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2HE9

Structure of the peptidylprolyl isomerase domain of the human NK-tumour recognition protein

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2006-06-10
DetectorRIGAKU RAXIS IV
Spacegroup nameP 21 21 2
Unit cell lengths64.753, 72.786, 73.014
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.910 - 2.000
R-factor0.14889
Rwork0.146
R-free0.19752
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ZCX
RMSD bond length0.017
RMSD bond angle1.515
Phasing softwarePHASER
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.070
High resolution limit [Å]2.0002.000
Number of reflections23807
<I/σ(I)>15.2
Completeness [%]99.998.7
Redundancy76.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP298Well solution: 21% Peg 3350, 0.25M potassium sulfate; Protein solution: 50 mM Tris pH 7.5, 100 mM NaCl, 1 mM DTT, 15 mg/mL protein, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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