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Recent Citations
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.
Lesion recognition by XPC, TFIIH and XPA in DNA excision repair. Kim J, Li CL et al. Nature. 2023 May 4;617(7959):170–175.
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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
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.
(More features...)Gallery Sample
This image of a clathrin cage uses flat shading and edge highlighting. It is a copy of a PDB molecule of the month image made by Graham Johnson and Dave Goodsell. David Goodsell pioneered this visualization style. This image was made with the Multiscale tool, silhouette edging, and surface lighting turned off.
Protein Data Bank model 1xi4.
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