C2 Domain Of Cytosolic Phospholipase A2, Nmr, Minimized Average Structure

Chain A, Human Cytosolic Phospholipase A2

Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2.

A considerable degree of variability exists in the way that 1H, 13C and 15N
chemical shifts are reported and referenced for biomolecules. In this article
we explore some of the reasons for this situation and propose guidelines for
future chemical shift referencing and for conversion from many common 1H, 13C
and 15N chemical shift standards, now used in biomolecular NMR, to those
proposed here.

Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J.,
Oldfield, E., Markley, J. L., and Sykes, B. D.
J. Biomol. NMR 6, 135-140 (1995).

1H, 13C and 15N chemical shift referencing in biomolecular NMR.

Calcium-Phospholipid Binding Domain From Cytosolic Phospholipase A2

phospholipase A2, group IVA [synthetic construct]

phosphatidylcholine 2-acylhydrolase [Homo sapiens]

phospholopid-binding protein [Homo sapiens]

phospholopid-binding protein [Mus musculus]

cytosolic phospholipase A2 [Rattus norvegicus]

cytosolic phospholipase A2 [Equus caballus]

cytosolic phospholipase A2 [Pongo abelii]

cytosolic phospholipase A2 isoform 2 [Homo sapiens]

cytosolic phospholipase A2 isoform 1 [Mus musculus]

cytosolic phospholipase A2 isoform 1 [Homo sapiens]

RecName: Full=Cytosolic phospholipase A2; Short=cPLA2; AltName: Full=Phospholipase A2 group IVA; Includes: RecName: Full=Phosph

A cDNA fragment encoding amino acids 1-138 of human cytosolic
Phospholipase A2 was subcloned into the NcoI/EcoRI sites of the
vector such that the 5' codons encoding the N-terminal polyHis-tag
were removed.

DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS, ETC.