Solution structure of the CH domain of human Calponin 1
RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Calponin H1, smooth muscle, Basic calponin
GSSGSSGNKLAQKYDHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKINESTQNWHQLENIGNFI KAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVGVSGPSSG
RIKEN Structural Genomics/Proteomics Initiative
target function,structures with the lowest energy,structures with the least restraint violations
torsion angle dynamics, restrainted molecular dynamics
1.10mM CH domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O
CH domain, F-actin binding, all-alpha, structural genomics, NPPSFA, RIKEN Structural Genomics/Proteomics Initiative, RSGI, STRUCTURAL PROTEIN
NKLAQKYDHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKINESTQNWHQLENIGNFIKAITKYG VKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVGV