- phenixbb - phenix-online.org

Re: [phenixbb] autosol w/ "no merge original index"?
by Tom Terwilliger 19 Dec '07

19 Dec '07

Hi Brian, Thanks for sending me the top of your hkl file....I added some random data after that and it runs on my version just fine. Can you possibly try again with the most recent version of phenix on the web site (rc6)? Thanks! -Tom T At 01:24 PM 12/19/2007, you wrote: >phenix 1.3b of 21-10-2007 > >confusion w/ "no merge original index" data file in phenix.autosol. this >should work, right? > >caveat - the 'nmoi' hkl is actually from scala, but that usually is fine >w/ e.g. solve-2.13. 'nmoi' requires declaration of cell='(numbers)' on >command line. > >phenix.autosol seems to go through all the usual checks fine, then >reports (in AutoSol_run_2_/LAST.LOG): >".... > The error seems to be at line 0 > Here is what the first few lines of this file look like: > 1 > -987 > 86.052 86.052 132.608 90.000 90.000 90.000 p41212 > You have set the keywords readdenzo and unmerged > Please check whether you should have set readformatted or readtrek or >premerged >...." > >... 'readdenzo' and 'unmerged' are just right for 'nmoi' files. etc. > >-bryan >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

Re: [phenixbb] autosol w/ "no merge original index"?
by Tom Terwilliger 19 Dec '07

19 Dec '07

Hi Bryan, Yes, "No merge original index" files should work fine. This file should be converted by the autosol wizard to premerged scalepack during the run. In your case this seems to be so as the file header that is being read during the middle of the run 1 -987 86.052 86.052 132.608 90.000 90.000 90.000 p41212 is premerged scalepack. Now what does not make sense is the error message "You have set the keywords readdenzo and unmerged". I am not sure where that has come from. I just ran a SAD dataset to test this with an unmerged original index file, and it ran fine for me. If this doesn't help, could you send me (terwilliger(a)lanl.gov) your input script and datafile ( or even the first 1000 lines of the datafile) and I can try to debug it. Thanks! -Tom T At 01:24 PM 12/19/2007, you wrote: >phenix 1.3b of 21-10-2007 > >confusion w/ "no merge original index" data file in phenix.autosol. this >should work, right? > >caveat - the 'nmoi' hkl is actually from scala, but that usually is fine >w/ e.g. solve-2.13. 'nmoi' requires declaration of cell='(numbers)' on >command line. > >phenix.autosol seems to go through all the usual checks fine, then >reports (in AutoSol_run_2_/LAST.LOG): >".... > The error seems to be at line 0 > Here is what the first few lines of this file look like: > 1 > -987 > 86.052 86.052 132.608 90.000 90.000 90.000 p41212 > You have set the keywords readdenzo and unmerged > Please check whether you should have set readformatted or readtrek or >premerged >...." > >... 'readdenzo' and 'unmerged' are just right for 'nmoi' files. etc. > >-bryan >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

autosol w/ "no merge original index"?
by Bryan W. Lepore 19 Dec '07

19 Dec '07

phenix 1.3b of 21-10-2007 confusion w/ "no merge original index" data file in phenix.autosol. this should work, right? caveat - the 'nmoi' hkl is actually from scala, but that usually is fine w/ e.g. solve-2.13. 'nmoi' requires declaration of cell='(numbers)' on command line. phenix.autosol seems to go through all the usual checks fine, then reports (in AutoSol_run_2_/LAST.LOG): ".... The error seems to be at line 0 Here is what the first few lines of this file look like: 1 -987 86.052 86.052 132.608 90.000 90.000 90.000 p41212 You have set the keywords readdenzo and unmerged Please check whether you should have set readformatted or readtrek or premerged ...." ... 'readdenzo' and 'unmerged' are just right for 'nmoi' files. etc. -bryan

1 0

Re: [phenixbb] MTZ intensities interpreted as amplitudes by autobuild command-line versions up to 1.3b/rc6
by Thomas C. Terwilliger 19 Dec '07

19 Dec '07

Hi again Peter, Yes, the AutoMR wizard (any version) will run correctly with input MTZ data that are intensities. However all versions up to now will pass this MTZ file on to AutoBuild without conversion to amplitudes and it will be incorrectly interpreted by AutoBuild. Note that this only applies to MTZ files. Any other source of amplitudes/intensities doesn't cause any problem. If you run from the GUI, you will have the chance to set the correct columns in AutoBuild, if amplitudes are available in your data file. From the command_line, for existing versions, you would need to say when you run AutoMR: input_labels='F SIGF' (or whatever your amplitudes are in this MTZ file) All the best, Tom T > Hi Tom, > > What about the AutoMR wizard. Can I use intensities there instead of amplitudes? I always get confused. > > Thanks, > > Peter > > 2007/12/18, Tom Terwilliger <terwilliger(a)lanl.gov>: >> Hi phenix.autobuild users, >> I'm sorry to report a serious bug that I have just noticed that applies to MTZ files for autobuild containing intensities. The >> problem is fixed now. I'm very sorry about this mistake. >> All the best, >> -Tom T >> >> >> THE PROBLEM: >> >> In all alpha and beta versions of phenix up to now (up to 1.3b/rc6), there has been a bug in autobuild in which the command >> >> phenix.autobuild data.mtz model.pdb >> >> will misinterpret intensity data as amplitudes if the input file is an mtz file (for example if the mtz file has IMEAN,SIGIMEAN and F,SIGF). (This can also happen in the GUI version, but you will have been presented on screen 3 with a list of data types (FP SIGFP) and columns from the input data file to match them and it is not so likely that you will have chosen to match FP with IMEAN.) >> >> You can tell if this has happened in your case by looking for >> something like (search for the string "Input labels:"): >> >> Input labels: ['IMEAN', 'SIGIMEAN', 'None', 'None', 'None', 'None', 'None', 'None', 'FreeR_flag'] >> >> in your log file (where the None's don't matter, just the first 2 column names. The columns in this list should be >> amplitude-containing columns only. If everything is ok.it should look instead like: >> >> Input labels: ['F', 'SIGF', 'None', 'None', 'None', 'None', 'None', 'None', 'None'] >> >> THE SOLUTION: >> >> In existing versions, the solution to this is to either (1) only have amplitude arrays in your mtz file, or (2) use the GUI and select the correct amplitude arrays, or (3) specify what amplitude columns to use with a command like: >> >> input_labels="F SIGF". >> >> Note that you cannot use intensity data from an mtz file with the existing versions of autobuild, only amplitude data. In the corrected version (1.3b/rc7, not yet out) , you will be able to use an mtz file with intensity data as long as there is no amplitude data in the same mtz file. >> >> Note also that all this applies equally to the refinement_file and hires_file data. Also note that if the file type is not mtz, then this bug does not apply (because the file is always imported and converted from intensities to amplitudes automatically). >> >> >> >> >> >> >> >> >> >> Thomas C. Terwilliger >> Mail Stop M888 >> Los Alamos National Laboratory >> Los Alamos, NM 87545 >> >> Tel: 505-667-0072 email: terwilliger(a)LANL.gov >> Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org >> ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu >> TB Structural Genomics Consortium web site: >> http://www.doe-mbi.ucla.edu/TB >> >> >> _______________________________________________ >> phenixbb mailing list >> phenixbb(a)phenix-online.org >> http://www.phenix-online.org/mailman/listinfo/phenixbb >> > _______________________________________________ > phenixbb mailing list > phenixbb(a)phenix-online.org > http://www.phenix-online.org/mailman/listinfo/phenixbb >

1 0

after_autosol
by Bryan W. Lepore 19 Dec '07

19 Dec '07

using phenix 1.3b of 21-10-2007, trying `phenix.autobuild after_autosol` : how does one identify the "highest-numbered AutoSol run", and that it is completed? what does `phenix.autobuild` want for such a solution e.g. in terms of files/directories? or does `phenix.autobuild after_autosol` need to be included in the command at the time when `phenix.autosol` is submitted? phenix.autobuild reads a lot of params from my AutoSol dir, but apparently no solutions -- even though `phenix.autosol show_runs` shows one. -bryan

2 1

chain definition in phenix
by Kornelius Zeth 19 Dec '07

19 Dec '07

Dear all, I'm trying to refine/rebuild a structure of 48 identical chains. In Refmac the small letters a, b, c and 0 1 2 for the chains work quite well and are distinguished. However that does not apply to Phenix which sees A equal to a. What might be the solution to use? Thanks and best wishes Kornelius ---------------------------------------------- Kornelius Zeth Max Planck Institute for Developmental Biology Dept. Protein Evolution Spemannstr. 35 72076 Tuebingen, Germany kornelius.zeth(a)tuebingen.mpg.de Tel -49 7071 601 323 Fax -49 7071 601 349

5 6

Re: [phenixbb] Resolution Limits in the transition from AutoMR to AutoBuild
by Tom Terwilliger 17 Dec '07

17 Dec '07

Hi Dale, Thanks for the notes! Here is what is supposed to happen: the autobuild wizard keeps all the data you supply. resolution=2.2 will set the resolution of model-building and density modification and refinement refinement_resolution=2.3 will set the resolution for refinement to 2.3 instead of the 2.2 defined by resolution=2.2 There is as you guessed a bug however somewhere in the communication between the autobuild wizard and phenix.refine, so the refinement_resolution did not get passed properly. I will fix that... Thanks! -Tom T . At 01:29 AM 12/17/2007, Dale Tronrud wrote: > The structure factors that I downloaded from the PDB for my >little MR project contains both reflections behind the beam stop >and reflections of higher resolution than even the original authors >would use. When setting up the MR I entered the more restrictive >resolution limits into the Wizard and Phaser appears to have obeyed. > > As near as I can tell from the log files, however, Resolve is >using all the data in the rebuild. I am including a copy of the >log file from the "best" refinement. I would prefer that only >data between 30 and 2.2A were used but it is clear that the >refinement is, at least, monitoring the fit to all the data. I >am presuming that the program is refining against the same data >it is monitoring. > > I would like to suggest that either the log file be clearer >about the resolution limits it is actually refining to, or the >plumbing that passes the resolution limits from the AutoMR wizard >to the AutoBuild wizard be checked. > >Dale Tronrud > >P.S. That's all my problems... For now. The project I'm working >on is cursed and brings out the worst in all the software I have >used. > Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

2 2

A Small Problem with Atom Types in AutoBuild
by Dale Tronrud 17 Dec '07

17 Dec '07

The probe model in my MR project comes from a Shelxl refinement, and the .pdb file does not contain atom types at the end of each ATOM statement as modern .pdb files do. I have magnesium atoms in my model and the atom names for these atoms are "MG" and are properly shifted one space to the left of place where atoms with single letter element symbols lie. Phaser has no problem with this .pdb file. Resolve, however, considers this to be a fatal error. Opening MR.1.pdb and reading coordinates Warning...unknown atom type "M " ...this may indicate characters in columns 77-78 of this PDB file that are not the element ID. This and all similar labels ignored Failed to read line in PDB entry The PDB line is: ATOM 2953 MG BCL B 1 26.429 2.746 -11.155 1.00 12.03 Sorry could not read model file MR.1.pdb Seems a little harsh to me. Especially since the error message doesn't make it back to the log file monitored by the Wizard. I was confused about what was causing the wizard to stop until I dug into the other files in the AutoBuild directory. Earlier in the log file the program worries about my atoms "NA" and "NB" but does conclude that they are nitrogen atoms. In the future I'll work with .pdb files with the extra atom types at the end of the line. Dale Tronrud

2 1

Resolution Limits in the transition from AutoMR to AutoBuild
by Dale Tronrud 17 Dec '07

