- phenixbb - phenix-online.org

Re: [phenixbb] Simple Phaser Question (Ed Pozharski
by Joseph Noel 27 Dec '10

27 Dec '10

Hi Ed, Yes, that is what I generally do but it sometimes is a slightly different so I wanted a more general approach. 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 ___________________________________________________________ On Dec 25, 2010, at 12:00 PM, phenixbb-request(a)phenix-online.org wrote: > Send phenixbb mailing list submissions to > phenixbb(a)phenix-online.org > > To subscribe or unsubscribe via the World Wide Web, visit > http://phenix-online.org/mailman/listinfo/phenixbb > or, via email, send a message with subject or body 'help' to > phenixbb-request(a)phenix-online.org > > You can reach the person managing the list at > phenixbb-owner(a)phenix-online.org > > When replying, please edit your Subject line so it is more specific > than "Re: Contents of phenixbb digest..." > > > Today's Topics: > > 1. Simple Phaser Question (Joseph Noel) > 2. Re: Simple Phaser Question (Ed Pozharski) > 3. Questions about phenix.refine with twin_law (Keitaro Yamashita) > 4. Re: Questions about phenix.refine with twin_law (Peter Zwart) > 5. Re: Questions about phenix.refine with twin_law (Pavel Afonine) > > > ---------------------------------------------------------------------- > > Message: 1 > Date: Fri, 24 Dec 2010 17:11:37 -0800 > From: Joseph Noel <noel(a)salk.edu> > To: phenixbb(a)phenix-online.org > Subject: [phenixbb] Simple Phaser Question > Message-ID: <5E3B81ED-4C13-488E-8C28-33DB29263AEF(a)salk.edu> > Content-Type: text/plain; charset="us-ascii" > > Hi All, > > I am working with a protein that is a physiological dimer. On occasion I obtain a unit cell with one monomer in the asymmetric unit but most often I obtain an enantiomorphic space group with an expanded C axis that contains two molecules in the asymmetric unit. Anyway, that is all moot to some extent. I am wondering if for the case of my NCS dimer, is there a way using Phaser in Phenix to ensure that when both monomers are found, they are "close together" representative of the physiological dimer? When I search with individual monomers I often obtain a solution with two monomers but in different asymmetric units. Of course, I could easily do the transformation to form the physiological NCS dimer for later refinement but just wondering if I could avoid this from the get go with the appropriate Phaser keyword input (GUI if possible). > > Thanks and Happy Holidays! > > 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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Simple Phaser Question
by Joseph Noel 25 Dec '10

25 Dec '10

Hi All, I am working with a protein that is a physiological dimer. On occasion I obtain a unit cell with one monomer in the asymmetric unit but most often I obtain an enantiomorphic space group with an expanded C axis that contains two molecules in the asymmetric unit. Anyway, that is all moot to some extent. I am wondering if for the case of my NCS dimer, is there a way using Phaser in Phenix to ensure that when both monomers are found, they are "close together" representative of the physiological dimer? When I search with individual monomers I often obtain a solution with two monomers but in different asymmetric units. Of course, I could easily do the transformation to form the physiological NCS dimer for later refinement but just wondering if I could avoid this from the get go with the appropriate Phaser keyword input (GUI if possible). Thanks and Happy Holidays! 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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Non-standard residue numbers in NCS restraints
by Sampson, Jared 23 Dec '10

23 Dec '10

Greetings all, My lab is working on a 3.2Å resolution structure with 6 NCS copies of an antibody Fab fragment with insertions in its CDR loops. The residue numbers of CDR loop H3, for example, include 100A, 100B, etc. in each of the heavy chains (Kabat numbering). There are observable differences between NCS copies in parts of the model due to crystal contacts and so forth, so we want to exclude those residues from the NCS. Phenix.refine, when given NCS restraints like the example below, produces a result with much higher R/Rfree values than when the same structure was run with "normal" continuous numbering (R/Rfree of .26/.30 compared to .21/.26 before changing to Kabat numbering). Reference selection: chain H and (resseq 1:100A or resseq 100H:113) Restrained selection: chain I and (resseq 1:100A or resseq 100H:113) Phenix version is 1.6.4-486. Any thoughts on what might be causing this or how to account for the non-standard numbers in NCS restraints? Thanks, Jared Sampson -- Jared Sampson Xiangpeng Kong Lab NYU Langone Medical Center New York, NY 10016 212-263-7898 ------------------------------------------------------------ This email message, including any attachments, is for the sole use of the intended recipient(s) and may contain information that is proprietary, confidential, and exempt from disclosure under applicable law. Any unauthorized review, use, disclosure, or distribution is prohibited. If you have received this email in error please notify the sender by return email and delete the original message. Please note, the recipient should check this email and any attachments for the presence of viruses. The organization accepts no liability for any damage caused by any virus transmitted by this email. =================================

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Problem with Molprobity analysis in phenix 1.6.4
by Mark A Saper 23 Dec '10

23 Dec '10

I am running phenix 1.6.4-486 with GUI and obtained high clash scores in the Molprobity calculations done by phenix.refine. I think I know why after doing some experiments with the current Molprobity running at http://molprobity.biochem.duke.edu/. If I take my well-refined structure as output by phenix (.pdb) and use it directly on the Molprobity web site, the clash score is much lower: 2.75 for 39 total bumps. Many of these involve residues or waters with high B factors. If I first remove all hydrogens from the phenix-refined .pdb file with a text editor, and upload it to the Molprobity web site, then add hydrogens, and then calculate clash score, the score is now 8.69 or 123 bumps for 14150 atoms. This is *identical* to what phenix calculates. Therefore, why doesn't phenix feed the refined coordinates directly into the Molprobity (probe) calculations? Has this change been made in one of the nightly builds? Thanks, Mark Mark A. Saper, Ph.D. Associate Professor of Biological Chemistry University of Michigan Biophysics, 3040 Chemistry Building 930 N University Ave Ann Arbor MI 48109-1055 U.S.A. saper(a)umich.edu phone (734) 764-3353 fax (734) 764-3323 http://www.biochem.med.umich.edu/?q=saper http://www.strucbio.umich.edu/

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Fwd: Fourth annual CCP4 summer school in USA, at APS, June 7-15
by Nathaniel Echols 22 Dec '10

