The Förster resonance energy transfer (FRET) between the Fenna-Matthews-Olson (FMO) protein complex and the chlorosomal baseplate (CBP) is investigated by using an idealized model. This simplified model is based on crystal structure and molecular dynamics conformations. Some of the further input, such as the transition dipole moments, was extracted from earlier molecular-level simulations. The resulting model mimics the effects of the relative position between the CBP and the FMO complex on the corresponding FRET efficiency under ideal conditions, involving about 1.3 billion FRET calculations per investigated model. In this idealized model and employing some approximations, it is found that FRET efficiency is almost completely independent of the FMO trimer orientation (displacement, distance, and rotation), despite FMO and CBP being highly structured complexes. Even removing individual FMO BChl triples will only reduce the FRET efficiency by up to 8.6%. An FMO containing only the least efficient BChl triple will retain about 25% of the FRET efficiency of a full FMO complex. In addition to its proposed function as an energetic funnel, FMO is thus identified to act as a highly robust spatial funnel for CBP excitation harvesting, independent of the mutual CBP-FMO orientation.