17 Dec '07

The structure factors that I downloaded from the PDB for my little MR project contains both reflections behind the beam stop and reflections of higher resolution than even the original authors would use. When setting up the MR I entered the more restrictive resolution limits into the Wizard and Phaser appears to have obeyed. As near as I can tell from the log files, however, Resolve is using all the data in the rebuild. I am including a copy of the log file from the "best" refinement. I would prefer that only data between 30 and 2.2A were used but it is clear that the refinement is, at least, monitoring the fit to all the data. I am presuming that the program is refining against the same data it is monitoring. I would like to suggest that either the log file be clearer about the resolution limits it is actually refining to, or the plumbing that passes the resolution limits from the AutoMR wizard to the AutoBuild wizard be checked. Dale Tronrud P.S. That's all my problems... For now. The project I'm working on is cursed and brings out the worst in all the software I have used. AutoBuild_run_3_/TEMP0/LIG_EDITED_EDITED_edit_model.pdb Monomer Library directory: "/usr/local/phenix-1.3b-rc6/ext_ref_files/mon_lib" Total number of atoms: 6255 Number of models: 1 Model: 0 Number of conformers: 1 Conformer: " " Number of atoms: 6255 Number of chains: 4 Number of residues, atoms: 352, 2697 Classifications: {'peptide': 352} Modifications used: {'COO': 1} Incomplete info: {'backbone_only': 1, 'truncation_to_alanine': 8} Link IDs: {'PTRANS': 16, 'TRANS': 333, 'PCIS': 2} Chain breaks: 8 Unresolved non-hydrogen bonds: 41 Unresolved non-hydrogen angles: 50 Unresolved non-hydrogen dihedrals: 32 Unresolved non-hydrogen chiralities: 3 Planarities with less than four sites: {'GLN:plan1': 2, 'GLN:plan2': 2, 'GLN%COO:plan2': 1, 'GLN%COO:plan1': 1, 'ASP:plan': 1, 'ARG:plan': 2} Unresolved non-hydrogen planarities: 26 Number of residues, atoms: 352, 2694 Classifications: {'peptide': 352} Modifications used: {'COO': 1} Incomplete info: {'backbone_only': 1, 'truncation_to_alanine': 10} Link IDs: {'PTRANS': 17, 'TRANS': 333, 'PCIS': 1} Chain breaks: 5 Unresolved non-hydrogen bonds: 44 Unresolved non-hydrogen angles: 54 Unresolved non-hydrogen dihedrals: 34 Unresolved non-hydrogen chiralities: 2 Planarities with less than four sites: {'GLN:plan1': 2, 'GLN:plan2': 2, 'GLN%COO:plan2': 1, 'GLN%COO:plan1': 1, 'ASP:plan': 2, 'GLU:plan': 1, 'ARG:plan': 2} Unresolved non-hydrogen planarities: 34 Number of residues, atoms: 7, 432 Unusual residues: {'BCL': 7} Classifications: {'undetermined': 7} Link IDs: {None: 6} Unresolved non-hydrogen bonds: 57 Unresolved non-hydrogen angles: 146 Unresolved non-hydrogen dihedrals: 8 Unresolved non-hydrogen chiralities: 12 Number of residues, atoms: 7, 432 Unusual residues: {'BCL': 7} Classifications: {'undetermined': 7} Link IDs: {None: 6} Unresolved non-hydrogen bonds: 57 Unresolved non-hydrogen angles: 146 Unresolved non-hydrogen dihedrals: 8 Unresolved non-hydrogen chiralities: 12 Time building chain proxies: 8.94, per 1000 atoms: 1.43 ================================== X-ray data ================================= F-obs: AutoBuild_run_3_/TEMP0/exptl_fobs_phases_freeR_flags.mtz:FP,SIGFP R-free flags: AutoBuild_run_3_/TEMP0/exptl_fobs_phases_freeR_flags.mtz:FreeR_flag Miller array info: AutoBuild_run_3_/TEMP0/exptl_fobs_phases_freeR_flags.mtz:FP,SIGFP Observation type: xray.amplitude Type of data: double, size=38159 Type of sigmas: double, size=38159 Number of Miller indices: 38159 Anomalous flag: False Unit cell: (169.1, 169.1, 169.1, 90, 90, 90) Space group: P 43 3 2 (No. 212) Systematic absences: 0 Centric reflections: 4505 Resolution range: 75.6238 2.14896 Completeness in resolution range: 0.839637 Completeness with d_max=infinity: 0.8396 Number of F-obs in resolution range: 38159 Number of F-obs <= 0: 0 Refinement resolution range: d_max = 75.6238 d_min = 2.1490 Miller array info: AutoBuild_run_3_/TEMP0/exptl_fobs_phases_freeR_flags.mtz:FreeR_flag Observation type: None Type of data: int, size=38159 Type of sigmas: None Number of Miller indices: 38159 Anomalous flag: False Unit cell: (169.1, 169.1, 169.1, 90, 90, 90) Space group: P 43 3 2 (No. 212) Systematic absences: 0 Centric reflections: 4505 Resolution range: 75.6238 2.14896 Completeness in resolution range: 0.839637 Completeness with d_max=infinity: 0.8396 Test (R-free flags) flag value: 0 Number of work/free reflections by resolution: work free %free bin 1: 75.6707 - 4.6295 [4755/4893] 4536 219 4.6% bin 2: 4.6295 - 3.6746 [4493/4607] 4248 245 5.5% bin 3: 3.6746 - 3.2101 [4414/4577] 4178 236 5.3% bin 4: 3.2101 - 2.9166 [4232/4498] 4007 225 5.3% bin 5: 2.9166 - 2.7075 [4221/4533] 4026 195 4.6% bin 6: 2.7075 - 2.5479 [4005/4483] 3792 213 5.3% bin 7: 2.5479 - 2.4203 [3811/4480] 3637 174 4.6% bin 8: 2.4203 - 2.3149 [3223/4472] 3066 157 4.9% bin 9: 2.3149 - 2.2258 [2846/4459] 2702 144 5.1% bin 10: 2.2258 - 2.1490 [2159/4445] 2042 117 5.4% overall 36234 1925 5.0% No array of experimental phases found. ========================== Anomalous scatterer groups ========================= All atoms refined with f_prime=0 and f_double_prime=0. ========================== Set up restraints manager ========================== Number of disulfides: simple=0, symmetry=0 Time building geometry restraints manager: 0.40 seconds Histogram of bond lengths: 1.12 - 1.26: 957 1.26 - 1.40: 1621 1.40 - 1.55: 3702 1.55 - 1.69: 131 1.69 - 1.83: 23 Bond restraints sorted by residual: atom i - atom j ideal model delta weight residual " O1A BCL B 6 " - " CGA BCL B 6 " 1.212 1.117 0.095 2.50e+03 2.25e+01 " O1A BCL D 6 " - " CGA BCL D 6 " 1.212 1.118 0.094 2.50e+03 2.22e+01 " C15 BCL D 6 " - " C16 BCL D 6 " 1.540 1.459 0.081 2.50e+03 1.63e+01 " C15 BCL B 6 " - " C16 BCL B 6 " 1.540 1.460 0.080 2.50e+03 1.60e+01 " N PRO A 188 " - " CD PRO A 188 " 1.473 1.418 0.055 5.10e+03 1.56e+01 ... (remaining 6429 not shown) Histogram of nonbonded interaction distances: 1.49 - 2.17: 9 2.17 - 2.85: 1981 2.85 - 3.53: 8408 3.53 - 4.22: 16251 4.22 - 4.90: 27426 Nonbonded interactions sorted by model distance: atom i - atom j model vdw sym.op. j " OG SER A 24 " - " C GLY C 23 " 1.486 3.270 " OG SER A 24 " - " N SER C 24 " 1.747 3.120 " OH TYR A 330 " - " OE1 GLN C 333 " 1.870 3.040 x-1/4,-z-1/4,y+1/4 " C ASN A 121 " - " N LEU A 122 " 1.941 3.350 x+1,y+1,z+1 " OG SER A 24 " - " O GLY C 23 " 1.956 3.040 ... (remaining 54070 not shown) Histogram of dihedral angle deviations from ideal: 0.00 - 22.73: 1959 22.73 - 45.46: 198 45.46 - 68.20: 68 68.20 - 90.93: 27 90.93 - 113.66: 1 Dihedral angle restraints sorted by residual: " CA ALA C 327 " " C ALA C 327 " " N PRO C 328 " " CA PRO C 328 " ideal model delta periodicty weight residual 180.00 -66.34 -113.66 1 4.00e-02 5.17e+02 " C2B BCL D 7 " " C3B BCL D 7 " " CAB BCL D 7 " " OBB BCL D 7 " ideal model delta periodicty weight residual 0.00 147.16 32.84 2 4.00e-02 4.31e+01 " C2B BCL B 7 " " C3B BCL B 7 " " CAB BCL B 7 " " OBB BCL B 7 " ideal model delta periodicty weight residual 0.00 147.20 32.80 2 4.00e-02 4.30e+01 ... (remaining 2250 not shown) ==================== Fixing bad ADP in input model (if any) =================== ============================== Scattering factors ============================= ----------X-ray scattering dictionary---------- Number of scattering types: 4 Type Number sf(0) Gaussians S 14 15.96 2 O 1076 7.97 2 N 1007 6.97 2 C 4158 5.97 2 sf(0) = scattering factor at diffraction angle 0. ====================== Modifying start model if requested ===================== atom_attributes_list is modified in-place to define missing element types when possible. ==================== Fixing bad ADP in input model (if any) =================== ================== Extract refinement strategy and selections ================= individual_sites = True rigid_body = False individual_adp = True group_adp = False tls = False individual_occupancies = False group_occupancies = False group_anomalous = False size = 6255 n_use = 6255 n_use_u_iso = 6255 n_use_u_aniso = 0 n_grad_site = 0 n_grad_u_iso = 0 n_grad_u_aniso = 0 n_grad_occupancy = 0 n_grad_fp = 0 n_grad_fdp = 0 n_anisotropic_flag = 0 total number of scatterers = 6255 ==================== Process input NCS or/and find new NCS ==================== NCS groups found in parameter file: 0 Automatic NCS search: Chains in this PDB file: ['A', 'C'] GROUPS BASED ON QUICK COMPARISON: [] Looking for invariant domains for ...: ['A', 'C'] [[[9, 366]], [[9, 366]]] Updated/new NCS groups: refinement.ncs.restraint_group { reference = chain A and (resseq 9:118 or resseq 128:207 or resseq 215:366 ) selection = chain C and (resseq 9:118 or resseq 128:207 or resseq 215:366 ) } ----------Building NCS restraints---------- NCS restraint group 1: NCS operator 1: Reference selection: "chain A and (resseq 9:118 or resseq 128:207 or resseq 215:366 )" Other selection: "chain C and (resseq 9:118 or resseq 128:207 or resseq 215:366 )" Number of atom pairs: 2603 Rotation={{-0.999509, -0.0190423, 0.0248896}, {0.0243783, 0.0266261, 0.999348}, {-0.0196926, 0.999464, -0.0261488}} Translation={{38.5072}, {-44.0643}, {42.3394}} Histogram of differences: 0.001760 - 0.701888: 2552 0.701888 - 1.402017: 14 1.402017 - 2.102145: 22 2.102145 - 2.802274: 6 2.802274 - 3.502402: 4 3.502402 - 4.202531: 5 RMS difference with respect to the reference: 0.312576 =================== Write initial parameters into .eff file =================== ============================ Non-default parameters =========================== A complete record of all parameters was written to the .eff file above. Below are only the non-defaults. #phil __ON__ refinement { input { pdb { file_name = "/usr/users/dale/structure/fmo-ct/tronrud_2007/AutoBuild_run_3_/TEMP0/LIG_EDITED_EDITED_edit_model.pdb" } xray_data { file_name = "AutoBuild_run_3_/TEMP0/exptl_fobs_phases_freeR_flags.mtz" labels = "FP,SIGFP" high_resolution = 2.2 r_free_flags { file_name = "AutoBuild_run_3_/TEMP0/exptl_fobs_phases_freeR_flags.mtz" label = "FreeR_flag" test_flag_value = 0 } } monomers { file_name = "/usr/users/dale/geometry/chromophores/bcl_tnt.cif" } } output { prefix = "AutoBuild_run_3_/TEMP0/Build_composite_refined_side_3" serial = 1 write_eff_file = False write_geo_file = False write_def_file = False export_final_f_model = *mtz cns write_maps = False } main { ordered_solvent = True ncs = True use_experimental_phases = False random_seed = 516344 } ncs { special_position_warnings_only = True restraint_group { reference = "chain A and (resseq 9:118 or resseq 128:207 or resseq 215:366 )" selection = "chain C and (resseq 9:118 or resseq 128:207 or resseq 215:366 )" } } ordered_solvent { low_resolution = 3 } mask { ignore_zero_occupancy_atoms = False } } #phil __OFF__ ============================= ml refinement start ============================= ----------structure factors based statistics (before refinement)---------- ----------X-ray data---------- |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.3243 r_free= 0.3131 ksol= 0.00 Bsol= 0.00 scale= 1.698 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (0.00,0.00,0.00,0.00,0.00,0.00); trace/3= 0.00 | | | | maximum likelihood estimate for coordinate error: 0.40 A | | x-ray target function (ml) for work reflections: 7.754289 | |-----------------------------------------------------------------------------| |-----------------------------------------------------------------------------| | Bin Resolution Compl. No. Refl. R-factors Targets | |number range work test work test work test| | 1: 75.6707 - 5.1788 0.97 3272 159 0.4168 0.3905 8.6988 8.5536| | 2: 5.1788 - 4.1106 0.98 3112 155 0.2200 0.2341 8.4215 8.4968| | 3: 4.1106 - 3.5910 0.97 3000 188 0.2279 0.2321 8.1284 8.1202| | 4: 3.5910 - 3.2627 0.97 2977 168 0.2388 0.2465 7.9459 8.0053| | 5: 3.2627 - 3.0288 0.95 2930 152 0.2747 0.2878 7.8061 7.8021| | 6: 3.0288 - 2.8502 0.93 2844 159 0.2741 0.2804 7.6418 7.6974| | 7: 2.8502 - 2.7075 0.93 2860 139 0.2757 0.3123 7.5349 7.6274| | 8: 2.7075 - 2.5896 0.89 2705 156 0.2878 0.3340 7.453 7.4977| | 9: 2.5896 - 2.4899 0.89 2715 135 0.2982 0.3356 7.3586 7.5621| | 10: 2.4899 - 2.4040 0.81 2488 115 0.3089 0.3543 7.3181 7.3706| | 11: 2.4040 - 2.3288 0.72 2176 109 0.3142 0.3613 7.3041 7.3373| | 12: 2.3288 - 2.2623 0.67 2018 110 0.3096 0.3293 7.3086 7.3357| | 13: 2.2623 - 2.2027 0.58 1742 104 0.3370 0.3823 7.3303 7.508| | 14: 2.2027 - 2.1490 0.46 1395 76 0.3749 0.3710 7.4161 7.4587| |-----------------------------------------------------------------------------| |-----------------------------------------------------------------------------| |R-free likelihood based estimates for figures of merit, absolute phase error,| |and distribution parameters alpha and beta (Acta Cryst. (1995). A51, 880-887)| | | | Bin Resolution No. Refl. FOM Phase Scale Alpha Beta | | # range work test error factor | | 1: 75.6707 - 5.1788 3272 159 0.64 39.15 1.16 1.12 4689001.73| | 2: 5.1788 - 4.1106 3112 155 0.79 26.44 2.03 1.66 3059064.97| | 3: 4.1106 - 3.5910 3000 188 0.82 24.63 2.13 1.94 1936112.07| | 4: 3.5910 - 3.2627 2977 168 0.81 25.88 2.18 2.02 1377840.11| | 5: 3.2627 - 3.0288 2930 152 0.78 28.52 2.16 2.01 1065329.57| | 6: 3.0288 - 2.8502 2844 159 0.76 30.45 2.06 1.97 856549.95| | 7: 2.8502 - 2.7075 2860 139 0.77 30.05 2.04 1.88 690049.30| | 8: 2.7075 - 2.5896 2705 156 0.75 31.56 1.99 1.78 594991.98| | 9: 2.5896 - 2.4899 2715 135 0.72 34.01 1.90 1.74 528160.82| | 10: 2.4899 - 2.4040 2488 115 0.71 35.26 1.94 1.68 488836.19| | 11: 2.4040 - 2.3288 2176 109 0.72 34.25 1.95 1.68 443633.67| | 12: 2.3288 - 2.2623 2018 110 0.73 33.21 1.92 1.64 434086.87| | 13: 2.2623 - 2.2027 1742 104 0.67 39.14 2.01 1.62 524747.84| | 14: 2.2027 - 2.1490 1395 76 0.56 47.31 2.05 1.54 720558.54| |alpha: min = 1.12 max = 2.02 mean = 1.74| |beta: min = 434086.87 max = 4689001.73 mean = 1388851.17| |figures of merit: min = 0.00 max = 1.00 mean = 0.74| |phase err.(work): min = 0.00 max = 89.94 mean = 31.97| |phase err.(test): min = 0.00 max = 89.63 mean = 32.13| |-----------------------------------------------------------------------------| ============================== Outliers rejection ============================= basic_wilson_outliers = 0 extreme_wilson_outliers = 2 beamstop_shadow_outliers = 6 total = 8 ====================== Target weights (before refinement) ===================== |-----------------------------------------------------------------------------| | XYZ refinement: T = Eexperimental * wxc * wxc_scale + Echem * wc | | wxc = 12.037420 wxc_scale = 0.500 wc = 1.000 | | angle between x-ray and geometry gradient vectors: 96.336 (deg) | | | | ADP refinement: T = Eexperimental * wxu * wxu_scale + Eadp * wu | | wxc = 0.231372 wxc_scale = 1.000 wc = 1.000 | | angle between Xray and ADP gradient vectors: 93.656 (deg) | |-----------------------------------------------------------------------------| ----------Initial model statistics (before refinement)---------- |-Geometry statistics: start--------------------------------------------------| | Histogram of deviations from ideal values for | | Bonds | Angles | Nonbonded contacts | | 0.000 - 0.009: 4797 | 0.000 - 2.504: 7924 | 1.486 - 1.828: 2 | | 0.009 - 0.019: 1097 | 2.504 - 5.009: 655 | 1.828 - 2.169: 7 | | 0.019 - 0.028: 284 | 5.009 - 7.513: 145 | 2.169 - 2.511: 30 | | 0.028 - 0.038: 144 | 7.513 - 10.018: 40 | 2.511 - 2.852: 1951 | | 0.038 - 0.047: 61 | 10.018 - 12.522: 8 | 2.852 - 3.193: 3550 | | 0.047 - 0.057: 31 | 12.522 - 15.026: 4 | 3.193 - 3.535: 4858 | | 0.057 - 0.066: 13 | 15.026 - 17.531: 2 | 3.535 - 3.876: 8239 | | 0.066 - 0.076: 3 | 17.531 - 20.035: 0 | 3.876 - 4.217: 8012 | | 0.076 - 0.085: 2 | 20.035 - 22.539: 0 | 4.217 - 4.559: 11917 | | 0.085 - 0.095: 2 | 22.539 - 25.044: 1 | 4.559 - 4.900: 15509 | |-----------------------------------------------------------------------------| |-Geometry statistics: start--------------------------------------------------| | Type | Count | Deviation from ideal | Targets | Target (sum) | | | | rmsd max min | | | | bond | 6434 | 0.012 0.095 0.000 | 0.323 | | | angle | 8779 | 1.693 25.044 0.000 | 0.420 | | | chirality | 905 | 0.089 0.406 0.000 | 0.199 | 0.156 | | planarity | 977 | 0.007 0.154 0.000 | 0.242 | | | dihedral | 2253 | 17.723 113.659 0.001 | 1.614 | | | nonbonded | 6434 | 4.142 4.900 1.486 | 0.255 | | |-----------------------------------------------------------------------------| |-ADP statistics (Wilson B = 25.121)------------------------------------------| | Atom | Number of | Isotropic or equivalent| Anisotropy lmin/max | | type |iso aniso | min max mean | min max mean | | - - - - |- - - - - - -| - - - - - - - - - - - -| - - - - - - - - - - | | all : 6255 0 7.67 118.66 27.52 None None None | | all(noH): 6255 0 7.67 118.66 27.52 None None None | | Sol. : 0 0 None None None None None None | | Mac. : 6255 0 7.67 118.66 27.52 None None None | | Hyd. : 0 0 None None None None None None | | - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - | | Distribution of isotropic (or equivalent) ADP for non-H atoms: | | Bin# value range #atoms | Bin# value range #atoms | | 0: 7.670 - 18.769: 1649 | 5: 63.165 - 74.264: 119 | | 1: 18.769 - 29.868: 2973 | 6: 74.264 - 85.363: 80 | | 2: 29.868 - 40.967: 840 | 7: 85.363 - 96.462: 50 | | 3: 40.967 - 52.066: 296 | 8: 96.462 - 107.561: 28 | | 4: 52.066 - 63.165: 198 | 9: 107.561 - 118.660: 22 | | =>continue=> | |-----------------------------------------------------------------------------| |-Occupancies statistics------------------------------------------------------| | occupancies: max = 1.00 min = 0.47 number of occupancies < 0.1 = 0 | |-----------------------------------------------------------------------------| *********************** REFINEMENT MACRO_CYCLE 1 OF 3 ************************* |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.3243 r_free= 0.3131 ksol= 0.00 Bsol= 0.00 scale= 1.698 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (0.00,0.00,0.00,0.00,0.00,0.00); trace/3= 0.00 | | | | maximum likelihood estimate for coordinate error: 0.40 A | | x-ray target function (ml) for work reflections: 7.754289 | |-----------------------------------------------------------------------------| ====================== bulk solvent modeling and scaling ====================== |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.2582 r_free= 0.2742 ksol= 0.35 Bsol= 50.00 scale= 2.164 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (2.32,2.32,2.32,0.00,0.00,-0.00); trace/3= 2.32 | | | | maximum likelihood estimate for coordinate error: 0.39 A | | x-ray target function (ml) for work reflections: 7.690252 | |-----------------------------------------------------------------------------| ========================== Target weights: x-ray data ========================= |-----------------------------------------------------------------------------| | XYZ refinement: T = Eexperimental * wxc * wxc_scale + Echem * wc | | wxc = 10.750300 wxc_scale = 0.500 wc = 1.000 | | angle between x-ray and geometry gradient vectors: 96.207 (deg) | | | | ADP refinement: T = Eexperimental * wxu * wxu_scale + Eadp * wu | | wxc = 0.205411 wxc_scale = 1.000 wc = 1.000 | | angle between Xray and ADP gradient vectors: 94.015 (deg) | |-----------------------------------------------------------------------------| ================================ xyz refinement =============================== |-LBFGS minimization----------------------------------------------------------| | start r-factor (work) = 0.2582 final r-factor (work) = 0.2348 | | start r-factor (free) = 0.2742 final r-factor (free) = 0.2713 | |-----------------------------------------------------------------------------| | T_start = wxc * wxc_scale * Exray + wc * Echem | | 42.5209 = 10.75 * 0.50 * 7.7632 + 1.00 * 0.7926 | | | | T_final = wxc * wxc_scale * Exray + wc * Echem | | 41.1803 = 10.75 * 0.50 * 7.6326 + 1.00 * 0.1541 | |-----------------------------------------------------------------------------| | number of iterations = 25 | number of function evaluations = 26 | |-----------------------------------------------------------------------------| ================================ ADP refinement =============================== ----------Individual ADP refinement---------- |-LBFGS minimization----------------------------------------------------------| | start r-factor (work) = 0.2348 final r-factor (work) = 0.2216 | | start r-factor (free) = 0.2713 final r-factor (free) = 0.2676 | |-----------------------------------------------------------------------------| | T_start = wxu * wxu_scale * Exray + wu * Eadp | | 1.5745 = 0.21 * 1.00 * 7.6326 + 1.00 * 0.0067 | | | | T_final = wxu * wxu_scale * Exray + wu * Eadp | | 1.5631 = 0.21 * 1.00 * 7.5874 + 1.00 * 0.0045 | |-----------------------------------------------------------------------------| | number of iterations = 23 | number of function evaluations = 24 | |-----------------------------------------------------------------------------| |-ADP statistics (Wilson B = 25.121)------------------------------------------| | Atom | Number of | Isotropic or equivalent| Anisotropy lmin/max | | type |iso aniso | min max mean | min max mean | | - - - - |- - - - - - -| - - - - - - - - - - - -| - - - - - - - - - - | | all : 6255 0 0.00 117.10 26.33 None None None | | all(noH): 6255 0 0.00 117.10 26.33 None None None | | Sol. : 0 0 None None None None None None | | Mac. : 6255 0 0.00 117.10 26.33 None None None | | Hyd. : 0 0 None None None None None None | | - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - | | Distribution of isotropic (or equivalent) ADP for non-H atoms: | | Bin# value range #atoms | Bin# value range #atoms | | 0: 0.000 - 11.710: 203 | 5: 58.550 - 70.260: 136 | | 1: 11.710 - 23.420: 3284 | 6: 70.260 - 81.969: 72 | | 2: 23.420 - 35.130: 1811 | 7: 81.969 - 93.679: 42 | | 3: 35.130 - 46.840: 395 | 8: 93.679 - 105.389: 25 | | 4: 46.840 - 58.550: 266 | 9: 105.389 - 117.099: 21 | | =>continue=> | |-----------------------------------------------------------------------------| *********************** REFINEMENT MACRO_CYCLE 2 OF 3 ************************* |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.2216 r_free= 0.2676 ksol= 0.35 Bsol= 50.00 scale= 2.155 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (2.32,2.32,2.32,0.00,0.00,-0.00); trace/3= 2.32 | | | | maximum likelihood estimate for coordinate error: 0.37 A | | x-ray target function (ml) for work reflections: 7.578854 | |-----------------------------------------------------------------------------| ================== ordered solvent: location/analysis/update ================== Start model: number = 0 b_iso_min = None (limit = 1.00) b_iso_max = None (limit = 50.00) b_iso_mean = None occupancy_min = None (limit = 0.10) occupancy_max = None (limit = 1.20) dist_sol_mol_min = None (limit = 1.80) dist_sol_mol_max = None (limit = 6.00) Peak search: maximum allowed number of peaks: 6250 number of peaks from mFobs-DFmodel map: 449 number of peaks from 2mFobs-DFmodel map: 2500 number of peaks after clustering: 392 Filter by distance & map next to the model: mapped sites are within: 0.520 - 5.987 number of sites selected in [dist_min= 1.80, dist_max= 6.00]: 291 from: 392 mapped sites are within: 1.816 - 5.987 Peak filtering (peak - peak close contact elimination): peaks rejected: 0 total number of peaks selected: 291 Final model: number = 291 b_iso_min = 26.33 (limit = 1.00) b_iso_max = 26.33 (limit = 50.00) b_iso_mean = 26.33 occupancy_min = 1.00 (limit = 0.10) occupancy_max = 1.00 (limit = 1.20) dist_sol_mol_min = 1.82 (limit = 1.80) dist_sol_mol_max = 5.99 (limit = 6.00) ====================== bulk solvent modeling and scaling ====================== |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.2037 r_free= 0.2379 ksol= 0.34 Bsol= 50.00 scale= 2.123 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (2.43,2.43,2.43,0.00,0.00,-0.00); trace/3= 2.43 | | | | maximum likelihood estimate for coordinate error: 0.32 A | | x-ray target function (ml) for work reflections: 