Our analysis clearly demonstrates that the investigated peptide presents a predominantly disordered, but not 'randomly disordered' conformational ensemble. On the one hand, its CD, IR, Raman and ROA spectroscopic fingerprints reveal minority signatures associated with ordered secondary-structure elements, and theoretical sampling of its conformational phase space reveals a few conformers clustered around ordered structures. On the other hand, the majority of the conformers present structures whose torsional angles localize in the PPII region of the Ramachandran plot, as already known for the case of intrinsically disordered proteins. However, in terms of their contribution towards the macroscopic spectroscopic observables, the distinction between 'ordered' and 'disordered' conformers is much less obvious than one could intuitively imagine. Indeed, by means of a multidimensional analysis and clustering procedure, we have been able to tidy up the conformational phase space and to filter out 20 representative conformers whose spectroscopic responses contribute in a major way to the ensemble-averaged observables. Only about 10 % of them present 'traditional' secondary structure elements such as α-helices or β-hairpins; the rest are varieties of coil structures, that contribute with equally important and diverse responses to the spectro-scopic fingerprint. In such a system, the very notions of 'structure' and 'order' or 'disorder' need to be challenged, as we will make clear.