- Chimera-users - RBVI Mailing Lists

Docking problem in my Protein ligand
by MUHAMMAD FURQAN AKBER 27 Aug '20

27 Aug '20

Hi hope you are fine? I cant find out the final result by protein ligand docking by chimera. This shows the error with pdb receptor. What can i do ?

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This Chimera plugin "sounds" interesting
by Eric Pettersen 27 Aug '20

27 Aug '20

Sonification for Structural Biology and Structure-based Drug Design - Paul Vickers <https://paulvickers.github.io/chison/>

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How to fit an atomic model into a topographic height volume
by Lee, Yun-Tzai (NIH/NCI) [F] 24 Aug '20

24 Aug '20

Dear Chimera developers, I am a research fellow who works at Frederick Biophysics Laboratory and working on an image processing project. I used Chimera to generate a topographic height volume data from a single plane image. You can find the attached file and use a command following to generate the topographic surface. % topography #0 height -40 smoothingIteration 5 But there is no option for me to fit the atomic model into the surface height volume by using Fit in Map tools. Can someone help me figure out what’s the issue? Is that possible to fit an atomic model into a height volume created by a single plane image or just simply need multiple planes? Thanks in advance. Best, Yun-Tzai

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INQUIRY
by Samiha I Amer 21 Aug '20

21 Aug '20

Hello Please how do I prevent chimera from renumbering my protein residue sequence in cases where I am working with a pdb structure that does not cover all the residues? For example, the attached pdb protein file (5trf.pdb) was downloaded from the pdb database with the first 9 residues missing. The first residue in the pdb structure is the 10th residue and this was numbered accordingly but whenever I upload such structures on Chimera, the numbering of the residues tend to scatter because chimera automatically numbers the first residue in the structure as 1, just as it appeared in the attached mol2 file. Please how do I avoid/correct such Thank you.

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Cannot dock molecule to targeted region?
by 孙业平 20 Aug '20

20 Aug '20

Dear all, I am trying to fit an antibody molecule to the cryo-EM density map for an antigen-antibody complex. The related files can be found at the following link https://drive.google.com/drive/folders/16ELIDsUxiNwRGp9ely2SRn-zjAdHCudH?us…. I first segmented the map ("emd_22158.map") and get the segment map ("emd_22158.seg") in chimera. Then I selected the regions corresponding to the antibody and use the "Fit to segments" tool of chimera to fit the antibody molecule. The "image1.png" shows the inital antibody postion and the expected docking postion in the segmented complex density (indicated by the red arrow). However, the antibody molecule cannot be fitted into the selected target region after this operation, but moved to the position shown in "image2.png (only the target regions are shown). I have tried to ungoup and regroup the target region to make its overall shape more simial to the antibody, and place the antibody into the region and ajust its orienation, but whatever I tried, the results are the same: the antibody will move to the position shown in "image2.png" after performing the "Fit to segments" action. I wonder whether it is impossible to dock the antibody to the expected position with chimera or there is anything wrong with my operation. Could you help me with this issue? I will appreciate any help from you. Best regards, Yeping Sun

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Fw: Open MTZ file
by Williams, Joanne 20 Aug '20

20 Aug '20

Hello! Can you help with the inquiry below? thanks, Jo ________________________________ From: Sharyn Endow, Ph.D. <sharyn.endow(a)duke.edu> Sent: Thursday, February 22, 2018 5:01 AM To: chimera(a)cgl.ucsf.edu Subject: Open MTZ file Is it possible to open an .mtz file in Chimera? ~~~~~~~~~~~~~~~~~~~~~~~~~~ Sharyn A. Endow, PhD Professor of Cell Biology, DUMC Professor of NBD, Duke-NUS PO Box 3709 450 Sands Bldg/Research Drive Durham, NC 27710 USA T 919 684-4311 F 919 681-9929 ~~~~~~~~~~~~~~~~~~~~~~~~~~~

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Minimized Structures vs. Unminimized
by Jordan Harriman 17 Aug '20

