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![[Figure 7]](qe5002fig7mag.jpg)
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Figure 7
FLEXR models reveal backbone heterogeneity. FLEXR includes the option to model alternate side-chain conformations starting at the Cα atom or create an entirely new residue. Model building using the latter approach and refining the models can reveal alternative backbone orientations. One example of this is the ligand-binding site loop containing Pro181–Ile185 in the B chain of the 1.28 Å resolution HIV-1 protease I50V mutant structure (PDB entry 2qd6). (a) The deposited structure has several alternate side-chain conformers but no backbone heterogeneity. (b) FLEXR recapitulates these alternative side-chain conformations, finds additional ones and reveals backbone conformational heterogeneity. The deposited 2mFo − DFc map is contoured at 1σ (blue) and the mFo − DFc map is contoured at 2.0σ (green) and −2.0σ (red). Arrows indicate areas of conformational heterogeneity. |
![[Figure 7]](qe5002fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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