- modeller_usage - salilab.org

can salign output a "structural mapping" of residues
by Benjamin SCHWARZ 08 Apr '11

08 Apr '11

As a first (naive) question on that mailing list, I wonder if (and how) it is possible to retrieve residues that are structurally aligned as a result of a aln.salign() run (object aln being of type alignment). To precise my question, I know a (multiple) sequence alignment is produced as a result of this salign command and can be output with aln.write(), but I am more concerned by the possible mapping of residues in the structural alignment, that might not be apparent in the sequence. --Ben.S

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IS SCWRL4 helpful for Models
by Ashish Runthala 07 Apr '11

07 Apr '11

MODELLER9v9 models couldn't be improved further with SCWRL4. There was no difference in the GDT, TM_Score and RMSD statistics of model with and without SCWRL usage. So are all the side chain rotamer loci best optimized with the Calpha atom topologies? Thanks Ashish Ashish Runthala, Lecturer, Structural Biology Cell, Biological Sciences Group, BITS, Pilani Rajasthan, INDIA

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Re: [modeller_usage] How to get Secondary Structure in Alignment file
by Thomas Evangelidis 06 Apr '11

06 Apr '11

Dear Ashish, Thomas, > I don't expect all this what you replied. > > See i understand all that what you told. But there is a big problem there, > to try multiple alignments and iterated trials to land on good models(which > itself is ambiguous, as you can't really discriminate good and bad model, > until you have answer or GDT). > Two important factors influence the ability to predict accurate models: the extent of structural conservation between target and template, and the correctness of alignment (Kryshtafovych et al 2005, PMID: 16187365). The alternative alignments serve as a means to optimize the alignment at regions of sparse sequence similarity, which usually do not include common SSEs. Apart from statistical potentials and protein geometry checks, I'm not aware of any other method to discriminate good and bad structures. > So i am developing a complete in-house algorithm to result in the best > representative alignment from > the considered templates against the target. So i want to incorporate > secondary structure information or localized fold topologies to generate a > 3D alignment file. Hence i am looking forward for a python script which can > be integrated with MODELLER to result in the information like this. > > Template1> HCLCH > Template2> HCLHH > Target> xxxxx > (H=Helix. C=Coil, L=Loop) > > I JUST NEED SECONDARY STRUCTURE INFORMATION OF EACH ALIGNED RESIDUE OF EACH > TEMPLATE, BASED ON ITS PROBABILITY TO LAND IN SAME FOLD, AS PER THE > AVAILABLE PROXIMAL RESIDUES. > > I'm not aware how you can get the sequence alignment in that form from MODELLER, but there must be a way perhaps with another program. Alternatively you can write a code snippet in python that will call PyMol or VMD to get the secondary structure of each residue of your templates (I can give you my scripts in case you are interested). > Ya, and by the way, SCRWL won't help if you choose bad template/alignment. > Refinement improves GDT_TS scores by just 4 or 5%. Good coordinate selection > is most important. MODELLER also can't result in good models, if you mix up > incorrect template informations, and the problem becomes more complex, when > the new fold comes up. > > I never said that. When sequence identity <35%, the rotamers of conserved residues may differ in up to 45% of the cases (Sanchez et al. 1997, PMID: 9485495 ). SCWRL4 is used upon optimum template(s) and alignment selection to optimize the rotamers. This approach has been also implemented by the best performing human-expert group in CASP8 (Venclovas et al 2009, PMID: 19639635). In essence, I use the alternative-alignment approach when I have to choose between templates that have 25-40% sequence identity with the target. Provided that all templates share the same fold (i.e. may belong to the same SCOP family or have high CE-MC mean *Z*-scores), the selection of multiple templates in that low sequence similarity level produces better models than those constructed from a single parent (Moult J 2005, PMID: 15939584; Dalton et al 2007, PMID: 17510171). HMOPAL (that's the name of my pipeline) aims to select the best template combination and alignment based on the native-likeness of the resulting homology models, as judged primarily by the DOPE-HR raw score, and secondarily by PROCHECK and WHATCHECK. regards, Thomas > Thanks for support. > Ashish > > > Ashish Runthala, > Lecturer, Structural Biology Cell, > Biological Sciences Group, > BITS, Pilani > Rajasthan, INDIA > > ----- Original Message ----- > From: "Thomas Evangelidis" <tevang3(a)gmail.com> > To: "Ashish Runthala" <ashishr(a)bits-pilani.ac.in> > Cc: "modeller usage" <modeller_usage(a)salilab.org> > Sent: Tuesday, March 29, 2011 4:46:20 AM GMT +05:30 Chennai, Kolkata, > Mumbai, New Delhi > Subject: Re: [modeller_usage] How to get Secondary Structure in Alignment > file > > > > > On 27 March 2011 10:05, Ashish Runthala < ashishr(a)bits-pilani.ac.in > > wrote: > > > Dear Thomas, > I will write it clearly this time. > Take simplest case.Suppose, I have a structural/sequence alignment of 3 > templates against a target sequence. Now, as modeller predicts tertiary > conformation for the target sequence, it surely predicts the alignment based > secondary structure information against all the templates. So now i want > that specific secondary structure information along with the alignment file > for the aligned templates against the target sequence. > Now my C script will take on this alignment file to generate the > representative best possible optimum alignment for the considered target > sequence. These models in my tried iterations for the CASP8 targets gave > excellent results. > > > So if I understand correctly, your script creates alternative alignments, > then runs Modeller to build a model of the target from each alignment, it > reads the secondary structure (SS) from each model, and based on this SS it > judges which alternative alignment is the optimum. Is this how it works? Can > you elaborate on the algorithm? What are the criteria to select the optimum > alignment and what is the answer you seek from the mailing list? > > > I think i made myself clear this time. > By the way, what you are working on. I think you are also working on the > same topics. What you have redefined? I am interested to know that. > > > I've been working on optimization at the alignment level in the past, but > in my approach the selection of the optimum alignment and template > combination is based on the overall native-likeness of the resulting > homology models, not just the secondary structure of the target. More > specifically, I create homology models at several levels of optimization and > refinement from alternative alignments and different