1H, 13C, and 15N backbone, side-chain, and heme chemical shift assignments for the oxidized form of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum

c-type cytochrome, heme covalently linked to polypeptide via thioether bonds

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
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1H, 13C, and 15N backbone, side-chain, and heme chemical shift assignments for oxidized and reduced forms of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum.

Cysteines are in thioether bonds to the heme
An N-terminal 21 amino acid signal sequence is not present and presumably was cleaved by the host organism.

cytochrome c [Acidiphilium multivorum AIU301]

cytochrome c, class I [Acidiphilium cryptum JF-5]

Cytochrome c, class I [Acidiphilium sp. PM]

cytochrome c2 [Acidiphilium sp. JA12-A1]

MULTISPECIES: cytochrome C [Acidiphilium]

[7%-biosynthetically directed 13C; 50%-U-15N]