22 Dec '10

---------- Forwarded message ---------- From: "Sanishvili, Ruslan" <rsanishvili(a)anl.gov> To: <phenixbb(a)phenix-online.org> Date: Wed, 22 Dec 2010 11:02:15 -0600 Subject: Fourth annual CCP4 summer school in USA, at APS, June 7-15 Dear Colleagues, Building on the success of the past 3 years, we are pleased to announce the fourth annual CCP4 summer school at Advanced Photon Source (APS), Argonne National Laboratory (ANL). All details can be found at http://www.ccp4.ac.uk/schools/APS-2011/index.php Title: "CCP4 school: From data collection to structure refinement and beyond" Dates: June 7 to 15. Site: Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois (Near Chicago), USA The school content: Data collection workshop the first two days: beamline training and data collection on GM/CA-CAT beamlines 23ID-B and 23ID-D. For data collection, only the participants' crystals will be used. Software workshop: The rest of the time after data collection will feature many modern crystallographic software packages taught by authors and other experts. It will be organized in three Sections – lectures, tutorials and hands-on trouble-shooting. There will be model data sets available for tutorials but data, provided by participants, will have higher priority for the hands-on sessions. Applicants: Graduate students, postdoctoral researchers and young scientists at the assistant professor level are encouraged to apply. Only 20 applicants will be selected for participation. Participants of the workshop are strongly encouraged to bring their own problem data sets or crystals so the problems can be addressed during data collection workshop and/or hands-on sessions. Application: Application deadline is April 8. Application form, the program, contact info and other details can be found at http://www.ccp4.ac.uk/schools/APS-2011/index.php Fees: There is no fee for the workshop. The students will be responsible for their transportation and lodging. The workshop organizers will arrange economical lodging at the Argonne Guest House. The workshop will also cover the expenses for all meals and refreshments. Garib, Ronan and Nukri Ruslan Sanishvili (Nukri), Ph.D. GM/CA-CAT Biosciences Division, ANL 9700 S. Cass Ave. Argonne, IL 60439 Tel: (630)252-0665 Fax: (630)252-0667 rsanishvili(a)anl.gov

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ADP restraints - distance power, average power, etc
by Joseph Noel 21 Dec '10

21 Dec '10

Hi All, I am refining a very well ordered structure at 1.45 A and find that after doing just about everything including optimization of weights, etc that there are still areas of positive density residing over S atoms of Met, backbone atoms, etc. I have added hydrogens and used them during refinement as well. The maps are of a high quality and Free R factors are quite good, ~ 17%. Is there anything that can be played with more such as values used in the ADP restraints window to try and achieve a difference map with far fewer areas of significant positive density (all greater then or equal to 4 sigma)? I am not sure exactly what effect the values of distance power, average power, etc will have on refinement. The other option I was thinking of was the scattering table options. I have other structures of this protein that extend to about 1.2. 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 ___________________________________________________________

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Re: [phenixbb] ADP restraints - distance power, average power, etc
by Joseph Noel 20 Dec '10

20 Dec '10

Dear Ed, Thanks so much for the suggestion about REFMAC but I seemed to have found out the issue. The positive density on Met sulfurs and backbone carbonyls and amide NHs does not appear when I calculate a "normal" sigmaa weighted mFo-dFc map. The positive density was appearing only when I checked the kicked map option. So the "extra" density seems to be due to generating kicked maps. Sorry about the confusion related to the sigma level. Just meant that the positive density was not insignificant in the kicked mFo-dFc maps. Density was visible on these specific areas starting around 3.5-4.0 sigma and visible in several places contoured up to 8 sigma. 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 ___________________________________________________________ On Dec 20, 2010, at 12:00 PM, phenixbb-request(a)phenix-online.org wrote: > Send phenixbb mailing list submissions to > phenixbb(a)phenix-online.org > > To subscribe or unsubscribe via the World Wide Web, visit > http://phenix-online.org/mailman/listinfo/phenixbb > or, via email, send a message with subject or body 'help' to > phenixbb-request(a)phenix-online.org > > You can reach the person managing the list at > phenixbb-owner(a)phenix-online.org > > When replying, please edit your Subject line so it is more specific > than "Re: Contents of phenixbb digest..." > > > Today's Topics: > > 1. ADP restraints - distance power, average power, etc (Joseph Noel) > 2. Re: ADP restraints - distance power, average power, etc > (Ralf W. Grosse-Kunstleve) > 3. Re: ADP restraints - distance power, average power, etc > (Pavel Afonine) > 4. Secondary structure restraints - where to specify file using > GUI? (Luke Rice) > 5. Re: Secondary structure restraints - where to specify file > using GUI? (Nathaniel Echols) > 6. Re: ADP restraints - distance power, average power, etc > (Joseph Noel) > 7. Re: ADP restraints - distance power, average power, etc > (Joseph Noel) > 8. Re: ADP restraints - distance power, average power, etc > (Ed Pozharski) > 9. Re: Secondary structure restraints - where to specify file > using GUI? (Luke Rice) > > > ---------------------------------------------------------------------- > > Message: 1 > Date: Sun, 19 Dec 2010 12:58:43 -0800 > From: Joseph Noel <noel(a)salk.edu> > To: phenixbb(a)phenix-online.org > Subject: [phenixbb] ADP restraints - distance power, average power, > etc > Message-ID: <2E132727-1B34-4ED5-98DA-2210B7D1FF48(a)salk.edu> > Content-Type: text/plain; charset="us-ascii" > > Hi All, > > I am refining a very well ordered structure at 1.45 A and find that after doing just about everything including optimization of weights, etc that there are still areas of positive density residing over S atoms of Met, backbone atoms, etc. I have added hydrogens and used them during refinement as well. The maps are of a high quality and Free R factors are quite good, ~ 17%. Is there anything that can be played with more such as values used in the ADP restraints window to try and achieve a difference map with far fewer areas of significant positive density (all greater then or equal to 4 sigma)? > > I am not sure exactly what effect the values of distance power, average power, etc will have on refinement. The other option I was thinking of was the scattering table options. I have other structures of this protein that extend to about 1.2. > > 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 > ___________________________________________________________ > >

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phenix.refine with simulated annealing
by zhangh1＠umbc.edu 18 Dec '10

18 Dec '10

Hi there, I was trying to perform a SA refinement for PDB# 2VZ8 using the following phenix script: random_seed=2679941 phenix.refine 2VZ8.pdb 2vz8.mtz simulated_annealing=true main.random_seed=${random_seed} output.prefix=${random_seed} >${PDB}-phx-sa.log where 2VZ8.pdb was downloaded from rcsb, and 2vz8.mtz was converted from the cif file by ccp4-cif2mtz. But it ended up with: ******************* =============================== refinement start ============================== Traceback (most recent call last): File "/users/hz9/TOOLS/PHENIX/phenix-1.6.4-486/phenix/phenix/command_line/refine.py", line 11, in <module> command_line.run(command_name="phenix.refine", args=sys.argv[1:]) File "/users/hz9/TOOLS/PHENIX/phenix-1.6.4-486/phenix/phenix/refinement/command_line.py", line 89, in run call_back_handler=call_back_handler) File "/users/hz9/TOOLS/PHENIX/phenix-1.6.4-486/phenix/phenix/refinement/driver.py", line 1182, in run call_back_handler = call_back_handler) File "/users/hz9/TOOLS/PHENIX/phenix-1.6.4-486/phenix/phenix/refinement/strategies.py", line 229, in refinement_machine xray_structure = model.xray_structure,) File "/users/hz9/TOOLS/PHENIX/phenix-1.6.4-486/phenix/phenix/refinement/strategies.py", line 133, in extract_from_pdb_header xray_structure = xray_structure) File "/users/hz9/TOOLS/PHENIX/phenix-1.6.4-486/cctbx_project/mmtbx/f_model.py", line 302, in __init__ twin_law_xyz = sgtbx.rt_mx(symbol=self.twin_law, r_den=12, t_den=144) RuntimeError: cctbx Error: Parse error: unexpected character: NULL ************************ I tried another smaller system and it works well. Not sure what happens, and thanks for any suggestion! Hailiang

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phenix.map_to_object for HA sites
by Michael Hothorn 17 Dec '10

17 Dec '10

Hi, I have a .pdb with heavy atoms that are dispersed all over the unit cell. I would like to move all of them (about 40) as close as possible to my refined structure. Could phenix.map_to_object do that for all heavy atoms at once, or would I need to do this in an atom by atom manner? Thanks Michael

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Map filenames are not honored [dev-610]
by Schubert, Carsten [PRDUS] 16 Dec '10

16 Dec '10

Hi, I just noticed that v610 does not honor map file names defined in the .def file. Instead it constructs its own file name from the prefix, serial and map_type settings. That works fine for run-of-the-mill fofc and 2fofc maps, but causes a clash in map filenames when one also computes kicked maps or other maps with non-default settings beside the default fofc and 2fofc maps. Cheers, Carsten

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phenix.find_tls_groups: a new tool for automated partitioning a model into TLS groups
by Joseph Noel 16 Dec '10

16 Dec '10

Pavel or Nat, Can you point me to the button in the GUI to use to run this? I am pretty much a GUI guy although not adverse to running things through the command like like the old days (yes, I was a command like geek when I started at Yale in 1990 and until I stopped (temporarily) doing anything worthwhile around 2001. Now that I am back in the lab doing work (but probably still not worthwhile) I have become addicted to GUIs and buttons. Blame my daughters! LOL 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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phenix.find_tls_groups: a new tool for automated partitioning a model into TLS groups
by Pavel Afonine 15 Dec '10

15 Dec '10

PHENIX users: starting dev-610 (development version of PHENIX) there is a new tool available for completely automated partitioning a model into TLS groups: http://www.phenix-online.org/download/nightly_builds.cgi To run: phenix.find_tls_groups model.pdb or if you have a multiple CPU machine: phenix.find_tls_groups model.pdb nproc=N where N is the number of CPUs available (thanks Nat for parallelization!). There is no parameters that a user is supposed to tweak (except defining the number of CPUs, if desired). The result of running the above command are atom selections that define TLS groups. These atom selections are ready to use in phenix.refine. This is available from PHENIX GUI too, where automatically defined TLS groups can be readily visualized and checked on the graphics (thanks Nat!). The algorithm is fast. For example, for a GroEL structure (3668 residues, 26957 atoms, 7 chains) it takes only 135 seconds using 1 CPU, and 44 seconds using 10 CPUs. Analogous job takes 3630 seconds using TLSMD server. For a lysozime structure it takes 9.5 seconds with one CPU, and 2.5 seconds using 10 CPUs. The timing results may vary depending on the performance of your computer. There is ongoing work that will slightly improve phenix.find_tls_groups within the next few weeks / a month; however the current version is functional and can be tried now. An example of such improvements are analyzing (scoring) user-defined TLS groups (for example, TLS groups from PDB file header), automated combining cross-chain TLS groups (non-contiguous segments) that will be obtained through connectivity analysis, better handling non-protein chains, and more. Integration with phenix.refine is also planned. Any feedback is very much appreciated! Thanks, Pavel.

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request for openmp compile comments
by Bryan Lepore 14 Dec '10

14 Dec '10

if anyone has specifically gotten automr to run on an openmp-compiled phenix installation with something like the specs i give below, i would appreciate any details you could offer. (in my hands, automr always crashes, refine works.) -Bryan any recent nightly release with --openmp gcc/g++ 4.4.5 (or thereabouts) 2.6.35-23-generic SMP i686 (or thereabouts) amd, intel, (or thereabouts) Ubuntu (recent - but not Fedora)

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phenix.refine use_experimental_phases vs target=mlhl
by Francis E Reyes 14 Dec '10

14 Dec '10

Are these settings redundant? i.e. what happens when you have target=mlhl, use_experimental_phases=False? Thanks! F --------------------------------------------- Francis E. Reyes M.Sc. 215 UCB University of Colorado at Boulder gpg --keyserver pgp.mit.edu --recv-keys 67BA8D5D 8AE2 F2F4 90F7 9640 28BC 686F 78FD 6669 67BA 8D5D

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AutoSol/PhaserSAD with more than one anomalously-scattering atom produces error...
by Francis E Reyes 13 Dec '10

13 Dec '10

Hi all I'm getting an error... "'InputEP_SAD' object has no attribute 'addSCAT_TYPE'" from autosol. Facts: - phenix-1.6-289 - SAD experiment with two types of anomalous scatterers in the xtal, data is the peak wavelength of one of the anomalous scatterers. - sites are input from a previous phaser run (ha_x.pdb_formatted.pdb) - the atom positions are likely correct, but the atom types are all the same atom (I'd like phenix/phaser to go through the list and reannotate/refine based on the proper heavy atom identities) - additional atom types/f'/f'' defined in autosol.eff, Using the documentation example "SAD with more than one anomalously-scattering atom" (http://www.phenix-online.org/documentation/autosol.htm). Thanks! F --------------------------------------------- Francis E. Reyes M.Sc. 215 UCB University of Colorado at Boulder gpg --keyserver pgp.mit.edu --recv-keys 67BA8D5D 8AE2 F2F4 90F7 9640 28BC 686F 78FD 6669 67BA 8D5D

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changing test set flag
by Michael Hothorn 11 Dec '10

11 Dec '10

Dear all, I used phenix.refine to generate the test set flag for my dataset which it did with a value of 1. I now use a program that expects the test set flag in the mtz file to be 0. Is there a simple way to change the flag from 1 to 0 keeping the flagged reflections identical? Thanks! Michael

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Help needs: SAD-phasing for Cobalt ion
by YoungJin 10 Dec '10

10 Dec '10

Dear helpers in phenix, I have anomalous data (Co; wavelength: 1.609A) that I want to use its Phase information from SAD-phasing method (autosol). As I have a native data (from nomal wavelength ~1A) with higher resolution (~2A) than SAD data (~2.5A), I wanted to apply phase information to this native data for further refinement: My goals were 1. I want to confirm where is my heavy metal is; 2. I want to refine further using native data as has higher resolution. At first, when I did autosol, it didn't give me perfect result. So far what I tired is as following: 'SAD peak' from imosflm generated mtz file (scaled), 'Phases' from first refmac generated mtz file from the native data, and 'MIR native' from the native data mtz file (imosflm and scaled). FOM: 0.186; overall score was 10.75 +/- 12.33. FYI. I input 2 sites and result suggested 3 sites. Each molecule has one binding site of metal ion. I was using old Mac version:1.6.4-486 Anyway, I simply passed the result over Autobuild. It ran and gave me better statistics as following: R/Rfree=0.2734/0.3312; CC 0.76. However (I have two molecules/ASU) one of models was not great. But this time, anomalous density map well phased(?!) to 2Fo-Fc map and I could see - it was before only one heavy metal I clearly could see- 2 heavy metal signal from 2 molecules and those positions are well matched with native density maps. So I continued phenix.refine using Autobuild made 'expt_fobs_phase_freeR_flags_1.mtz'. The question is the statistics from anomalous data itself (it has slight dispcrepancy between anomalous map and 2Fo-Fc/Fo-Fc map due to phase problem) or even those from native data is better than my current model which came from native data set (SAD-phased as described above) with higher resolution. I think one of main reasons is one of molecule has a lid that does not perfectly fit into current density map. However, in terms of heavy metal position and the active site is better from current map (Autobuild generated model). FYI: current model has R/Rfree=0.21/0.27(best was 0.21/0.26); 0.19/0.24 (for native data only used model) .... Am I too concerning for statistics or is there something I am missing? Now my questions are as following plus any suggestions are welcome: 1. For SAD-phasing, could you tell me which is best way to do so with my case (one data from the edge of heavy metal (lower resolution) and native data (higher resolution) or where is the point I can convince. Also I tried to use DANO/SIGDANO column (from hkl2000 and ccp4) but seems like it (Autosol) doesn't take them into account. Could you tell me how can I improve phase by using anomalous data? 2. In case of Co, does anyone have experience about coordination numbers? I thought it should have 6 (or 4) coordination numbers. The question what I have now is about the numbers and their lengths ... I though it should be within 2A, but not true for my current models (And somehow distorted octahedron or else with 2.07-3.28A). I also searched PDB files, and found that many deviations from 1.98 to 2.82A (depending on corresponding atoms and resolutions: 3KOI, 3KON, 2DD5, and 2XJM). I would appreciate if you can give me any tips regarding this issue. Many thanks in advance, Young-Jin

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phenix.phaser ep_sad mode
by Bryan Lepore 09 Dec '10

09 Dec '10

dev-601 i found an ep_sad script on the phaser wiki^[1] that works ok^[2] for old versions. for the dev-601 phaser, i think it comes down to me not understanding this line : LLGComplete CRYStal insulin COMPLETE ON SCATtering ELEMent S i tried jumbling the commands/arguments around^[3], leading to syntax errors for each attempt (output excerpt below). if this "should work", i'll gladly return to the manual - or is there something unusual between versions, am i missing something, etc.... -Bryan [1]http://www.phaser.cimr.cam.ac.uk/index.php/Experimental_Phasing#Combined_MR_and_SAD_Phasing [2] seem not to write ATOM records in the .pdb when sites are in fact found. [3]http://www.phaser.cimr.cam.ac.uk/index.php/Keywords#LLGCOMPLETE output excerpt : MODE EP_SAD TITLe sad phasing insulin with best AutoMR solution HKLIn truncate.mtz CRYStal insulin DATAset sad LABIn F+=F(+) SIG+=SIGF(+) F-=F(-) SIG-=SIGF(-) ! LLGComplete CRYStal insulin COMPLETE ON SCATtering ELEMent S LLGComplete CRYStal  <B><FONT COLOR="#FF8800"> $TEXT:Warning: $$ Baubles Markup $$ ------------------------------------------------------------------------------------- SYNTAX ERROR: Use (optionally) COMPLETE TYPE SCATTERER ELEMENT CLUSTER SIGMA NCYC CLASH ANOM REAL MAPS or METHOD -------------------------------------------------------------------------------------

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phaser ep_sad zscore
by Bryan Lepore 09 Dec '10

09 Dec '10

dev-601 in phaser ep_sad mode, i tried ZSCORE SOLVED 0 to get more sites output, and i can see a peak of about Z=4 in the stdout, but no peaks are written to the .pdb am i applying ZSCORE wrong here? -Bryan

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reflection outliers detection in phenix.refine
by guanrj＠foxmail.com 08 Dec '10

08 Dec '10

Hi All I have a question regarding reflection outliers detection in phenix.refine: in my input reflection file, there are 24432 reflections, but only 22769 of them were used in refinement. I checked the log file and saw 1663 outliers. (below if from the log) basic_wilson_outliers = 14 extreme_wilson_outliers = 18 beamstop_shadow_outliers = 0 model_based_outliers = 1657 total = 1663 What is the "model_based_outliers"? What causes so many reflections rejected and not used in the refinement? Thanks Rongjin

