NMR solution structure of human Saposin C
Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles.
SDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSG LVPR
residual dipolar couplings measured in two different alignment media. Pf1 and fd phages
experiments for residual dipolar coupling measurements
structures were calculated with: 1806 NOE-derived destance constriants (no intra-residue NOEs used), 28 hydrogen bonds, 135 dihedral restraints, 276 residual dipolar couplings. Residues 1-3 and 79-84 are disordered. Superimposition of structures is from residues 4-78.
distance geometry and simulated annealing
disulfide bridges, alpha-helices, MEMBRANE PROTEIN