Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil.

Planelles-Herrero VJ, Hartman JJ, Robert-Paganin J, Malik FI, Houdusse A, Nat Commun 8(1):190 (2017) Europe PMC

SASDCW4 – Bovine β Cardiac Myosin S1 fragment (Myosin-7) MgADP.VO4+OM

Bovine β Cardiac Myosin S1 fragment
MWI(0) 113 kDa
MWexpected 117 kDa
VPorod 162 nm3
log I(s) 1.50×10-1 1.50×10-2 1.50×10-3 1.50×10-4
Bovine β Cardiac Myosin S1 fragment small angle scattering data  s, nm-1
ln I(s)
Bovine β Cardiac Myosin S1 fragment Guinier plot ln 1.50×10-1 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Bovine β Cardiac Myosin S1 fragment Kratky plot 1.104 0 √3 sRg
p(r)
Bovine β Cardiac Myosin S1 fragment pair distance distribution function Rg: 3.7 nm 0 Dmax: 12.6 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Bovine β Cardiac Myosin S1 fragment (Myosin-7) MgADP.VO4+OM in 10 mM HEPES, 50 mM NaCl, 1 mM NaN3, 2.5 mM MgCl2, 2 mM ADP, 1 mM TCEP, pH 7.5 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a CCD AVIEX detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured. 41 successive 0.500 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted.

BATCH mode

Bovine β Cardiac Myosin S1 fragment (BCS1 (myosin-7))
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   116.6 kDa
 
UniProt   Q9BE39
Sequence   FASTA