template combinations. > The resulting models are sorted according to the DOPE-HR score, and the best > of them undergo side-chain optimization with SCWRL4, and extensive > stereochemical tests with the programs PROCHECK and WHAT_CHECK to select the > best of them. The whole procedure is streamlined and parallelized with a > combination of bash and python scripts. However, it has been tested only on > my cases and a few CASP9 targets. More details can be found at: > > https://sites.google.com/site/hmopalpipeline/home (I will update the > website tomorrow) > > > > > Thanks in advance, > > Ashish > > Ashish Runthala, > Lecturer, Structural Biology Cell, > Biological Sciences Group, > BITS, Pilani > Rajasthan, INDIA > > ----- Original Message ----- > From: "Thomas Evangelidis" < tevang3(a)gmail.com > > To: "Ashish Runthala" < ashishr(a)bits-pilani.ac.in > > > > > Cc: "modeller usage" < modeller_usage(a)salilab.org > > Sent: Saturday, March 26, 2011 6:06:02 PM GMT +05:30 Chennai, Kolkata, > Mumbai, New Delhi > Subject: Re: [modeller_usage] How to get Secondary Structure in Alignment > file > > > > On 26 March 2011 07:47, Ashish Runthala < ashishr(a)bits-pilani.ac.in > > wrote: > > > Dear Thomas, > You mentioned the free tools in details. I appreciate that. But what i > don't understand is to manually call everyone, and then keep on doing it, is > tedious but fun it is. > > > So if I get it right this time, you didn't ask what commercial free tools > are available to display your sequence alignment along with the secondary > structure, is that correct? Could you please be more careful with your > syntax cause it's kind of difficult to follow you. > > > I had a query that template secondary structure information is there in > templates, but with indels, that may be disturbed. I mean the native > information is deteriorated. > > So if based on indels, available in current alignment, if i can link > directly to a python script. So that my next programme to generate the > optimal alignment will become successful, as i did all of these several > times manually, to design the algorithm to generate best representative > alignment. > > > So you want to write a python script that can cope with indels inside SSEs. > Namely, given a structure-based alignment between your target and templates, > you want to select which of the following alignments is the optimum: > > target > HCSIHHSC > Template1> HCSIHISC > Template2> HCSHHISC > ------------------------------------------------------- > target > HCS-IHHSC > Template1> HCS-IHISC > Template2> HCSH-HISC > ------------------------------------------------------- > target > HCSI-HHSC > Template1> HCS-IHISC > Template2> HCS-HHISC > > etc. > > > Is this what you seek? > > > > > > > > Will you please elaborate this time. > > > Thanks, > Ashish > > > Ashish Runthala, > Lecturer, Structural Biology Cell, > Biological Sciences Group, > BITS, Pilani > Rajasthan, INDIA > > > > > ----- Original Message ----- > From: "Thomas Evangelidis" < tevang3(a)gmail.com > > To: "Ashish Runthala" < ashishr(a)bits-pilani.ac.in > > Cc: "modeller" < modeller_usage(a)salilab.org > > Sent: Friday, March 25, 2011 4:50:42 PM GMT +05:30 Chennai, Kolkata, > Mumbai, New Delhi > Subject: Re: [modeller_usage] How to get Secondary Structure in Alignment > file > > Maestro from Schrodinger can display both the predicted secondary structure > elements (SSE) of the target and the SSE of the templates above the > alignment dynamically (namely if you change the alignment the SSEs are > changed accordingly). > > Alternatively you can use the following commercial free tools: > > ESPript ( http://espript.ibcp.fr/ESPript/ESPript/ ): can create an image > of your alignment with the SSEs of your templates above it. No SSE of the > target is displayed though. > > MolIDE ( http://dunbrack.fccc.edu/molide/index.php ): I have the notion > that this alignment editor (and not only) can display both the predicted SSE > of the target and the SSE of the templates. However, I didn't manage to run > it yet due to compilation problems. I intend to give it a try in the near > future. > > STRAP ( http://3d-alignment.eu/ ): it can do both but the GUI is not handy > in Linux (windows and fonts are unequal, etc.). > > Finally you can add a row with the secondary structure (as you wrote it in > your email) above each sequence in your alignment editor. I prefer Jalview > and like to play around with groups and colors. See the attached image for > an example. SSE of your templates can be retrieved from PDB (e.g. > http://www.pdb.org/pdb/explore/sequenceText.do?structureId=2IXF&chainId=A) whereas the SSE of your target can be predicted by Jpred3 ( > http://www.compbio.dundee.ac.uk/www-jpred/ ). > > > HTH, > > Thomas > > > > > On 25 March 2011 05:47, Ashish Runthala < ashishr(a)bits-pilani.ac.in > > wrote: > > > Dear Modellers, > Suppose i have two templates, and a target sequence. Instead of sequence > alignment based file, i want to consider the secondary structure > information, like given below > > Template1> HCSIHISC > Template2> HCSHHISC > > H=Helix, C=Coil, S-Strand, I=Indels > > Is it possible to get the alignment in this case for multiple templates > against the target sequence( whose structure can also be represented as best > aligned folds) > > Thanks > Ashish > > Ashish Runthala, > Lecturer, Structural Biology Cell, > Biological Sciences Group, > BITS, Pilani > Rajasthan, INDIA > _______________________________________________ > modeller_usage mailing list > modeller_usage(a)salilab.org > https://salilab.org/mailman/listinfo/modeller_usage > > > > -- > > > ====================================================================== > > Thomas Evangelidis > > PhD student > > Biomedical Research Foundation, Academy of Athens > > 4 Soranou Ephessiou , 115 27 Athens, Greece > > email: tevang(a)bioacademy.gr > > tevang3(a)gmail.com > > > website: https://sites.google.com/site/thomasevangelidishomepage/ > > > > > > > -- > > > ====================================================================== > > Thomas Evangelidis > > PhD student > > Biomedical Research Foundation, Academy of Athens > > 4 Soranou Ephessiou , 115 27 Athens, Greece > > email: tevang(a)bioacademy.gr > > tevang3(a)gmail.com > > > website: https://sites.google.com/site/thomasevangelidishomepage/ > > > > > > > -- > > > ====================================================================== > > Thomas Evangelidis > > PhD student > > Biomedical Research Foundation, Academy of Athens > > 4 Soranou Ephessiou , 115 27 Athens, Greece > > email: tevang(a)bioacademy.gr > > tevang3(a)gmail.com > > > website: https://sites.google.com/site/thomasevangelidishomepage/ > > > > -- ====================================================================== Thomas Evangelidis PhD student Biomedical Research Foundation, Academy of Athens 4 Soranou Ephessiou , 115 27 Athens, Greece email: tevang(a)bioacademy.gr tevang3(a)gmail.com website: https://sites.google.com/site/thomasevangelidishomepage/