7.486761 | |-----------------------------------------------------------------------------| ========================== Target weights: x-ray data ========================= |-----------------------------------------------------------------------------| | XYZ refinement: T = Eexperimental * wxc * wxc_scale + Echem * wc | | wxc = 6.888030 wxc_scale = 0.500 wc = 1.000 | | angle between x-ray and geometry gradient vectors: 121.803 (deg) | | | | ADP refinement: T = Eexperimental * wxu * wxu_scale + Eadp * wu | | wxc = 0.171233 wxc_scale = 1.000 wc = 1.000 | | angle between Xray and ADP gradient vectors: 117.753 (deg) | |-----------------------------------------------------------------------------| ================================ xyz refinement =============================== |-LBFGS minimization----------------------------------------------------------| | start r-factor (work) = 0.2037 final r-factor (work) = 0.1944 | | start r-factor (free) = 0.2379 final r-factor (free) = 0.2423 | |-----------------------------------------------------------------------------| | T_start = wxc * wxc_scale * Exray + wc * Echem | | 26.1593 = 6.89 * 0.50 * 7.5465 + 1.00 * 0.1690 | | | | T_final = wxc * wxc_scale * Exray + wc * Echem | | 25.8504 = 6.89 * 0.50 * 7.4673 + 1.00 * 0.1330 | |-----------------------------------------------------------------------------| | number of iterations = 25 | number of function evaluations = 27 | |-----------------------------------------------------------------------------| ================================ ADP refinement =============================== ----------Individual ADP refinement---------- |-LBFGS minimization----------------------------------------------------------| | start r-factor (work) = 0.1944 final r-factor (work) = 0.1882 | | start r-factor (free) = 0.2423 final r-factor (free) = 0.2396 | |-----------------------------------------------------------------------------| | T_start = wxu * wxu_scale * Exray + wu * Eadp | | 1.2834 = 0.17 * 1.00 * 7.4673 + 1.00 * 0.0047 | | | | T_final = wxu * wxu_scale * Exray + wu * Eadp | | 1.2813 = 0.17 * 1.00 * 7.4563 + 1.00 * 0.0045 | |-----------------------------------------------------------------------------| | number of iterations = 18 | number of function evaluations = 19 | |-----------------------------------------------------------------------------| |-ADP statistics (Wilson B = 25.121)------------------------------------------| | Atom | Number of | Isotropic or equivalent| Anisotropy lmin/max | | type |iso aniso | min max mean | min max mean | | - - - - |- - - - - - -| - - - - - - - - - - - -| - - - - - - - - - - | | all : 6546 0 2.33 119.19 25.98 None None None | | all(noH): 6546 0 2.33 119.19 25.98 None None None | | Sol. : 291 0 3.23 59.44 29.93 None None None | | Mac. : 6255 0 2.33 119.19 25.79 None None None | | Hyd. : 0 0 None None None None None None | | - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - | | Distribution of isotropic (or equivalent) ADP for non-H atoms: | | Bin# value range #atoms | Bin# value range #atoms | | 0: 2.330 - 14.016: 627 | 5: 60.762 - 72.449: 124 | | 1: 14.016 - 25.703: 3737 | 6: 72.449 - 84.135: 75 | | 2: 25.703 - 37.389: 1297 | 7: 84.135 - 95.822: 35 | | 3: 37.389 - 49.076: 396 | 8: 95.822 - 107.508: 18 | | 4: 49.076 - 60.762: 219 | 9: 107.508 - 119.195: 18 | | =>continue=> | |-----------------------------------------------------------------------------| *********************** REFINEMENT MACRO_CYCLE 3 OF 3 ************************* |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.1882 r_free= 0.2396 ksol= 0.34 Bsol= 50.00 scale= 2.114 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (2.43,2.43,2.43,0.00,0.00,-0.00); trace/3= 2.43 | | | | maximum likelihood estimate for coordinate error: 0.33 A | | x-ray target function (ml) for work reflections: 7.449879 | |-----------------------------------------------------------------------------| ================== ordered solvent: location/analysis/update ================== Start model: number = 291 b_iso_min = 3.23 (limit = 1.00) b_iso_max = 59.44 (limit = 50.00) b_iso_mean = 29.93 occupancy_min = 1.00 (limit = 0.10) occupancy_max = 1.00 (limit = 1.20) dist_sol_mol_min = 2.06 (limit = 1.80) dist_sol_mol_max = 5.96 (limit = 6.00) Peak search: maximum allowed number of peaks: 6250 number of peaks from mFobs-DFmodel map: 420 number of peaks from 2mFobs-DFmodel map: 2405 number of peaks after clustering: 300 Filter by distance & map next to the model: mapped sites are within: 0.214 - 5.940 number of sites selected in [dist_min= 1.80, dist_max= 6.00]: 118 from: 300 mapped sites are within: 1.802 - 5.940 Peak filtering (peak - peak close contact elimination): peaks rejected: 0 total number of peaks selected: 118 Final model: number = 398 b_iso_min = 3.23 (limit = 1.00) b_iso_max = 49.81 (limit = 50.00) b_iso_mean = 28.22 occupancy_min = 1.00 (limit = 0.10) occupancy_max = 1.00 (limit = 1.20) dist_sol_mol_min = 1.80 (limit = 1.80) dist_sol_mol_max = 5.96 (limit = 6.00) ====================== bulk solvent modeling and scaling ====================== |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.1875 r_free= 0.2312 ksol= 0.33 Bsol= 50.00 scale= 2.126 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (3.18,3.18,3.18,0.00,0.00,-0.00); trace/3= 3.18 | | | | maximum likelihood estimate for coordinate error: 0.31 A | | x-ray target function (ml) for work reflections: 7.433926 | |-----------------------------------------------------------------------------| ========================== Target weights: x-ray data ========================= |-----------------------------------------------------------------------------| | XYZ refinement: T = Eexperimental * wxc * wxc_scale + Echem * wc | | wxc = 4.792070 wxc_scale = 0.500 wc = 1.000 | | angle between x-ray and geometry gradient vectors: 137.678 (deg) | | | | ADP refinement: T = Eexperimental * wxu * wxu_scale + Eadp * wu | | wxc = 0.173077 wxc_scale = 1.000 wc = 1.000 | | angle between Xray and ADP gradient vectors: 129.742 (deg) | |-----------------------------------------------------------------------------| ================================ xyz refinement =============================== |-LBFGS minimization----------------------------------------------------------| | start r-factor (work) = 0.1875 final r-factor (work) = 0.1857 | | start r-factor (free) = 0.2312 final r-factor (free) = 0.2341 | |-----------------------------------------------------------------------------| | T_start = wxc * wxc_scale * Exray + wc * Echem | | 18.0062 = 4.79 * 0.50 * 7.4550 + 1.00 * 0.1437 | | | | T_final = wxc * wxc_scale * Exray + wc * Echem | | 17.9146 = 4.79 * 0.50 * 7.4304 + 1.00 * 0.1110 | |-----------------------------------------------------------------------------| | number of iterations = 25 | number of function evaluations = 27 | |-----------------------------------------------------------------------------| ================================ ADP refinement =============================== ----------Individual ADP refinement---------- |-LBFGS minimization----------------------------------------------------------| | start r-factor (work) = 0.1857 final r-factor (work) = 0.1818 | | start r-factor (free) = 0.2341 final r-factor (free) = 0.2331 | |-----------------------------------------------------------------------------| | T_start = wxu * wxu_scale * Exray + wu * Eadp | | 1.2906 = 0.17 * 1.00 * 7.4304 + 1.00 * 0.0046 | | | | T_final = wxu * wxu_scale * Exray + wu * Eadp | | 1.2897 = 0.17 * 1.00 * 7.4228 + 1.00 * 0.0050 | |-----------------------------------------------------------------------------| | number of iterations = 9 | number of function evaluations = 9 | |-----------------------------------------------------------------------------| |-ADP statistics (Wilson B = 25.121)------------------------------------------| | Atom | Number of | Isotropic or equivalent| Anisotropy lmin/max | | type |iso aniso | min max mean | min max mean | | - - - - |- - - - - - -| - - - - - - - - - - - -| - - - - - - - - - - | | all : 6653 0 0.00 118.91 25.71 None None None | | all(noH): 6653 0 0.00 118.91 25.71 None None None | | Sol. : 398 0 0.00 55.54 31.76 None None None | | Mac. : 6255 0 2.01 118.91 25.32 None None None | | Hyd. : 0 0 None None None None None None | | - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - | | Distribution of isotropic (or equivalent) ADP for non-H atoms: | | Bin# value range #atoms | Bin# value range #atoms | | 0: 0.000 - 11.891: 364 | 5: 59.455 - 71.345: 131 | | 1: 11.891 - 23.782: 3643 | 6: 71.345 - 83.236: 75 | | 2: 23.782 - 35.673: 1625 | 7: 83.236 - 95.127: 43 | | 3: 35.673 - 47.564: 492 | 8: 95.127 - 107.018: 20 | | 4: 47.564 - 59.455: 243 | 9: 107.018 - 118.909: 17 | | =>continue=> | |-----------------------------------------------------------------------------| ======================= ordered solvent: final clean up ======================= Start model: number = 398 b_iso_min = 0.00 (limit = 1.00) b_iso_max = 55.54 (limit = 50.00) b_iso_mean = 31.76 occupancy_min = 1.00 (limit = 0.10) occupancy_max = 1.00 (limit = 1.20) dist_sol_mol_min = 2.05 (limit = 1.80) dist_sol_mol_max = 5.96 (limit = 6.00) Final model: number = 388 b_iso_min = 3.51 (limit = 1.00) b_iso_max = 49.97 (limit = 50.00) b_iso_mean = 31.36 occupancy_min = 1.00 (limit = 0.10) occupancy_max = 1.00 (limit = 1.20) dist_sol_mol_min = 2.05 (limit = 1.80) dist_sol_mol_max = 5.96 (limit = 6.00) ----------X-ray data---------- |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.1831 r_free= 0.2329 ksol= 0.33 Bsol= 50.00 scale= 2.114 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (3.18,3.18,3.18,0.00,0.00,-0.00); trace/3= 3.18 | | | | maximum likelihood estimate for coordinate error: 0.32 A | | x-ray target function (ml) for work reflections: 7.422958 | |-----------------------------------------------------------------------------| |-----------------------------------------------------------------------------| | Bin Resolution Compl. No. Refl. R-factors Targets | |number range work test work test work test| | 1: 75.6707 - 5.1788 0.97 3272 159 0.2130 0.2552 8.1276 8.228| | 2: 5.1788 - 4.1106 0.98 3112 155 0.1356 0.1644 7.8761 8.0672| | 3: 4.1106 - 3.5910 0.97 3000 188 0.1468 0.1750 7.7387 7.8215| | 4: 3.5910 - 3.2627 0.97 2977 168 0.1558 0.1979 7.5865 7.8088| | 5: 3.2627 - 3.0288 0.95 2930 152 0.1709 0.2266 7.4557 7.5858| | 6: 3.0288 - 2.8502 0.93 2844 159 0.1755 0.2362 7.2991 7.4461| | 7: 2.8502 - 2.7075 0.93 2860 139 0.1762 0.2620 7.2285 7.4876| | 8: 2.7075 - 2.5896 0.89 2705 156 0.1910 0.2717 7.1596 7.3038| | 9: 2.5896 - 2.4899 0.89 2715 135 0.2060 0.2556 7.0999 7.3902| | 10: 2.4899 - 2.4040 0.81 2488 115 0.2115 0.3023 7.0774 7.2784| | 11: 2.4040 - 2.3288 0.72 2176 109 0.2299 0.3153 7.0902 7.1912| | 12: 2.3288 - 2.2623 0.67 2018 110 0.2312 0.2806 7.1132 7.2823| | 13: 2.2623 - 2.2027 0.58 1742 104 0.2705 0.3734 7.181 7.532| | 14: 2.2027 - 2.1490 0.46 1395 76 0.3164 0.3752 7.339 7.432| |-----------------------------------------------------------------------------| |-----------------------------------------------------------------------------| |R-free likelihood based estimates for figures of merit, absolute phase error,| |and distribution parameters alpha and beta (Acta Cryst. (1995). A51, 880-887)| | | | Bin Resolution No. Refl. FOM Phase Scale Alpha Beta | | # range work test error factor | | 1: 75.6707 - 5.1788 3272 159 0.84 21.52 2.03 1.91 1706271.76| | 2: 5.1788 - 4.1106 3112 155 0.92 13.72 2.19 2.12 1119490.86| | 3: 4.1106 - 3.5910 3000 188 0.90 16.33 2.16 2.10 948218.23| | 4: 3.5910 - 3.2627 2977 168 0.88 18.25 2.15 2.06 723060.91| | 5: 3.2627 - 3.0288 2930 152 0.86 20.64 2.12 2.04 602696.08| | 6: 3.0288 - 2.8502 2844 159 0.85 21.95 2.09 2.03 469088.14| | 7: 2.8502 - 2.7075 2860 139 0.84 22.75 2.07 2.01 423879.11| | 8: 2.7075 - 2.5896 2705 156 0.83 23.91 2.02 1.89 364459.47| | 9: 2.5896 - 2.4899 2715 135 0.80 26.95 1.96 1.80 333699.76| | 10: 2.4899 - 2.4040 2488 115 0.80 26.92 1.99 1.83 318772.98| | 11: 2.4040 - 2.3288 2176 109 0.80 27.04 2.01 1.79 305463.63| | 12: 2.3288 - 2.2623 2018 110 0.81 26.41 2.04 1.78 298736.36| | 13: 2.2623 - 2.2027 1742 104 0.76 30.75 2.14 1.86 366985.74| | 14: 2.2027 - 2.1490 1395 76 0.63 41.90 2.25 1.80 624233.56| |alpha: min = 1.78 max = 2.12 mean = 1.95| |beta: min = 298736.36 max = 1706271.76 mean = 657914.19| |figures of merit: min = 0.00 max = 1.00 mean = 0.84| |phase err.(work): min = 0.00 max = 90.00 mean = 23.00| |phase err.(test): min = 0.00 max = 89.39 mean = 23.30| |-----------------------------------------------------------------------------| ====================== bulk solvent modeling and scaling ====================== |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.1826 r_free= 0.2324 ksol= 0.34 Bsol= 65.65 scale= 2.111 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (0.00,0.00,0.00,0.00,0.00,-0.00); trace/3= 0.00 | | | | maximum likelihood estimate for coordinate error: 0.32 A | | x-ray target function (ml) for work reflections: 7.421608 | |-----------------------------------------------------------------------------| ----------X-ray data---------- |--(resolution: 2.15 - 75.62 A; n_refl. = 38159)------------------------------| | | | r_work= 0.1826 r_free= 0.2324 ksol= 0.34 Bsol= 65.65 scale= 2.111 | | | | overall anisotropic scale matrix (Cartesian basis; B11,B22,B33,B12,B13,B23):| | (0.00,0.00,0.00,0.00,0.00,-0.00); trace/3= 0.00 | | | | maximum likelihood estimate for coordinate error: 0.32 A | | x-ray target function (ml) for work reflections: 7.421608 | |-----------------------------------------------------------------------------| |-----------------------------------------------------------------------------| | Bin Resolution Compl. No. Refl. R-factors Targets | |number range work test work test work test| | 1: 75.6707 - 5.1788 0.97 3272 159 0.2125 0.2562 8.1276 8.23| | 2: 5.1788 - 4.1106 0.98 3112 155 0.1356 0.1646 7.8765 8.0679| | 3: 4.1106 - 3.5910 0.97 3000 188 0.1471 0.1753 7.7395 7.8223| | 4: 3.5910 - 3.2627 0.97 2977 168 0.1557 0.1975 7.5862 7.8097| | 5: 3.2627 - 3.0288 0.95 2930 152 0.1700 0.2270 7.4544 7.5859| | 6: 3.0288 - 2.8502 0.93 2844 159 0.1744 0.2359 7.2964 7.4451| | 7: 2.8502 - 2.7075 0.93 2860 139 0.1754 0.2619 7.227 7.4839| | 8: 2.7075 - 2.5896 0.89 2705 156 0.1902 0.2712 7.1561 7.3014| | 9: 2.5896 - 2.4899 0.89 2715 135 0.2054 0.2548 7.0962 7.3838| | 10: 2.4899 - 2.4040 0.81 2488 115 0.2109 0.3026 7.0744 7.2786| | 11: 2.4040 - 2.3288 0.72 2176 109 0.2295 0.3132 7.088 7.1878| | 12: 2.3288 - 2.2623 0.67 2018 110 0.2309 0.2813 7.112 7.2824| | 13: 2.2623 - 2.2027 0.58 1742 104 0.2704 0.3724 7.1801 7.5313| | 14: 2.2027 - 2.1490 0.46 1395 76 0.3163 0.3749 7.3386 7.432| |-----------------------------------------------------------------------------| |-----------------------------------------------------------------------------| |R-free likelihood based estimates for figures of merit, absolute phase error,| |and distribution parameters alpha and beta (Acta Cryst. (1995). A51, 880-887)| | | | Bin Resolution No. Refl. FOM Phase Scale Alpha Beta | | # range work test error factor | | 1: 75.6707 - 5.1788 3272 159 0.83 21.68 2.02 1.90 1729678.56| | 2: 5.1788 - 4.1106 3112 155 0.92 13.76 2.19 2.11 1122862.76| | 3: 4.1106 - 3.5910 3000 188 0.90 16.38 2.16 2.10 950321.91| | 4: 3.5910 - 3.2627 2977 168 0.88 18.29 2.16 2.07 725331.21| | 5: 3.2627 - 3.0288 2930 152 0.86 20.71 2.13 2.04 606450.12| | 6: 3.0288 - 2.8502 2844 159 0.85 22.01 2.10 2.04 469766.50| | 7: 2.8502 - 2.7075 2860 139 0.84 22.78 2.08 2.02 424394.38| | 8: 2.7075 - 2.5896 2705 156 0.83 23.83 2.03 1.89 361907.39| | 9: 2.5896 - 2.4899 2715 135 0.80 26.81 1.97 1.81 330530.78| | 10: 2.4899 - 2.4040 2488 115 0.80 26.80 1.99 1.84 316100.00| | 11: 2.4040 - 2.3288 2176 109 0.80 26.93 2.01 1.80 303267.90| | 12: 2.3288 - 2.2623 2018 110 0.81 26.36 2.05 1.79 297871.94| | 13: 2.2623 - 2.2027 1742 104 0.76 30.68 2.15 1.87 365788.30| | 14: 2.2027 - 2.1490 1395 76 0.63 41.83 2.25 1.81 622797.66| |alpha: min = 1.79 max = 2.11 mean = 1.95| |beta: min = 297871.94 max = 1729678.56 mean = 660171.29| |figures of merit: min = 0.00 max = 1.00 mean = 0.84| |phase err.(work): min = 0.00 max = 89.91 mean = 23.00| |phase err.(test): min = 0.00 max = 89.92 mean = 23.31| |-----------------------------------------------------------------------------| |-ADP statistics (Wilson B = 25.121)------------------------------------------| | Atom | Number of | Isotropic or equivalent| Anisotropy lmin/max | | type |iso aniso | min max mean | min max mean | | - - - - |- - - - - - -| - - - - - - - - - - - -| - - - - - - - - - - | | all : 6643 0 5.23 122.12 28.89 None None None | | all(noH): 6643 0 5.23 122.12 28.89 None None None | | Sol. : 388 0 6.73 53.19 34.57 None None None | | Mac. : 6255 0 5.23 122.12 28.54 None None None | | Hyd. : 0 0 None None None None None None | | - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - | | Distribution of isotropic (or equivalent) ADP for non-H atoms: | | Bin# value range #atoms | Bin# value range #atoms | | 0: 5.229 - 16.918: 693 | 5: 63.676 - 75.366: 120 | | 1: 16.918 - 28.608: 3694 | 6: 75.366 - 87.055: 73 | | 2: 28.608 - 40.297: 1313 | 7: 87.055 - 98.744: 43 | | 3: 40.297 - 51.987: 450 | 8: 98.744 - 110.434: 19 | | 4: 51.987 - 63.676: 221 | 9: 110.434 - 122.123: 17 | | =>continue=> | |-----------------------------------------------------------------------------| ================= overall refinement statistics: step by step ================= ****************** REFINEMENT STATISTICS STEP BY STEP ****************** leading digit, like 1_, means number of macro-cycle 0 : statistics at the very beginning when nothing is done yet 1_bss: bulk solvent correction and/or (anisotropic) scaling 1_xyz: refinement of coordinates 1_adp: refinement of ADPs (Atomic Displacement Parameters) 1_wat: ordered solvent update (add / remove) ------------------------------------------------------------------------ R-factors, x-ray target values and norm of gradient of x-ray target stage r-work r-free xray_target_w xray_target_t 0 : 0.3243 0.3131 7.754289e+00 7.797944e+00 1_bss: 0.2582 0.2742 7.690252e+00 7.754360e+00 1_xyz: 0.2348 0.2713 7.623999e+00 7.734510e+00 1_adp: 0.2216 0.2676 7.578854e+00 7.714267e+00 2_bss: 0.2037 0.2379 7.486761e+00 7.615026e+00 2_xyz: 0.1944 0.2423 7.473436e+00 7.629683e+00 2_adp: 0.1882 0.2396 7.449879e+00 7.620893e+00 3_bss: 0.1875 0.2312 7.433926e+00 7.596287e+00 3_xyz: 0.1857 0.2341 7.435421e+00 7.607941e+00 3_adp: 0.1818 0.2331 7.418785e+00 7.599553e+00 3_bss: 0.1826 0.2324 7.421608e+00 7.597030e+00 ------------------------------------------------------------------------ stage k_sol b_sol b11 b22 b33 b12 b13 b23 0 : 0.000 0.000 0.000 0.000 0.000 0.000 0.000 0.000 1_bss: 0.347 50.000 2.318 2.318 2.318 0.000 0.000 -0.000 1_xyz: 0.347 50.000 2.318 2.318 2.318 0.000 0.000 -0.000 1_adp: 0.347 50.000 2.318 2.318 2.318 0.000 0.000 -0.000 2_bss: 0.337 50.000 2.425 2.425 2.425 0.000 0.000 -0.000 2_xyz: 0.337 50.000 2.425 2.425 2.425 0.000 0.000 -0.000 2_adp: 0.337 50.000 2.425 2.425 2.425 0.000 0.000 -0.000 3_bss: 0.335 50.000 3.181 3.181 3.181 0.000 0.000 -0.000 3_xyz: 0.335 50.000 3.181 3.181 3.181 0.000 0.000 -0.000 3_adp: 0.335 50.000 3.181 3.181 3.181 0.000 0.000 -0.000 3_bss: 0.337 65.653 0.000 0.000 0.000 0.000 0.000 -0.000 ------------------------------------------------------------------------ stage <pher> fom alpha beta 0 : 31.982 0.7396 1.7443 1387840.945 1_bss: 29.194 0.7699 1.9599 974799.679 1_xyz: 28.118 0.7819 1.9866 928279.367 1_adp: 27.348 0.7902 1.9633 892955.282 2_bss: 24.199 0.8225 1.9720 689127.593 2_xyz: 24.569 0.8186 1.9572 710017.017 2_adp: 23.913 0.8260 1.9393 697946.465 3_bss: 23.043 0.8347 1.9776 647848.901 3_xyz: 23.264 0.8326 1.9689 664228.536 3_adp: 22.951 0.8359 1.9502 655975.202 3_bss: 23.013 0.8352 1.9517 659994.149 ------------------------------------------------------------------------ stage angl bond chir dihe plan repu geom_target 0 : 1.693 0.012 0.089 17.723 0.007 4.142 1.5608e-01 1_bss: 1.693 0.012 0.089 17.723 0.007 4.142 1.5608e-01 1_xyz: 1.635 0.010 0.087 18.407 0.008 4.141 1.4451e-01 1_adp: 1.635 0.010 0.087 18.407 0.008 4.141 1.4451e-01 2_bss: 1.635 0.010 0.087 18.407 0.008 4.135 1.6105e-01 2_xyz: 1.421 0.009 0.083 18.369 0.007 4.141 1.2821e-01 2_adp: 1.421 0.009 0.083 18.369 0.007 4.141 1.2821e-01 3_bss: 1.421 0.009 0.083 18.369 0.007 4.136 1.3974e-01 3_xyz: 1.283 0.007 0.075 17.946 0.007 4.138 1.0907e-01 3_adp: 1.283 0.007 0.075 17.946 0.007 4.138 1.0907e-01 3_bss: 1.283 0.007 0.075 17.946 0.007 4.138 1.0822e-01 ------------------------------------------------------------------------ Maximal deviations: stage angl bond chir dihe plan repu |grad| 0 : 25.044 0.095 0.406113.659 0.154 1.486 1.5120e-01 1_bss: 25.044 0.095 0.406113.659 0.154 1.486 1.5120e-01 1_xyz: 25.658 0.089 0.312115.970 0.157 1.921 6.5351e-02 1_adp: 25.658 0.089 0.312115.970 0.157 1.921 6.5351e-02 2_bss: 25.658 0.089 0.312115.970 0.157 1.816 6.3368e-02 2_xyz: 23.516 0.082 0.391119.400 0.155 1.926 4.8056e-02 2_adp: 23.516 0.082 0.391119.400 0.155 1.926 4.8056e-02 3_bss: 23.516 0.082 0.391119.400 0.155 1.802 4.8972e-02 3_xyz: 23.841 0.048 0.338113.663 0.152 1.976 3.4188e-02 3_adp: 23.841 0.048 0.338113.663 0.152 1.976 3.4188e-02 3_bss: 23.841 0.048 0.338113.663 0.152 1.976 3.4255e-02 ------------------------------------------------------------------------ |-----overall-----|---macromolecule----|------solvent-------| stage b_max b_min b_ave b_max b_min b_ave b_max b_min b_ave 0 : 118.66 7.67 27.52 117.10 0.00 26.33 26.33 26.33 26.33 1_bss: 118.66 7.67 27.52 117.10 0.00 26.33 26.33 26.33 26.33 1_xyz: 118.66 7.67 27.52 119.19 2.33 25.79 59.44 3.23 29.93 1_adp: 117.10 0.00 26.33 119.19 2.33 25.79 49.81 3.23 28.22 2_bss: 117.10 0.00 26.33 119.19 2.33 25.79 49.81 3.23 28.22 2_xyz: 117.10 0.00 26.33 118.91 2.01 25.32 55.54 0.00 31.76 2_adp: 119.19 2.33 25.98 122.12 5.23 28.54 53.19 6.73 34.57 ------------------------------------------------------------------------ stage Deviation of refined model from start model max min mean 0 : 0.000 0.000 0.000 1_bss: 0.000 0.000 0.000 1_xyz: 2.308 0.002 0.111 1_adp: 2.308 0.002 0.111 2_bss: 2.308 0.002 0.111 2_xyz: 2.461 0.002 0.117 2_adp: 2.461 0.002 0.117 3_bss: 2.461 0.002 0.117 3_xyz: 2.748 0.003 0.122 3_adp: 2.748 0.003 0.122 3_bss: 2.748 0.003 0.122 ------------------------------------------------------------------------ stage number of ordered solvent 0 : 0 1_bss: 0 1_xyz: 0 1_adp: 0 2_bss: 291 2_xyz: 291 2_adp: 291 3_bss: 398 3_xyz: 398 3_adp: 398 3_bss: 388 ------------------------------------------------------------------------ ===================== NCS restraints at end of refinement ===================== NCS restraint group 1: NCS operator 1: Reference selection: "chain A and (resseq 9:118 or resseq 128:207 or resseq 215:366 )" Other selection: "chain C and (resseq 9:118 or resseq 128:207 or resseq 215:366 )" Number of atom pairs: 2603 Rotation={{-0.999497, -0.0191321, 0.0252909}, {0.0247831, 0.0263321, 0.999346}, {-0.0197855, 0.99947, -0.0258447}} Translation={{38.4881}, {-44.0747}, {42.34}} Histogram of differences: 0.002570 - 0.054938: 2350 0.054938 - 0.107305: 233 0.107305 - 0.159673: 16 0.159673 - 0.212040: 2 0.212040 - 0.264408: 1 0.264408 - 0.316775: 1 RMS difference with respect to the reference: 0.037521 Writing refined structure to PDB file: AutoBuild_run_3_/TEMP0/Build_composite_refined_side_3.pdb n_use = 6643 n_use_u_iso = 6643 n_use_u_aniso = 0 n_grad_site = 0 n_grad_u_iso = 6643 n_grad_u_aniso = 0 n_grad_occupancy = 0 n_grad_fp = 0 n_grad_fdp = 0 n_anisotropic_flag = 0 total number of scatterers = 6643 Writing map coefficients to MTZ file: /usr/users/dale/structure/fmo-ct/tronrud_2007/AutoBuild_run_3_/TEMP0/Build_composite_refined_side_3_001_map_coeffs.mtz Writing refined fmodel to MTZ file: /usr/users/dale/structure/fmo-ct/tronrud_2007/AutoBuild_run_3_/TEMP0/Build_composite_refined_side_3_001_f_model.mtz # Date 2007/12/14 11:38:03 Final R(work) = 0.1826, R(free) = 0.2324

