Solution structure of the CH domain from human Vav-3 protein
RIKEN Structural Genomics/Proteomics Initiative (RSGI)
GSSGSSGMEPWKQCAQWLIHCKVLPTNHRVTWDSAQVFDLAQTLRDGVLLCQLLNNLRAHSINLKEINLRPQMSQFLCLK NIRTFLTACCETFGMRKSELFEAFDLFDVRDFGKVIETLSRLSRTPIALATGIRPFPSGPSSG
RIKEN Structural Genomics/Proteomics Initiative
NPPSFA, National Project on Protein Structural and Functional Analyses
target function,structures with the lowest energy,structures with the least restraint violations
torsion angle dynamics, restrainted molecular dynamics
1.23mM CH domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O
all alpha, calponin homology domain, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, SIGNALING PROTEIN, PROTEIN BINDING
MEPWKQCAQWLIHCKVLPTNHRVTWDSAQVFDLAQTLRDGVLLCQLLNNLRAHSINLKEINLRPQMSQFLCLKNIRTFLT ACCETFGMRKSELFEAFDLFDVRDFGKVIETLSRLSRTPIALATGIRPFP