3 3

Multistart simulated annealing refinement
by Joseph Noel 08 Dec '10

08 Dec '10

Hi All, I'm sure this has already been addressed but is there a way through the PHENIX GUI to carry out multistart simulated annealing refinement either with different starting seeds (velocities) or temperatures automatically or does one have to start a fresh run each time? Thanks! Joe P.S. Similar procedure as described in the PNAS paper: "Multistart simulated annealing refinement of the crystal structure of the 70S ribosome" ___________________________________________________________ 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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phenix.fmodel or other utility: calculate HL's as well?
by Francis E Reyes 08 Dec '10

08 Dec '10

I love the phenix cmd line utilities, however is there one that'll calculate HLA/HLB/HLC/HLD given FModel/Phimodel? My expectation is that phenix.fmodel would do this with an option toggle or something. F --------------------------------------------- Francis E. Reyes M.Sc. 215 UCB University of Colorado at Boulder gpg --keyserver pgp.mit.edu --recv-keys 67BA8D5D 8AE2 F2F4 90F7 9640 28BC 686F 78FD 6669 67BA 8D5D

2 1

No clash evaluation between symmetry mates in phenix.refine
by Keitaro Yamashita 08 Dec '10

08 Dec '10

Dear Phenix developers, I have a question about phenix.refine. I'm refining complex structure against X-ray diffraction data with packing disorder. (Some domains overlap with their symmetry mates (4-fold), so their occupancies are set to 0.25) So I want phenix.refine to ignore clashes between symmetry mates. Can phenix.refine exclude any interaction between symmetry mates from geometric term in target function: E = E(x-ray) + E(geometry)? Is there any option? Thank you very much in advance, K. Yamashita

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switch off anti-bump restrain
by Agnieszka 08 Dec '10

08 Dec '10

Hi, I have double conformation of my residue. There is a water molecule that interacts with conformation A. In the same time the water is very close to conformation B. During the refinement the water is pushed out. I try to switch off the site refinement of the water and some atoms of conformation b but it didn't work out for me. Do you know how can I switch off the anti-bump restrain of this two guys? Thank you Agnieszka Kiliszek

2 1

ncs restraints
by Timothy Springer 08 Dec '10

08 Dec '10

Hi, I am using NCS restraints for 4 copies of a molecule at 3.05 Å. We are using the standard weights: coordinate_sigma = 0.05 b_factor_weight = 10 and the 4 molecules look identical. What are suggested values for looser restraints? One of my colleagues said that varying them did not make a difference- ncs was still very strict. Is there a way to make them less strict? Thanks, Timothy A. Springer, Ph.D.

4 4

phaser version
by Bryan Lepore 08 Dec '10

08 Dec '10

using dev-596 from source, i see `phenix.phaser --version` is Phaser-2.2.4 (svn ) that's true for dev-601 (Intel binary) also. the phaser wiki says 2.3 is the latest, and to compile it from the phenix distribution. so... wondering how to get phaser 2.3 (before asking questions about ep_sad...) -Bryan

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anyone with a scalepack file with R3 or R32 using rhombohedral axes?
by Ralf W. Grosse-Kunstleve 08 Dec '10

08 Dec '10

I'm looking for a little help from the phenix user community. Does anyone have a scalepack output file with data in space group R3 or R32 using rhombohedral axes, i.e. unit cell parameters a=b=c, alpha=beta=gamma? What is the space group symbol in the file? I'm only interested to know this for files that are the direct output of scalepack. I'd like to verify that this part of the scalepack documentation is actually true: http://www.hkl-xray.com/hkl_web1/hkl/manual_online.pdf Page 139: 146 R3 R3 in hexagonal setting 446 H3 R3 in primitive setting 155 R32 R32 in hexagonal setting 455 H32 R32 in primitive setting If this is actually true, it is the exact opposite of what's used by the PDB. Thanks in advance for feedback. Ralf

2 1

modelling of a novel protein
by intekhab alam 08 Dec '10

08 Dec '10

Hi I am trying to solve the structure of RNA polymerase in complex with its protein primer. The size of protein primer is 70 amino acids which i complexed with the polymerase and collected a data of the complex crysta at 2.3A. The space group is C2 and after Molecular replacemnet with full length polymerase in auto MR i got 3 subunits in ASU. The parameters of MR solution RFZ=71.5 TFZ=41.2 PAK=0 LLG=8812 suggests that the solution is correct. I used autobuild for model building which gave me the model of the polymerase as well as some extra density that i am considering as the other protein. After several round of refinemnt i have R and R free of 27and 32 respectively. My queries: 1. I want to know ,how can i improve my R as well as R free. 2. How can i model other protein as the density is weak and not complete, how can i improve the map of the other protein so that i can b ebale to trace the c-alpha backbone, i was able to model only 10 amino acids so far. Please guide. Regards -- INTEKHAB ALAM LABORATORY OF STRUCTURAL BIOINFORMATICS KOREA UNIVERSITY, SEOUL

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distorted (collapsed) zinc-finger motifs
by Hasan Demirci 07 Dec '10

07 Dec '10

Hi, I am in the middle of refining a 3.5 A (low resolution) ribonucleo-protein complex structure. Two of the proteins in this complex contain "zinc-finger" motif. These zinc-finger motifs instead of forming a cysteine-zinc interactions, cysteines are forming di or in these case tetra-sulfide bridges. Initially, zinc is centered but after refinement 4 cysteines come out collapsed and forming covalent bonds to each other and also distorted and zinc is not at the center anymore. Below is the phenix.refine zn_link.param file I am using. Many thanks for advice, Hasan Demirci ---------------------------------------------------------------------------- refinement.pdb_interpretation { disulfide_distance_cutoff = 0.1 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain D and resname ZN and resid 306 residue_selection_2 = chain D and resname CYS and resid 9 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain D and resname ZN and resid 306 residue_selection_2 = chain D and resname CYS and resid 12 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain D and resname ZN and resid 306 residue_selection_2 = chain D and resname CYS and resid 26 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain D and resname ZN and resid 306 residue_selection_2 = chain D and resname CYS and resid 31 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain N and resname ZN and resid 307 residue_selection_2 = chain N and resname CYS and resid 24 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain N and resname ZN and resid 307 residue_selection_2 = chain N and resname CYS and resid 27 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain N and resname ZN and resid 307 residue_selection_2 = chain N and resname CYS and resid 40 } refinement.pdb_interpretation.apply_cif_link { data_link = ZN-CYS residue_selection_1 = chain N and resname ZN and resid 307 residue_selection_2 = chain N and resname CYS and resid 43 } # data_link_ZN-CYS # loop_ _chem_link_bond.link_id _chem_link_bond.atom_1_comp_id _chem_link_bond.atom_id_1 _chem_link_bond.atom_2_comp_id _chem_link_bond.atom_id_2 _chem_link_bond.type _chem_link_bond.value_dist _chem_link_bond.value_dist_esd ZN-CYS 1 ZN 2 SG single 2.340 0.020 loop_ _chem_link_angle.link_id _chem_link_angle.atom_1_comp_id _chem_link_angle.atom_id_1 _chem_link_angle.atom_2_comp_id _chem_link_angle.atom_id_2 _chem_link_angle.atom_3_comp_id _chem_link_angle.atom_id_3 _chem_link_angle.value_angle _chem_link_angle.value_angle_esd ZN-CYS 1 ZN 2 SG 2 CB 109.000 3.000 ---------------------------------------------------------------------------------------------------- -- Hasan DeMirci, Ph.D. Postdoctoral Fellow Department of Molecular Biology, Cellular Biology & Biochemistry Brown University 185 Meeting Street Providence, RI 02912 (401) 863-3652 lab (SFH) (401) 863-6124 lab (ship st) (401) 226-7852 cell Hasan_DeMirci(a)Brown.edu demircha99(a)gmail.com

