Solution structure and characterization of the heme chaperone CcmE
FAADLNSNLNLFYTPSEIVNGKTDTGVKPEAGQRIRVGGMVTVGSMVRDPNSLHVQFAVHDSLGGEILVTYDDLLPDLFR EGQGIVAQGVLGEDGKLAATEVLAKHDENYMPPEVAEAMGQKHEKLDYSQQKSATQ
The structure was determined using triple-resonance NMR spectroscopy on 13C and 15N double labeled apoCcmE.
1866 meaningful NOEs and 89 dihedral angle constraints.
simulated annealing, torsion angle dyanamics, restrained energy minimization
2.0 mM apoCcmE, 20 mM phosphate, 90% H2O, 10% D2O
Pearlman, Case, Caldwell, Ross, Cheatham, Ferguson, Seibel, Singh, Weiner, Kollman
all-beta protein, heme delivery, cytochrome c maturation, OB-(oligonucleotide binding)fold, CHAPERONE
LNSNLNLFYTPSEIVNGKTDTGVKPEAGQRIRVGGMVTVGSMVRDPNSLHVQFAVHDSLGGEILVTYDDLLPDLFREGQG IVAQGVLGEDGKLAATEVLAKHDENYMPPEVAEAMGQKHEKLDYSQQKSATQ