Table 1. Structural characterization of p97 mutants^a.

p97 mutations	Location in the structure with bound ADP	Location in structure with bound ATPγS	Closest residues in ADP form		Closest residues in ATPγS form
			From D1	From N	From D1	From N
R53A	N–surf, exposedb	N–surf, exposedb	None	None	None	None
R86A	N–D1 int, buriedc	Exposedd	E261	D204	None	None
R93Ce	N–D1 int, buried	N–D1 int, buried	None	E195	None	E194
R95G/Ce	N–D1 int, buried	N–D1 int, buried	G263	E196	K386	D204
R155H/C/P/Le	N–D1 int, buried	Exposed	K386	None	None	None
G157Re	N–D1 int, buried	Exposed	N443	None	None	None
R159H/Ce	N–D1 int, buried	Exposed	A232	I126	None	E124
R191Qe	N–D1 int, buried	N–D1 int, buried	None	E162,D121	None	E162,E195
L198We	N–D1 int, buried	N–D1 int, buried	None	V87,R86	None	N90,R93
A232Ee	N–D1 int, buried	Exposed	I437d	G125f	M442f	None
T262Ae	N–D1 int, buried	N–D1 int, buried	R225	None	E221	R64
N387He	N–D1 int, buried	Exposed	None	R155,R159g	None	N199,R95
aAll mutants form hexamers in solution.
b'N–surf, exposed' means that the mutation is located on the surface of the N-domain exposed to solvent.
c‘N–D1 int, buried' means that the mutation is located at the interface between the N- and D1-domains and is buried.
dThis residue is exposed to solvent.
eThose mutations were identified in patients with IBMPFD (Haubenberger et al, 2005; Hubbers et al, 2007; Djamshidian et al, 2009; Schroder et al, 2005; Watts et al, 2004; Watts et al, 2007; Kumar et al, 2010).
fInteracting with residues from a neighbouring subunit.
gInteracting with main chain atoms of the indicated residue.