1 0

Re: [phenixbb] Problem with AutoBuild and Alternative Conformations
by Thomas C. Terwilliger 17 Dec '07

17 Dec '07

Hi again Dale, I spoke too quickly...it is not so easy to change the code as I hoped. However here is a work-around that may be preferable anyhow: 1. Remove your ligand from the PDB file to be rebuilt and put it in "lig.pdb" 2. add to your commands for autobuild: input_lig_file_list=lig.pdb This will put all the contents of lig.pdb at the end of all PDB files just before refinement. All the best, Tom T Hi Dale, Your hypothesis: "I suspect that the coder assumed that all alternative conformations mutually exclusive and involve the same subset of the residue." is quite correct. (I am the coder in question). I think that I may be able to fix this particular problem and take care of the cases you have in this structure by simply allowing all conformations of ligands in the input file to be kept during rebuilding. With luck, this will work and will be in the final 1.3b version due out very shortly. The autobuild wizard still will not know how to build multiple conformations into a structure. For the time being it will have to stick with building one conformation. Thanks very much for the suggestion! -Tom T > Hi, > > I desire to resolve a crystal, who's structure factors I've downloaded > from the PDB, using my new high resolution model of this protein from a different species. I have decided to use the AutoMR wizard from Phenix for the chore. The MR seems to work just find, but I've run into a problem with the follow-up AutoBuild. > > This protein has a peptide chain that I would like rebuilt with the > proper amino acid sequence and seven Bchl-a molecules that I would like to be carried through to the end. Since the probe is from a high res refinement it contains quite a few groups with alternative conformations. This is not a problem in the protein part as it is being rebuilt and comes back with a single conformation for each residue. The Bchl-a molecules, however, are being horribly mutilated. > > In the Bchl-a groups, the "A" conformation is being promoted to > be the "main" (and only) conformation and the "B", "C", "D", "E", and, yes, the "F" conformations are lost. A Bchl-a molecule is much larger than an amino acid so it is quite possible, and reasonable, for one part to have a "A" and "B" pair of conformations, another part to have a "C" and "D" pair, and somewhere else for there to be a "E" and "F" pair. When conformation "C", "D", "E", and "F" are discarded whole sections of the Bchl-a molecule disappear > completely. This is bad. > > I suspect that the coder assumed that all alternative conformations > mutually exclusive and involve the same subset of the residue. I would prefer a more careful analysis to uncover the fact that "A" and "B" go together, and "C" and "D" go together. If there is a need to reduce the complexity of the model, (and I would prefer that all the alternatives make it through to the end) could the program keep "A", "C", and "E", or whatever makes sense for any particular residue? Better yet, instead of always keeping the first alternative of a set, could it keep the one with the highest occupancy? > > I'm using phenix-1.3b-rc6 on a Fedora 6 PC. > > Thanks, > Dale Tronrud >

2 1

Re: [phenixbb] Problem with AutoBuild and Alternative Conformations
by Thomas C. Terwilliger 17 Dec '07

17 Dec '07

Hi Dale, Your hypothesis: "I suspect that the coder assumed that all alternative conformations mutually exclusive and involve the same subset of the residue." is quite correct. (I am the coder in question). I think that I may be able to fix this particular problem and take care of the cases you have in this structure by simply allowing all conformations of ligands in the input file to be kept during rebuilding. With luck, this will work and will be in the final 1.3b version due out very shortly. The autobuild wizard still will not know how to build multiple conformations into a structure. For the time being it will have to stick with building one conformation. Thanks very much for the suggestion! -Tom T > Hi, > > I desire to resolve a crystal, who's structure factors I've downloaded > from the PDB, using my new high resolution model of this protein from a > different species. I have decided to use the AutoMR wizard from Phenix > for the chore. The MR seems to work just find, but I've run into a > problem with the follow-up AutoBuild. > > This protein has a peptide chain that I would like rebuilt with the > proper amino acid sequence and seven Bchl-a molecules that I would like > to be carried through to the end. Since the probe is from a high res > refinement it contains quite a few groups with alternative conformations. > This is not a problem in the protein part as it is being rebuilt and > comes back with a single conformation for each residue. The Bchl-a > molecules, however, are being horribly mutilated. > > In the Bchl-a groups, the "A" conformation is being promoted to > be the "main" (and only) conformation and the "B", "C", "D", "E", > and, yes, the "F" conformations are lost. A Bchl-a molecule is much > larger than an amino acid so it is quite possible, and reasonable, > for one part to have a "A" and "B" pair of conformations, another > part to have a "C" and "D" pair, and somewhere else for there to > be a "E" and "F" pair. When conformation "C", "D", "E", and "F" > are discarded whole sections of the Bchl-a molecule disappear > completely. This is bad. > > I suspect that the coder assumed that all alternative conformations > mutually exclusive and involve the same subset of the residue. I > would prefer a more careful analysis to uncover the fact that "A" and > "B" go together, and "C" and "D" go together. If there is a need to > reduce the complexity of the model, (and I would prefer that all the > alternatives make it through to the end) could the program keep "A", > "C", and "E", or whatever makes sense for any particular residue? > Better yet, instead of always keeping the first alternative of a set, > could it keep the one with the highest occupancy? > > I'm using phenix-1.3b-rc6 on a Fedora 6 PC. > > Thanks, > Dale Tronrud >

1 0

[Fwd: Auto-discard notification]
by Paul Adams 17 Dec '07

17 Dec '07

-- Paul Adams Deputy Division Director, Physical Biosciences Division, LBL Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Head, Berkeley Center for Structural Biology Building 64, Room 248 Tel: 510-486-4225, Fax: 510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road, BLDG 64R0121 Berkeley, CA 94720, USA. --

1 0

relative pathnames in .def or .eff files for phenix.refine?
by Schubert, Carsten [PRDUS] 14 Dec '07

14 Dec '07

Hi, would it be possible to add the option of using relative pathnames instead of full pathnames when .def and .eff files are written by phenix.refine? Would make transfer of files/projects easier. Cheers Carsten

1 0

Re: [phenixbb] Very very small Phaser Bug
by Tom Terwilliger 11 Dec '07

11 Dec '07

Hi James, Yes this sounds like a bug to me. I think it is a mis-communication between the automr wizard and phaser. We'll check it out. Thank you! -Tom T At 10:05 PM 12/10/2007, you wrote: >This is a fairly trivial bug, but I thought I'd report it anyway (I'm >not sure whether the problem is with the phenix.automr (rc6 build) or >with all phaser implementations (the one included is: 2.1.1 so I've >emailed both lists): > >when running phaser in data that was scaled in P 31 2 1, I used >phenix.automr to automate MR searches in all spacegroups that are >indistinguishable by systematic absences with: > >phenix.automr template.pdb final_P3121.sca RMS=1 mass=17000 >rebuild_after_mr=False copies=1 use_all_plausible_sg=True > >The program correctly finds the solution in P3221 with a log >likelihood gain of 1000 vs 20 for P3121, everything is fine in the >outputted PDB CRYST1 line and MTZ; however the log file annoyingly >mentions the spacegroup for the last time with "Final space group:P 31 >2 1" even though elsewhere in the log file it correctly lists >"SpaceGroup of Solution: P 32 2 1". I've excerpted the log file >below. If this is the intended behaviour and not a bug, then I >apologize but find it quite counterintuitive. > >Just a small bug, haven't seen if this behaviour occurs in other >systematic absence-equivalent space groups. > >Best, > >jf > >**BEGIN LOG > > SpaceGroup of Solution: P 32 2 1 > > SINGLE solution > > Solution written to PDB file: /Users/jfraser/data/AutoMR_run_7_/MR.1.pd >b > Solution written to MTZ file: /Users/jfraser/data/AutoMR_run_7_/MR.1.mt >z > Solution log-likelihood gain: 1056.73 > Solution annotation (history): RFZ=11.9 TFZ=27.5 PAK=0 LLG=850 LLG=1057 > > > >AUTOMR RUN: 7 > >Files in directory : AutoMR_run_7_ > > > >CRITERIA FOR PHASER MR RUN: >selection_criteria_rot : Percent_of_best >selection_criteria_rot_value : 75 >use_all_plausible_sg : Yes >overlap_allowed : > >List of space groups tested: >['P 3 2 1', 'P 31 2 1', 'P 32 2 1'] > >Final space group:P 31 2 1 > >CURRENT ENSEMBLES: > >ENSEMBLE ID: ensemble_1 >FILE: template.pdb RMS = 1.0 >ENSEMBLES USED IN SEARCH: ensemble_1 > >**************** SOLUTION MR ******* > > Log likelihood gain for solution MR: 1056.7344 > Output PDB files for solution MR: MR.1.pdb > Output MTZ files for solution MR: MR.1.mtz > >**END LOG > > >-- >James Fraser >jamesfraser(a)berkeley.edu >Alber Lab >356 Stanley Hall, QB3 >UC Berkeley >Berkeley, CA 94720 >http://ucxray.berkeley.edu/~jfraser/ >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

Very very small Phaser Bug
by James Fraser 11 Dec '07

11 Dec '07

This is a fairly trivial bug, but I thought I'd report it anyway (I'm not sure whether the problem is with the phenix.automr (rc6 build) or with all phaser implementations (the one included is: 2.1.1 so I've emailed both lists): when running phaser in data that was scaled in P 31 2 1, I used phenix.automr to automate MR searches in all spacegroups that are indistinguishable by systematic absences with: phenix.automr template.pdb final_P3121.sca RMS=1 mass=17000 rebuild_after_mr=False copies=1 use_all_plausible_sg=True The program correctly finds the solution in P3221 with a log likelihood gain of 1000 vs 20 for P3121, everything is fine in the outputted PDB CRYST1 line and MTZ; however the log file annoyingly mentions the spacegroup for the last time with "Final space group:P 31 2 1" even though elsewhere in the log file it correctly lists "SpaceGroup of Solution: P 32 2 1". I've excerpted the log file below. If this is the intended behaviour and not a bug, then I apologize but find it quite counterintuitive. Just a small bug, haven't seen if this behaviour occurs in other systematic absence-equivalent space groups. Best, jf **BEGIN LOG SpaceGroup of Solution: P 32 2 1 SINGLE solution Solution written to PDB file: /Users/jfraser/data/AutoMR_run_7_/MR.1.pd b Solution written to MTZ file: /Users/jfraser/data/AutoMR_run_7_/MR.1.mt z Solution log-likelihood gain: 1056.73 Solution annotation (history): RFZ=11.9 TFZ=27.5 PAK=0 LLG=850 LLG=1057 AUTOMR RUN: 7 Files in directory : AutoMR_run_7_ CRITERIA FOR PHASER MR RUN: selection_criteria_rot : Percent_of_best selection_criteria_rot_value : 75 use_all_plausible_sg : Yes overlap_allowed : List of space groups tested: ['P 3 2 1', 'P 31 2 1', 'P 32 2 1'] Final space group:P 31 2 1 CURRENT ENSEMBLES: ENSEMBLE ID: ensemble_1 FILE: template.pdb RMS = 1.0 ENSEMBLES USED IN SEARCH: ensemble_1 **************** SOLUTION MR ******* Log likelihood gain for solution MR: 1056.7344 Output PDB files for solution MR: MR.1.pdb Output MTZ files for solution MR: MR.1.mtz **END LOG -- James Fraser jamesfraser(a)berkeley.edu Alber Lab 356 Stanley Hall, QB3 UC Berkeley Berkeley, CA 94720 http://ucxray.berkeley.edu/~jfraser/

1 0

automr with muti components (NMR models)
by ming lu 09 Dec '07

09 Dec '07

Hi everyones I am trying automr to solve the structure of my protein. It has three domains, each domain has NMR structure available. So the sequence identity of my search model is 100%. I tried use mutiple components as search models, but I had a hard time to obtain a interpretable solution. Any suggestions on the use of mutiple components as search models? or suggestions on how to use NMR structure as search models? Thanks for your help. Ming

3 3

Can geometry restraints include non-ideal target values?
by Joe Krahn 07 Dec '07

07 Dec '07

I see that phenix is using the same kind of simplistic statistical restraints as CCP4. Are there plans to improve the geometry restraints once the rest of phenix is stable? The problem with simple statistical restraints as used by CCP4 is that they completely ignore correlations due to interactions of multiple restraints. This is particularly bad for puckered rings like proline and nucleic acids. Nucleic acids get around this by using a fixed sugar pucker, which results in a lot of bad geometries for non-helical nucleic acids (many of which make it in to the PDB). However, if you consider the geometries "ideal value" and "ideal value esd" as just another way to write a harmonic restraint, then it is possible to make an improved restraint library. In this case, some individual geometry restraints will have target values that restrain towards non-ideal values in order to produce the correct result when all terms are combined. The problem is that these terms will give higher RMSD values, which would probably confuse software like REFMAC, which is designed to tweak restraint weights based on RMSDs. So, does phenix have any built-in restraint adjustments that is based on current rmsds? If so, is there a way to disable it? Joe Krahn

3 4

Hydrogens of ligands generated in elbow explode in coot realspace refinement
by Schubert, Carsten [PRDUS] 06 Dec '07

06 Dec '07

Hi, when I refine a ligand with hydrogens in coot using realspace refinement, the hydrogens explode into the surrounding density. This only happens with ligand/cif files generated in elbow and not libcheck. Coot apparently needs and additional loop in the .cif file: _chem_comp_tree.xxxx, which is missing from the elbow output. Unfortunately the geometry generated by libcheck is pretty dismal, so I can probably get around this by running libcheck on the refined coords from elbow ... Nigel, is it possible to fix elbow for the next rc? PS I am running the latest phenix (rc6) and coot 0.33 if that helps. Cheers Carsten

2 1

Question about adding hydrogrens with reduce -- parameters for phenix.refine
by Schubert, Carsten [PRDUS] 06 Dec '07

06 Dec '07

Hi I am trying to generate a model with all hydrogens placed using reduce. To my surprise it only applies hydrogens to a selected few residues. How do I coax reduce to add ALL hydrogens to my model, according to the Richardson Lab paper this should be possible? The help from reduce was not helpful in that regard. Or is adding all hydrogens a bad idea? Along those lines. If I would use another tool to generate the hydrogens, like CNS(X) or Maeastro, how compatible are the parameter files? Thanks for any input Carsten

3 4

Re: [phenixbb] Forcing autobuild wizard to do a complete rebuild
by Tom Terwilliger 03 Dec '07

03 Dec '07

Hi Carsten, Yes, I see this is unclear. All commands listed at the end of the documentation for each wizard can be applied at the command line. (Not just the ones labelled command-line only). All the best, Tom T At 11:15 AM 12/3/2007, you wrote: >Thanks Tom, Peter > >As a follow-up question, which may have been addressed in the >manual, but I don't recall seeing it: Does the (wizard) command line >accept ALL keywords under the autobuild/autosol scope or ONLY the >ones listed as "command-line-only"? I assumed (wrongfully?) that the >command line only accepts the keywords explicitely listed under >"command-line-only", and the rest is reserved for scripts/input files. > >I know, I could test this out, but a general clarification by the >experts and an addition to the manual, if necessary, would be great. > >Cheers, > > Carsten > > > > > -----Original Message----- > > From: phenixbb-bounces(a)phenix-online.org > > [mailto:[email protected]]On Behalf Of Tom > > Terwilliger > > Sent: Monday, December 03, 2007 12:59 PM > > To: PHENIX user mailing list > > Subject: Re: [phenixbb] Forcing autobuild wizard to do a complete > > rebuild > > > > > > Hi Carsten, > > > > You can tell the autobuild wizard from the command line: > > > > rebuild_in_place=False > > > > You can also set this in the GUI on the 2nd input screen at the top > > of the screen. > > > > I hope that helps! > > -Tom T > > > > At 10:17 AM 12/3/2007, you wrote: > > >Content-class: urn:content-classes:message > > >Content-Type: multipart/alternative; > > > boundary="----_=_NextPart_001_01C835D0.68A40BB9" > > > > > >Hi, > > > > > >I am using the autobuild wizard in the latest phenix release to > > >rebuild a model from a MR solution. Since the MR-template I used > > >has been modified with chainsaw, its sequence identity to the target > > >sequence is fairly high. The autobuild wizard therefore uses the > > >rebuilt-in-place mode to rebuild the model. How can I force the > > >wizard to do a complete rebuild? > > > > > >Thanks > > > > > > Carsten > > >_______________________________________________ > > >phenixbb mailing list > > >phenixbb(a)phenix-online.org > > >http://www.phenix-online.org/mailman/listinfo/phenixbb > > > > > > > > > > Thomas C. Terwilliger > > Mail Stop M888 > > Los Alamos National Laboratory > > Los Alamos, NM 87545 > > > > Tel: 505-667-0072 email: terwilliger(a)LANL.gov > > Fax: 505-665-3024 SOLVE web site: >http://solve.lanl.gov >PHENIX web site: http:www.phenix-online.org >ISFI Integrated Center for Structure and Function Innovation web >site: http://techcenter.mbi.ucla.edu >TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB > > >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb > > >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

