The conformational dependences of 15N,15N and 1H,15N trans-H-bond spin-spin scalar couplings, h2J(N,N) and h1J(N,H), have been investigated by sum-over-states density-functional-perturbation theory. The distance and angular dependence of the h2J(N,N) and h1J(N,H) coupling constants in the H-bonded arrangement between acetylethylamine and imidazole molecules were examined for a wide range of mutual orientations. These molecules were used to model a structurally important H-bond between the amide backbone of Arg7 and the remote imidazole side chain of His106 in the 44 kDa trimeric enzyme chorismate mutase from Bacillus subtilis. The magnitude of h1J(N,H) is relatively insensitive to the sampled rotations around three orthogonal axes centered on the tertiary N-atom of the imidazole, whereas values of h2J(N,N) demonstrated a strong dependence on the value of the cone angle θ aligned with the amide group involved in the H-bond. Simple functional approximations have been generated, enabling back calculations of the N⋅⋅⋅N distance and angle θ of the H-bond, provided that the experimental values of both h2J(N,N) and h1J(N,H) coupling constants are available.