The article also fails to mention that the structure of many proteins doesn't correspond to their "natural folding" but is modified by other proteins (e.g. chaperones), or is determined by the complex to which the protein belongs, i.e. cannot be predicted with data based on isolated proteins. Furthermore most proteins were measured in crystallized (i.e. not their natural) form, so the resulting static structure is likely not representative (even less if parts of the protein are "moving" to perform their function). So it would be quite naive to assume that from now on you can just throw a sequence into the black box and the right structure comes out.