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Re: [modeller_usage] modeller_usage Digest, Vol 10, Issue 62
by Ashish Runthala 05 Apr '11

05 Apr '11

Dear MODELLERS, There is a small bug. If there is a space gap" " left in an alignment file, somehow by mistake. MODELLER doesn't ignore it to consider the next character in the specified sequence array details. Ashish Ashish Runthala, Lecturer, Structural Biology Cell, Biological Sciences Group, BITS, Pilani Rajasthan, INDIA ----- Original Message ----- From: "modeller usage-request" <modeller_usage-request(a)salilab.org> To: "modeller usage" <modeller_usage(a)salilab.org> Sent: Tuesday, April 5, 2011 10:48:08 AM GMT +05:30 Chennai, Kolkata, Mumbai, New Delhi Subject: modeller_usage Digest, Vol 10, Issue 62 Send modeller_usage mailing list submissions to modeller_usage(a)salilab.org To subscribe or unsubscribe via the World Wide Web, visit https://salilab.org/mailman/listinfo/modeller_usage or, via email, send a message with subject or body 'help' to modeller_usage-request(a)salilab.org You can reach the person managing the list at modeller_usage-owner(a)salilab.org When replying, please edit your Subject line so it is more specific than "Re: Contents of modeller_usage digest..." Today's Topics: 1. Re: modelling a protein withtow chains (Modeller Caretaker) 2. Re: modeller_usage Digest, Vol 10, Issue 61 (Ashish Runthala) ---------------------------------------------------------------------- Message: 1 Date: Mon, 04 Apr 2011 18:01:11 -0700 From: Modeller Caretaker <modeller-care(a)salilab.org> Subject: Re: [modeller_usage] modelling a protein withtow chains To: Houcemeddine Othman <houcemoo(a)gmail.com> Cc: modeller_usage(a)salilab.org Message-ID: <4D9A69D7.1070702(a)salilab.org> Content-Type: text/plain; charset=ISO-8859-1; format=flowed On 4/4/11 5:06 PM, Houcemeddine Othman wrote: > I try to model an heterodimer using this alignment If it's a heterodimer, why are you imposing symmetry restraints? The two subunits won't be the same. > each time it gives me this error message > define__595E> Number of selected atoms in sets 2 & 3 is not the > same: 121 128 You can't make two differently-sized sets of atoms symmetric. > Can you tell me please what's wrong in my alignment file There's nothing wrong with your alignment file. But remove the symmetry restraint from your Python script (in this case, use the automodel class rather than MyModel). Ben Webb, Modeller Caretaker -- modeller-care(a)salilab.org http://www.salilab.org/modeller/ Modeller mail list: http://salilab.org/mailman/listinfo/modeller_usage ------------------------------ Message: 2 Date: Tue, 5 Apr 2011 10:43:50 +0530 (IST) From: Ashish Runthala <ashishr(a)bits-pilani.ac.in> Subject: Re: [modeller_usage] modeller_usage Digest, Vol 10, Issue 61 To: modeller usage <modeller_usage(a)salilab.org> Message-ID: <21943615.630261301980430322.JavaMail.root(a)mailserver.bits-pilani.ac.in> Content-Type: text/plain; charset=utf-8 Sir, *****The whole protein will be moved, of course, but only the RMSD of the selection will be minimized.********** This is not the case. When we use the rotation and translation matrices, on X,Y, and Z sequentially as i did in my program, even if you specify chunk length, entire matrix is translated, you don't choose a subset there. So entire matrix transformation takes place. But lastly for RMSD fit, you just check for selected atoms. Hence, RMSD displayed seems for chunk, but in background entire protein RMSD can be computed, which is not asked by the user. Ashish Ashish Runthala, Lecturer, Structural Biology Cell, Biological Sciences Group, BITS, Pilani Rajasthan, INDIA ----- Original Message ----- From: "modeller usage-request" <modeller_usage-request(a)salilab.org> To: "modeller usage" <modeller_usage(a)salilab.org> Sent: Tuesday, April 5, 2011 5:36:59 AM GMT +05:30 Chennai, Kolkata, Mumbai, New Delhi Subject: modeller_usage Digest, Vol 10, Issue 61 Send modeller_usage mailing list submissions to modeller_usage(a)salilab.org To subscribe or unsubscribe via the World Wide Web, visit https://salilab.org/mailman/listinfo/modeller_usage or, via email, send a message with subject or body 'help' to modeller_usage-request(a)salilab.org You can reach the person managing the list at modeller_usage-owner(a)salilab.org When replying, please edit your Subject line so it is more specific than "Re: Contents of modeller_usage digest..." Today's Topics: 1. Re: salign: specify chains to superpose (Modeller Caretaker) 2. Modeller 9.9 release (Modeller Caretaker) 3. modelling a protein withtow chains (Houcemeddine Othman) ---------------------------------------------------------------------- Message: 1 Date: Fri, 01 Apr 2011 13:47:28 -0700 From: Modeller Caretaker <modeller-care(a)salilab.org> Subject: Re: [modeller_usage] salign: specify chains to superpose To: Yingjie Lin <Yingjie.Lin(a)mssm.edu> Cc: modeller <modeller_usage(a)salilab.org> Message-ID: <4D9639E0.7020406(a)salilab.org> Content-Type: text/plain; charset=ISO-8859-1; format=flowed On 03/31/2011 09:08 AM, Yingjie Lin wrote: > I wonder what is the best way to superpose two multi-chain proteins, > and explicitly specify the chains to include in superposition. I know > that I can read only the wanted chains into the alignment, but I also > want to make sure that the other chains move according to the > superposition. Just to be clear here, we should distinguish structural *alignment* (which is what SALIGN does) from superposition (which is what selection.superpose() does). Superposition simply rotates and translates