While we focus on the DHDDS domain, as this is the region that clearly associates to the membrane and has such a strong phenotype if membrane interactions are disturbed, the NgBR domain also associates to the membrane. Past research has described a multipass transmembrane domain, as well as two possible membrane-binding helices, in the NgBR N-terminal region. While some putative transmembrane helices are inconsistent with currently available structural data, there is strong evidence that NgBR has at least one transmembrane helix to anchor the protein to the ER membrane. Our simulated h-cisPT has the first 75 residues of the NgBR N-terminus cleaved, removing any transmembrane helices. As a result, the lack of NgBR N-terminus membrane association observed in our simulations is not evidence against the presence of such a TM domain, or evidence that NgBR also interacts with the membrane.