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Re: [phenixbb] Using Reference Structure in Phenix Refine
by John Pascal 05 Dec '10

05 Dec '10

Got it! Thank you, Pavel and Jeff. Best, John -- John Pascal, PhD ph 215.503.4596 Assistant Professor fx 215.923.2117 Thomas Jefferson University Biochemistry & Molecular Biology 233 South 10th Street, BLSB 804 Philadelphia, Pennsylvania 19107 ---------------------------------------------------------------- This message was sent using IMP, the Internet Messaging Program.

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Using Reference Structure in Phenix Refine
by John Pascal 05 Dec '10

05 Dec '10

Hello Everyone, I am refining against low resolution data, and I would like to use a higher resolution model that is available as a reference structure. There are multiple copies of the molecule in the asymmetric unit, each with a different chain ID. Does the reference PDB file need to contain multiple copies, such that there is a match for each chain (e.g. RESIDs and SEGIDs)? Or does phenix figure out that the reference structure refers to several copies of the molecule, and you only need a single copy in the reference molecule PDB file? Or will NCS restraints take care of this? Thanks. -John -- John Pascal, PhD ph 215.503.4596 Assistant Professor fx 215.923.2117 Thomas Jefferson University Biochemistry & Molecular Biology 233 South 10th Street, BLSB 804 Philadelphia, Pennsylvania 19107 ---------------------------------------------------------------- This message was sent using IMP, the Internet Messaging Program.

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Can PHENIX write the peak list to a PDB file?
by Joe Krahn 04 Dec '10

04 Dec '10

PHENIX has an option to find positive and negative peaks, but only lists them in the log file along with the residue they are closest to. Is it possible to write out the actual peak coordinates, such as to a PDB file? Thanks, Joe Krahn

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heavy atom search within phaser molecular replacement
by Bryan Lepore 03 Dec '10

03 Dec '10

i know that phaser will find heavy atoms in autosol, and that "MR-SAD" can be run as two separate steps, such that with some scripting, one could in principle cycle through a bunch of heavy atom searches using MR phases. however, it is not clear to me whether phaser can be run such that e.g. the refined MR solutions can have their anomalous Fourier's searched for peaks in a single MR job. seems possible in principle - before i go trying this, any comments would be appreciated.... i.e. run heavy atom searches as part of molecular replacement, for convenience. hope that makes sense. -Bryan

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Issue with phenix.superpose_maps
by Stephen Graham 03 Dec '10

03 Dec '10

Hi all, I'm trying to use phenix.superpose_maps through the GUI to get superposed maps covering the same region of NCS-related chains A and B for a figure. I have used PDB Tools to split the model into two files with only chain A or chain B. However, when I run superpose_maps specifying the two individual chains for the input PDB files but the same mtz file for the map coefficients I only get one output map (I think it overwrites the output file...). Selected input from the generated .eff file is as follows: input_files { map_1 = "/home/stepheng/blah/Native_refine_6_map_coeffs.mtz" labels_1 = 2FOFCWT,PH2FOFCWT map_2 = "/home/stepheng/blah/Native_refine_6_map_coeffs.mtz" labels_2 = 2FOFCWT,PH2FOFCWT pdb_1 = "/home/stepheng/blah/Native_refine_6_chainA.pdb" d_min_1 = None pdb_2 = "/home/stepheng/blah/Native_refine_6_chainB.pdb" d_min_2 = None output_dir = "/home/stepheng/blah" } And the end of the output is as follows: saving CCP4 map to Native_refine_6_map_coeffs_superposed.ccp4 Wrote Native_refine_6_chainA_superposed.pdb Wrote Native_refine_6_map_coeffs_superposed.ccp4 saving CCP4 map to Native_refine_6_map_coeffs_superposed.ccp4 Wrote Native_refine_6_chainB_superposed.pdb Wrote Native_refine_6_map_coeffs_superposed.ccp4 A bug? Stephen P.S. Incidentally, is there any reason you write both maps in a P1 box rather than putting map 2 on top of map 1 in the position of the first (reference) model? The latter would be more convenient as you can then re-use your carefully chosen pymol viewing matrices for all figures... -- Dr Stephen Graham 1851 Research Fellow Cambridge Institute for Medical Research Wellcome Trust/MRC Building Addenbrooke's Hospital, Hills Road Cambridge, CB2 0XY, UK Phone: +44 1223 762 638

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question about xtriage
by crystallogrphy 03 Dec '10

03 Dec '10

Hi, I am checking the space group of my data set using phenix.xtriage. However, the program terminated in the following scripts. Does anyone knows why and what should I do? Thanks! phenix.xtriage B13_native.sca Traceback (most recent call last): File "/usr/local/phenix-1.6.4-486/cctbx_project/mmtbx/command_line/xtriage.py", line 20, in <module> xtriage.run(args=sys.argv[1:]) File "/usr/local/phenix-1.6.4-486/cctbx_project/mmtbx/scaling/xtriage.py", line 866, in run output_file = open( params.scaling.input.parameters.reporting.log ,'w') IOError: [Errno 13] Permission denied: 'logfile.log'

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force field of PHENIX.refine ?
by chene＠umbi.umd.edu 02 Dec '10

