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Crystal structure of mouse PCDH15 EC11-EL |
This entry was created with PDB-REDO version 7.31. |
From original header | |||||||
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Spacegroup | P 43 21 2 | a: 57.680 Å | b: 57.680 Å | c: 159.180 Å | α: 90.00° | β: 90.00° | γ: 90.00° |
Resolution | 1.40 Å | Reflections | 53914 | Test set | 2696 (5.0%) | ||
R | 0.1690 | R-free | 0.1950 | ||||
According to PDB-REDO | |||||||
Resolution | 1.40 Å | Reflections | 53914 | Test set | 2696 (5.0%) | ||
Twin | false | Radiation damage | N/A | ||||
PDB-REDO files | |||||||
Re-refined and rebuilt structure | Re-refined (only) structure |
All files
(compressed) |
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Links | |||||||
PDBe | RCSB PDB | 3D bionotes | Proteopedia |
Original | PDB-REDO | |
---|---|---|
Crystallographic refinement | ||
R | 0.1834 | 0.1680 |
R-free | 0.2080 | 0.1969 |
Bond length RMS Z-score | 0.289 | 0.403 |
Bond angle RMS Z-score | 0.606 | 0.641 |
Model quality | ||
Ramachandran plot normality | -1.640 37 | -1.306 45 |
Rotamer normality | -1.360 71 | -0.127 91 |
Coarse packing | -0.494 36 | -0.546 34 |
Fine packing | -1.061 50 | -0.926 56 |
Bump severity | 0.016 45 | 0.010 58 |
Hydrogen bond satisfaction | 0.928 85 | 0.916 72 |
WHAT_CHECK | Report | Report |
Kleywegt-like plot |
Description | Count |
---|---|
Rotamers changed | 3 |
Side chains flipped | 0 |
Waters removed | 35 |
Peptides flipped | 0 |
Chiralities fixed | 0 |
Residues fitting density better | 36 |
Residues fitting density worse | 1 |