Table 1.

Major domain–domain interactions in the equilibrated oxy‐FMN‐CaM complex. Contacts are defined as a distance ≤3.5 Å

Residue A	Residue B	Average contacts per picosecond	Selected atom–atom pair	MD distance and St. Dev. over final 50 ns b	Previous experimental work a
Chain A heme domain to chain B FMN domain
HemeA‐Arg452	FMN‐Glu546	4.331	A‐NH2/B‐OE1	3.11 ± 0.51 Å	35, 36
HemeA‐Asn449	FMN‐Glu546	1.891	A‐ND2/B‐OE2	4.13 ± 1.10 Å	35, 36
HemeA‐Lys155	FMN‐Glu603	1.626	A‐NZ/B‐OE1	4.79 ± 2.14 Å	37
HemeA‐Glu156	FMN‐Lys607	1.406	A‐OE1/B‐NZ	5.44 ± 2.74 Å	Reported here
HemeA‐Ser207	FMN‐Asn595	1.219	A‐O/B‐ND2	3.79 ± 0.94 Å	Reported here
HemeA‐Asn208	FMN‐Gly594	1.063	A‐ND2/B‐O	3.58 ± 1.15 Å	33
Chain A of heme domain to calmodulin
HemeA‐Arg86	CaM‐Asp122	5.224	A‐NH1/C‐OD2	2.78 ± 0.27 Å	25
HemeA‐Arg83	CaM‐Glu127	4.357	A‐NH2/C‐OE1	3.71 ± 1.88 Å	38
HemeA‐Gln97	CaM‐Asp133	1.291	A‐NE2/C‐O	3.27 ± 0.63 Å	Reported here
Chain B FMN domain to calmodulin
FMN‐Arg536	CaM‐Glu47	5.076	B‐NH2/C‐OE1	2.99 ± 0.34 Å	22
FMN‐Arg576	CaM‐Glu83	4.568	B‐NH1/C‐OE2	3.23 ± 0.66 Å	Reported here
FMN‐Glu551	CaM‐Lys94	2.805	B‐OE1/C‐NZ	3.55 ± 1.22 Å	Reported here
FMN‐Lys568	CaM‐Glu87	2.443	B‐NZ/C‐OD2	3.32 ± 0.92 Å	22
FMN‐Lys574	CaM‐Asp93	1.854	B‐NZ/C‐OD2	2.67 ± 0.09 Å	Reported here

^aResidue previously identified to be important for either enzyme activity or domain interactions as referenced in corresponding study in either iNOS or an analogous residue in either eNOS or nNOS.

^bFor a more in depth view of the nature and dynamics of each contact, refer to Supporting Information Fig. S3.