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1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state

Publication Type:

Journal Article

Authors:

Jacobs,D.M.; Messens,J.; Wechselberger,R.W.; Brosens,E.; Willem,R.; Wyns,L.; Martin,J.C.

Source:

J. Biomol. NMR, Volume 20, Issue 1, p.95 - 96 (2001)

URL:

PM:11430763

Keywords:

Adenosine Triphosphatases; chemistry; Arsenite Transporting ATPases; Bacterial Proteins; Carbon; Hydrogen; Ion Pumps; Multienzyme Complexes; Nitrogen; Nuclear Magnetic Resonance; Biomolecular; Oxidation-Reduction; Protein Conformation; Recombinant Fusion P

Notes:

DA - 20010629
IS - 0925-2738 (Print)
LA - eng
PT - Letter
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Proteins)
RN - 0 (Ion Pumps)
RN - 0 (Multienzyme Complexes)
RN - 0 (Recombinant Fusion Proteins)
RN - 1333-74-0 (Hydrogen)
RN - 7440-44-0 (Carbon)
RN - 7727-37-9 (Nitrogen)
RN - EC 3.6.1.- (Adenosine Triphosphatases)
RN - EC 3.6.3.16 (Arsenite Transporting ATPases)
SB - IM