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Recent Citations
Structural basis of amine odorant perception by a mammal olfactory receptor. Guo L, Cheng J et al. Nature. 2023 Jun 1;618(7963):193–200.
Ligand and G-protein selectivity in the κ-opioid receptor. Han J, Zhang J et al. Nature. 2023 May 11;617(7960):417-425.
MELD-Bracket ranks binding affinities of diverse sets of ligands. Parui S, Robertson JC et al. J Chem Inf Model. 2023 May 8;63(9):2857-2865.
Molecular basis of translation termination at noncanonical stop codons in human mitochondria. Saurer M, Leibundgut M et al. Science. 2023 May 5;380(6644):531-536.
Structural basis of BAM-mediated outer membrane β-barrel protein assembly. Shen C, Chang S et al. Nature. 2023 May 4;617(7959):85–193.
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April 19, 2023
Chimera production release 1.17.1 is now available, fixing an issue with 1.17 for Windows and Linux. See the release notes for details.
April 13, 2023
Chimera production release 1.17 is now available. Updating is required to keep using the tools that run Blast Protein, Modeller, and multiple sequence alignment with Clustal Omega or MUSCLE, as these will soon stop working in older versions. See the release notes for details.
December 21, 2022
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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 in addition to nearly all the capabilities of Chimera (details...).
Chimera is no longer under active development. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.
Feature Highlight
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A structure can be colored to show attributes such as residue conservation. Opening a sequence alignment in Chimera shows it in Multalign Viewer and automatically associates sequences with structures as appropriate. Residues of alignment-associated structures are assigned conservation values; available measures include entropy, variability, and sum-of-pairs. The figure was created using the PFAM Carb_anhydrase seed alignment PF00194_seed.slx (see image) and includes 2D labels and a color key. See also: mapping sequence conservation
(More features...)Gallery Sample
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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