Table 3.

Computed structural properties

Residue	Interatomic distance* Å from 653 residue to Gly-710	SASA of fully exposed residue† Å2	Static structure SASA† Å2 (% exposed)		Molecular synamic SASA averages‡ Å2 (% exposed)
			653 residue	Tyr713	653 residue	Tyr713
Ser (wild-type) γ oxygen	3.0	80.0	7.2 (9%)	78.40 (42%)	40.38 (50%)	88.53 (47%)
Ala	N/A	67	5.40 (8%)	77.50 (41%)	40.21 (60%)	96.58 (51%)
Cys γ sulfur	2.7	104	6.10 (6%)	77.70 (41%)	61.79 (60%)	99.26 (53%)
Thr γ1 oxygen	4.2	102	8.20 (8%)	76.30 (41%)	25.92 (25%)	87.66 (47%)
Tyr hydroxyl	6.8	187	47.3 (25%)	67.3 (36%)	125.25 (70%)	136.81 (73%)
Phe	N/A	175	34.10 (19%)	70.40 (38%)	102.85 (59%)	65.13 (35%)
Glu ε1 oxygen/ε2 Oxygen	2.9/4.1	138	14.10 (10%)	71.60 (38%)	11.21 (8%)	71.12 (38%)
Asp δ1 oxygen/δ2 Oxygen	5.2/3.9	106	13.70 (13%)	75.40 (40%)	38.96 (37%)	72.66 (38%)

NA, not applicable because of lack of a functional group.

^*The interatomic distance between the functional group of the 653 residue and Gly-710 carbonyl oxygen were calculated using the PyMOL program.

^†SASA within the structural model of wtATP7B and SWISS-MODEL generated models containing the substitutions were calculated using the AREAIMOL program. The SASA or cavity surface area is defined as the surface traced by the center of a sphere with the radius of a water molecule (0.15 mm) as it is rolled over the surface of a molecular model of the solution (66). The SASA for each amino acid side chain is given when the Gly-X-Gly is an extended conformation (67). These values are taken to represent the maximum SASA and are provided for comparison and as a reference point to the SASA reported for the static structure.

^‡Average SASAs were calculated using the molecular dynamics calculations, as described in Methods.