TABLE 1:

Binding affinity of hsNXF1-N proteins for Kapβ2 and Impβ.

Kapβ	hsNXF1-N	Kda (nM)	ΔH (kcal/mol)	TΔSb (kcal/mol/K)	Kd,mutant/Kd,wild type
Kapβ2	Wild type	40.5 ± 12.6	−17.21 ± 1.25	−7.31 ± 1.42	—
	21-30/A	127.9 ± 19.5	−13.93 ± 2.65	−4.68 ± 2.56	3.2
	71-75/A	215.3.8 ± 61.4	−12.91 ± 1.12	−3.98 ± 1.27	5.4
	21-30, 71-75/A	n.d.	n.d.	n.d.	≫6c
Impβ	Wild type	Kd1 6 ± 5 Kd2 1519 ± 225	−7.51 ± 0.07 −4.60 ± 0.55	3.40 ± 0.58 3.20 ± 0.49	—
	21-30/A	2234 ± 52	−2.48 ± 0.52	5.09 ± 0.53	372d
	71-75/A	Kd1 6 ± 2	−7.73 ± 0.28	3.26 ± 0.48	1 (Kd1)
		Kd2 2461 ± 723	−3.28 ± 0.58	4.22 ± 0.60	2 (Kd2)
	21-30, 71-75/A	n.d.	n.d.	n.d.	>400d,e

n.d., not detectable. All experiments were performed three to five times (±SD).

^aStoichiometry, 0.9–1.1.

^bTΔS = ΔH – ΔG.

^cThe lowest measurable K_d of 215 nM in the Kapβ2–hsNXF1-N series was used to estimate K_d,mutant/K_{d,wild type}.

^dRatio taken using K_{d1,wild type}.

^eThe lowest measurable K_d of 2.23 μM in the Impβ–hsNXF1-N series was used to estimate K_d,mutant/K_{d,wild type}.