Copper(I) loaded form of the first domain of the human copper chaperone for SOD1, CCS

Chembiochem : a European journal of chemical biology
Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants.

GSFT gateway system.
We have removed residues MASDSGNQ at the Nterminus
and residues SGQLQN at the Cterminus because they are unstructured

The Apo Form Of Hma Domain Of Copper Chaperone For Superoxide Dismutase

copper chaperone for superoxide dismutase [Hylobates lar]

copper chaperone for superoxide dismutase [Pan troglodytes]

copper chaperone for superoxide dismutase [Pongo pygmaeus]

copper chaperone for superoxide dismutase [Callithrix jacchus]

copper chaperone for superoxide dismutase [Homo sapiens]

superoxide dismutase copper chaperone [Homo sapiens]

copper chaperone for superoxide dismutase [synthetic construct]

PREDICTED: copper chaperone for superoxide dismutase [Pongo abelii]

PREDICTED: copper chaperone for superoxide dismutase [Pan paniscus]

RecName: Full=Copper chaperone for superoxide dismutase; AltName: Full=Superoxide dismutase copper chaperone

torsion angle dynamics, molecular dynamics

apo form of the first domain of the human copper chaperone for SOD1, CCS

We have used the web interface AMPS-NMR (AMBER-based Portal Server for NMR structures)within the WeNMR project available at http://py-enmr.cerm.unifi.it/access/index/amps-nmr

Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman