Table 1.

Methyl-bearing amino acid residues of mutant calmodulin with perturbed amplitudes $(O_{\mathrm{axis}}^2)$ of fast motion

E84K			D58N			M124L			D95N
CaM methyl	$\widehat{\widehat{r}}$a	Db, Å	CaM methyl	$\widehat{\widehat{r}}$	D, Å	CaM methyl	$\widehat{\widehat{r}}$	D, Å	CaM methyl	$\widehat{\widehat{r}}$	D, Å
L18δS	−3.90	21.0c	A15β	−5.56	19.3d	A88β	−2.96	16.8d	I63γ	3.58	31.1d
L39δR	3.89	13.6	I52δ	5.67	11.9	L105δR	−3.50	4.3
L39δS	2.60	15.5	V55γR	6.93	11.4	L116δR	4.66	4.2
M71ɛ	−3.10	9.7	V55γS	7.36	9.9	L124ae	−18.4	N/A
M72ɛ	−4.05	11.5	A128β	−4.57	36.9	L124b	−16.3	N/A
M76ɛ	2.70	6.2	Δ τe, ps
V91γR	−3.69	13.2	T26γ	26.3	8.2
L116δR	2.96	26.3	I63δ	−11.2	9.9
M145ɛ	4.06	12.2

^a Standardized residuals calculated according to Eq. 1.

^b Distances from the methyl carbon of the perturbed residue and Cɛ of K84 in E84K, Cγ of D58 in D58N, Cɛ of M124 in M124L, and Cγ of D95N.

^c Distances measured in the E84K-RS20 crystal structure (PDB code 1vrk).

^d Distances measured in the CaM-smMLCKp crystal structure (PDB code 1cdl).

^e Methyl groups of L124 were not stereospecifically assigned in the mutant complex.