TABLE 1.

Summary of K_d values used in kinetic modeling with monomeric αSNAP

Reaction	Name	Kd	Source
αSNAP + SC ⇌ αSNAP·SC	K1	450 nm	Direct measurement (Fig. 2A)
αSNAP + αSNAP·SC ⇌ (αSNAP)2·SC	K2	450 nm	Direct measurement (Fig. 2A)
αSNAP + (αSNAP)2·SC ⇌ (αSNAP)3·SC	K3	450 nm	Direct measurement (Fig. 2A)
αSNAP + (αSNAP)3·SC ⇌ (αSNAP)4·SC	K4	450 nm	Direct measurement (Fig. 2A)
αSNAP·SC + NSF ⇌ αSNAP·SC·NSF	K5	1200 nm	Km of αSNAP for SC disassembly by NSF (Fig. 2C)
(αSNAP)2·SC + NSF ⇌ (αSNAP)2·SC·NSF	K6	1200 nm	Km of αSNAP for SC disassembly by NSF (Fig. 2C)
(αSNAP)3·SC + NSF ⇌ (αSNAP)3·SC·NSF	K7	1200 nm	Km of αSNAP for SC disassembly by NSF (Fig. 2C)
(αSNAP)4·SC + NSF ⇌ (αSNAP)4·SC·NSF	K8	1200 nm	Km of αSNAP for SC disassembly by NSF (Fig. 2C)
αSNAP + NSF ⇌ αSNAP·NSF	K9	4700 nm	Km of αSNAP for the ATPase activity of NSF (Fig. 2D)
αSNAP + αSNAP·NSF ⇌ (αSNAP)2·NSF	K10	4700 nm	Km of αSNAP for the ATPase activity of NSF (Fig. 2D)
αSNAP + (αSNAP)2·NSF ⇌ (αSNAP)3·NSF	K11	4700 nm	Km of αSNAP for the ATPase activity of NSF (Fig. 2D)
αSNAP + (αSNAP)3·NSF ⇌ (αSNAP)4·NSF	K12	4700 nm	Km of αSNAP for the ATPase activity of NSF (Fig. 2D)
αSNAP·NSF + SC ⇌ αSNAP·SC·NSF	K13	120 nm	Thermodynamic cycle ((K1 × K5)/K9)
(αSNAP)2·NSF + SC ⇌ (αSNAP)2·SC·NSF	K14	12 nm	Thermodynamic cycle ((K13 × K17)/K10)
(αSNAP)3·NSF + SC ⇌ (αSNAP)3·SC·NSF	K15	1.1 nm	Thermodynamic cycle ((K14 × K18)/K11)
(αSNAP)4·NSF + SC ⇌ (αSNAP)4·SC·NSF	K16	0.11 nm	Thermodynamic cycle ((K15 × K19)/K12)
αSNAP·SC·NSF + αSNAP ⇌ (αSNAP)2·SC·NSF	K17	450 nm	Thermodynamic cycle ((K2 × K5)/K6)
(αSNAP)2·SC·NSF + αSNAP ⇌ (αSNAP)3·SC·NSF	K18	450 nm	Thermodynamic cycle ((K3 × K6)/K7)
(αSNAP)3·SC·NSF + αSNAP ⇌ (αSNAP)4·SC·NSF	K19	450 nm	Thermodynamic cycle ((K4 × K7)/K8)