To distinguish the effects of the environment and those of the internal conformations of the pigment molecules, used the conformations from the QM/MM MD trajectory and performed TD-LC-DFTB calculations for the excited states neglecting the effect of the environment, without protein environment is not as large as found in organic solvent in experiment, one has to keep in mind that sampling over multiple conformations can only be achieved for a low-level quantum method such as TD-LC-DFTB. On one hand, such low-level theory can provide a qualitative trend along a trajectory whereas on the other hand, high-level quantum method such as DFT/MRCI can be used to obtain a quantitative benchmark based on single conformations as shown in Table , Fig. , and Fig. for the gas-phase as well as inside a protein environment for the QM/MM-optimized and the crystal structures. Moreover, based on the QM/MM-optimized structures and shown in Fig. the DFT/MRCI method without protein environment is yielding a similar blue-shift as the experimental values in organic solvents (see Table ). The largest differences for the average energies can be observed in the case of the Chl-c2 molecules, while the second-largest energy shifts are observed for the Chl-c1 pigments. These findings again strongly suggest that the environment is playing a key role in the control of the Q y excitation energies of the Chl-c pigments and significantly affects the energy ladder within the present FCP complex. As an additional point, we have investigated the role of the local protein environment around the Chl-c molecules to observe whether any major structural change can potentially induce artifacts in the calculation of the excitation energies. However, as explained in Section S5, the small RMSD values of the C-α atoms belonging to nearby amino acid residues as well as of the Chl-c1/c2 pigments rule out this possibility (see Fig. ).