Re: [phenixbb] Forcing autobuild wizard to do a complete rebuild
by Tom Terwilliger 03 Dec '07

03 Dec '07

Hi Carsten, You can tell the autobuild wizard from the command line: rebuild_in_place=False You can also set this in the GUI on the 2nd input screen at the top of the screen. I hope that helps! -Tom T At 10:17 AM 12/3/2007, you wrote: >Content-class: urn:content-classes:message >Content-Type: multipart/alternative; > boundary="----_=_NextPart_001_01C835D0.68A40BB9" > >Hi, > >I am using the autobuild wizard in the latest phenix release to >rebuild a model from a MR solution. Since the MR-template I used >has been modified with chainsaw, its sequence identity to the target >sequence is fairly high. The autobuild wizard therefore uses the >rebuilt-in-place mode to rebuild the model. How can I force the >wizard to do a complete rebuild? > >Thanks > > Carsten >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

2 1

Forcing autobuild wizard to do a complete rebuild
by Schubert, Carsten [PRDUS] 03 Dec '07

03 Dec '07

Hi, I am using the autobuild wizard in the latest phenix release to rebuild a model from a MR solution. Since the MR-template I used has been modified with chainsaw, its sequence identity to the target sequence is fairly high. The autobuild wizard therefore uses the rebuilt-in-place mode to rebuild the model. How can I force the wizard to do a complete rebuild? Thanks Carsten

1 0

phenix gui startup problem
by david albesa-jove 30 Nov '07

30 Nov '07

Dear phenix users, After installation of phenix using phenix-installer-1.3b-rc6-intel-linux-2.6-x86_64.tar and setting up the environmental variables, phenix gui fails to startup giving the following error: (99, 'Cannot assign requested address'). See bellow for further details. Thanks for your help, David ************************************************************8 [root@bio-daj2 phenix2]# phenix +++++++++++++++++++++++++++++++++++ Warning +++++++++++++++++++++++++++++++++++ Hostname is bio-daj2.cmmi.ic.ac.uk but fully qualified domain is bio-daj2 +++++++++++++++++++++++++++++++++++ Warning +++++++++++++++++++++++++++++++++++ +++++++++++++++++++++++++++++++++++ Warning +++++++++++++++++++++++++++++++++++ IP nslookup is ls-saf-g34b.saf.ic.ac.uk but FQDN is bio-daj2 +++++++++++++++++++++++++++++++++++ Warning +++++++++++++++++++++++++++++++++++ Running the PHENIX GUI with /usr/local/phenix-1.3b-rc6/build/intel- linux-2.6-x86_64/base/bin/python PHENIX distribution located in /usr/local/phenix-1.3b-rc6/phenix Exception in thread Thread-1: Traceback (most recent call last): File "/usr/local/phenix-1.3b-rc6/build/intel- linux-2.6-x86_64/base/lib/python2.5/threading.py", line 460, in __bootstrap self.run() File "/usr/local/phenix-1.3b-rc6/build/intel- linux-2.6-x86_64/base/lib/python2.5/threading.py", line 440, in run self.__target(*self.__args, **self.__kwargs) File "/usr/local/phenix-1.3b-rc6/phenix/wxGUI/GUIServer.py", line 14, in __init__ PhenixServer.PhenixServer.__init__(self, port, GUIRequestHandler) File "/usr/local/phenix-1.3b-rc6/phenix/phenix/server/PhenixServer.py", line 50, in __init__ ddbs = apply(func, (server_address, handler),{}) File "/usr/local/phenix-1.3b-rc6/phenix/phenix/server/SocketServer.py", line 333, in __init__ self.server_bind() File "/usr/local/phenix-1.3b-rc6/phenix/phenix/server/PhenixServer.py", line 65, in server_bind SocketServer.ThreadingTCPServer.server_bind(self) File "/usr/local/phenix-1.3b-rc6/phenix/phenix/server/SocketServer.py", line 344, in server_bind self.socket.bind(self.server_address) File "<string>", line 1, in bind error: (99, 'Cannot assign requested address') ======================================================= David Albesa-Jove PhD Centre for Molecular Microbiology and Infection Division of Cell and Molecular Biology Flowers Building, Level 1 South Kensington Campus Imperial College London London. SW7 2AZ. Tel: 020.7594.3070 e-mail: d.albesa-jove(a)imperial.ac.uk

2 1

HHMI X-ray lab manager/Research Scientist Job
by Marcelo Carlos Sousa 28 Nov '07

28 Nov '07

To all interested parties: A Research Scientist / X-ray lab manager position in the lab of Tom Cech in Boulder, Colorado is open. Job Description: The Howard Hughes Medical Institute, a leading biomedical research organization, is seeking an experienced scientist to manage our X-ray crystallography facility at the Cech research laboratory at the University of Colorado campus in Boulder. The facility is equipped with two Rigaku generators and R-Axis IV++ detectors for data collection, a linux cluster, and Macintosh computers for calculations and graphics, and a Fluidigm microfluidics crystallizer. The successful candidate will (1) Carry out routine maintenance on these instruments and coordinate service under service contracts; (2) perform routine Unix system administration and crystallographic software management; (3) provide basic training in the use of x-ray crystallographic equipment and software to users; and (4) engage in independent or collaborative research. Preferred qualifications include a Ph.D. degree in an appropriate field of science or technology, and three years of experience in a Research Specialist level position. Previous experience in Unix/Linux system administration and routine maintenance of crystallography hardware is essential. HHMI offers an excellent salary and comprehensive benefits package. Interested candidates please forward a statement of interest, CV, publications and references by December 30, 2007 to Ms. Robbie Haywood Oglesby, Administrative Assistant, 1200 Moursund Ave S101, Houston, Texas 77030 or e-mail regiondjobs(a)hhmi.org (Include Research Specialist - Cech Laboratory in the subject line of your e-mail). ____________________________________________ Marcelo C. Sousa, Ph.D. Department of Chemistry and Biochemistry Cristol Chemistry Building. Room 100 215 UCB University of Colorado at Boulder Boulder, CO 80309 Phone: (303) 735 4341 Fax: (303) 492 5894

1 0

ICSG 2008 Oxford: First announcement
by Tom Terwilliger 27 Nov '07

27 Nov '07

Dear PHENIX users, You may be interested in this announcement for the International Conference on Structural Genomics to be held in Oxford, UK Sept. 20-24, 2008. All the best, Tom T Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

hydrogens in low resolution structure refinement
by Stefanie Krieg 16 Nov '07

16 Nov '07

Dear all! I am refining two structures at 3.0 and 2.7 A. In some older threads on this board I found that you recommended adding hydrogens to the pdb file even at this resolution. I tried that (adding hydrogens with reduce and refine with riding hydrogens) but inspite of what I read in your postings, my R-Factors went up by 1% (not down as was predicted). Are there any other keywords which could be changed or do you have any other ideas why this could be? Thanks in advance! Stefanie

3 2

Re: [phenixbb] use of wavelength_list=
by Tom Terwilliger 12 Nov '07

12 Nov '07

Hi Bryan, phenix.autosol uses the values in wavelength_list to guess scattering factors if you do not supply values for scattering factors. All the best, -Tom T At 03:21 PM 11/10/2007, you wrote: >does phenix use the 'wavelength_list=' command line flag in calculations? >or is it used for no more than data set labeling e.g. derivatives, as >solve works? > >-bryan >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

use of wavelength_list=
by Bryan W. Lepore 10 Nov '07

10 Nov '07

does phenix use the 'wavelength_list=' command line flag in calculations? or is it used for no more than data set labeling e.g. derivatives, as solve works? -bryan

1 0

Collaborative Crystallography Program - Advanced Light Source
by Paul Adams 09 Nov '07

09 Nov '07

The Berkeley Center for Structural Biology (BCSB) is pleased to announce the launch of a Collaborative Crystallography Pilot Program (CC) at the Advanced Light Source in Berkeley. Through this program, scientists will be able to send protein crystals to BCSB staff researchers for data collection and analysis. The CC Pilot Program can provide an number of benefits to researchers: * Obtain high quality data and analysis through collaborating with expert beamline researchers; * Rapid turn around on projects; * Reduced travel costs. Thumbnail Description: ====================== The Collaborative Crystallography program will be piloted on beamlines 5.0.1 and 5.0.2 for one year; if successful it will be implemented on a permanent basis. CC proposals will go through the regular ALS General User proposal review process for beamtime allocation. Proposals will be reviewed and ranked by the Proposal Study Panel, and beamtime will be allocated accordingly. BCSB staff will schedule the projects to fit into the available resources. Only non-proprietary projects will be accepted. As a condition of participation, BCSB staff researchers who participate in data collection and/or analysis must be appropriately acknowledged - typically being included as authors on publications and in PDB depositions. Please consult the website for additional information at: http://bcsb.als.lbl.gov/wiki/index.php/Collaborative_Crystallography. How To Apply: ============= To submit a proposal, go to: http://alsusweb.lbl.gov/4DCGI/WEB_GetForm/PXProposalEntry.shtml/ Initialize. For question 3 select "Collaborative PX 501/502." For question 9, please describe a specific research project with a clear end point. In order to request CC time for January/February, 2008, proposals must be submitted by November 15, 2007. -- Paul Adams Deputy Division Director, Physical Biosciences Division, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Head, Berkeley Center for Structural Biology Building 64, Room 248 Tel: 510-486-4225, Fax: 510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 64R0121 Berkeley, CA 94720, USA. --

1 0

Re: [phenixbb] phenix.autobuild opinion on sequence file
by Tom Terwilliger 09 Nov '07

09 Nov '07

Hi Bryan, I haven't tried your approach, but my guess would be that the correct sequence file will be the better way to go... The side chains are fitted after building main-chain so the sequence is not going to affect the main-chain build in any direct way (though the sequence will help the wizard in identifying and correcting places where loops are built with the wrong number of residues). -Tom T At 01:32 PM 11/8/2007, you wrote: >i was thinking about giving phenix.autobuild a poly-Ser/Gly,Ala-intact (or >other incomplete variant) _sequence_file_, so it doesn't inter alia put >arginine into strands... though the solvent content will be imprecise.. > >has anyone noticed if such a trick was more/less favorable to the (proper) >complete sequence approach? any pertinent detail or criticisms >appreciated. > >-bryan >_______________________________________________ >phenixbb mailing list >phenixbb(a)phenix-online.org >http://www.phenix-online.org/mailman/listinfo/phenixbb Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

phenix.autobuild opinion on sequence file
by Bryan W. Lepore 08 Nov '07

08 Nov '07

i was thinking about giving phenix.autobuild a poly-Ser/Gly,Ala-intact (or other incomplete variant) _sequence_file_, so it doesn't inter alia put arginine into strands... though the solvent content will be imprecise.. has anyone noticed if such a trick was more/less favorable to the (proper) complete sequence approach? any pertinent detail or criticisms appreciated. -bryan

1 0

problem finding large no of sites in high symmetry
by Banumathi Sankaran 08 Nov '07

08 Nov '07

Hi, I am working with a data set collected in P23 space group. I am expecting 23 Se sites. Hyss gives me warning:run time error for finding large no of site. I did not interupt the run. I waited for 1hr and still it could not find sites. Shelx gave me out of 100 solutions only one had good CC and found 15 sites. IS there a way that this problem can be solved in hyss ? Thanks Banu

2 2

Re: [phenixbb] Advice about phasing procedure and phase extension in AutoSol-AutoBuild
by Tom Terwilliger 08 Nov '07

08 Nov '07

Hi Carsten, >1. can I input known HA-positions into the AutoSol wizard to help >Hyss find other positions? Does Hyss actually eliminate bogus sites? >Solve seems to refine bogus sites to occupancies ~0.1-0.5 but with a >B-factor of one, but does not toss them. How does Hyss handle this situation? As far as I know, you cannot seed hyss with sites. If you have SAD data, try the autosol wizard which uses Phaser. Phaser has a good LLG map algorithm for finding addtional sites. >2. What is the best way to handle phase extension in the Wizards, >how would one go about this? I would like to fine-tune the >resolution steps myself as not to jump to far out to higher resolution. The wizards use the defaults for phase extension in resolve. If you want to fine-tune the resolution steps you can say, resolve_command_list=" 's_step 0.05 ' " Note the 2 sets of quotation marks.... This will use steps of 0.05 A for phase extension (type phenix.autobuild --help resolve_command_list for documentation of this command) >3. What quality indicators should I look at? A couple of FOMs in the >resolve runs were in the region of 0.7, but the maps were not >interpretable and resolve failed to build anything. Anything else I >should look at? Best is the R-factor at the end of density modification. If it's around 0.30 you are doing well. 0.4 is bad, 0.25 is great. All the best, Tom T Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

Advice about phasing procedure and phase extension in AutoSol-AutoBuild
by Schubert, Carsten [PRDUS] 08 Nov '07

08 Nov '07

Hi, I am trying to bootstrap my way into a couple of weak derivatives using a combination of Solve and the AutoSol and AutoBuild wizards. I have probably one or two fairly weak diffracting derivatives (~3A) with low FOMs (~0.3) from Solve, the native extend to ~2.A. I have a couple of questions about how to best proceed with the phasing procedure using either the wizards or a Solve/Resolve combination. 1. can I input known HA-positions into the AutoSol wizard to help Hyss find other positions? Does Hyss actually eliminate bogus sites? Solve seems to refine bogus sites to occupancies ~0.1-0.5 but with a B-factor of one, but does not toss them. How does Hyss handle this situation? 2. What is the best way to handle phase extension in the Wizards, how would one go about this? I would like to fine-tune the resolution steps myself as not to jump to far out to higher resolution. 3. What quality indicators should I look at? A couple of FOMs in the resolve runs were in the region of 0.7, but the maps were not interpretable and resolve failed to build anything. Anything else I should look at? Thanks Carsten

1 0

Re: [phenixbb] autobuild 'hires_file'->now FreeR flags, merging, ...
by Tom Terwilliger 07 Nov '07

07 Nov '07

Hi Bryan, >On Tue, 6 Nov 2007, Thomas C. Terwilliger wrote: > > The problem is in that version of phenix. I'm sorry about that! Can you > >that solved it, thanks. Oh good. > >> [1 A] in phenix.autobuild, e.g. a SAD dataset, does the flag > >> 'hires_file=w1.sca' (help says "Merge in hires data"), mean that phases > >> will be extended to a high resolution limit as found in w1.sca? (vide > >> infra) > > > > Yes, that is correct. > >ok, then i have to ask - is phenix merging each reflection? i.e, i >wouldn't want to do this w/ a derivative and hi-res native, right? Yes, it is merging in each reflection, if I understand the question. Yes, you might do it with phases from a native+derivative and a hi-res native. (We're only talking about doing this in autobuild, after you have "experimental" phases from something.) -Tom T Thomas C. Terwilliger Mail Stop M888 Los Alamos National Laboratory Los Alamos, NM 87545 Tel: 505-667-0072 email: terwilliger(a)LANL.gov Fax: 505-665-3024 SOLVE web site: http://solve.lanl.gov PHENIX web site: http:www.phenix-online.org ISFI Integrated Center for Structure and Function Innovation web site: http://techcenter.mbi.ucla.edu TB Structural Genomics Consortium web site: http://www.doe-mbi.ucla.edu/TB

1 0

error message running example
by Kairies, Norman 07 Nov '07

07 Nov '07

Hi - I tried to run the example: phenix.run_example gene-5-mad However, it stopped, with following error messages: Done with gene-5-mad ...Your results are in the directory: gene-5-mad/AutoSol_run_1_ Missing the summary file: gene-5-mad/AutoSol_run_1_/ Something did not work properly...not all output files produced and the LAST.LOG reports: ************************************************************************ *** 6769 SOLVE STATUS 07-nov-07 12:47:15 6770 6771 DATASET TITLE: SOLVE 07-Nov-07 STATUS 6772 STATUS: UNABLE TO FIND UNIQUE NAME FOR SCRATCH 6773 ------------------------------------------------------------------------ --- 6774 Sorry -- ERROR ENDING. SEE the end of your log file or output STATUS 6775 and solve.log 6776 for more information STATUS Any idea what is going wrong? (phenix version 1.3 beta rc4, 64bit computer, 2 dual core proc.) Many thanks, Norman

2 1

autobuild 'hires_file'
by Bryan W. Lepore 07 Nov '07

07 Nov '07

i have phenix 2007_08_18_1856, (and i think latest cci apps). i have a jumble of questions, i'll try step by step: [1 A] in phenix.autobuild, e.g. a SAD dataset, does the flag 'hires_file=w1.sca' (help says "Merge in hires data"), mean that phases will be extended to a high resolution limit as found in w1.sca? (vide infra) [1 B] can the labels be the same as the 'other' data (the documentation suggests this)? i have tried a few things like : phenix.autobuild data=resolve.mtz hires_file=high_resolution.mtz input_hires_labels='FPnat SIGFPnat' seq_file=seq.txt ... and i see Cell: [99.810997009277344, 99.810997009277344, 140.37300109863281, 90.0, 90.0, 90.0] New resolution: 2.20520367253 High-res file input labels: ['FPnat', 'SIGFPnat'] ... which is good, but the job promptly fails with this cryptic (to me) error message: ************************************************************ Failed to carry out AutoBuild_datafile_info_inputs: 'all_input_hires_labels' ************************************************************ ... (google:all_input_hires_labels and looking through docs quick didn't find it) -bryan

2 2

PDB deposition of tls refined structure
by Rene Jorgensen 01 Nov '07

01 Nov '07

Dear phenix users, I am about to deposit a 2.5A structure at the PDB. The structure has been refined using phenix.refine with strategy=tls+individual_sites +individual_adp, which actually works very well but (because of the tls refinement) also results in the output of ANISOU records for the atoms in the PDB file. When using PDB_extract during the PDB submission process the ANISOU record is picked up as regular anisotropic refinement although the resolution is too low for that. Should I just accept it and leave it as it is or should I correct the info in the Auto Dep Input Tool (ADIT) to isotropic with just the regular b-factor values? Thanks in advance, Rene Jorgensen

2 1

Pango
by Frank von Delft 01 Nov '07

01 Nov '07

Hi, I just installed the latest phenix version (long overdue), and it burps with the following when I try to run the GUI. Looks like an absolute path was left lying around, no? Cheers phx ---------------------------------------------------- Running the PHENIX GUI with /usr/local/phenix/1.3b/phenix-1.3b/build/intel-linux-2.4/base/bin/python PHENIX distribution located in /usr/local/phenix/1.3b/phenix-1.3b/phenix Shell variable SSH_PATH not set Variable PYMOL_PATH set to /usr/local/phenix/1.3b/phenix-1.3b/pymol Shell variable RSH_PATH not set (python:31886): Pango-WARNING **: No builtin or dynamically loaded modules were found. Pango will not work correctly. This probably means there was an error in the creation of: '/net/ribbon/scratch1/phenix/phenix-1.3b/build/intel-linux-2.4/base/etc/pango/pango.modules' You should create this file by running pango-querymodules. (python:31886): Pango-WARNING **: pango_shape called with bad font, expect ugly output (python:31886): Pango-WARNING **: pango_font_get_glyph_extents called with null font argument, expect ugly output (python:31886): Pango-WARNING **: pango_font_get_metrics called with null font argument, expect ugly output (python:31886): Pango-WARNING **: _pango_cairo_font_install called with bad font, expect ugly output ----------------------------------------------------

2 1

Re: [phenixbb] lower limits on grid spacing/binning
by Ralf W. Grosse-Kunstleve 31 Oct '07

31 Oct '07

Probably, the original poster already got more than he bargained for, but for the records, a few more comments: > All FFT based structure factor programs require that the sampling > rates along each axis be even. I don't think this is true, unless I'm misunderstanding what "sampling rate" means. The FFT in phenix is based on FFTPACK (written in the 80s) which works for any number of grid points. FFTw also supports arbitrary gridding. > They may have other required factors > depending on the space group, but they will be happy to inform you > if you make a choice it doesn't like. They are also more efficient > when the prime factors of the sampling rates are small numbers. Try > to stick with multiples of 2,3, and 5 if possible. That's good advice. FFTPACK is fastest for transform sizes that are multiples of 2,3,4 and 5. The map calculation algorithms in phenix automatically take this into account. > All FFT programs will fail if you > sample your map courser than twice that frequency, as SFALL did for > you. This may be true for SFALL, but not for the FFT algorithms in the phenix libraries ($PHENIX/cctbx/include/cctbx/maptbx/structure_factors.h). The critical reference is: David A. Langs (2002), J. Appl. Cryst. 35, 505. As short as it is, this was an incredibly important paper. In retrospect, it is amazing that it took so long for someone to discover the trick. Ralf