17 Aug '20

Hi there, I have a protein I'm modifying, for a total of 28 unique mutations. My question is if it's possible to tell the energetic difference between a minimized structure vs. an unminimized structure. Following that, if it's possible to rank minimized structures in terms of greatest stability. Is there some quantifiable output I can use to compare structures? Best, Jordan

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Dock-preparation
by JAVAD KARIMBAYLI 17 Aug '20

17 Aug '20

Hi! I have got a problem and searched all previous posts for solutions but failed to find one. Therefore, I would be very much thankful to have your guidance. I have generated my protein model in I-Tasser and now I would like to do dock-prep. (Attached model-PDB file) However, when I run it: *Tools .. Strct edit .. Dockprep **All selected ** Add hydrogens (also consider H-bonds)* *Incomplete side chains:replace(Dunbrack 2010 rotamer library)* *Protonation states fro: his (residue-name-based)* *standart residues: AMBER ff14SB* *other residues: AM1-BCC* *Output:* No incomplete side chains No SEQRES records for model1 (1).pdb (#0) chain A; guessing terminii instead Chain-initial residues that are actual N terminii: MET 1.A Chain-initial residues that are not actual N terminii: Chain-final residues that are actual C terminii: Chain-final residues that are not actual C terminii: LEU 522.A 470 hydrogen bonds Removing spurious proton from 'C' of LEU 522.A Hydrogens added Charge model: AMBER ff14SB Non-standard atom names: ILE HD3 (ILE 18.A HD3, ILE 31.A HD3, ILE 42.A HD3 + 26 others) ILE HD1 (ILE 18.A HD1, ILE 31.A HD1, ILE 42.A HD1 + 26 others) ILE HD2 (ILE 18.A HD2, ILE 31.A HD2, ILE 42.A HD2 + 26 others) Total charge for #0: 9.382 The following residues had non-integral charges: ILE 18.A -0.0558 ILE 31.A -0.0558 ILE 42.A -0.0558 ILE 77.A -0.0558 ILE 96.A -0.0558 ILE 132.A -0.0558 ILE 136.A -0.0558 ILE 151.A -0.0558 ILE 153.A -0.0558 ILE 163.A -0.0558 ILE 184.A -0.0558 ILE 193.A -0.0558 ILE 223.A -0.0558 ILE 236.A -0.0558 ILE 250.A -0.0558 ILE 256.A -0.0558 ILE 284.A -0.0558 ILE 297.A -0.0558 ILE 321.A -0.0558 ILE 370.A -0.0558 ILE 378.A -0.0558 ILE 401.A -0.0558 ILE 416.A -0.0558 ILE 436.A -0.0558 ILE 447.A -0.0558 ILE 450.A -0.0558 ILE 480.A -0.0558 ILE 489.A -0.0558 ILE 495.A -0.0558 Correct charges are unknown for 3 non-standard atom names in otherwise standard residues Charges of 0.0 were assigned to the unknown atoms So, please kindly help me to solve the issue. Yours Sincerely Javad Karimbayli

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Modeling of mutlichain protein complex
by amit gaur 16 Aug '20

16 Aug '20

Hi, I am trying to model a multichain protein complex using modeller extension in chimera. But, I do.nt know how to do that? Can some one help me with this ? Thanks -- *Dr. Amit Gaur* *Post Doctoral ResearcherPI: Dr. Ji-Fang ZhangThomas Jefferson University* *1020, Locust Street, Suite 418* *Philadelphia, PA 19107*

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The command like volume zone in X
by Zheng, Fengwei 14 Aug '20

14 Aug '20

Dear Developer, I am wodering if there is a command of Chimera can achieve the same function like "volume zone" in ChimeraX? I tried the command "vol zone #2 near #0:.a range 2", but the chimera always said "unknow keyword #2"~ Another thing is that I wonder if there is a command of ChimeraX can achieve the same function like "turn z 2 360 precess 20" in Chimera (to achieve the Wobble motion / "wiggle-rock" motion, like nutation in pymol)~ The I tried 1.14, 1.15 and the latest daily built versions of Chimera. The ChimeraX version I used is 1.0, Many thanks! Best, Fengwei

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