6M8P
Human ERAP1 bound to phosphinic pseudotripeptide inhibitor DG013
This is a non-PDB format compatible entry.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-2 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-06-09 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.979 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 125.790, 548.684, 589.056 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.400 - 3.310 |
R-factor | 0.2859 |
Rwork | 0.285 |
R-free | 0.29520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yd0 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.605 |
Data reduction software | XDS (Jun 1, 2017) |
Data scaling software | Aimless (0.5.32) |
Phasing software | PHASER (2.8.0) |
Refinement software | PHENIX (1.14_3211) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.110 | 50.110 | 3.370 |
High resolution limit [Å] | 2.989 | 16.370 | 3.310 |
Rmerge | 1.396 | 0.194 | 5.545 |
Rmeas | 1.543 | 0.211 | 6.127 |
Rpim | 0.645 | 0.083 | 2.569 |
Number of reflections | 809932 | 5300 | 29452 |
<I/σ(I)> | 1.3 | 8.2 | 0.3 |
Completeness [%] | 99.1 | 96.5 | 99.9 |
Redundancy | 10.8 | 11.3 | 10.8 |
CC(1/2) | 0.940 | 0.992 | 0.139 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 1.3M Ammonium sulfate, 100mM MES |