We study wild type and mutants of the A and B domain of protein G using all-atom Go-models. Our data substantiate the usefulness of such simulation for probing the folding mechanism of proteins and demonstrate that multifunnel versions of such models also allow probing of more complicated funnel landscapes. In our case, such models reproduce the experimentally observed distributions of the GA98 and GB98 mutants which differ only by one residue but fold into different structures. They also reveal details on the folding mechanism in these two proteins.