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\section{Summary and Outlook}  In this paper we present ProCS15: a program that computes the isotropic chemical shielding values of backbone atoms and C$\beta$ given a protein structure in less than a second. ProCS accounts for the effect of backbone dihedral angle changes, dihedral angle-changes of the side-chain and the two closest neighbors, hydrogen bonding to the backbone amide group and H$\alpha$ as well as ring-current effects \cite{Christensen_2011} on the hydrogen atoms and assumes that these effects are additive. The backbone, side-chain and hydrogen bonding terms are based on ca 2.35 million OPBE/6-31G(d,p)//PM6 calculations on tripeptides and small structural models hydrogen-bonding.  ProCS15 reproduces the chemical shielding values computed using PCM/OPBE/6-31G(d,p)//PM6-D3H+ for ubiquitin and Protein G with RMSD values (after linear regression) of up to 2.5 ppm for carbon atoms, 0.9 ppm for hydrogen atoms, and 0.4 ppm for nitrogen. These deviations, which presumably result from the assumption of additivity, doe not appear to preclude equal or better accuracy when comparison to experiment because the accuracies of the chemical shifts computed using ProCS15 (based on linear regression of the chemical shifts, cf. Eq \ref{eqn:scaling}) are very similar to the corresponding DFT calculations for ubiquitin and Protein G. The largest RMSD values observed for carbon, hydrogen, and nitrogen are, respectively, 2.2 (2.8) ppm, 0.4 (0.4) ppm, and 4.7 (4.6) ppm for ProCS15 (PCM/OPBE/6-31G(d,p)).