Supplementary information

From the following article:

Structure of a beta1-adrenergic G-protein-coupled receptor

Tony Warne, Maria J. Serrano-Vega, Jillian G. Baker, Rouslan Moukhametzianov, Patricia C. Edwards, Richard Henderson, Andrew G. W. Leslie, Christopher G. Tate & Gebhard F. X. Schertler

Nature 454, 486-491(24 July 2008)

doi:10.1038/nature07101

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The file includes Supplementary Figures 1-10 and Supplementary Tables 1-3. Supplementary Table 1 presents data processing and structure refinement statistics. Supplementary Table 2 presents data on the stability of beta1 receptor mutants containing alanine residues throughout cytoplasmic loop 2. Supplementary Table 3 presents the amino acid residues involved in crystal contacts. Supplementary Fig. 1 is an alignment of the primary sequences of turkey beta1AR and the human beta-adrenergic receptors and Supplementary Fig. 2 shows the structures of agonists and antagonists discussed in the main text. Supplementary Fig. 3 shows G protein coupling data and basal activity for beta1AR-m23 in a cell-based assay. Supplementary Figs. 4 and 5 describe the crystallographic packing of receptor molecules and show the location of the ordered detergent molecules. Supplementary Fig. 6 shows the B-factor variation for the structures of rhodopsin, beta1AR and beta2AR. Supplementary Fig. 7 describes the rmsd according to sequence for the comparison between the beta1 and beta2 receptors and between molecules A and B of beta1AR-m23. Supplementary Fig. 8 depicts electron density maps for the Na+ ion and the ordered water molecule in H6. Supplementary Fig. 9 is an omit map of cytoplasmic loop 2 and Supplementary Fig. 10 shows the extracellular surface charge distribution for the beta1 and beta2 receptors.

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