Table 1.
Statistics of data collection and model refinement
| Native ANK repeats/AS | SeMet-ANK repeats/AS | R1-9/Nav1.2_ABD-C | |
|---|---|---|---|
| Data collection | |||
| Space group | R32 | R32 | P4222 |
| Cell dimensions | |||
| a, b, c (Å) | 179.9, 179.9, 304.5 | 179.7, 179.7, 304.9 | 102.3, 102.3, 106.0 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 90 |
| Resolution range (Å) | 50–4.0 (4.07–4.0) | 50–3.5 (3.56–3.5) | 50–2.5 (2.54–2.5) |
| Rmerge (%)* | 8.7 (45.8) | 12.1 (78.3) | 7.7 (74.8) |
| I/σI | 17.1 (3.4) | 22.5 (2.2) | 29.8 (3.5) |
| Completeness (%) | 98.9 (99.3) | 96.0 (97.2) | 99.4 (100) |
| Redundancy | 4.3 (4.4) | 10.2 (9.0) | 9.5 (9.7) |
| Structure refinement | |||
| Resolution (Å) | 50–3.5 (3.62–3.5) | 50–2.5 (2.64–2.5) | |
| Rcryst/Rfree (%)† | 22.0 (35.0)/25.3 (36.6) | 18.8 (22.7)/23.8 (24.5) | |
| r.m.s.d. bonds (Å)/angles (°) | 0.013/1.5 | 0.015/1.5 | |
| Average B factor | 113.5 | 63.5 | |
| No. of atoms | |||
| Protein atoms | 6260 | 2243 | |
| Water molecules | 0 | 74 | |
| Other molecules | 45 | 57 | |
| Ramachandran plot‡ | |||
| Favored regions (%) | 94.7 | 97.7 | |
| Allowed regions (%) | 5.2 | 2.3 | |
| Outliers (%) | 0.1 | 0.0 | |
*
Rmerge = Σ|Ii − Im|/ΣIi, where Ii is the intensity of the measured reflection and Im is the mean intensity of all symmetry related reflections.
†
Rcryst = Σ||Fobs| − |Fcalc||/Σ|Fobs|, where Fobs and Fcalc are observed and calculated structure factors, respectively. Rfree = ΣT||Fobs| − |Fcalc||/ΣT|Fobs|, where T is a test data set of about 5% of the total reflections randomly chosen and set aside prior to refinement.
‡
Defined by MolProbity.
Numbers in parentheses represent the value for the highest resolution shell.