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Figure 3
χ2 and χ1 distributions of the catalytic His41 and Asp89 residues, respectively, of FD observed in the ensemble structures of (a) wild-type FD (original PDB entry 1dsu ) and (b) the R202A (R218A) mutant (original PDB entry 4cbn ). The arrows indicate the angular value compatible with the active conformation of the serine protease catalytic site. The dashed arrow for wild-type FD indicates that there are no active conformations of His41 (His57) and Asp89 (Asp102) at the same time in the same copy. Both structures contain two copies in the asymmetric unit; data are shown in blue and green for chains A and B, respectively.

Journal logoBIOLOGICAL
ISSN: 1399-0047
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