02 Dec '10

Dear authors of PHENIX, I just want to know what force field is used by phenix.refine, especially for simulated annealing, CHARMM, AMBER, or what else? Thanks. Chen Chen Chen, PhD, Research Associate Center for Advanced Research in Biotechnology (CARB), University of Maryland Biotechnology Institute (UMBI), 9600 Gudelsky Drive, Rockville, MD 20850 240-314-6122

3 2

distance constrain in phenix
by r n 02 Dec '10

02 Dec '10

Hi I would like to do distance restrain refinement for metal coordination. How can I do metal - protein strict distance restrain refinement in phenix? Thanks ram

3 4

Hydrogen occupancies
by Florian Sauer 01 Dec '10

01 Dec '10

Dear all, I'm currently refining a small protein against 0.96A data using phenix.refine (1.6-486) from the GUI. Refinement without hydrogens yielded Rwork/free of 12.4/14.2. I then added H-atoms with phenix.reduce and switched to individual refinement of hydrogens which dropped the R-factors to 11.3/13.4. After this refinement the occupancies of some hydrogens dropped to 0 which makes me a little concerned. See e.g.: ATOM 752 H LYS A 45 -7.443 2.613 9.537 1.00 4.73 H ATOM 753 HA LYS A 45 -9.707 1.128 9.401 0.55 2.42 H ATOM 754 HB2 LYS A 45 -8.476 2.797 7.435 1.00 10.58 H ATOM 755 HB3 LYS A 45 -9.795 1.948 7.166 0.95 8.70 H ATOM 756 HG2 LYS A 45 -10.840 3.210 8.889 0.00 33.83 H ATOM 757 HG3 LYS A 45 -9.604 4.206 8.775 0.00 33.83 H ATOM 758 HD2 LYS A 45 -11.227 3.615 6.563 0.00 62.10 H ATOM 759 HD3 LYS A 45 -11.508 4.867 7.507 0.00 62.10 H ATOM 760 HE2 LYS A 45 -9.229 5.527 6.985 1.00 83.62 H ATOM 761 HE3 LYS A 45 -9.348 4.488 5.786 0.00 83.86 H ATOM 762 HZ1 LYS A 45 -10.909 5.758 4.853 1.00 99.63 H ATOM 763 HZ2 LYS A 45 -11.131 6.534 6.042 0.35100.44 H ATOM 764 HZ3 LYS A 45 -9.917 6.715 5.257 0.39100.08 H I would like to ask whether it is possible in phenix to group the occupancies to keep them at the same value as the rest of the residue but still refine xyz and isotropic adp of the individual hydrogens? Thank you in advance for your answers, Florian

2 1

wander wall interaction
by subhash bihani 01 Dec '10

01 Dec '10

hi all I am working on a enzyme-ligand complex structure. For some analysis I need to remove wander wall interactions between protein and ligand. How can I do that in Phenix? Something similar to igroup statement in CNS? Thanks in adwance -- Subhash Bihani Scientific Officer Solid State Physics Division Bhabha Atomic Research Centre Trombay, Mumbai-85 Ph. 25594688 (o) alternate email: subhashbihani(a)yahoo.co.in

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phaser and threads
by Bryan Lepore 01 Dec '10

01 Dec '10

[ dev-595 ] [ GNU/Linux 2.6.31-20-generic #58-Ubuntu SMP four-processors ] [ compiled from source with --no-gui --no-apps --openmp ] i noticed phaser splits the rotation onto 2 threads - just wondering why that might be, since i used nproc=4 on the command line.... oh, hmmm... i seem to have just got this at the packing function : |python: malloc.c:4591: _int_malloc: Assertion `(unsigned long)(size) >= (unsigned long)(nb)' failed. -Bryan

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building from source : svn_checkout
by Bryan Lepore 01 Dec '10

01 Dec '10

[ dev-596 from source using --no-gui --no-apps --openmp ] README-DEV mentions ./bin/svn_checkout ... i cannot find this (but i do find bundle_update and recompile). any pointers appreciated. -Bryan

2 1

Refinement of a complex with a symmetric inhibitor lying on the axis of symmetry
by Ina Lindemann 01 Dec '10

01 Dec '10

Hi, I try to refine a crystal structure of a protein - inhibitor complex. The protein is a homodimer and the two molecules have a crystallographic symmetry. The space group is P6122. The symmetric inhibitor binds symmetrically to the protein so that I refine the half of it. The core of the inhibitor is a five-membered ring with a nitrogen lying directly on the axis of symmetry. I achieved to refine this by setting the occupancy to 1.0. And now, here is my problem: Two C atoms of this ring system are bound across the symmetry axis - how could I include this in the refinement? Is there any possibility to generate restraints to the other part of the inhibitor (of the symmetry equivalent)?? Thanks for your help in advance, Ina Ina Lindemann Philipps-Universität Marburg Pharmazeutische Chemie AG Klebe Marbacher Weg 6 35032 Marburg Tel.: 06421/2825908

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autosol : unmerged data with input_phase_file
by Bryan Lepore 30 Nov '10

30 Nov '10

dev-595 i gather that autosol will not take unmerged data when the input_phase_file originates from merged data. e.g. in "method #2 for MRSAD". -Bryan

2 2

dev-590 compile from source : -lGLU, -lGL
by Bryan Lepore 30 Nov '10

30 Nov '10

[ dev-590 ] [ gcc 4.4.4 ] [ GNU/Linux 32-bit ] [ Ubuntu 10.10-ish ] * OpenGL/GLUT is of unstable nature* got an error compiling from source (see after sig). i tried using --openmp first, then --openmp --nogui in the same build directory and the error occurs both times. just trying this out, not critical - was interested to know if there's an easy workaround anyone might think of (besides touching GL/GLUT - shudder ). -Bryan /usr/bin/ld: cannot find -lGLU /usr/bin/ld: cannot find -lGL collect2: ld returned 1 exit status scons: *** [lib/gltbx_fonts_ext.so] Error 1

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sculptor : "Wrong alignment format:"
by Bryan Lepore 29 Nov '10

29 Nov '10

(starting a new thread?) trouble with alignment format. tried this : fubar.fas : Sorry: Unknown file(s): fubar.fas fubar.fasta : Sorry: Wrong alignment format: fubar.fasta i compared to one that worked yesterday and its not obvious : first sequence is the target, the pdb sequence is in there (somewhere), i changed a ">sp" to ">gi".... if anyone knows what i'm missing here,... -Bryan