3 2

lower limits on grid spacing/binning
by Terry Lang 30 Oct '07

30 Oct '07

Hey Everyone, I have been told by several crystallographers that the general rule of thumb for grid spacing when generating a map is one third the resolution (eg If your crystal structure has a resolution of 1.2 A, your grid spacing should be 0.4). Is there a mathematical reason why this ratio should be maintained or is this simply a holdover from slower computers with lower memory? More importantly for my application, is there a lower limit on how fine the grid spacing can be? In other words, is there a lower limit at which one is oversampling the data for a particular resolution? Any information and/or references would be greatly appreciated. Sincerely, Terry -- P. Therese Lang Post Doc Alber Lab, UC Berkeley

3 2

linking residues question
by Crystal K. Chuang 26 Oct '07

26 Oct '07

Hello all, I was wondering if there is a tool in RESOLVE that, when used through PHENIX, links up individual chains of residues and ties in symmetry related fragments so that, as a result, packs everything together to generate more of a globular unit? Many thanks, -Crystal

2 1

NCS interpretation
by Claudia Scotti 25 Oct '07

25 Oct '07

Dear list, I'm trying to undestand the NCS symmetry in a unit cell with 8 molecules (2 A resolution). The unit cell is almost orthorhombic (68.900 79.240 90.040 89.97 90.04 89.97), but only P1 + twinning worked for MR and for refining the structure (Rfree=0.22; Rcryst=0.18). The crystal simulated a P222 space group (the best seemed to be P21212), so I'd expect NCS axis parallel to . Now I've used phenix.simple_ncs_from_pdb to get the symmtery operators (see ouput below). I've read the manual, but I'm nevertheless finding it difficult to " see" the NCS axis. Any suggestions, please, on how to interpret the output, please, and "draw" the axis or on any alternatives on how to proceed? Many many thanks and a huge apology for the naive question (this is only my third strutcure...). Claudia --------------------------------------------------------------------------- # simple_ncs_from_pdb # # Find ncs among chains in a PDB file # type simple_ncs_from_pdb --help for help Parameters used for simple_ncs_from_pdb: find_ncs { temp_dir = "" min_length = 10 njump = 1 njump_recursion = 10 min_length_recursion = 50 min_percent = 95 max_rmsd = 2 quick = True max_rmsd_user = 3 domain_finding_parameters { find_invariant_domains = True initial_rms = 0.5 match_radius = 2 similarity_threshold = 0.75 smooth_length = 0 min_contig_length = 3 min_fraction_domain = 0.2 max_rmsd_domain = 2 } verbose = False } Chains in this PDB file: ['A', 'B', 'C', 'D', 'E', 'F', 'G', 'H'] GROUPS BASED ON QUICK COMPARISON: [['A', 'B', 'C', 'D', 'E', 'F', 'G', 'H']] Looking for invariant domains for ...: ['A', 'B', 'C', 'D', 'E', 'F', 'G', 'H'] [[[19, 130], [148, 253]], [[21, 130], [148, 253]], [[21, 130], [148, 253]], [[19, 128], [149, 253]], [[19, 130], [148, 253]], [[21, 128], [148, 253]], [[19, 130], [149, 253]], [[21, 129], [149, 253]]] GROUP 1 Summary of NCS group with 8 operators: ID of chain/residue where these apply: [['A', 'B', 'C', 'D', 'E', 'F', 'G', 'H'], [[[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]], [[20, 117], [121, 130], [149, 253]]]] RMSD (A) from chain A: 0.0 0.46 0.47 0.53 0.54 0.48 0.48 0.59 Number of residues matching chain A:[213, 212, 212, 211, 212, 210, 213, 211] Source of NCS info: sortwaterxyzout.pdb OPERATOR 1 CENTER: 19.3475 -10.7352 7.9738 ROTA 1: 1.0000 0.0000 0.0000 ROTA 2: 0.0000 1.0000 0.0000 ROTA 3: 0.0000 0.0000 1.0000 TRANS: 0.0000 0.0000 0.0000 OPERATOR 2 CENTER: 53.8092 24.2127 11.0612 ROTA 1: 0.9998 0.0043 -0.0190 ROTA 2: 0.0045 -0.9999 0.0114 ROTA 3: -0.0190 -0.0115 -0.9998 TRANS: -34.3014 13.1765 20.2795 OPERATOR 3 CENTER: 55.6227 -15.2644 6.2461 ROTA 1: -0.9928 -0.0019 -0.1198 ROTA 2: -0.0045 -0.9986 0.0530 ROTA 3: -0.1197 0.0532 0.9914 TRANS: 75.3327 -25.9880 9.2016 OPERATOR 4 CENTER: 21.4489 28.7297 12.8232 ROTA 1: -0.9923 0.0066 0.1235 ROTA 2: -0.0001 0.9985 -0.0545 ROTA 3: -0.1236 -0.0541 -0.9909 TRANS: 38.7377 -38.6213 24.9897 OPERATOR 5 CENTER: 33.2332 16.3336 52.0552 ROTA 1: 0.9959 0.0207 -0.0884 ROTA 2: -0.0168 0.9988 0.0450 ROTA 3: 0.0892 -0.0433 0.9951 TRANS: -9.4176 -28.8046 -46.0499 OPERATOR 6 CENTER: 35.8216 -23.2140 56.1297 ROTA 1: -0.9985 -0.0249 -0.0490 ROTA 2: -0.0273 0.9985 0.0479 ROTA 3: 0.0477 0.0492 -0.9976 TRANS: 57.2101 10.9031 63.4545 OPERATOR 7 CENTER: 70.2188 11.8599 54.2973 ROTA 1: -0.9987 0.0207 0.0473 ROTA 2: -0.0234 -0.9981 -0.0569 ROTA 3: 0.0460 -0.0580 0.9973 TRANS: 86.6599 5.8364 -48.7180 OPERATOR 8 CENTER: 67.5293 -27.9008 58.5120 ROTA 1: 0.9959 -0.0146 0.0888 ROTA 2: -0.0120 -0.9995 -0.0303 ROTA 3: 0.0892 0.0291 -0.9956 TRANS: -53.5269 -35.9247 61.0251 NCS operators written in format for resolve to: simple_ncs_from_pdb.resolve NCS operators written in format for phenix.refine to: simple_ncs_from_pdb.ncs NCS written as ncs object information to: simple_ncs_from_pdb.ncs_spec Claudia Scotti Dipartimento di Medicina Sperimentale Sezione di Patologia Generale Universita' di Pavia Piazza Botta, 10 27100 Pavia Italia Tel. 0039 0382 986335/8/1 Facs 0039 0382 303673 _________________________________________________________________ Explore the seven wonders of the world http://search.msn.com/results.aspx?q=7+wonders+world&mkt=en-US&form=QBRE