one protein, without changing the alignment, to minimize the RMSD between Calpha atoms in aligned residues. Structural alignment also adds or removes gaps, changing the aligned residues. If you really want to do superposition, simply use selection.superpose() and just give it a selection of atoms in the chains you want to superpose. The whole protein will be moved, of course, but only the RMSD of the selection will be minimized. If you want to do a structural alignment, your first suggestion is probably better - read in just the chains you want, make the alignment, then rotate and translate the full protein accordingly. Ben Webb, Modeller Caretaker -- modeller-care(a)salilab.org http://www.salilab.org/modeller/ Modeller mail list: http://salilab.org/mailman/listinfo/modeller_usage ------------------------------ Message: 2 Date: Mon, 04 Apr 2011 12:03:57 -0700 From: Modeller Caretaker <modeller-care(a)salilab.org> Subject: [modeller_usage] Modeller 9.9 release To: modeller_announce(a)salilab.org, modeller_usage(a)salilab.org Message-ID: <4D9A161D.50202(a)salilab.org> Content-Type: text/plain; charset=ISO-8859-1; format=flowed The new version of Modeller, 9.9, is now available for download! Please see the download page at http://salilab.org/modeller/ for more information. If you have a license key for Modeller 8 or 9, there is no need to reregister for Modeller 9.9 - the same license key will work. (It won't do any harm to reregister if you want to, though!) 9.9 is primarily a bugfix release relative to the last public release (9v8). Major user-visible changes include: # The Windows version of Modeller is now only supported on XP Service Pack 2 or later. If you want to run Modeller on Windows 98, ME, 2000, or NT, use Modeller 9v8. # Added support for Python 2.7 to Windows and Linux Modeller; Python 2.5 is now supported on all platforms. # Initial models generated by automodel now always contain valid PDB coordinates, i.e. each coordinate is in the range -999.999 to 9999.999. # During loop modeling, if atoms are missing from the initial model, loopmodel.loop.write_defined_only can be set True to write out PDBs containing only non-loop atoms present in the initial model. # When reading new-style PDB files (with element names in columns 77-78) Modeller will now use this information to determine whether an atom is a hydrogen. (With old-style or non-conformant PDB files, it will continue to guess based on the atom name, so will not read mercury ions for example unless env.io.hydrogen=True, since it cannot unambiguously determine whether HG is mercury or "hydrogen bonded to CG".) See the Modeller manual for a full change log: http://salilab.org/modeller/9.9/manual/node38.html If you encounter bugs in Modeller 9.9, please see http://salilab.org/modeller/9.9/manual/node10.html for information on how to report them. Note: you are receiving this email either because you subscribed to the modeller_usage mailing list, or you provided this address when you requested a Modeller license and you ticked the "notify me of new releases" box. In the latter case, if you no longer wish to receive announcements of new Modeller releases, simply reply to this email and let us know. Ben Webb, Modeller Caretaker -- modeller-care(a)salilab.org http://www.salilab.org/modeller/ Modeller mail list: http://salilab.org/mailman/listinfo/modeller_usage ------------------------------ Message: 3 Date: Tue, 5 Apr 2011 01:06:57 +0100 From: Houcemeddine Othman <houcemoo(a)gmail.com> Subject: [modeller_usage] modelling a protein withtow chains To: modeller_usage(a)salilab.org Message-ID: <BANLkTikUh9qOU-NsGxRqOB4+Q7Dqy+uTWg(a)mail.gmail.com> Content-Type: text/plain; charset="iso-8859-1" Hi I try to model an heterodimer using this alignment >P1;1DZB2 structureX:1DZB2:1:A:107:B:::: QVKLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPEQGLEWIGRIDPANGNTKYDPKFQGKATITADTSSNTAYLQLSSLTSEDTAVYYCAR-----WDWYFDVWGQGTTVTVSSG/ ------------DIELTQSPSSMYTSLGERVTITCKASQDINSYLRWFQQKPGKSPKTLIYYATSLADGVPSRFSGSGSGQDYSLTISSLESDDTTTYYCLQHGESPYTFGGGTKLEIK---------* >P1;atc sequence::::::::: -VKLQQSGGGLVQPGGSLKLSCAASGFDFSRYWMSWVRQAPGKGLEWIGEINPDSSTINYTPSLKDTFIISRDNAKNTLYLQMSKVRSEDTALYYCARQGYDGYHWYFDVWGQGTTVTVSSE/ SLDLGGGGGGGGDIQLTQSPSSLSASVGETVTLTCGASENIYGGLNWYQRKQGKSPQLLIYGATKLADGMSSRFSGGGSGRQYFLKITSLHPDDVATYYCQNVLSNPLTFGAGTKLELKRADAAPTVS* each time it gives me this error message define__595E> Number of selected atoms in sets 2 & 3 is not the same: 121 128 Can you tell me please what's wrong in my alignment file script used: # Homology modeling by the automodel class # # Demonstrates how to build multi-chain models, and symmetry restraints # from modeller import * from modeller.automodel import * # Load the automodel class log.verbose() # Override the 'special_restraints' and 'user_after_single_model' methods: class MyModel(automodel): def special_restraints(self, aln): # Constrain the A and B chains to be identical (but only restrain # the C-alpha atoms, to reduce the number of interatomic distances # that need to be calculated): s1 = selection(self.chains['A']).only_atom_types('CA') s2 = selection(self.chains['B']).only_atom_types('CA') self.restraints.symmetry.append(symmetry(s1, s2, 1.0)) def user_after_single_model(self): # Report on symmetry violations greater than 1A after building # each model: self.restraints.symmetry.report(1.0) env = environ() # directories for input atom files env.io.atom_files_directory = './' a = MyModel(env, alnfile = 'ali.pir', knowns = '1DZB2', sequence = 'atc') a.starting_model= 1 a.ending_model = 1 a.make()

