Table I. ITC analysis of interactions... | Rockefeller University Press

Table I.

ITC analysis of interactions between the SPSB2 SPRY domain and wild-type or mutant iNOS N-terminal peptides

Peptide	Sequence	K_d
		nM
A	Ac-KEEKDINNNVKKT-NH₂	13.3 ± 3.0
B	Ac-KEAKDINNNVKKT-NH₂	14.0 ± 3.0
C	Ac-KEEADINNNVKKT-NH₂	127 ± 23
D	Ac-KEAADINNNVKKT-NH₂	65.4 ± 7.4
E	Ac-KEEKAINNNVKKT-NH₂	21,600 ± 750
F	Ac-KEEKDANNNVKKT-NH₂	23.5 ± 9.9
G	Ac-KEEKDIANNVKKT-NH₂	17,200 ± 7,400
H	Ac-KEEKDIQNNVKKT-NH₂	40,500 ± 7,200
I	Ac-KEEKDINANVKKT-NH₂	826 ± 20
J	Ac-KEEKDINNAVKKT-NH₂	ND^a
K	Ac-KEEKDINNQVKKT-NH₂	ND^a
L	Ac-KEEKDINNNAKKT-NH₂	56.8 ± 11.2
M	Ac-KEEKDINNNVKAT-NH₂	29.8 ± 12.2
N	Ac-KEEKDINNNAKAT-NH₂	180 ± 39
O	Ac-KEEADINNNAKAT-NH₂	311 ± 37

Peptide	Sequence	K_d
		nM
A	Ac-KEEKDINNNVKKT-NH₂	13.3 ± 3.0
B	Ac-KEAKDINNNVKKT-NH₂	14.0 ± 3.0
C	Ac-KEEADINNNVKKT-NH₂	127 ± 23
D	Ac-KEAADINNNVKKT-NH₂	65.4 ± 7.4
E	Ac-KEEKAINNNVKKT-NH₂	21,600 ± 750
F	Ac-KEEKDANNNVKKT-NH₂	23.5 ± 9.9
G	Ac-KEEKDIANNVKKT-NH₂	17,200 ± 7,400
H	Ac-KEEKDIQNNVKKT-NH₂	40,500 ± 7,200
I	Ac-KEEKDINANVKKT-NH₂	826 ± 20
J	Ac-KEEKDINNAVKKT-NH₂	NDa
K	Ac-KEEKDINNQVKKT-NH₂	NDa
L	Ac-KEEKDINNNAKKT-NH₂	56.8 ± 11.2
M	Ac-KEEKDINNNVKAT-NH₂	29.8 ± 12.2
N	Ac-KEEKDINNNAKAT-NH₂	180 ± 39
O	Ac-KEEADINNNAKAT-NH₂	311 ± 37

Typical ITC raw data and titration curves are shown in Fig. S1. Bold letters indicate the amino acid substitution. The K_d column shows dissociation constants with errors from the Origin-calculated association constants transferred as the same fractions of primary values.

Binding affinity was too low to be determined under these conditions.

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