QuantumBio announces the availability of the NMRScore Application, an accurate and fast approach to calculate NMR chemical shifts for biological systems. It also allows for three-dimensional structure determination of protein-ligand complexes in structure-based drug design.

NMRScore offers superior performance to that of energy-based scoring functions associated with docking programs in ranking native-like structures and differentiating these poses from decoy poses. Therefore, by combining conventional docking programs with NMRScore results in an approach that can robustly determine the binding site structure for a protein-ligand complex without having to resort to an expensive, time-comsuming xray refinement.

NMRScore algorithm utilizes a ligand binding mode scoring function based upon DivCon’s NMR chemical shift perturbation (CSP) prediction implementation coupled with experimental CSP values using the divide-and-conquer method. CSP is exquisitely sensitive on the orientation of the ligand inside the binding pocket, giving NMRScore an advantage over traditional NMR chemical shift calculations by offering an accurate and straightforward approach to score different poses.

NMRScore features include:

  • Clear differentiation between native and non-native poses.
  • Calculation of binding-induced chemical shift perturbations for an entire protein-ligand complex at the quantum mechanical level.
  • Determination of ligand orientation inside a protein binding pocket when used in conjuction with a docking program.
  • Visualization through the MOE/DivCon GUI.
  • Superior perfromance in a user-friendly format.

To learn more about NMRScore, please contact QuantumBio.