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Re: [modeller_usage] modeller_usage Digest, Vol 10, Issue 61
by Ashish Runthala 04 Apr '11

04 Apr '11

Sir, *****The whole protein will be moved, of course, but only the RMSD of the selection will be minimized.********** This is not the case. When we use the rotation and translation matrices, on X,Y, and Z sequentially as i did in my program, even if you specify chunk length, entire matrix is translated, you don't choose a subset there. So entire matrix transformation takes place. But lastly for RMSD fit, you just check for selected atoms. Hence, RMSD displayed seems for chunk, but in background entire protein RMSD can be computed, which is not asked by the user. Ashish Ashish Runthala, Lecturer, Structural Biology Cell, Biological Sciences Group, BITS, Pilani Rajasthan, INDIA ----- Original Message ----- From: "modeller usage-request" <modeller_usage-request(a)salilab.org> To: "modeller usage" <modeller_usage(a)salilab.org> Sent: Tuesday, April 5, 2011 5:36:59 AM GMT +05:30 Chennai, Kolkata, Mumbai, New Delhi Subject: modeller_usage Digest, Vol 10, Issue 61 Send modeller_usage mailing list submissions to modeller_usage(a)salilab.org To subscribe or unsubscribe via the World Wide Web, visit https://salilab.org/mailman/listinfo/modeller_usage or, via email, send a message with subject or body 'help' to modeller_usage-request(a)salilab.org You can reach the person managing the list at modeller_usage-owner(a)salilab.org When replying, please edit your Subject line so it is more specific than "Re: Contents of modeller_usage digest..." Today's Topics: 1. Re: salign: specify chains to superpose (Modeller Caretaker) 2. Modeller 9.9 release (Modeller Caretaker) 3. modelling a protein withtow chains (Houcemeddine Othman) ---------------------------------------------------------------------- Message: 1 Date: Fri, 01 Apr 2011 13:47:28 -0700 From: Modeller Caretaker <modeller-care(a)salilab.org> Subject: Re: [modeller_usage] salign: specify chains to superpose To: Yingjie Lin <Yingjie.Lin(a)mssm.edu> Cc: modeller <modeller_usage(a)salilab.org> Message-ID: <4D9639E0.7020406(a)salilab.org> Content-Type: text/plain; charset=ISO-8859-1; format=flowed On 03/31/2011 09:08 AM, Yingjie Lin wrote: > I wonder what is the best way to superpose two multi-chain proteins, > and explicitly specify the chains to include in superposition. I know > that I can read only the wanted chains into the alignment, but I also > want to make sure that the other chains move according to the > superposition. Just to be clear here, we should distinguish structural *alignment* (which is what SALIGN does) from superposition (which is what selection.superpose() does). Superposition simply rotates and translates one protein, without changing the alignment, to minimize the RMSD between Calpha atoms in aligned residues. Structural alignment also adds or removes gaps, changing the aligned residues. If you really want to do superposition, simply use selection.superpose() and just give it a selection of atoms in the chains you want to superpose. The whole protein will be moved, of course, but only the RMSD of the selection will be minimized. If you want to do a structural alignment, your first suggestion is probably better - read in just the chains you want, make the alignment, then rotate and translate the full protein accordingly. Ben Webb, Modeller Caretaker -- modeller-care(a)salilab.org http://www.salilab.org/modeller/ Modeller mail list: http://salilab.org/mailman/listinfo/modeller_usage ------------------------------ Message: 2 Date: Mon, 04 Apr 2011 12:03:57 -0700 From: Modeller Caretaker <modeller-care(a)salilab.org> Subject: [modeller_usage] Modeller 9.9 release To: modeller_announce(a)salilab.org, modeller_usage(a)salilab.org Message-ID: <4D9A161D.50202(a)salilab.org> Content-Type: text/plain; charset=ISO-8859-1; format=flowed The new version of Modeller, 9.9, is now available for download! Please see the download page at http://salilab.org/modeller/ for more information. If you have a license key for Modeller 8 or 9, there is no need to reregister for Modeller 9.9 - the same license key will work. (It won't do any harm to reregister if you want to, though!) 