difference map gives the possible place of the whole ligand, and I > assume there should be some overlaps between them. Am I right? > > Charles >

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Re: [phenixbb] following on the anomalous map
by CPMAS Chen 29 Aug '14

29 Aug '14

HI, Gabor, Thanks for you suggestion. I tried this method, it did not give out NO sites for Br. why there is apparent anomalous signal and I cannot identify any Br sites? As Nat pointed out, other atoms should have very weak anomalous signal diffracted at Br absorption peak (3.8e- for Br, versus 0.2e- for the sulfurs). In the difference map, I can clearly see some peaks at high sigma (> 6), but the anomalous difference map(they are all generated by phenix.refine or phenix.maps) is almost featureless, or the peaks has no overlaps. The anomalous difference gives the possible place of Br while the difference map gives the possible place of the whole ligand, and I assume there should be some overlaps between them. Am I right? Charles On Wed, Aug 27, 2014 at 6:28 AM, Gabor Bunkoczi <gb360(a)cam.ac.uk> wrote: > Hi Charles, > > I could be totally misunderstanding what you are trying to achieve, but I > think what you need to do is an MR-SAD calculation. First, solve the > structure with MR (use the macromolecule from the non-Br structure, or use > your current model if you have done refinement on it), and use the > Phaser-EP GUI, and select "SAD starting from MR model". This should > highlight any Br you may have, and gives you a PDB-file with all the peaks > (you can also get a proper anomalous map, but this is only useful for > visualization - the peak search will identify any peaks you may have). > > Let me know if you need more details! > > BW, Gabor > > > On 2014-08-26 14:49, CPMAS Chen wrote: > >> Thanks. Nat. >> >> Since I have some MET and CYT in the protein, could I try to supply >> their sulfur as the initial anomalous scatters? >> >> As for the anomalous isomorphous difference map, would it be useful I >> compare the datasets acquired at 1A wavelength and at the Br >> absorption peak (~0.92A)? >> >> Appreciate your help >> >> Charles >> >> On Mon, Aug 25, 2014 at 5:08 PM, Nathaniel Echols <nechols(a)lbl.gov> >> wrote: >> >> On Sun, Aug 24, 2014 at 6:46 AM, CPMAS Chen <cpmasmit(a)gmail.com> >>> wrote: >>> >>> Here is the point I am not clear. If I am using phenix.refine to >>>> generate LLG map, how do I pick the anomalous group since I have >>>> not placed them in the model yet? >>>> >>> >>> You can't. The LLG map only becomes really useful once you have >>> some anomalous scatterers placed and refined - this is how Phaser >>> substructure completion works. If your molecules have no other >>> significant anomalous scatterers other than the expected Br, the LLG >>> map won't do you much good. >>> >>> By the way, when I choose ion_placement and specify Br, the result >>>> comes with no Br. >>>> >>> >>> Not too surprising, since the code is tuned to look for ions, not >>> part of a covalent molecule, and halides also tend to bond >>> non-specifically and we haven't figured out how to deal with that >>> yet. >>> >>> I want to find whether the Br-containing ligand is seen in my >>>> protein which I have a high resolution structure available. >>>> >>>> I have data collected at Br wavelength, peak or higher position. >>>> Phenix.xtriage reported that the anomalous signal is present to >>>> about 4A. However, both AutoSol or MR-SAD cannot identify the Br >>>> position. Simply say, AutoSol or MR-SAD can not generate any >>>> solution. Well, of course, the simple answer would be that there >>>> is no such ligand cocrystallized. >>>> >>> >>> The simplest explanation is that you just don't have enough >>> anomalous signal to determine the substructure, which can be true >>> even if your ligand is bound. Running experimental phasing to >>> figure this out is unnecessary and time-consuming. >>> >>> Anyway, I am trying to see if the anomalous difference map or >>>> LLG(generated by phenix.maps, this would be the initial one I >>>> assume) can tell me anything more useful. >>>> >>>> So, my question on this topic would be what is a better way you >>>> guys would recommend to identify these Br-ligands? By the way, I >>>> did have the native datasets for the same protein with ligand. >>>> >>> >>> I think in this case I would start with the simple anomalous >>> difference map. If you run phenix.find_peaks_holes (it's in the >>> GUI, of course) and give anomalous data as input, it can pick out >>> the highest peaks in the anomalous map. If the ligand really is >>> bound and the Br site is ordered I would expect this to be >>> detectable. Another alternative is to compute an anomalous >>> isomorphous difference map between a dataset collected at or above >>> (in eV) the Br peak, and a dataset collected below the peak. This >>> will allow you to visualize the wavelength-dependent difference in >>> anomalous scattering, and it's going to be specific for elements >>> with absorption edges within that energy range. But I really don't >>> think this should be necessary to answer your question. >>> >>> -Nat >>> >> >> -- >> >> *************************************************** >> >> Charles Chen >> >> Research Associate >> >> University of Pittsburgh School of Medicine >> >> Department of Anesthesiology >> >> ****************************************************** >> >> >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://phenix-online.org/mailman/listinfo/phenixbb >> > > -- > ################################################## > > Dr Gabor Bunkoczi > > Cambridge Institute for Medical Research > Wellcome Trust/MRC Building > Addenbrooke's Hospital > Hills Road > Cambridge CB2 0XY > ################################################## > -- *************************************************** Charles Chen Research Associate University of Pittsburgh School of Medicine Department of Anesthesiology ******************************************************

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How to tighten ligand geometry in phenix.refine?
by Blankenfeldt, Wulf 28 Aug '14

28 Aug '14

Dear all, I am currently trying to refine a cacodylate ion that partially occupies the phosphate binding site of a PLP cofactor – partially meaning ~90%, in fact I am leaving the PLP out altogether. When I am refining this in phenix. refine, the cacodylate becomes “ugly”: the tetraeder gets slightly squashed and the atoms are flying apart a bit such that they are not automatically connected in Coot any more. I am now wondering if I can tighten the geometry just for the cacodylate to prevent this from happening, either by sending a magical command or by fiddling with the dictionary. Can anyone advise me, please? Regards, Wulf ________________________________ Helmholtz-Zentrum für Infektionsforschung GmbH | Inhoffenstraße 7 | 38124 Braunschweig | www.helmholtz-hzi.de Das HZI ist seit 2007 zertifiziertes Mitglied im "audit berufundfamilie" Vorsitzende des Aufsichtsrates: MinDir’in Bärbel Brumme-Bothe, Bundesministerium für Bildung und Forschung Stellvertreter: MinDirig Rüdiger Eichel, Niedersächsisches Ministerium für Wissenschaft und Kultur Geschäftsführung: Prof. Dr. Dirk Heinz; Franziska Broer Gesellschaft mit beschränkter Haftung (GmbH) Sitz der Gesellschaft: Braunschweig Handelsregister: Amtsgericht Braunschweig, HRB 477

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