Family of 30 conformers of a mono-heme ferrocytochrome c from Shewanella putrefaciens solved by NMR
Solution structure of a monoheme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implications.
ADLQDAEAIYNKACTVCHSMGVAGAPKSHNTADWEPRLAKGVDNLVKSVKTGLNAMPPGGMCTDCTDEDYKAAIEFMSKA K
minimized AVERAGE structure of S. putrefaciens MONO-HEME C-TYPE CYTOCHROME SCYA
SEQUENCE Recombinant protein, without the signaling peptide. The first three amino-acids (Ala Asp Leu) have been added for protein expression purposes.
simulated annealing in the dihedral angle space in dyana in 15000 steps; 30 structures with the lowest target function out of a total number of 250 generated structures constitute the REM family - subject to restrained energy minimization in AMBER
1.5 mM Cytochrome c: 100 mM phosphate buffer; reduced with dithyonite
Guntert, P., Mumenthaler, C., Wuthrich, K.
haem protein, ferrocytochrome, electron transport, gram negative, bacteria, ScyA Shewanella Putrefaciens, mono haem, all-alpha, OXYGEN STORAGE-TRANSPORT COMPLEX