9.9 is primarily a bugfix release relative to the last public release (9v8). Major user-visible changes include: # The Windows version of Modeller is now only supported on XP Service Pack 2 or later. If you want to run Modeller on Windows 98, ME, 2000, or NT, use Modeller 9v8. # Added support for Python 2.7 to Windows and Linux Modeller; Python 2.5 is now supported on all platforms. # Initial models generated by automodel now always contain valid PDB coordinates, i.e. each coordinate is in the range -999.999 to 9999.999. # During loop modeling, if atoms are missing from the initial model, loopmodel.loop.write_defined_only can be set True to write out PDBs containing only non-loop atoms present in the initial model. # When reading new-style PDB files (with element names in columns 77-78) Modeller will now use this information to determine whether an atom is a hydrogen. (With old-style or non-conformant PDB files, it will continue to guess based on the atom name, so will not read mercury ions for example unless env.io.hydrogen=True, since it cannot unambiguously determine whether HG is mercury or "hydrogen bonded to CG".) See the Modeller manual for a full change log: http://salilab.org/modeller/9.9/manual/node38.html If you encounter bugs in Modeller 9.9, please see http://salilab.org/modeller/9.9/manual/node10.html for information on how to report them. Note: you are receiving this email either because you subscribed to the modeller_usage mailing list, or you provided this address when you requested a Modeller license and you ticked the "notify me of new releases" box. In the latter case, if you no longer wish to receive announcements of new Modeller releases, simply reply to this email and let us know. Ben Webb, Modeller Caretaker -- modeller-care(a)salilab.org http://www.salilab.org/modeller/ Modeller mail list: http://salilab.org/mailman/listinfo/modeller_usage ------------------------------ Message: 3 Date: Tue, 5 Apr 2011 01:06:57 +0100 From: Houcemeddine Othman <houcemoo(a)gmail.com> Subject: [modeller_usage] modelling a protein withtow chains To: modeller_usage(a)salilab.org Message-ID: <BANLkTikUh9qOU-NsGxRqOB4+Q7Dqy+uTWg(a)mail.gmail.com> Content-Type: text/plain; charset="iso-8859-1" Hi I try to model an heterodimer using this alignment >P1;1DZB2 structureX:1DZB2:1:A:107:B:::: QVKLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPEQGLEWIGRIDPANGNTKYDPKFQGKATITADTSSNTAYLQLSSLTSEDTAVYYCAR-----WDWYFDVWGQGTTVTVSSG/ ------------DIELTQSPSSMYTSLGERVTITCKASQDINSYLRWFQQKPGKSPKTLIYYATSLADGVPSRFSGSGSGQDYSLTISSLESDDTTTYYCLQHGESPYTFGGGTKLEIK---------* >P1;atc sequence::::::::: -VKLQQSGGGLVQPGGSLKLSCAASGFDFSRYWMSWVRQAPGKGLEWIGEINPDSSTINYTPSLKDTFIISRDNAKNTLYLQMSKVRSEDTALYYCARQGYDGYHWYFDVWGQGTTVTVSSE/ SLDLGGGGGGGGDIQLTQSPSSLSASVGETVTLTCGASENIYGGLNWYQRKQGKSPQLLIYGATKLADGMSSRFSGGGSGRQYFLKITSLHPDDVATYYCQNVLSNPLTFGAGTKLELKRADAAPTVS* each time it gives me this error message define__595E> Number of selected atoms in sets 2 & 3 is not the same: 121 128 Can you tell me please what's wrong in my alignment file script used: # Homology modeling by the automodel class # # Demonstrates how to build multi-chain models, and symmetry restraints # from modeller import * from modeller.automodel import * # Load the automodel class log.verbose() # Override the 'special_restraints' and 'user_after_single_model' methods: class MyModel(automodel): def special_restraints(self, aln): # Constrain the A and B chains to be identical (but only restrain # the C-alpha atoms, to reduce the number of interatomic distances # that need to be calculated): s1 = selection(self.chains['A']).only_atom_types('CA') s2 = selection(self.chains['B']).only_atom_types('CA') self.restraints.symmetry.append(symmetry(s1, s2, 1.0)) def user_after_single_model(self): # Report on symmetry violations greater than 1A after building # each model: self.restraints.symmetry.report(1.0) env = environ() # directories for input atom files env.io.atom_files_directory = './' a = MyModel(env, alnfile = 'ali.pir', knowns = '1DZB2', sequence = 'atc') a.starting_model= 1 a.ending_model = 1 a.make()

