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Recent Citations

Structural basis of human transcription-DNA repair coupling. Kokic G, Wagner FR et al. Nature. 2021 Oct 14;598(7880):368-372.

The stress-sensing domain of activated IRE1α forms helical filaments in narrow ER membrane tubes. Tran NH, Carter SD et al. Science. 2021 Oct 1;374(6563):52-57.

A practical guide to large-scale docking. Bender BJ, Gahbauer S et al. Nat Protoc. 2021 Oct;16(10):4799-4832.

Gastric proton pump with two occluded K+ engineered with sodium pump-mimetic mutations. Abe K, Yamamoto K et al. Nat Commun. 2021 Sep 29;12(1):5709.

Structural insights into the inhibition of undecaprenyl pyrophosphate synthase from Gram-positive bacteria. Workman SD, Day J et al. J Med Chem. 2021 Sep 23;64(18):13540-13550.

(Previously featured citations...)

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December 18, 2020

Chimera production release 1.15 is now available. See the release notes for what's new.

December 11, 2020

The RBVI wishes you a safe and happy holiday season! See our 2020 card and the gallery of previous cards back to 1985.

November 4, 2020

A 1.15 production release candidate is available, including a fix to work with the new PDB fetch locations (see the release notes). Please try it and report any problems.

(Previous news...)

Upcoming Events

November 9, 2021

SBGrid webinar 3pm PST Nov 9 (noon Nov 10 New Zealand time): Second speaker Tom Goddard (3:30pm) will show using AlphaFold-predicted structures for cryoEM modeling in ChimeraX [register for webinar].

UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. It is available free of charge for noncommercial use. Commercial users, please see Chimera commercial licensing.

We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages and completely new features. ChimeraX includes a significant subset of Chimera features (with more to come, see the missing features list) and is under active development. Users may choose to use both programs, and it is fine to have both installed.

Chimera is no longer under active development, and is only updated for critical maintenance. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.

Feature Highlight

unmatched structures superimposed structures

Superimposing Structures

There are several ways to superimpose structures in Chimera:
•  MatchMaker performs a fit after automatically identifying which residues should be paired. Pairing uses both sequence and secondary structure, allowing similar structures to be superimposed even when their sequence similarity is low to undetectable.
The figure shows five distantly related proteins (pairwise sequence identities <25%) from the SCOP WD40 superfamily before and after MatchMaker superposition with default parameters.
•  Structures can be matched using a pre-existing sequence alignment.
•  The exact atoms to pair can be specified with the match command. This works on any type of structure, while the preceding methods apply only to peptide and nucleotide chains.
•  Structures can be superimposed manually by activating/deactivating them for motion and using the mouse.

(More features...)

Gallery Sample

Orexin Receptor Complex

The image shows the structure of the human OX2 orexin receptor bound to the insomnia drug suvorexant, Protein Data Bank entry 4s0v. The drug is shown as spheres colored by element, and the receptor as ribbons with secondary structure elements rainbow-colored from blue at the N-terminus to red at the C-terminus. (More samples...)

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