3 4

Re: [phenixbb] NCS interpretation
by Thomas C. Terwilliger 25 Oct '07

25 Oct '07

Hi Claudia, It looks to me like your ncs is almost exactly 222 symmetry, plus a centering. You can tell it is 222 symmetry because all the operators are zeroes except along the diagonal, and the diagonal elements are all 1 or -1 (or close to it). That means that the 4 unique operators go like: x y z -x -y z -x y -z x -y -z The 8 operators appear to be 2 sets of 4, with a centering operation... I made a little PDB file (at the end of this message) that shows the symmetry in these operators. If you run phenix.simple_ncs_from_pdb on it you should get back something similar to your operators. If you run the phenix.autobuild wizard one cycle of rebuilding (not rebuild_in_place) then it will try to find the most compact arrangement of your molecules, and it will also try to find the point group(s) of the molecule... in this case I think it will fail to find the point group though (as it failed with my test model made from your operators). Question: do your molecules pack nicely with this arrangement? -Tom T CRYST1 68.900 79.240 90.040 89.97 90.04 89.97 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014514 -0.000008 0.000010 0.00000 SCALE2 0.000000 0.012620 -0.000007 0.00000 SCALE3 0.000000 0.000000 0.011106 0.00000 ATOM 1 N GLY A 11 14.343 3.315 16.927 1.00 45.51 ATOM 2 CA GLY A 11 14.811 1.998 17.345 1.00 45.51 ATOM 3 C GLY A 11 15.247 1.270 16.077 1.00 45.51 ATOM 4 O GLY A 11 14.898 1.674 14.948 1.00 45.51 ATOM 5 N GLY A 12 16.012 0.197 16.221 1.00 45.51 ATOM 6 CA GLY A 12 16.552 -0.502 15.059 1.00 45.51 ATOM 7 C GLY A 12 16.175 -1.959 15.092 1.00 45.51 ATOM 8 O GLY A 12 16.336 -2.626 16.122 1.00 45.51 ATOM 9 N GLY A 13 15.633 -2.483 13.985 1.00 45.51 ATOM 10 CA GLY A 13 15.426 -3.925 13.898 1.00 45.51 ATOM 11 C GLY A 13 16.417 -4.451 12.863 1.00 45.51 ATOM 12 O GLY A 13 16.869 -3.746 11.948 1.00 45.51 ATOM 13 N GLY A 14 16.817 -5.708 13.039 1.00 45.51 ATOM 14 CA GLY A 14 17.838 -6.300 12.198 1.00 45.51 ATOM 15 C GLY A 14 17.499 -7.728 11.801 1.00 45.51 ATOM 16 O GLY A 14 16.579 -8.347 12.326 1.00 45.51 ATOM 17 N GLY A 15 18.236 -8.243 10.821 1.00 45.51 ATOM 18 CA GLY A 15 18.016 -9.590 10.322 1.00 45.51 ATOM 19 C GLY A 15 18.896 -9.857 9.116 1.00 45.51 ATOM 20 O GLY A 15 19.799 -9.094 8.774 1.00 45.51 ATOM 21 N GLY A 16 18.579 -10.960 8.439 1.00 45.51 ATOM 22 CA GLY A 16 19.312 -11.427 7.265 1.00 45.51 ATOM 23 C GLY A 16 18.358 -11.735 6.103 1.00 45.51 ATOM 24 O GLY A 16 17.381 -12.470 6.253 1.00 45.51 ATOM 25 N GLY A 17 18.665 -11.180 4.919 1.00 45.51 ATOM 26 CA GLY A 17 17.900 -11.402 3.696 1.00 45.51 ATOM 27 C GLY A 17 17.912 -12.860 3.238 1.00 45.51 ATOM 28 O GLY A 17 18.722 -13.663 3.702 1.00 45.51 ATOM 29 N GLY A 18 17.039 -13.175 2.273 1.00 45.51 ATOM 30 CA GLY A 18 16.903 -14.515 1.711 1.00 45.51 ATOM 31 C GLY A 18 18.197 -15.177 1.241 1.00 45.51 ATOM 32 O GLY A 18 18.412 -16.379 1.421 1.00 45.51 ATOM 33 N GLY A 19 19.088 -14.380 0.652 1.00 45.51 ATOM 34 CA GLY A 19 20.343 -14.917 0.178 1.00 45.51 ATOM 35 C GLY A 19 21.578 -14.472 0.955 1.00 45.51 ATOM 36 O GLY A 19 22.675 -14.340 0.406 1.00 45.51 ATOM 37 N GLY A 20 21.386 -14.238 2.266 1.00 45.51 ATOM 38 CA GLY A 20 22.494 -14.027 3.191 1.00 45.51 ATOM 39 C GLY A 20 22.894 -12.620 3.608 1.00 45.51 ATOM 40 O GLY A 20 23.593 -12.505 4.614 1.00 45.51 ATOM 41 N GLY A 21 22.517 -11.538 2.925 1.00 45.51 ATOM 42 CA GLY A 21 22.940 -10.189 3.303 1.00 45.51 ATOM 43 C GLY A 21 22.343 -9.681 4.631 1.00 45.51 ATOM 44 O GLY A 21 21.143 -9.824 4.862 1.00 45.51 ATOM 45 N GLY A 22 23.105 -9.075 5.551 1.00 45.51 ATOM 46 CA GLY A 22 22.566 -8.357 6.707 1.00 45.51 ATOM 47 C GLY A 22 21.798 -7.088 6.339 1.00 45.51 ATOM 48 O GLY A 22 22.103 -6.402 5.353 1.00 45.51 ATOM 49 N GLY A 23 20.753 -6.790 7.130 1.00 45.51 ATOM 50 CA GLY A 23 20.048 -5.519 6.978 1.00 45.51 ATOM 51 C GLY A 23 19.765 -4.940 8.347 1.00 45.51 ATOM 52 O GLY A 23 19.689 -5.665 9.347 1.00 45.51 ATOM 53 N GLY A 24 19.555 -3.628 8.334 1.00 45.51 ATOM 54 CA GLY A 24 19.129 -2.901 9.522 1.00 45.51 ATOM 55 C GLY A 24 18.093 -1.892 9.118 1.00 45.51 ATOM 56 O GLY A 24 18.258 -1.184 8.123 1.00 45.51 ATOM 57 N GLY A 25 17.006 -1.822 9.877 1.00 45.51 ATOM 58 CA GLY A 25 15.964 -0.840 9.590 1.00 45.51 ATOM 59 C GLY A 25 15.738 0.058 10.803 1.00 45.51 ATOM 60 O GLY A 25 15.499 -0.461 11.884 1.00 45.51 ATOM 61 N GLY A 26 15.823 1.380 10.651 1.00 45.51 ATOM 62 CA GLY A 26 15.526 2.319 11.738 1.00 45.51 ATOM 63 C GLY A 26 14.091 2.813 11.699 1.00 45.51 ATOM 64 O GLY A 26 13.604 3.245 10.648 1.00 45.51 ATOM 65 N GLY A 27 13.366 2.776 12.830 1.00 45.51 ATOM 66 CA GLY A 27 11.964 3.126 12.862 1.00 45.51 ATOM 67 C GLY A 27 11.719 4.242 13.876 1.00 45.51 ATOM 68 O GLY A 27 12.295 4.231 14.981 1.00 45.51 ATOM 69 N GLY B 31 48.655 10.108 2.312 1.00 45.51 ATOM 70 CA GLY B 31 49.109 11.422 1.870 1.00 45.51 ATOM 71 C GLY B 31 49.565 12.166 3.121 1.00 45.51 ATOM 72 O GLY B 31 49.240 11.774 4.261 1.00 45.51 ATOM 73 N GLY B 32 50.323 13.241 2.951 1.00 45.51 ATOM 74 CA GLY B 32 50.881 13.956 4.094 1.00 45.51 ATOM 75 C GLY B 32 50.497 15.410 4.052 1.00 45.51 ATOM 76 O GLY B 32 50.636 16.066 3.011 1.00 45.51 ATOM 77 N GLY B 33 49.974 15.945 5.163 1.00 45.51 ATOM 78 CA GLY B 33 49.762 17.387 5.237 1.00 45.51 ATOM 79 C GLY B 33 50.770 17.929 6.247 1.00 45.51 ATOM 80 O GLY B 33 51.243 17.236 7.161 1.00 45.51 ATOM 81 N GLY B 34 51.161 19.186 6.049 1.00 45.51 ATOM 82 CA GLY B 34 52.195 19.792 6.864 1.00 45.51 ATOM 83 C GLY B 34 51.857 21.223 7.251 1.00 45.51 ATOM 84 O GLY B 34 50.925 21.832 6.736 1.00 45.51 ATOM 85 N GLY B 35 52.610 21.752 8.210 1.00 45.51 ATOM 86 CA GLY B 35 52.394 23.104 8.698 1.00 45.51 ATOM 87 C GLY B 35 53.295 23.388 9.884 1.00 45.51 ATOM 88 O GLY B 35 54.208 22.633 10.217 1.00 45.51 ATOM 89 N GLY B 36 52.986 24.498 10.554 1.00 45.51 ATOM 90 CA GLY B 36 53.739 24.981 11.709 1.00 45.51 ATOM 91 C GLY B 36 52.806 25.299 12.885 1.00 45.51 ATOM 92 O GLY B 36 51.823 26.028 12.745 1.00 45.51 ATOM 93 N GLY B 37 53.138 24.758 14.069 1.00 45.51 ATOM 94 CA GLY B 37 52.395 24.991 15.304 1.00 45.51 ATOM 95 C GLY B 37 52.409 26.454 15.745 1.00 45.51 ATOM 96 O GLY B 37 53.207 27.256 15.256 1.00 45.51 ATOM 97 N GLY B 38 51.553 26.777 16.722 1.00 45.51 ATOM 98 CA GLY B 38 51.422 28.123 17.272 1.00 45.51 ATOM 99 C GLY B 38 52.722 28.796 17.709 1.00 45.51 ATOM 100 O GLY B 38 52.928 29.996 17.511 1.00 45.51 ATOM 101 N GLY B 39 53.627 28.009 18.290 1.00 45.51 ATOM 102 CA GLY B 39 54.889 28.557 18.734 1.00 45.51 ATOM 103 C GLY B 39 56.111 28.108 17.939 1.00 45.51 ATOM 104 O GLY B 39 57.218 27.987 18.468 1.00 45.51 ATOM 105 N GLY B 40 55.895 27.858 16.634 1.00 45.51 ATOM 106 CA GLY B 40 56.986 27.642 15.691 1.00 45.51 ATOM 107 C GLY B 40 57.384 26.232 15.283 1.00 45.51 ATOM 108 O GLY B 40 58.065 26.108 14.265 1.00 45.51 ATOM 109 N GLY B 41 57.025 25.156 15.985 1.00 45.51 ATOM 110 CA GLY B 41 57.447 23.804 15.614 1.00 45.51 ATOM 111 C GLY B 41 56.827 23.279 14.304 1.00 45.51 ATOM 112 O GLY B 41 55.623 23.414 14.094 1.00 45.51 ATOM 113 N GLY B 42 57.575 22.665 13.377 1.00 45.51 ATOM 114 CA GLY B 42 57.017 21.932 12.239 1.00 45.51 ATOM 115 C GLY B 42 56.262 20.664 12.636 1.00 45.51 ATOM 116 O GLY B 42 56.589 19.990 13.624 1.00 45.51 ATOM 117 N GLY B 43 55.203 20.352 11.869 1.00 45.51 ATOM 118 CA GLY B 43 54.507 19.080 12.049 1.00 45.51 ATOM 119 C GLY B 43 54.201 18.484 10.692 1.00 45.51 ATOM 120 O GLY B 43 54.103 19.197 9.686 1.00 45.51 ATOM 121 N GLY B 44 53.997 17.171 10.724 1.00 45.51 ATOM 122 CA GLY B 44 53.552 16.429 9.553 1.00 45.51 ATOM 123 C GLY B 44 52.528 15.420 9.988 1.00 45.51 ATOM 124 O GLY B 44 52.715 14.724 10.988 1.00 45.51 ATOM 125 N GLY B 45 51.427 15.337 9.251 1.00 45.51 ATOM 126 CA GLY B 45 50.396 14.354 9.569 1.00 45.51 ATOM 127 C GLY B 45 50.151 13.441 8.371 1.00 45.51 ATOM 128 O GLY B 45 49.889 13.946 7.289 1.00 45.51 ATOM 129 N GLY B 46 50.245 12.121 8.536 1.00 45.51 ATOM 130 CA GLY B 46 49.931 11.168 7.466 1.00 45.51 ATOM 131 C GLY B 46 48.499 10.669 7.538 1.00 45.51 ATOM 132 O GLY B 46 48.034 10.247 8.603 1.00 45.51 ATOM 133 N GLY B 47 47.753 10.690 6.421 1.00 45.51 ATOM 134 CA GLY B 47 46.352 10.333 6.419 1.00 45.51 ATOM 135 C GLY B 47 46.093 9.205 5.423 1.00 45.51 ATOM 136 O GLY B 47 46.648 9.205 4.307 1.00 45.51 ATOM 137 N GLY C 51 59.494 -28.736 16.518 1.00 45.51 ATOM 138 CA GLY C 51 58.985 -27.399 16.806 1.00 45.51 ATOM 139 C GLY C 51 58.707 -26.740 15.458 1.00 45.51 ATOM 140 O GLY C 51 59.187 -27.203 14.402 1.00 45.51 ATOM 141 N GLY C 52 57.935 -25.663 15.452 1.00 45.51 ATOM 142 CA GLY C 52 57.542 -25.027 14.199 1.00 45.51 ATOM 143 C GLY C 52 57.918 -23.570 14.199 1.00 45.51 ATOM 144 O GLY C 52 57.638 -22.850 15.166 1.00 45.51 ATOM 145 N GLY C 53 58.591 -23.105 13.139 1.00 45.51 ATOM 146 CA GLY C 53 58.814 -21.669 13.001 1.00 45.51 ATOM 147 C GLY C 53 57.956 -21.201 11.828 1.00 45.51 ATOM 148 O GLY C 53 57.614 -21.954 10.905 1.00 45.51 ATOM 149 N GLY C 54 57.544 -19.937 11.888 1.00 45.51 ATOM 150 CA GLY C 54 56.633 -19.392 10.901 1.00 45.51 ATOM 151 C GLY C 54 57.024 -17.987 10.472 1.00 45.51 ATOM 152 O GLY C 54 57.877 -17.339 11.070 1.00 45.51 ATOM 153 N GLY C 55 56.412 -17.526 9.385 1.00 45.51 ATOM 154 CA GLY C 55 56.696 -16.207 8.845 1.00 45.51 ATOM 155 C GLY C 55 55.968 -16.006 7.530 1.00 45.51 ATOM 156 O GLY C 55 55.109 -16.788 7.123 1.00 45.51 ATOM 157 N GLY C 56 56.369 -14.940 6.838 1.00 45.51 ATOM 158 CA GLY C 56 55.784 -14.538 5.562 1.00 45.51 ATOM 159 C GLY C 56 56.871 -14.290 4.508 1.00 45.51 ATOM 160 O GLY C 56 57.827 -13.546 4.735 1.00 45.51 ATOM 161 N GLY C 57 56.706 -14.908 3.327 1.00 45.51 ATOM 162 CA GLY C 57 57.613 -14.750 2.194 1.00 45.51 ATOM 163 C GLY C 57 57.662 -13.318 1.661 1.00 45.51 ATOM 164 O GLY C 57 56.806 -12.493 1.982 1.00 45.51 ATOM 165 N GLY C 58 58.646 -13.053 0.793 1.00 45.51 ATOM 166 CA GLY C 58 58.854 -11.745 0.181 1.00 45.51 ATOM 167 C GLY C 58 57.629 -11.111 -0.475 1.00 45.51 ATOM 168 O GLY C 58 57.399 -9.902 -0.386 1.00 45.51 ATOM 169 N GLY C 59 56.811 -11.940 -1.124 1.00 45.51 ATOM 170 CA GLY C 59 55.624 -11.431 -1.772 1.00 45.51 ATOM 171 C GLY C 59 54.303 -11.837 -1.126 1.00 45.51 ATOM 172 O GLY C 59 53.279 -12.000 -1.795 1.00 45.51 ATOM 173 N GLY C 60 54.336 -12.000 0.209 1.00 45.51 ATOM 174 CA GLY C 60 53.124 -12.164 1.004 1.00 45.51 ATOM 175 C GLY C 60 52.671 -13.547 1.444 1.00 45.51 ATOM 176 O GLY C 60 51.856 -13.610 2.364 1.00 45.51 ATOM 177 N GLY C 61 53.122 -14.663 0.870 1.00 45.51 ATOM 178 CA GLY C 61 52.651 -15.991 1.265 1.00 45.51 ATOM 179 C GLY C 61 53.082 -16.427 2.680 1.00 45.51 ATOM 180 O GLY C 61 54.246 -16.269 3.045 1.00 45.51 ATOM 181 N GLY C 62 52.213 -16.984 3.533 1.00 45.51 ATOM 182 CA GLY C 62 52.606 -17.639 4.782 1.00 45.51 ATOM 183 C GLY C 62 53.407 -18.924 4.576 1.00 45.51 ATOM 184 O GLY C 62 53.219 -19.662 3.599 1.00 45.51 ATOM 185 N GLY C 63 54.348 -19.178 5.501 1.00 45.51 ATOM 186 CA GLY C 63 55.061 -20.454 5.503 1.00 45.51 ATOM 187 C GLY C 63 55.175 -20.959 6.924 1.00 45.51 ATOM 188 O GLY C 63 55.134 -20.181 7.886 1.00 45.51 ATOM 189 N GLY C 64 55.379 -22.269 7.006 1.00 45.51 ATOM 190 CA GLY C 64 55.657 -22.931 8.274 1.00 45.51 ATOM 191 C GLY C 64 56.729 -23.958 8.051 1.00 45.51 ATOM 192 O GLY C 64 56.681 -24.718 7.082 1.00 45.51 ATOM 193 N GLY C 65 57.717 -23.986 8.937 1.00 45.51 ATOM 194 CA GLY C 65 58.782 -24.980 8.829 1.00 45.51 ATOM 195 C GLY C 65 58.857 -25.811 10.107 1.00 45.51 ATOM 196 O GLY C 65 58.967 -25.235 11.179 1.00 45.51 ATOM 197 N GLY C 66 58.785 -27.140 10.016 1.00 45.51 ATOM 198 CA GLY C 66 58.945 -28.019 11.179 1.00 45.51 ATOM 199 C GLY C 66 60.372 -28.512 11.338 1.00 45.51 ATOM 200 O GLY C 66 60.980 -28.998 10.378 1.00 45.51 ATOM 201 N GLY C 67 60.957 -28.413 12.544 1.00 45.51 ATOM 202 CA GLY C 67 62.343 -28.758 12.763 1.00 45.51 ATOM 203 C GLY C 67 62.460 -29.818 13.856 1.00 45.51 ATOM 204 O GLY C 67 61.756 -29.750 14.882 1.00 45.51 ATOM 205 N GLY D 71 25.199 42.149 2.692 1.00 45.51 ATOM 206 CA GLY D 71 24.683 40.814 2.408 1.00 45.51 ATOM 207 C GLY D 71 24.408 40.159 3.758 1.00 45.51 ATOM 208 O GLY D 71 24.894 40.621 4.811 1.00 45.51 ATOM 209 N GLY D 72 23.631 39.085 3.768 1.00 45.51 ATOM 210 CA GLY D 72 23.239 38.453 5.024 1.00 45.51 ATOM 211 C GLY D 72 23.609 36.994 5.024 1.00 45.51 ATOM 212 O GLY D 72 23.322 36.273 4.060 1.00 45.51 ATOM 213 N GLY D 73 24.284 36.527 6.082 1.00 45.51 ATOM 214 CA GLY D 73 24.500 35.090 6.222 1.00 45.51 ATOM 215 C GLY D 73 23.645 34.628 7.398 1.00 45.51 ATOM 216 O GLY D 73 23.309 35.384 8.322 1.00 45.51 ATOM 217 N GLY D 74 23.226 33.366 7.342 1.00 45.51 ATOM 218 CA GLY D 74 22.317 32.827 8.333 1.00 45.51 ATOM 219 C GLY D 74 22.703 31.420 8.763 1.00 45.51 ATOM 220 O GLY D 74 23.551 30.768 8.163 1.00 45.51 ATOM 221 N GLY D 75 22.093 30.964 9.853 1.00 45.51 ATOM 222 CA GLY D 75 22.373 29.644 10.393 1.00 45.51 ATOM 223 C GLY D 75 21.649 29.449 11.711 1.00 45.51 ATOM 224 O GLY D 75 20.795 30.235 12.120 1.00 45.51 ATOM 225 N GLY D 76 22.048 28.382 12.403 1.00 45.51 ATOM 226 CA GLY D 76 21.465 27.984 13.682 1.00 45.51 ATOM 227 C GLY D 76 22.556 27.733 14.733 1.00 45.51 ATOM 228 O GLY D 76 23.507 26.985 14.503 1.00 45.51 ATOM 229 N GLY D 77 22.398 28.353 15.913 1.00 45.51 ATOM 230 CA GLY D 77 23.308 28.193 17.043 1.00 45.51 ATOM 231 C GLY D 77 23.353 26.762 17.577 1.00 45.51 ATOM 232 O GLY D 77 22.492 25.940 17.261 1.00 45.51 ATOM 233 N GLY D 78 24.339 26.494 18.443 1.00 45.51 ATOM 234 CA GLY D 78 24.543 25.185 19.056 1.00 45.51 ATOM 235 C GLY D 78 23.317 24.558 19.718 1.00 45.51 ATOM 236 O GLY D 78 23.082 23.350 19.631 1.00 45.51 ATOM 237 N GLY D 79 22.506 25.392 20.368 1.00 45.51 ATOM 238 CA GLY D 79 21.319 24.889 21.021 1.00 45.51 ATOM 239 C GLY D 79 19.998 25.300 20.380 1.00 45.51 ATOM 240 O GLY D 79 18.977 25.469 21.052 1.00 45.51 ATOM 241 N GLY D 80 20.026 25.461 19.044 1.00 45.51 ATOM 242 CA GLY D 80 18.812 25.629 18.253 1.00 45.51 ATOM 243 C GLY D 80 18.363 27.014 17.813 1.00 45.51 ATOM 244 O GLY D 80 17.545 27.079 16.896 1.00 45.51 ATOM 245 N GLY D 81 18.822 28.129 18.384 1.00 45.51 ATOM 246 CA GLY D 81 18.355 29.459 17.988 1.00 45.51 ATOM 247 C GLY D 81 18.783 29.890 16.571 1.00 45.51 ATOM 248 O GLY D 81 19.945 29.727 16.202 1.00 45.51 ATOM 249 N GLY D 82 17.913 30.451 15.720 1.00 45.51 ATOM 250 CA GLY D 82 18.305 31.101 14.469 1.00 45.51 ATOM 251 C GLY D 82 19.112 32.383 14.670 1.00 45.51 ATOM 252 O GLY D 82 18.932 33.124 15.647 1.00 45.51 ATOM 253 N GLY D 83 20.051 32.631 13.741 1.00 45.51 ATOM 254 CA GLY D 83 20.770 33.904 13.735 1.00 45.51 ATOM 255 C GLY D 83 20.881 34.406 12.312 1.00 45.51 ATOM 256 O GLY D 83 20.833 33.627 11.352 1.00 45.51 ATOM 257 N GLY D 84 21.091 35.715 12.228 1.00 45.51 ATOM 258 CA GLY D 84 21.367 36.374 10.959 1.00 45.51 ATOM 259 C GLY D 84 22.445 37.397 11.176 1.00 45.51 ATOM 260 O GLY D 84 22.404 38.159 12.144 1.00 45.51 ATOM 261 N GLY D 85 23.429 37.418 10.286 1.00 45.51 ATOM 262 CA GLY D 85 24.499 38.408 10.388 1.00 45.51 ATOM 263 C GLY D 85 24.573 39.237 9.110 1.00 45.51 ATOM 264 O GLY D 85 24.676 38.659 8.037 1.00 45.51 ATOM 265 N GLY D 86 24.507 40.566 9.199 1.00 45.51 ATOM 266 CA GLY D 86 24.667 41.443 8.034 1.00 45.51 ATOM 267 C GLY D 86 26.096 41.929 7.868 1.00 45.51 ATOM 268 O GLY D 86 26.709 42.414 8.826 1.00 45.51 ATOM 269 N GLY D 87 26.676 41.826 6.660 1.00 45.51 ATOM 270 CA GLY D 87 28.063 42.164 6.437 1.00 45.51 ATOM 271 C GLY D 87 28.181 43.222 5.341 1.00 45.51 ATOM 272 O GLY D 87 27.472 43.155 4.318 1.00 45.51 ATOM 273 N GLY E 91 28.742 29.848 62.009 1.00 45.51 ATOM 274 CA GLY E 91 29.268 28.524 62.325 1.00 45.51 ATOM 275 C GLY E 91 29.601 27.861 60.992 1.00 45.51 ATOM 276 O GLY E 91 29.146 28.306 59.917 1.00 45.51 ATOM 277 N GLY E 92 30.394 26.799 61.019 1.00 45.51 ATOM 278 CA GLY E 92 30.839 26.162 59.784 1.00 45.51 ATOM 279 C GLY E 92 30.491 24.697 59.784 1.00 45.51 ATOM 280 O GLY E 92 30.755 23.990 60.765 1.00 45.51 ATOM 281 N GLY E 93 29.862 24.211 58.707 1.00 45.51 ATOM 282 CA GLY E 93 29.672 22.770 58.574 1.00 45.51 ATOM 283 C GLY E 93 30.575 22.310 57.433 1.00 45.51 ATOM 284 O GLY E 93 30.932 23.063 56.514 1.00 45.51 ATOM 285 N GLY E 94 31.010 21.055 57.516 1.00 45.51 ATOM 286 CA GLY E 94 31.962 20.521 56.563 1.00 45.51 ATOM 287 C GLY E 94 31.613 19.105 56.133 1.00 45.51 ATOM 288 O GLY E 94 30.754 18.444 56.709 1.00 45.51 ATOM 289 N GLY E 95 32.268 18.648 55.070 1.00 45.51 ATOM 290 CA GLY E 95 32.027 17.319 54.532 1.00 45.51 ATOM 291 C GLY E 95 32.800 17.123 53.242 1.00 45.51 ATOM 292 O GLY E 95 33.656 17.919 52.857 1.00 45.51 ATOM 293 N GLY E 96 32.443 16.044 52.547 1.00 45.51 ATOM 294 CA GLY E 96 33.076 15.644 51.293 1.00 45.51 ATOM 295 C GLY E 96 32.027 15.367 50.207 1.00 45.51 ATOM 296 O GLY E 96 31.080 14.606 50.410 1.00 45.51 ATOM 297 N GLY E 97 32.218 15.979 49.027 1.00 45.51 ATOM 298 CA GLY E 97 31.351 15.794 47.868 1.00 45.51 ATOM 299 C GLY E 97 31.346 14.358 47.346 1.00 45.51 ATOM 300 O GLY E 97 32.208 13.552 47.700 1.00 45.51 ATOM 301 N GLY E 98 30.396 14.067 46.448 1.00 45.51 ATOM 302 CA GLY E 98 30.233 12.750 45.841 1.00 45.51 ATOM 303 C GLY E 98 31.491 12.136 45.229 1.00 45.51 ATOM 304 O GLY E 98 31.741 10.932 45.335 1.00 45.51 ATOM 305 N GLY E 99 32.312 12.976 44.600 1.00 45.51 ATOM 306 CA GLY E 99 33.529 12.486 43.993 1.00 45.51 ATOM 307 C GLY E 99 34.820 12.923 44.677 1.00 45.51 ATOM 308 O GLY E 99 35.862 13.101 44.040 1.00 45.51 ATOM 309 N GLY E 100 34.742 13.096 46.009 1.00 45.51 ATOM 310 CA GLY E 100 35.925 13.289 46.841 1.00 45.51 ATOM 311 C GLY E 100 36.337 14.685 47.284 1.00 45.51 ATOM 312 O GLY E 100 37.120 14.771 48.229 1.00 45.51 ATOM 313 N GLY E 101 35.882 15.787 46.687 1.00 45.51 ATOM 314 CA GLY E 101 36.314 17.127 47.086 1.00 45.51 ATOM 315 C GLY E 101 35.830 17.565 48.483 1.00 45.51 ATOM 316 O GLY E 101 34.658 17.387 48.812 1.00 45.51 ATOM 317 N GLY E 102 36.661 18.146 49.358 1.00 45.51 ATOM 318 CA GLY E 102 36.215 18.802 50.589 1.00 45.51 ATOM 319 C GLY E 102 35.396 20.070 50.347 1.00 45.51 ATOM 320 O GLY E 102 35.600 20.804 49.370 1.00 45.51 ATOM 321 N GLY E 103 34.421 20.311 51.240 1.00 45.51 ATOM 322 CA GLY E 103 33.684 21.573 51.208 1.00 45.51 ATOM 323 C GLY E 103 33.515 22.086 52.622 1.00 45.51 ATOM 324 O GLY E 103 33.540 21.317 53.591 1.00 45.51 ATOM 325 N GLY E 104 33.282 23.393 52.686 1.00 45.51 ATOM 326 CA GLY E 104 32.952 24.059 53.939 1.00 45.51 ATOM 327 C GLY E 104 31.867 25.063 53.674 1.00 45.51 ATOM 328 O GLY E 104 31.931 25.816 52.701 1.00 45.51 ATOM 329 N GLY E 105 30.851 25.077 54.528 1.00 45.51 ATOM 330 CA GLY E 105 29.772 26.049 54.379 1.00 45.51 ATOM 331 C GLY E 105 29.640 26.889 55.646 1.00 45.51 ATOM 332 O GLY E 105 29.507 26.319 56.719 1.00 45.51 ATOM 333 N GLY E 106 29.689 28.218 55.547 1.00 45.51 ATOM 334 CA GLY E 106 29.474 29.102 56.697 1.00 45.51 ATOM 335 C GLY E 106 28.033 29.568 56.807 1.00 45.51 ATOM 336 O GLY E 106 27.447 30.035 55.824 1.00 45.51 ATOM 337 N GLY E 107 27.413 29.467 57.995 1.00 45.51 ATOM 338 CA GLY E 107 26.014 29.786 58.166 1.00 45.51 ATOM 339 C GLY E 107 25.841 30.852 59.247 1.00 45.51 ATOM 340 O GLY E 107 26.514 30.805 60.295 1.00 45.51 ATOM 341 N GLY F 111 40.788 -8.794 48.156 1.00 45.51 ATOM 342 CA GLY F 111 40.376 -10.101 47.653 1.00 45.51 ATOM 343 C GLY F 111 39.900 -10.901 48.862 1.00 45.51 ATOM 344 O GLY F 111 40.184 -10.544 50.025 1.00 45.51 ATOM 345 N GLY F 112 39.172 -11.984 48.629 1.00 45.51 ATOM 346 CA GLY F 112 38.597 -12.753 49.728 1.00 45.51 ATOM 347 C GLY F 112 39.015 -14.196 49.644 1.00 45.51 ATOM 348 O GLY F 112 38.921 -14.816 48.577 1.00 45.51 ATOM 349 N GLY F 113 39.517 -14.760 50.750 1.00 45.51 ATOM 350 CA GLY F 113 39.759 -16.199 50.778 1.00 45.51 ATOM 351 C GLY F 113 38.734 -16.800 51.737 1.00 45.51 ATOM 352 O GLY F 113 38.220 -16.152 52.661 1.00 45.51 ATOM 353 N GLY F 114 38.378 -18.056 51.481 1.00 45.51 ATOM 354 CA GLY F 114 37.334 -18.714 52.242 1.00 45.51 ATOM 355 C GLY F 114 37.693 -20.151 52.586 1.00 45.51 ATOM 356 O GLY F 114 38.653 -20.720 52.078 1.00 45.51 ATOM 357 N GLY F 115 36.924 -20.732 53.503 1.00 45.51 ATOM 358 CA GLY F 115 37.157 -22.096 53.947 1.00 45.51 ATOM 359 C GLY F 115 36.228 -22.444 55.095 1.00 45.51 ATOM 360 O GLY F 115 35.289 -21.721 55.428 1.00 45.51 ATOM 361 N GLY F 116 36.542 -23.570 55.733 1.00 45.51 ATOM 362 CA GLY F 116 35.767 -24.113 56.846 1.00 45.51 ATOM 363 C GLY F 116 36.672 -24.454 58.037 1.00 45.51 ATOM 364 O GLY F 116 37.675 -25.156 57.900 1.00 45.51 ATOM 365 N GLY F 117 36.294 -23.965 59.230 1.00 45.51 ATOM 366 CA GLY F 117 37.006 -24.228 60.477 1.00 45.51 ATOM 367 C GLY F 117 37.011 -25.707 60.863 1.00 45.51 ATOM 368 O GLY F 117 36.247 -26.506 60.322 1.00 45.51 ATOM 369 N GLY F 118 37.846 -26.047 61.854 1.00 45.51 ATOM 370 CA GLY F 118 37.991 -27.409 62.357 1.00 45.51 ATOM 371 C GLY F 118 36.695 -28.125 62.731 1.00 45.51 ATOM 372 O GLY F 118 36.521 -29.322 62.483 1.00 45.51 ATOM 373 N GLY F 119 35.755 -27.381 63.313 1.00 45.51 ATOM 374 CA GLY F 119 34.494 -27.972 63.699 1.00 45.51 ATOM 375 C GLY F 119 33.286 -27.520 62.884 1.00 45.51 ATOM 376 O GLY F 119 32.161 -27.442 63.385 1.00 45.51 ATOM 377 N GLY F 120 33.534 -27.217 61.597 1.00 45.51 ATOM 378 CA GLY F 120 32.466 -26.988 60.630 1.00 45.51 ATOM 379 C GLY F 120 32.048 -25.573 60.262 1.00 45.51 ATOM 380 O GLY F 120 31.395 -25.426 59.229 1.00 45.51 ATOM 381 N GLY F 121 32.362 -24.517 61.013 1.00 45.51 ATOM 382 CA GLY F 121 31.921 -23.162 60.680 1.00 45.51 ATOM 383 C GLY F 121 32.567 -22.575 59.409 1.00 45.51 ATOM 384 O GLY F 121 33.780 -22.676 59.230 1.00 45.51 ATOM 385 N GLY F 122 31.834 -21.943 58.483 1.00 45.51 ATOM 386 CA GLY F 122 32.407 -21.156 57.390 1.00 45.51 ATOM 387 C GLY F 122 33.122 -19.888 57.856 1.00 45.51 ATOM 388 O GLY F 122 32.752 -19.259 58.857 1.00 45.51 ATOM 389 N GLY F 123 34.195 -19.525 57.132 1.00 45.51 ATOM 390 CA GLY F 123 34.857 -18.246 57.379 1.00 45.51 ATOM 391 C GLY F 123 35.189 -17.594 56.055 1.00 45.51 ATOM 392 O GLY F 123 35.333 -18.267 55.026 1.00 45.51 ATOM 393 N GLY F 124 35.363 -16.279 56.141 1.00 45.51 ATOM 394 CA GLY F 124 35.825 -15.484 55.012 1.00 45.51 ATOM 395 C GLY F 124 36.812 -14.471 55.514 1.00 45.51 ATOM 396 O GLY F 124 36.581 -13.817 56.532 1.00 45.51 ATOM 397 N GLY F 125 37.932 -14.337 54.813 1.00 45.51 ATOM 398 CA GLY F 125 38.932 -13.344 55.197 1.00 45.51 ATOM 399 C GLY F 125 39.191 -12.382 54.041 1.00 45.51 ATOM 400 O GLY F 125 39.496 -12.841 52.950 1.00 45.51 ATOM 401 N GLY F 126 39.063 -11.072 54.252 1.00 45.51 ATOM 402 CA GLY F 126 39.386 -10.074 53.227 1.00 45.51 ATOM 403 C GLY F 126 40.803 -9.546 53.360 1.00 45.51 ATOM 404 O GLY F 126 41.228 -9.155 54.453 1.00 45.51 ATOM 405 N GLY F 127 41.582 -9.510 52.266 1.00 45.51 ATOM 406 CA GLY F 127 42.974 -9.124 52.319 1.00 45.51 ATOM 407 C GLY F 127 43.237 -7.953 51.373 1.00 45.51 ATOM 408 O GLY F 127 42.715 -7.924 50.242 1.00 45.51 ATOM 409 N GLY G 131 75.299 -2.784 62.188 1.00 45.51 ATOM 410 CA GLY G 131 74.881 -1.484 62.702 1.00 45.51 ATOM 411 C GLY G 131 74.405 -0.675 61.499 1.00 45.51 ATOM 412 O GLY G 131 74.692 -1.020 60.334 1.00 45.51 ATOM 413 N GLY G 132 73.672 0.403 61.740 1.00 45.51 ATOM 414 CA GLY G 132 73.096 1.179 60.647 1.00 45.51 ATOM 415 C GLY G 132 73.508 2.624 60.745 1.00 45.51 ATOM 416 O GLY G 132 73.410 3.233 61.818 1.00 45.51 ATOM 417 N GLY G 133 74.011 3.200 59.645 1.00 45.51 ATOM 418 CA GLY G 133 74.247 4.640 59.631 1.00 45.51 ATOM 419 C GLY G 133 73.222 5.245 58.675 1.00 45.51 ATOM 420 O GLY G 133 72.712 4.604 57.744 1.00 45.51 ATOM 421 N GLY G 134 72.860 6.498 58.941 1.00 45.51 ATOM 422 CA GLY G 134 71.816 7.159 58.185 1.00 45.51 ATOM 423 C GLY G 134 72.169 8.600 57.854 1.00 45.51 ATOM 424 O GLY G 134 73.127 9.168 58.370 1.00 45.51 ATOM 425 N GLY G 135 71.400 9.186 56.941 1.00 45.51 ATOM 426 CA GLY G 135 71.628 10.555 56.510 1.00 45.51 ATOM 427 C GLY G 135 70.700 10.910 55.364 1.00 45.51 ATOM 428 O GLY G 135 69.765 10.186 55.022 1.00 45.51 ATOM 429 N GLY G 136 71.012 12.043 54.737 1.00 45.51 ATOM 430 CA GLY G 136 70.236 12.592 53.627 1.00 45.51 ATOM 431 C GLY G 136 71.143 12.947 52.441 1.00 45.51 ATOM 432 O GLY G 136 72.143 13.652 52.586 1.00 45.51 ATOM 433 N GLY G 137 70.769 12.468 51.243 1.00 45.51 ATOM 434 CA GLY G 137 71.482 12.745 50.000 1.00 45.51 ATOM 435 C GLY G 137 71.483 14.227 49.627 1.00 45.51 ATOM 436 O GLY G 137 70.714 15.018 50.174 1.00 45.51 ATOM 437 N GLY G 138 72.317 14.579 48.641 1.00 45.51 ATOM 438 CA GLY G 138 72.459 15.946 48.151 1.00 45.51 ATOM 439 C GLY G 138 71.160 16.661 47.781 1.00 45.51 ATOM 440 O GLY G 138 70.982 17.855 48.039 1.00 45.51 ATOM 441 N GLY G 139 70.225 15.918 47.190 1.00 45.51 ATOM 442 CA GLY G 139 68.962 16.508 46.808 1.00 45.51 ATOM 443 C GLY G 139 67.754 16.044 47.615 1.00 45.51 ATOM 444 O GLY G 139 66.630 15.967 47.112 1.00 45.51 ATOM 445 N GLY G 140 68.001 15.731 48.900 1.00 45.51 ATOM 446 CA GLY G 140 66.932 15.489 49.863 1.00 45.51 ATOM 447 C GLY G 140 66.519 14.069 50.218 1.00 45.51 ATOM 448 O GLY G 140 65.864 13.911 51.247 1.00 45.51 ATOM 449 N GLY G 141 66.839 13.021 49.457 1.00 45.51 ATOM 450 CA GLY G 141 66.402 11.661 49.777 1.00 45.51 ATOM 451 C GLY G 141 67.048 11.065 51.044 1.00 45.51 ATOM 452 O GLY G 141 68.260 11.170 51.226 1.00 45.51 ATOM 453 N GLY G 142 66.315 10.423 51.963 1.00 45.51 ATOM 454 CA GLY G 142 66.889 9.628 53.050 1.00 45.51 ATOM 455 C GLY G 142 67.610 8.367 52.574 1.00 45.51 ATOM 456 O GLY G 142 67.244 7.745 51.566 1.00 45.51 ATOM 457 N GLY G 143 68.683 8.002 53.297 1.00 45.51 ATOM 458 CA GLY G 143 69.350 6.727 53.039 1.00 45.51 ATOM 459 C GLY G 143 69.682 6.064 54.358 1.00 45.51 ATOM 460 O GLY G 143 69.821 6.729 55.393 1.00 45.51 ATOM 461 N GLY G 144 69.861 4.751 54.260 1.00 45.51 ATOM 462 CA GLY G 144 70.324 3.948 55.384 1.00 45.51 ATOM 463 C GLY G 144 71.316 2.943 54.874 1.00 45.51 ATOM 464 O GLY G 144 71.089 2.297 53.850 1.00 45.51 ATOM 465 N GLY G 145 72.435 2.806 55.576 1.00 45.51 ATOM 466 CA GLY G 145 73.439 1.821 55.184 1.00 45.51 ATOM 467 C GLY G 145 73.700 0.850 56.332 1.00 45.51 ATOM 468 O GLY G 145 74.000 1.301 57.428 1.00 45.51 ATOM 469 N GLY G 146 73.577 -0.459 56.109 1.00 45.51 ATOM 470 CA GLY G 146 73.902 -1.465 57.126 1.00 45.51 ATOM 471 C GLY G 146 75.321 -1.986 56.991 1.00 45.51 ATOM 472 O GLY G 146 75.749 -2.366 55.895 1.00 45.51 ATOM 473 N GLY G 147 76.098 -2.029 58.087 1.00 45.51 ATOM 474 CA GLY G 147 77.492 -2.410 58.032 1.00 45.51 ATOM 475 C GLY G 147 77.757 -3.587 58.968 1.00 45.51 ATOM 476 O GLY G 147 77.233 -3.628 60.098 1.00 45.51 ATOM 477 N GLY H 151 63.195 -41.496 48.742 1.00 45.51 ATOM 478 CA GLY H 151 63.714 -40.174 48.407 1.00 45.51 ATOM 479 C GLY H 151 64.044 -39.490 49.730 1.00 45.51 ATOM 480 O GLY H 151 63.591 -39.921 50.811 1.00 45.51 ATOM 481 N GLY H 152 64.831 -38.424 49.688 1.00 45.51 ATOM 482 CA GLY H 152 65.274 -37.768 50.914 1.00 45.51 ATOM 483 C GLY H 152 64.919 -36.305 50.891 1.00 45.51 ATOM 484 O GLY H 152 65.179 -35.611 49.900 1.00 45.51 ATOM 485 N GLY H 153 64.287 -35.805 51.961 1.00 45.51 ATOM 486 CA GLY H 153 64.090 -34.364 52.073 1.00 45.51 ATOM 487 C GLY H 153 64.991 -33.883 53.207 1.00 45.51 ATOM 488 O GLY H 153 65.351 -34.621 54.137 1.00 45.51 ATOM 489 N GLY H 154 65.420 -32.627 53.106 1.00 45.51 ATOM 490 CA GLY H 154 66.369 -32.075 54.052 1.00 45.51 ATOM 491 C GLY H 154 66.013 -30.654 54.460 1.00 45.51 ATOM 492 O GLY H 154 65.151 -30.007 53.874 1.00 45.51 ATOM 493 N GLY H 155 66.666 -30.179 55.517 1.00 45.51 ATOM 494 CA GLY H 155 66.418 -28.844 56.035 1.00 45.51 ATOM 495 C GLY H 155 67.190 -28.625 57.322 1.00 45.51 ATOM 496 O GLY H 155 68.050 -29.411 57.719 1.00 45.51 ATOM 497 N GLY H 156 66.827 -27.538 58.001 1.00 45.51 ATOM 498 CA GLY H 156 67.458 -27.116 59.249 1.00 45.51 ATOM 499 C GLY H 156 66.408 -26.828 60.330 1.00 45.51 ATOM 500 O GLY H 156 65.457 -26.075 60.117 1.00 45.51 ATOM 501 N GLY H 157 66.602 -27.422 61.520 1.00 45.51 ATOM 502 CA GLY H 157 65.733 -27.224 62.676 1.00 45.51 ATOM 503 C GLY H 157 65.722 -25.781 63.177 1.00 45.51 ATOM 504 O GLY H 157 66.580 -24.976 62.812 1.00 45.51 ATOM 505 N GLY H 158 64.770 -25.481 64.070 1.00 45.51 ATOM 506 CA GLY H 158 64.600 -24.156 64.658 1.00 45.51 ATOM 507 C GLY H 158 65.855 -23.527 65.261 1.00 45.51 ATOM 508 O GLY H 158 66.100 -22.324 65.137 1.00 45.51 ATOM 509 N GLY H 159 66.681 -24.354 65.902 1.00 45.51 ATOM 510 CA GLY H 159 67.895 -23.849 66.502 1.00 45.51 ATOM 511 C GLY H 159 69.189 -24.290 65.825 1.00 45.51 ATOM 512 O GLY H 159 70.231 -24.454 66.465 1.00 45.51 ATOM 513 N GLY H 160 69.112 -24.482 64.495 1.00 45.51 ATOM 514 CA GLY H 160 70.295 -24.683 63.666 1.00 45.51 ATOM 515 C GLY H 160 70.714 -26.083 63.244 1.00 45.51 ATOM 516 O GLY H 160 71.499 -26.178 62.301 1.00 45.51 ATOM 517 N GLY H 161 70.265 -27.178 63.858 1.00 45.51 ATOM 518 CA GLY H 161 70.704 -28.522 63.478 1.00 45.51 ATOM 519 C GLY H 161 70.221 -28.982 62.088 1.00 45.51 ATOM 520 O GLY H 161 69.048 -28.815 61.755 1.00 45.51 ATOM 521 N GLY H 162 71.055 -29.572 61.221 1.00 45.51 ATOM 522 CA GLY H 162 70.613 -30.248 60.001 1.00 45.51 ATOM 523 C GLY H 162 69.800 -31.516 60.260 1.00 45.51 ATOM 524 O GLY H 162 70.007 -32.235 61.248 1.00 45.51 ATOM 525 N GLY H 163 68.826 -31.775 59.371 1.00 45.51 ATOM 526 CA GLY H 163 68.095 -33.040 59.421 1.00 45.51 ATOM 527 C GLY H 163 67.928 -33.575 58.016 1.00 45.51 ATOM 528 O GLY H 163 67.951 -32.820 57.035 1.00 45.51 ATOM 529 N GLY H 164 67.702 -34.883 57.970 1.00 45.51 ATOM 530 CA GLY H 164 67.375 -35.569 56.728 1.00 45.51 ATOM 531 C GLY H 164 66.295 -36.574 57.007 1.00 45.51 ATOM 532 O GLY H 164 66.363 -37.313 57.991 1.00 45.51 ATOM 533 N GLY H 165 65.280 -36.606 56.153 1.00 45.51 ATOM 534 CA GLY H 165 64.205 -37.580 56.316 1.00 45.51 ATOM 535 C GLY H 165 64.077 -38.439 55.061 1.00 45.51 ATOM 536 O GLY H 165 63.942 -37.886 53.980 1.00 45.51 ATOM 537 N GLY H 166 64.132 -39.766 55.180 1.00 45.51 ATOM 538 CA GLY H 166 63.922 -40.669 54.043 1.00 45.51 ATOM 539 C GLY H 166 62.484 -41.142 53.940 1.00 45.51 ATOM 540 O GLY H 166 61.900 -41.598 54.930 1.00 45.51 ATOM 541 N GLY H 167 61.863 -41.062 52.750 1.00 45.51 ATOM 542 CA GLY H 167 60.465 -41.390 52.583 1.00 45.51 ATOM 543 C GLY H 167 60.298 -42.473 51.518 1.00 45.51 ATOM 544 O GLY H 167 60.971 -42.438 50.470 1.00 45.51

