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Recent Citations

Structure of the trehalose-6-phosphate phosphatase from Brugia malayi reveals key design principles for anthelmintic drugs. Farelli JD, Galvin BD et al. PLoS Pathog. 2014 Jul 3;10(7):e1004245.

Regulation of the mammalian elongation cycle by subunit rolling: a eukaryotic-specific ribosome rearrangement. Budkevich TV, Giesebrecht J et al. Cell. 2014 Jul 3;158(1):121-31.

Protruding knob-like proteins violate local symmetries in an icosahedral marine virus. Gipson P, Baker ML et al. Nat Commun. 2014 Jul 2;5:4278.

Enhancing UCSF Chimera through web services. Huang CC, Meng EC et al. Nucleic Acids Res. 2014 Jul;42(Web Server issue):W478-84.

Structural rearrangements of a polyketide synthase module during its catalytic cycle. Whicher JR, Dutta S et al. Nature. 2014 Jun 26;510(7506):560-4.

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News

May 13, 2014

Chimera production release 1.9 is now available. See the release notes for new features since the 1.8 release series.

April 23, 2014

A production release candidate (version 1.9) is now available; please try it and report any problems. See the release notes for changes relative to the previous release.

October 31, 2013

Chimera production release 1.8.1 is now available. Changes since 1.8 are mainly to fix problems with Mac OS X 10.9 (Mavericks). See the release notes for further details and for a list of new features since the 1.7 release.

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UCSF Chimera is a highly extensible program for interactive visualization and analysis of molecular structures and related data, including density maps, supramolecular assemblies, sequence alignments, docking results, trajectories, and conformational ensembles. High-quality images and animations can be generated. Chimera includes complete documentation and several tutorials, and can be downloaded free of charge for academic, government, non-profit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics, funded by the National Institutes of Health (NIGMS P41-GM103311).

Feature Highlight

sidechain rotamers

Rotamers

Amino acid sidechains adopt different conformational states, or rotamers. Rotamers from the Dunbrack backbone-dependent library or the Richardson "penultimate" library can be viewed, evaluated, and incorporated into structures with the Rotamers tool. A residue can be changed into a different conformation of the same type of amino acid or mutated into a different type. Rotamer torsion angles and library probability values are listed in a dialog, along with (optionally) hydrogen bonds, clashes, and agreement with electron density data. Only rotamers chosen in the list are displayed. When a single rotamer is chosen, it can be incorporated into the structure. The image includes 2D labels.

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Gallery Sample

G Protein Interface Surface

Heterotrimeric G protein (Protein Data Bank entry 1gg2) with the alpha subunit shown in green, the beta subunit in light blue, and the gamma subunit in brown. The Intersurf tool was used to show the interface between the alpha and beta subunits. The interface surface is colored to show the distance between atoms across the interface (red for closer together, blue for farther apart). (More samples...)