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International Conference on Structural Genomics May 10-14, 2011, Toronto -- registration now open
by Tom Terwilliger 29 Nov '10

29 Nov '10

Dear Colleagues, We are pleased to announce that registration is now open for the International Conference on Structural Genomics 2011, which will 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, structural/chemical biology, and their impact on research in biology, medicine and disease. A substantial number of short talks will be selected from submitted poster abstracts. Also, a limited number of student travel fellowships will be available for travel to this meeting. 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

1 0

occupancy refinement
by Dalibor Milic 25 Nov '10

25 Nov '10

Dear all! How to refine occupancies of mutually dependent structural fragments found in alternate conformations, but not consecutive in a sequence? E.g. I want to refine occupancies of two alternate conformations of residues 30 and 451 (see below the corresponding parts of a PDB file). Because of the nature of the structural disorder, an occupancy for altLoc A should be strictly the same in both fragments - the same is valid for altLoc B. Of course, the sum of occupancies for altLoc A and B should add up to 1. Thanks for your suggestions, Dalibor Milic ... ATOM 376 N AGLU A 30 23.241 86.975 31.961 0.52 17.13 N ATOM 377 N BGLU A 30 18.971 88.677 32.817 0.48 9.05 N ATOM 378 CA AGLU A 30 23.240 85.507 31.907 0.52 18.89 C ATOM 379 CA BGLU A 30 19.108 87.234 32.991 0.48 10.00 C ATOM 380 CB AGLU A 30 21.848 84.946 32.256 0.52 18.78 C ATOM 381 CB BGLU A 30 17.727 86.562 33.046 0.48 11.01 C ATOM 382 CG AGLU A 30 21.247 85.562 33.524 0.52 26.38 C ATOM 383 CG BGLU A 30 16.935 87.037 34.275 0.48 19.26 C ATOM 384 CD AGLU A 30 20.264 84.659 34.277 0.52 33.36 C ATOM 385 CD BGLU A 30 15.694 86.223 34.542 0.48 26.60 C ATOM 386 OE1AGLU A 30 19.437 83.968 33.620 0.52 31.85 O ATOM 387 OE1BGLU A 30 15.401 85.288 33.762 0.48 33.05 O ATOM 388 OE2AGLU A 30 20.310 84.678 35.535 0.52 29.12 O ATOM 389 OE2BGLU A 30 15.007 86.527 35.538 0.48 30.95 O ATOM 390 C AGLU A 30 23.750 84.946 30.575 0.52 18.22 C ATOM 391 C BGLU A 30 19.976 86.652 31.877 0.48 10.17 C ATOM 392 O AGLU A 30 24.319 83.853 30.534 0.52 19.40 O ATOM 393 O BGLU A 30 20.621 85.606 32.059 0.48 10.67 O ... ATOM 4627 N AALA A 451 31.047 82.837 22.335 0.52 18.30 N ATOM 4628 N BALA A 451 29.107 84.432 26.354 0.48 9.81 N ATOM 4629 CA AALA A 451 31.958 83.502 23.284 0.52 18.73 C ATOM 4630 CA BALA A 451 29.655 85.424 27.274 0.48 9.73 C ATOM 4631 CB AALA A 451 32.880 84.486 22.541 0.52 20.38 C ATOM 4632 CB BALA A 451 30.469 86.474 26.478 0.48 11.60 C ATOM 4633 C AALA A 451 31.176 84.206 24.406 0.52 18.79 C ATOM 4634 C BALA A 451 28.556 86.128 28.089 0.48 6.84 C ATOM 4635 O AALA A 451 30.019 84.593 24.197 0.52 18.25 O ATOM 4636 O BALA A 451 27.441 86.357 27.604 0.48 6.81 O ... -- Dalibor Milic, Dr. Sc. Laboratory of General and Inorganic Chemistry Department of Chemistry Faculty of Science University of Zagreb Horvatovac 102a HR-10000 Zagreb Croatia phone: +385 1 460 6377 fax: +385 1 460 6341 e-mail: dmilic(a)chem.pmf.hr

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Re: [phenixbb] occupancy refinement
by Dalibor Milic 25 Nov '10

25 Nov '10

Just an additional comment to my previous e-mail: the refined final value of occupancies in the expression occupancy(AGLU A 30) = occupancy(BGLU A 30) = occupancy(AALA A 451) = occupancy(BALA A 451) were not equal to 0.50 and I got occupancy(AGLU A 30) + occupancy(BGLU A 30) = occupancy(AALA A 451) + occupancy(BALA A 451) < 1.00. Regards, Dalibor -- Dalibor Milic Laboratory of General and Inorganic Chemistry Department of Chemistry Faculty of Science University of Zagreb Horvatovac 102a HR-10000 Zagreb Croatia phone: +385 1 460 6377 fax: +385 1 460 6341 e-mail: dmilic(a)chem.pmf.hr

1 0

same origin
by r n 24 Nov '10

24 Nov '10

Hi all I wanted to compare the two models from two data set. I want the MR replacement in same origin to compare their them with respect to the map and model. I tried reforigin in ccp4 , it gave me some error , that I am not aware or not clear. I did tried overlay the two model and rfree is going up. Most likely different hands, so Is there any way to compare the two model and data and modify them in Phenix either reindex or shift the model origin to same in all cases. Thought phenix.xmanip could help, not seen any option to do it command line or in the GUI. I did tried def file, but phenix.xmanip params.def , it complains me that unknown file or keyword? any help will be appreciated. Thanks ram

2 2

sculptor
by Bryan Lepore 22 Nov '10

22 Nov '10

dev-572 I am checking out sculptor, looks pretty cool, but I provided what i thought was a clustal format alignment to sculptor using --verbose, and it reports "Sorry: Wrong alignment format:" that's it. sounds like user error, but i'm not sure where to proceed next. i tried mafft and clustalw2 output for this. a sample of a bit of the top of the .aln is below. -Bryan p.s: shouldn't readseq convert it to .pir? that'd be code 14 PIR/CODATA? CLUSTAL format alignment by MAFFT L-INS-i (v6.833b) gi|16132042|ref --ANVRLQVEGLSGQLEKNVRAQLSTIESDEVTPDRRFRARVDDAIREGLKALGYYQPTI gi|157163695|re --ANVRLQVEGLSGQLEKNVRAQLSTIESDEVTPDRRFRARVDDAIREGLKALGYYQPTI

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