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modelling a protein withtow chains
by Houcemeddine Othman 04 Apr '11

04 Apr '11

Hi I try to model an heterodimer using this alignment >P1;1DZB2 structureX:1DZB2:1:A:107:B:::: QVKLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPEQGLEWIGRIDPANGNTKYDPKFQGKATITADTSSNTAYLQLSSLTSEDTAVYYCAR-----WDWYFDVWGQGTTVTVSSG/ ------------DIELTQSPSSMYTSLGERVTITCKASQDINSYLRWFQQKPGKSPKTLIYYATSLADGVPSRFSGSGSGQDYSLTISSLESDDTTTYYCLQHGESPYTFGGGTKLEIK---------* >P1;atc sequence::::::::: -VKLQQSGGGLVQPGGSLKLSCAASGFDFSRYWMSWVRQAPGKGLEWIGEINPDSSTINYTPSLKDTFIISRDNAKNTLYLQMSKVRSEDTALYYCARQGYDGYHWYFDVWGQGTTVTVSSE/ SLDLGGGGGGGGDIQLTQSPSSLSASVGETVTLTCGASENIYGGLNWYQRKQGKSPQLLIYGATKLADGMSSRFSGGGSGRQYFLKITSLHPDDVATYYCQNVLSNPLTFGAGTKLELKRADAAPTVS* each time it gives me this error message define__595E> Number of selected atoms in sets 2 & 3 is not the same: 121 128 Can you tell me please what's wrong in my alignment file script used: # Homology modeling by the automodel class # # Demonstrates how to build multi-chain models, and symmetry restraints # from modeller import * from modeller.automodel import * # Load the automodel class log.verbose() # Override the 'special_restraints' and 'user_after_single_model' methods: class MyModel(automodel): def special_restraints(self, aln): # Constrain the A and B chains to be identical (but only restrain # the C-alpha atoms, to reduce the number of interatomic distances # that need to be calculated): s1 = selection(self.chains['A']).only_atom_types('CA') s2 = selection(self.chains['B']).only_atom_types('CA') self.restraints.symmetry.append(symmetry(s1, s2, 1.0)) def user_after_single_model(self): # Report on symmetry violations greater than 1A after building # each model: self.restraints.symmetry.report(1.0) env = environ() # directories for input atom files env.io.atom_files_directory = './' a = MyModel(env, alnfile = 'ali.pir', knowns = '1DZB2', sequence = 'atc') a.starting_model= 1 a.ending_model = 1 a.make()

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Modeller 9.9 release
by Modeller Caretaker 04 Apr '11

