Table 1.

Crystallographic data collection and refinement statistics.

Data set 1	nNOS D597N-2	nNOS D597N-3	nNOS D597N/M336V-6
Data collection
PDB code	5G0N	5G0O	5G0P
Space group	P212121	P212121	P212121
Cell dimensions a, b, c (Å)	51.8 110.2 164.2	51.7 110.7 164.2	51.6 111.2 164.3
Resolution (Å)	1.94 (2.00–1.94)	1.85 (1.90–1.85)	2.10 (2.19–2.10)
Rmerge2	0.107 (1.230)	0.119 (2.463)	0.155 (1.998)
Rpim3	0.053 (0.664)	0.058 (1.208)	0.105 (1.353)
CC 1/24	0.997 (0.610)	0.998 (0.659)	0.995 (0.451)
I/σI	9.1 (1.1)	7.1 (0.7)	6.8 (0.8)
No. unique reflections	70,703	81,212	55,639
Completeness (%)	99.6 (93.4)	99.9 (100.0)	99.3 (99.1)
Redundancy	5.0 (4.2)	5.1 (5.1)	5.4 (5.5)
Refinement
Resolution (Å)	1.94	1.85	2.10
No. reflections used	70,518	80,907	55,529
Rwork/Rfree 5	0.175/0.216	0.193/0.233	0.200/0.245
No. atoms
Protein	6683	6687	6684
Ligand/ion	173	175	173
Water	498	460	332
R.m.s. deviations
Bond lengths (Å)	0.007	0.008	0.009
Bond angles (deg)	1.14	1.17	1.17

¹See Figure 1 for the inhibitor chemical formula.

² $R_{\mathit{merge}}=\frac{{\displaystyle \sum _{\mathit{hkl}}}{\displaystyle \sum _j}\mid I_{\mathit{hkl},j}-<I_{\mathit{hkl}}>\mid }{{\displaystyle \sum _{\mathit{hkl}}}{\displaystyle \sum _j}{I}_{\mathit{hkl},j}}$ I is the observed intensity and <I> is the average intensity over multiple symmetry related observations.

³ $R_{\mathit{pim}}=\frac{{\displaystyle \sum _{\mathit{hkl}}}\sqrt{\frac{1}{n-1}}{\displaystyle \sum _{j=1}^n}\mid I_{\mathit{hkl},j}-<I_{\mathit{hkl}\mid }}{{\displaystyle \sum _{\mathit{hkl}}}{\displaystyle \sum _j}{I}_{\mathit{hkl},j}}$ Precision indicating R factor.

⁴CC ½ values are calculated by splitting the data randomly in half. The RMS Correlation Ratio (RCR) is calculated from a scatter plot of pairs of DeltaI from the two subsets (halves) by comparing the RMS value (excluding extremes) projected on the line with slope = 1 (“correlation”) with the RMS value perpendicular to this (“error”).

⁵R_free was calculated with the 5% of reflections set aside throughout the refinement.