Statistics of crystallographic data collection and refinement
| Data collection . | IQSEC1_Apo-CaM/IQ/Sec7-PH . | IQSEC2_Apo-CaM/IQ/Sec7-PH . |
|---|---|---|
| Space group | P 21 21 21 | P 1 21 1 |
| Wavelength (Å) | 0.97891 | 1.099 |
| Unit cell parameters | ||
| a, b, c (Å) | 67.010, 81.436, 124.762 | 61.132, 76.274, 68.502 |
| α, β, γ (°) | 90.000, 90.000, 90.000 | 90.000, 101.04, 90.000 |
| Resolution range (Å) | 50.00–2.00 (2.03–2.00) | 56.08–3.48 (3.53–3.48) |
| No. of unique reflections | 46,959 (2,345) | 7,998 (389) |
| Redundancy | 10.1 (10.3) | 3.4 (3.5) |
| I/σ | 27.26 (3.38) | 13.74 (2.66) |
| Completeness (%) | 99.8 (100.0) | 99.1 (99.5) |
| Rmergea (%) | 6.8 (48.4) | 9.1 (37.5) |
| CC1/2b | 0.988 (0.940) | 0.992 (0.857) |
| Structure refinement | ||
| Resolution (Å) | 2.00 | 3.48 |
| Rworkc (%) | 19.78 | 26.06 |
| Rfreed (%) | 25.23 | 35.14 |
| Root-mean-square deviation | ||
| Bonds (Å) | 0.0072 | 0.0096 |
| Angles (°) | 0.78 | 1.6008 |
| Average B factor (Å2) | 38.4 | 85.7 |
| No. of atoms | ||
| Protein | 4,162 | 3,632 |
| Ligand/ion | 18 | 0 |
| Water | 268 | 3 |
| B Factors (Å2) | ||
| Proteins | 38.4 | 85.8 |
| Ligand/ion | 48.8 | 0 |
| Water | 36.9 | 37.8 |
| Ramachandran plot (%) | ||
| Preferred | 96.89 | 98.6 |
| Allowed | 3.11 | 1.4 |
| Outliers | 0 | 0 |
| Data collection . | IQSEC1_Apo-CaM/IQ/Sec7-PH . | IQSEC2_Apo-CaM/IQ/Sec7-PH . |
|---|---|---|
| Space group | P 21 21 21 | P 1 21 1 |
| Wavelength (Å) | 0.97891 | 1.099 |
| Unit cell parameters | ||
| a, b, c (Å) | 67.010, 81.436, 124.762 | 61.132, 76.274, 68.502 |
| α, β, γ (°) | 90.000, 90.000, 90.000 | 90.000, 101.04, 90.000 |
| Resolution range (Å) | 50.00–2.00 (2.03–2.00) | 56.08–3.48 (3.53–3.48) |
| No. of unique reflections | 46,959 (2,345) | 7,998 (389) |
| Redundancy | 10.1 (10.3) | 3.4 (3.5) |
| I/σ | 27.26 (3.38) | 13.74 (2.66) |
| Completeness (%) | 99.8 (100.0) | 99.1 (99.5) |
| Rmergea (%) | 6.8 (48.4) | 9.1 (37.5) |
| CC1/2b | 0.988 (0.940) | 0.992 (0.857) |
| Structure refinement | ||
| Resolution (Å) | 2.00 | 3.48 |
| Rworkc (%) | 19.78 | 26.06 |
| Rfreed (%) | 25.23 | 35.14 |
| Root-mean-square deviation | ||
| Bonds (Å) | 0.0072 | 0.0096 |
| Angles (°) | 0.78 | 1.6008 |
| Average B factor (Å2) | 38.4 | 85.7 |
| No. of atoms | ||
| Protein | 4,162 | 3,632 |
| Ligand/ion | 18 | 0 |
| Water | 268 | 3 |
| B Factors (Å2) | ||
| Proteins | 38.4 | 85.8 |
| Ligand/ion | 48.8 | 0 |
| Water | 36.9 | 37.8 |
| Ramachandran plot (%) | ||
| Preferred | 96.89 | 98.6 |
| Allowed | 3.11 | 1.4 |
| Outliers | 0 | 0 |
Numbers in parentheses represent the values for the highest-resolution shell.
Rmerge = ∑|Ii − <I>|/∑Ii, where Ii is the intensity of the measured reflection and <I> is the mean intensity of all symmetry-related reflections.
CC1/2 was defined in Karplus and Diederichs (2012).
Rwork = ∑W||Fcalc| − |Fobs||/∑|Fobs|, where Fobs and Fcalc are observed and calculated structure factors. W is a working dataset of about 95% of the total unique reflections randomly chosen and used for refinement.
Rfree = ∑T||Fcalc| − |Fobs||/∑|Fobs|, where T is a test dataset of about 5% of the total unique reflections randomly chosen and set aside prior to refinement.