3EZE

COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE


SOLUTION NMR
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDMX500500
2BrukerDMX600600
3BrukerDMX750750
NMR Refinement
MethodDetailsSoftware
simulated annealingTHE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM CNS MODIFIED TO INCORPORATE COUPLING CONSTANT RESTRAINTS (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-103), CARBON CHEMICAL SHIFT RESTRAINTS, (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, AND RESIDUAL DIPOLAR COUPLING RESTRAINTS (CLORE ET AL. J. MAGN. RESON 131, 159-162 (1998); J. MAGN 133, 216-221 (1998)). IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO MEANING. BEST FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 1 - 250 (RESIDUES 251 - 259 ARE DISORDERED IN SOLUTION) OF ENZYME I AND RESIDUES 301-385 OF HPR. RESIDUES 251-259 ARE OMITTED FROM THE MEAN STRUCTURECNS
NMR Ensemble Information
Conformer Selection CriteriaREGULARIZED MEAN STRUCTURE
Conformers Calculated Total Number40
Conformers Submitted Total Number1
Additional NMR Experimental Information
DetailsTHE 3D STRUCTURE OF THE EIN-HPR COMPLEX WAS SOLVED BY MULTI HETERONUCLEAR NMR AND IS BASED ON 5475
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1refinementCNSBRUNGER
2structure solutionCNS (SEE ABOVE)