04 Apr '11

The new version of Modeller, 9.9, is now available for download! Please see the download page at http://salilab.org/modeller/ for more information. If you have a license key for Modeller 8 or 9, there is no need to reregister for Modeller 9.9 - the same license key will work. (It won't do any harm to reregister if you want to, though!) 9.9 is primarily a bugfix release relative to the last public release (9v8). Major user-visible changes include: # The Windows version of Modeller is now only supported on XP Service Pack 2 or later. If you want to run Modeller on Windows 98, ME, 2000, or NT, use Modeller 9v8. # Added support for Python 2.7 to Windows and Linux Modeller; Python 2.5 is now supported on all platforms. # Initial models generated by automodel now always contain valid PDB coordinates, i.e. each coordinate is in the range -999.999 to 9999.999. # During loop modeling, if atoms are missing from the initial model, loopmodel.loop.write_defined_only can be set True to write out PDBs containing only non-loop atoms present in the initial model. # When reading new-style PDB files (with element names in columns 77-78) Modeller will now use this information to determine whether an atom is a hydrogen. (With old-style or non-conformant PDB files, it will continue to guess based on the atom name, so will not read mercury ions for example unless env.io.hydrogen=True, since it cannot unambiguously determine whether HG is mercury or "hydrogen bonded to CG".) See the Modeller manual for a full change log: http://salilab.org/modeller/9.9/manual/node38.html If you encounter bugs in Modeller 9.9, please see http://salilab.org/modeller/9.9/manual/node10.html for information on how to report them. Note: you are receiving this email either because you subscribed to the modeller_usage mailing list, or you provided this address when you requested a Modeller license and you ticked the "notify me of new releases" box. In the latter case, if you no longer wish to receive announcements of new Modeller releases, simply reply to this email and let us know. Ben Webb, Modeller Caretaker -- modeller-care(a)salilab.org http://www.salilab.org/modeller/ Modeller mail list: http://salilab.org/mailman/listinfo/modeller_usage

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salign: specify chains to superpose
by Yingjie Lin 01 Apr '11

01 Apr '11

Hi Modellers, I wonder what is the best way to superpose two multi-chain proteins, and explicitly specify the chains to include in superposition. I know that I can read only the wanted chains into the alignment, but I also want to make sure that the other chains move according to the superposition. Here are two ways we could think of: 1. read only the wanted chains and do superposition. Then move the other chains accordingly using functions like selection.rotate_origin(), selection.rotate_mass_center() and selection.transform(). 2. model1 <= all chains in protein A model2 <= all chains in protein B model3 <= the chain(s) selected for superposition in protein B first, superpose model3 to model1 (model3 is moved) second, superpose model2 to model3 (model2 is moved) Are there any better ways? Thank you. Yingjie

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Are gap in target and template same.
by Ashish Runthala 01 Apr '11

01 Apr '11

Dear Modellers, I am facing an interesting problem. Are gaps in target and template same, as shown below. Target AAAAA AA--A AA--A Template AA--A AAAAA AA--A CaseI CaseII CaseIII Are these three cases I,II, & III modelled the same way. How will the gap penalties be incorporated in these three cases, when the modeller calculates the alignment score. PLEASE PROVIDE ME COMPLETE DETAILS ABOUT GAP PENALTIES IN THESE THREE CASES. Thanks Ashish Ashish Runthala, Lecturer, Structural Biology Cell, Biological Sciences Group, BITS, Pilani Rajasthan, INDIA

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Re: [modeller_usage] modeller_usage Digest, Vol 10, Issue 59
by Ashish Runthala 01 Apr '11

01 Apr '11

Dear Lin, I wrote a script in C to do all that. You can use it to do the analysis for specific chains. You can even do the analysis for specific segment of residues in a specific chain. If you want, I will provide you the help by providing the binary. Ashish Ashish Runthala, Lecturer, Structural Biology Cell, Biological Sciences Group, BITS, Pilani Rajasthan, INDIA ----- Original Message ----- From: "modeller usage-request" <modeller_usage-request(a)salilab.org> To: "modeller usage" <modeller_usage(a)salilab.org> Sent: Friday, April 1, 2011 10:01:26 AM GMT +05:30 Chennai, Kolkata, Mumbai, New Delhi Subject: modeller_usage Digest, Vol 10, Issue 59 Send modeller_usage mailing list submissions to modeller_usage(a)salilab.org To subscribe or unsubscribe via the World Wide Web, visit https://salilab.org/mailman/listinfo/modeller_usage or, via email, send a message with subject or body 'help' to modeller_usage-request(a)salilab.org You can reach the person managing the list at modeller_usage-owner(a)salilab.org When replying, please edit your Subject line so it is more specific than "Re: Contents of modeller_usage digest..." Today's Topics: 1. unsubscribing (Bo Yang) 2. salign: specify chains to superpose (Yingjie Lin) 3. salign: specify chains to superpose (Yingjie Lin) 4. Are gap in target and template same. (Ashish Runthala) ---------------------------------------------------------------------- Message: 1 Date: Thu, 31 Mar 2011 08:07:11 -0700 (PDT) From: Bo Yang <n62star(a)yahoo.com> Subject: [modeller_usage] unsubscribing To: modeller_usage(a)salilab.org Message-ID: <676504.10553.qm(a)web36906.mail.mud.yahoo.com> Content-Type: text/plain; charset="us-ascii" unsubscribing

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