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3OBG

Conformational plasticity of p38 MAP kinase DFG mutants in response to inhibitor binding

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X4A
Synchrotron siteNSLS
BeamlineX4A
Temperature [K]93
Detector technologyCCD
DetectorADSC QUANTUM 4
Wavelength(s)0.98
Spacegroup nameP 21 21 21
Unit cell lengths65.118, 73.697, 77.080
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.250 - 2.800
R-factor0.22216
Rwork0.214
R-free0.32284
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1zyj
RMSD bond length0.023
RMSD bond angle2.246
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.2503.020
High resolution limit [Å]2.8002.800
Rmerge0.143
Number of reflections9563
<I/σ(I)>11.32.2
Completeness [%]99.199.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP629510-15% PEG 4000, 0.1M Cacodylic acid, 50 mM n-octyl-beta-D-glucoside, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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PDB entries from 2024-10-30

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