Table 1. Data collection and refinement statistics.
Numbers in parentheses represent the value for the lowest/highest resolution shell (innermost/outermost shells).
| Hd 1NES1NiR (as-isolated) | Hd 1NES1NiR (nitrite-soaked) | |
|---|---|---|
| Ligands | W1 | NO2/NO |
| Data collection | ||
| Space group | P6522 | P6522 |
| Wavelength (Å) | 0.9795 | 0.9795 |
| a, b, c (Å) | 77.07, 77.07, 754.55 | 77.72, 77.72, 758.20 |
| Resolution (Å) | 66.75–2.05 (66.75–10.85/2.09–2.05) | 126.37–2.10 (126.37–5.7/2.14–2.10) |
| No. of reflections, total/unique | 363227/85026 | 987567/81889 |
| R merge † (%) | 12.1 (2.9/92.6) | 21.6 (6.2/284.5) |
| R p.i.m. ‡ (%) | 8.4 (1.9/67.7) | 6.4 (2.0/82.8) |
| I/σ(I) | 3.5 (9.5/0.8) | 7.7 (24.0/0.9) |
| CC1/2 | 0.995 (0.998/0.610) | 0.998 (0.998/0.426) |
| Completeness (%) | 98.7 (99.8/98.2) | 100 (100/100) |
| Multiplicity | 4.3 (3.4/4.4) | 12.1 (10.6/12.3) |
| Refinement | ||
| R work §/R free ¶ | 0.227/0.279 | 0.172/0.227 |
| Resolution (Å) | 66.75–2.05 | 126.37–2.25 |
| No. of atoms | ||
| Protein | 9630 | 9625 |
| Ligand/ion | 9 | 17 |
| Water | 528 | 639 |
| Average B factor (Å2) | ||
| Protein | 51.8 | 54.9 |
| Ligand/ion | 47.1 | 52.3 |
| Water | 50.5 | 52.6 |
| R.m.s. deviations | ||
| ond lengths (Å) | 0.007 | 0.007 |
| Bond angles (°) | 1.511 | 1.601 |
| Ramachandran plot | ||
| Favored (%) | 96.6 | 97.2 |
| Allowed (%) | 99.8 | 99.7 |
| PDB entry | 6tfo | 6tfd |
†
, where I
i is the intensity of the measured reflection and I
m is the mean intensity of all symmetry related reflections.
‡
where I
i is the intensity of the measured reflection, I
m is the mean intensity of all symmetry related reflections and n is the redundancy.
§
, where F
obs and F
calc are the observed and calculated structure factors, respectively.
¶
, where T is a test data set of 5% of the total reflections randomly chosen and set aside prior to refinement.