Evidence for a dual binding mode of dockerin modules to cohesins -- Carvalho et al. 104 (9): 3089 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Carvalho et al. 10.1073/pnas.0611173104.

Supporting Information

Files in this Data Supplement:

SI Table 2
SI Table 3
SI Table 4
SI Table 5

Table 2. X-ray data and structure quality statistics for the C. thermocellum S45A-T46A mutant Coh-Doc complex

Data quality	Coh-DocS45A-T46A
Cell parameters
a, Å	48.6
b, Å	92.7
c, Å	49.9
b, Âº	94.0
Space group	P2₁
X-ray source	ID14-EH3, ESRF
Wavelength, Å	0.931
Resolution of data (outer shell), Å	28.41-2.00 (2.11-2.00)
R _merge (outer shell), % *	25.9 (23.1)
Mn(I)/sd (outer shell)	4.8 (5.7)
Completeness (outer shell), %	95.8 (95.8)
Multiplicity (outer shell)	3.5 (3.3)
Structure quality
n Âº protein atoms	3,197
n Âº ligand atoms	14
n Âº solvent waters	562
Resolution used in refinement, Å	20.00-2.03
R _work / R_free, % ^Â†	17.8 / 23.0
rmsd 1-2 bonds, Å	0.007
rms deviation 1-3 bonds, degrees	0.973
rms deviation chiral volume. Å³	0.069
Avg. cohesin B value (whole chain), Å²
Molecule A	9
Molecule C	9
Avg. dockerin B value (whole chain), Å²
Molecule B	10
Calcium 1	5
Calcium 2	8
Molecule D	7
Calcium 1	8
Calcium 2	6
Phosphate 1 avg. B value, Å²	18
Phosphate 2 avg. B value, Å²	22
Avg. solvent waters B value, Å²	19

*R_merge = S| I-<I> | / S<I>, where I is the observed intensity, <I> is the statistically weighted average intensity of multiple observations.

^Â†R_work = S ||F_calc| - |F_obs||/ S |F_obs| ´ 100, where F_calc and F_obs are the calculated and observed structure factor amplitudes, respectively (R_free is calculated for a randomly chosen 10% of the reflections).

Table 3. Ligands of the calcium ions in the type I and type II dockerin modules

		Type I		Type II
		Residue	Atom	Residue	Atom
Ca1	n	Asp2	Od1	Asp102	Od1
	n+2	Asn4	Od1	Val104	O
	n+4	Asp6	Od1	Asp106	Od2
	n+6	Thr8	O	Ser108	O
	n+8	water - Asn10	O - Od1	water - Asn110	O - Od1
	n+11	Asp13	Od1 e Od2	Asp113	Od1 e Od2
Ca2	n	Asp36	Od1	Asp135	Od1
	n+2	Asp38	Od1	Asn137	Od1
	n+4	Asn40	Od1	Asn139	Od1
	n+6	Ser42	O	Ala141	O
	n+8	water - Asn44	O - Od1	water - Asn143	O - Od1
	n+11	Asp47	Od1 e Od2	Asp146	Od1 e Od2

Table 4. The hydrophobic residues at the interface of the Type I Coh-Doc complex

	Native	S45A-T46A mutant
Cohesin	Ala 36
	Val 41
	Ala 72
	Ile 79
	Val 81
	Leu 83
	Ala 85
Dockerin	Val 21	Leu 55
	Leu 22	Leu 56
	Val 48	Leu 14
	Leu 49	-
	Leu 50	Met 16
		Leu 22
		Ala 24
		Ile 25