The solution structure of bovine cytochrome b(5) mutant (E44A/E48A/E56A/D60
A) has been obtained from H-1 NMR spectra measured at 600 MHz. The final RM
SD values with respect to the average structure are (0. 056 +/- 0. 009) nm
and (0. 105 +/- 0. 010) nm for backbone and all heavy atoms, respectively.
The solution structure, when compared with the X-ray structure of wild type
, has no significant changes in the whole folding and secondary structure.
Small changes are restricted to local conformation near mutated sites.