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Recent Citations

Structure and dynamics of the CGRP receptor in apo and peptide-bound forms. Josephs TM, Belousoff MJ et al. Science. 2021 Apr 9;372(6538):eabf7258.

Oncohistone mutations enhance chromatin remodeling and alter cell fates. Bagert JD, Mitchener MM et al. Nat Chem Biol. 2021 Apr;17(4):403-411.

The effect of spike mutations on SARS-CoV-2 neutralization. Rees-Spear C, Muir L et al. Cell Rep. 2021 Mar 23;34(12):108890.

Structural insights into membrane remodeling by SNX1. Zhang Y, Pang X et al. Proc Natl Acad Sci USA. 2021 Mar 9;118(10):e2022614118.

Parallel molecular mechanisms for enzyme temperature adaptation. Pinney MM, Mokhtari DA et al. Science. 2021 Mar 5;371(6533):eaay2784.

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News

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.

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Upcoming Events

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

Ramachandran plot 1jfuA 1jfu chain A

Ramachandran Plot

Protein backbone angles can be shown in a Ramachandran Plot along with probability contours (green lines) from a reference set of well-determined structures. Each amino acid residue is shown as a dot in a graph of φ vs. ψ, more commonly known as a Ramachandran plot or Ramachandran map. Residues are shown as blue dots, or when selected, as red dots. In the example, all helix residues have been selected. Conversely, clicking a dot in the plot will select the corresponding residue in the structure. When the plot has mouse focus, the cursor position (x = φ, y = ψ) is reported under the plot.

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Gallery Sample

Peroxiredoxin Wreath

Peroxiredoxins are enzymes that help cells cope with stressors such as high levels of reactive oxygen species. The image shows a decameric peroxiredoxin from human red blood cells (Protein Data Bank entry 1qmv), styled as a holiday wreath.

See also the RBVI holiday card gallery.

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