TABLE 6.

Structural parameters of P. furiosus ACAPT and homologs known to affect protein stability^a

Parameter	Name or value
PDB ID	1MJF	1INL	1UIR	1IY9	1XJ5	2B2C	1ZDZ
Sourceb	P. furiosus	T. maritima	T. thermophilus	B. subtilis	A. thaliana	C. elegans	Human
Sequence length	281	296	314	275	334	314	304
Probable molecular assemblyb	2	4	4	4	4	2	2
Resolution (Å)c	1.80	1.50	2.00	2.30	2.70	2.80	2.12
Optimal growth temp (°C)	100	80	70	35	25	25	37
Protein
No. of loopsc	21	22	24	20	20	22	21
No. of residues/loop (avg.)	4.19	4.33	4.04	4.65	7.48	5.86	5.00
No. of hydrogen bondsd	252	277	309	236	265	235	274
No. of hydrogen bonds/residue	0.90	0.94	0.98	0.86	0.79	0.75	0.90
No. of salt bridges	11	12	16	8	5	11	17
No. of CASTp pocketse	32	36	32	33	44	41	39
Largest CASTp pocket (Å3)e	637	895	2596	1606	1337	665	1185
Dimer
Total surface area (Å2)f	18367	22292	22288	18869	19932	20917	19655
Accessible surface area (Å2)f	19738	24246	23415	20449	20715	22270	20885
Interface accessible surface (Å2)f	1741	1609	1787	1581	1820	1634	1661
% Interface surface areaf	14.82	11.66	13.20	13.17	13.92	12.52	13.23
Interface lengthf	39	42	40	40	49	45	39
Interface breadthf	35	33	37	33	39	33	39
% Polar atoms at interfacef	35.26	45.91	30.00	31.21	33.63	35.17	38.68
% Nonpolar atoms at interfacef	64.70	54.00	70.00	69.70	66.30	64.80	61.30
No. of interface hydrogen bondsf	19	24	16	12	24	14	20
No. of interface salt bridgesf		2	2	0	0	0	0
No. of bridging HOH moleculesf	23	0	15	0	0	6	20

^aComparisons were made between the best-aligning chains for each structure. PDB ID, Protein Data Bank identification.

^bPISA (www.ebi.ac.uk/msd-srv/prot_int/pistart.html).

^cProtein Data Bank (www.rcsb.org/pdb).

^dCHIMERA (www.cgl.ucsf.edu/chimera).

^eCASTp (sts.bioengr.uic.edu/castp).

^fProtein-Protein Interaction Server (www.biochem.ucl.ac.uk/bsm/PP/server).