1 0

Support for KNIME?
by Schubert, Carsten [PRDUS] 24 Oct '07

24 Oct '07

Hi, I was wondering if anybody has looked into integrating phenix with KNIME (http://www.knime.org/), as part of a pipeline for structure solution. Is this something the developers have looked into? Cheers, Carsten

2 1

problems with map quality, refinement and R/Rfree
by Joe Smith 19 Oct '07

19 Oct '07

Hi all, We have data sets for a protein-RNA complex at 3.2 A resolution. . The data belong to the space group I4122 and contains one molecule of Protein-RNA complex (300AA and 16nt; 66% solvent content) in the asym unit. We have managed to get phases using Se-SAD and the present model contains 60% of the protein atoms (250 residues many of them build as Ala) and almost complete RNA (16nt). We could not locate ~20 % of the residues (present in various loops as well as at N- and C-terminal ends). First 120 residues present at N-terminal end seem to have poor relatively main-chain density and almost no side chain density. RNA and 130 residues present at the C-terminal end have good electron density for main-chain as well as side chain. The solution seems to be correct as molecular replacement trials with this model gave same solution in Phaser, Molrep and AMoRe. Solution seems to be also correct because as expected one RNA strand present in asym unit pairs with another one coming from symmetry related molecule. We have checked data in space group I4122 with CCP4 (SFCHECK, cumulative intensity distribution), Yeates server as well as Phenix.xtriage. In all the cases it indicates no twinning. However if I process the data in lower symmetry space group it does indicate presence of almost perfect twin. We realize that this could be just because of processing data in lower symmetry space group and data in all probability may still be fine. The problem is now with refinement and model building. Refinement with CNS and Refamc gave considerably higher value of R and R free. In CNS1.1, refinement with small changes in the model some time leads to large shift in R and R-free value. Refmac: R=36; Rfree=47 CNS1.1: R=40-59; R-free=45-63 However in both the cases map looks more or less same (with reasonably good density for the main-chain as well as RNA) I tried refining with phenix.refine and there is some improvement in the R(34%) and Rfree(40%) values. I think may be robust bulk solvent correction incorporated in phenix.refine has helped in this case. However, I still see no improvement in the map quality for the first 120 residues. In the absence of any clear density I am unable to build any further. I feel N-terminal domain is bit flexible and may have overall poor density. I have used Se position as well as predicted secondary structure in assigning the amino acid in the map but due to few breaks in the N-terminal domain as well as poor density I am unable to assign any amino acid into the poly ala main chain. Frankly speaking, I do not know how to proceed further. I welcome any kind of suggestions which could help us in this case. Regards Joe

1 0

1.3 beta rc3 version FC2 gui error
by Balasundaresan 12 Oct '07

12 Oct '07

Dear Author, I downloaded and installed the 1.3 beta rc3 version(GUI) in FEDORA CORE 2.0 and everything went well during installation and sourced it in .cshrc. while typing phenix in the command line I faced the below error, Traceback (most recent call last): File "/usr/local/phenix-1.3b-rc3/phenix/wxGUI/wxPhenix.py", line 11, in <module> import wx File "/usr/local/phenix-1.3b-rc3/build/intel-linux-2.6/base/lib/python2.5/site-packages/wx-2.8-gtk2-ansi/wx/__init__.py", line 45, in <module> from wx._core import * File "/usr/local/phenix-1.3b-rc3/build/intel-linux-2.6/base/lib/python2.5/site-packages/wx-2.8-gtk2-ansi/wx/_core.py", line 4, in <module> import _core_ ImportError: libstdc++.so.6: cannot open shared object file: No such file or directory any opinion or suggestions are welcome... regards Bala -- Balasundaresan <d-bala(a)aist.go.jp>

3 2

phenix.refine python error !!
by john kryst 12 Oct '07

12 Oct '07

Hi all !!! I have recently updated phenix version to phenix-1.3b-rc3. After that when i run phenix.refine it runs properly. But while writing the pdb file it is giving the following error. Traceback (most recent call last): File "/usr/local/phenix-1.3b-rc3/phenix/phenix/command_line/refine.py", line 5, in <module> command_line.run(command_name="phenix.refine", args=sys.argv[1:]) File "/usr/local/phenix-1.3b-rc3/phenix/phenix/refinement/command_line.py", line 89, in run refine_object.write_refined_pdb(f_pdb) File "/usr/local/phenix-1.3b-rc3/phenix/phenix/refinement/driver.py", line 1101, in write_refined_pdb pdb_header.write_remark_3(info = m_info, out = f) File "/usr/local/phenix-1.3b-rc3/mmtbx/mmtbx/pdb_header.py", line 21, in write_remark_3 info.show_remark_3(out = out) File "/usr/local/phenix-1.3b-rc3/mmtbx/mmtbx/model_statistics.py", line 483, in show_remark_3 self.data_x.show_remark_3(out = out) File "/usr/local/phenix-1.3b-rc3/mmtbx/mmtbx/f_model.py", line 2034, in show_remark_3 bin.n_work, bin.n_free, bin.r_work*100., bin.r_free*100.) TypeError: unsupported operand type(s) for *: 'NoneType' and 'float' I am using fedora 5, python 2.4.2. I have used phenix-installer-1.3b-rc3-intel-linux-2.4.tar. It was working fine in the last build. Google'ing the error didn't help much. Thanks for your inputs. regards John

2 1

Hires input file problem
by Troy E Messick 11 Oct '07

11 Oct '07

Hi all, I seem to be having a problem specifying the labels for the Hires dataset for an Autobuild run. Here is my input script: input_data_file sharp.mtz input_labels 'Fdm' 'SIGFPsha' 'PHIdm' 'FOMdm' 'HLAdm' 'HLBdm' 'HLCdm' 'HLDdm' 'FreeR_flag' input_pdb_file ab.pdb input_seq_file seq.dat input_hires_file output.native.sca Here is the error from the AutoBuild.log file: ************************************************************ Failed to carry out AutoBuild_datafile_info_inputs: 'all_input_hires_labels' ************************************************************ I've tried to use the mtz file from the ImportRawData_run directory and specify the columns by substituting the last line in my input script file with: input_hires_file output_PHX.mtz input_hires_labels 'output.native' 'SIGoutput.native' which are the only labels I could find from mtzdump and that doesn't work either. What am I missing here? Any suggestions would be greatly appreciated. Thanks, Troy

5 4

"Aromatic" question
by Claudia Scotti 10 Oct '07

10 Oct '07

Dear list, I've refined a protein at 2.0 A resolution with its ligand, a small molecule which includes a phenyl group. For this, I used elbow to generate the cif file, and in this file the atoms of the phenyl ring are correctly defined as "aromatic". However, the pdb output of the refinement shows a boat configuration for the 6 carbon atoms ring, with a very nice fit to the electron density. This would suggest a flexible cyclohexyl- substituent instead of the expected, typically planar phenyl ring. As my chemistry is poor, I'd really need some suggestions on where I'm wrong: did I give the wrong cif file or does phenix recognise a better fitting in a boat structure, indicating that my ligand phenyl moiety has been reduced somehow to a cyclohexyl one? Or is the aromatic ring of the phenyl group not so planar as I've supposed it to be until now? Any help would be very appreciated. Many many thanks, Claudia Claudia Scotti Dipartimento di Medicina Sperimentale Sezione di Patologia Generale Universita' di Pavia Piazza Botta, 10 27100 Pavia Italia Tel. 0039 0382 986335/8/1 Facs 0039 0382 303673 _________________________________________________________________ Connect to the next generation of MSN Messenger http://imagine-msn.com/messenger/launch80/default.aspx?locale=en-us&source=…

5 6