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1FPZ

CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]100
Detector technologyCCD
Collection date2000-01-01
DetectorADSC
Spacegroup nameP 65
Unit cell lengths131.930, 131.930, 140.240
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 2.000
R-factor0.202

*

Rwork0.202
R-free0.25300
RMSD bond length0.012
RMSD bond angle1.580
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.120
High resolution limit [Å]2.0002.000
Rmerge0.0600.380
Total number of observations319770

*

Number of reflections90055
<I/σ(I)>9.3
Completeness [%]96.791.6
Redundancy3.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP54

*

Hanlon, N., (1998) Protein Sci., 7, 508.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoirPEG800024 (%(w/v))
31reservoirsodium acetate0.1 (M)
41reservoirammonium sulfate0.4 (M)
51reservoirphosphopeptide1 (mM)

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PDB entries from 2024-05-15

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