Figure 3.
Figure 3. Structural quality of the AE1 repeat-swapped model compared with that of the x-ray structure. A five-residue window average of the ProQM score is plotted as a function of residue number. The position of putative binding site residues is indicated by vertical gray lines. The position of TM segments is shown as blocks, colored according to Fig. 1. Data are shown for one protomer of the dimeric model, generated by superposing the dimerization domain onto that of the AE1 crystal structure dimer, whose orientation was determined using the OPM server (Lomize et al., 2006). Clashes at the interface were energy minimized. The global ProQM scores of the minimized crystal structure and model are 0.726 and 0.690, and the MolProbity scores are 2.08 and 1.37, respectively.

Structural quality of the AE1 repeat-swapped model compared with that of the x-ray structure. A five-residue window average of the ProQM score is plotted as a function of residue number. The position of putative binding site residues is indicated by vertical gray lines. The position of TM segments is shown as blocks, colored according to Fig. 1. Data are shown for one protomer of the dimeric model, generated by superposing the dimerization domain onto that of the AE1 crystal structure dimer, whose orientation was determined using the OPM server (Lomize et al., 2006). Clashes at the interface were energy minimized. The global ProQM scores of the minimized crystal structure and model are 0.726 and 0.690, and the MolProbity scores are 2.08 and 1.37, respectively.

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