- phenixbb - phenix-online.org

Automated Mg & K ions picking
by Hasan Demirci 02 Jan '11

02 Jan '11

Hi, I have a low resolution data and I am trying to place Mg++ and K+ ions. As far as I know for ligand search at least 3 atoms required. Is it possible to do an automated search of these single atom ions by using phenix similar to automated water picking protocol? Thanks. -- 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

2 1

MACOSX_DEPLOYMENT_TARGET mismatch between PHENIX and Coot
by Ben Eisenbraun 30 Dec '10

30 Dec '10

Howdy PHENIXians, One of my users reported this error: File "/programs/i386-mac/coot/coot-latest/lib/python2.7/sysconfig.py", line 300, in _init_posix raise IOError(msg) IOError: $MACOSX_DEPLOYMENT_TARGET mismatch: now "10.4" but "10.5" during configure The person is running on OS X Intel, using a PHENIX nightly and trying to call Coot. It looks like the PHENIX nightlies are built with MACOSX_DEPLOYMENT_TARGET=10.4, and the Coot I built used M_D_T=10.5 and Python is unhappy about this. It's easy to test this: $ export MACOSX_DEPLOYMENT_TARGET=10.3 $ phenix.python Traceback (most recent call last): File "/programs/i386-mac/phenix/dev-606/phenix-dev-606/build/mac-intel-osx/base/Python.framework/Versions/Current/lib/python2.7/site.py", line 553, in <module> <snip> IOError: $MACOSX_DEPLOYMENT_TARGET mismatch: now "10.3" but "10.4" during configure Or if you have access to one of our installations: $ phenix.python import os os.system('coot') Results in the original error pasted above. After playing a bit, I came up with a workaround. If you just set the M_D_T to 10.5 before starting Coot and _after_ starting PHENIX, it all seems to work. E.g. I can start Coot using this script: $ cat coot.py #!/usr/bin/env phenix.python import os os.putenv('MACOSX_DEPLOYMENT_TARGET', '10.5') os.system('coot') And since the 'coot' binary in the PATH is a wrapper script, I can just set it in the environment there. My question is: does Python actually need this? Is my workaround going to break something? I'm not enough of a Pythonista to be able to tell from looking at the sysconfig code if this will be an issue. There is a comment in the source: # On MacOSX we need to check the setting of the environment variable # MACOSX_DEPLOYMENT_TARGET: configure bases some choices on it so # it needs to be compatible. But it's not clear to me when it's going to be used. I'm almost certainly going to implement the workaround, so I'm mostly posting this for the list archives and to see if anyone has a better idea. Thanks. -ben -- | Ben Eisenbraun | SBGrid Consortium | http://sbgrid.org | | Harvard Medical School | http://hms.harvard.edu |

3 5

LigandFit (distorted manesium hexahydrate cluster)
by Hasan Demirci 28 Dec '10

28 Dec '10

Dear All, I am trying to run " LigandFit " with the following hydrated magnesium hexahydrate cluster (without the hydrogens) pdb. "HETATM 7 MG MG6 A 1 -53.936 117.342 91.273 1.00128.70 A MG HETATM 2 O1 MG6 A 1 -55.351 117.224 89.749 1.00128.62 A O HETATM 3 O2 MG6 A 1 -52.532 117.421 92.718 1.00127.25 A O HETATM 4 O3 MG6 A 1 -55.370 118.284 92.428 1.00127.74 A O HETATM 5 O4 MG6 A 1 -53.253 119.219 90.518 1.00128.43 A O HETATM 6 O5 MG6 A 1 -54.385 115.379 91.937 1.00127.84 A O HETATM 7 O6 MG6 A 1 -52.566 116.391 89.994 1.00128.62 A O " LigandFit automatically runs the elbow and creates a new search pdb file with hydroges and while doing this, elbow totally screws up the original starting geometry of the Oxygen atoms within the cluster after the addition of hydrogens. "HETATM 1 MG MG6 A 1 -53.913 117.323 91.231 1.00128.70 A MG HETATM 2 O1 MG6 A 1 -55.140 117.947 90.141 1.00128.62 A O HETATM 3 O2 MG6 A 1 -53.080 118.061 92.589 1.00127.25 A O HETATM 4 O3 MG6 A 1 -55.453 117.480 92.061 1.00127.74 A O HETATM 5 O4 MG6 A 1 -52.768 118.528 90.669 1.00128.43 A O HETATM 6 O5 MG6 A 1 -53.676 115.727 91.923 1.00127.84 A O HETATM 7 O6 MG6 A 1 -53.363 116.194 90.004 1.00128.62 A O HETATM 8 H11 MG6 A 1 -55.461 117.161 89.473 1.00128.62 A H HETATM 9 H21 MG6 A 1 -52.333 117.378 92.967 1.00127.25 A H HETATM 10 H31 MG6 A 1 -55.430 118.350 92.700 1.00127.74 A H HETATM 11 H41 MG6 A 1 -53.300 119.422 90.378 1.00128.43 A H HETATM 12 H51 MG6 A 1 -54.636 115.255 92.077 1.00127.84 A H HETATM 13 H61 MG6 A 1 -52.319 116.372 89.793 1.00128.62 A H " Is it a bug or am I making something wrong? Does the search pdb HAVE TO be covalently linked? or can I search for a cluster? Thanks. -- Hasan DeMirci

2 1

ramachandran_restraints
by José Trincão 28 Dec '10

28 Dec '10

Dear all, I am refining a structure to 2.9 A, with pretty bad experimental data (P1, ~5400 residues in the A.U. (4 mol), anisotropic, fairly incomplete...). I have been running phenix.refine with NCS, 1 ADP per residue, lower target weights, TLS. My R/Rfree are stuck at about 2.4/3.05. I was getting around 2% ramachandran outliers at every cycle so I have been giving the nightly builds a shot. Now I get 0.2% outliers without changing any parameters for the ramachandra_restraints but it is forcing some of the peptide bonds out of the density. What can I tweak to improve the refinement? Thanks all in advance! Jose José Trincão, PhD CQFB@FCT-UNL 2829-516 Caparica, Portugal "It's very hard to make predictions... especially about the future" - Niels Bohr

3 2

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 > ___________________________________________________________ > >

3 2

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 ___________________________________________________________

2 1

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. =================================

2 1

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/

6 7

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

1 0

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 ___________________________________________________________

7 16