1JMQ

YAP65 (L30K mutant) WW domain in Complex with GTPPPPYTVG peptide


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
12D NOESY1.2 mM WW domain; 2.4 mM peptide GTPPPPYTVG; 10mM potassium phosphate buffer pH6; 100mM NaCl; 0.1 mM DTT; 0.1 mM EDTA,90% H20, 10% D20100mM NaCl61 atm288
22D TOCSY1.2 mM WW domain; 2.4 mM peptide GTPPPPYTVG; 10mM potassium phosphate buffer pH6; 100mM NaCl; 0.1 mM DTT; 0.1 mM EDTA,90% H20, 10% D20100mM NaCl61 atm288
32D NOESY1.2 mM WW domain; 2.4 mM peptide GTPPPPYTVG; 10mM potassium phosphate buffer pH6; 100mM NaCl; 0.1 mM DTT; 0.1 mM EDTA,100%D20100mM NaCl61 atm288
42D TOCSY1.2 mM WW domain; 2.4 mM peptide GTPPPPYTVG; 10mM potassium phosphate buffer pH6; 100mM NaCl; 0.1 mM DTT; 0.1 mM EDTA,100%D20100mM NaCl61 atm288
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX600
2BrukerDMX750
NMR Refinement
MethodDetailsSoftware
simulated annealing2000K, 200 runs, force constants for NOE 50 kcalmol-1rad-2, 590 restraints including 20 hydrogen bond restraintsXwinNMR
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number200
Conformers Submitted Total Number20
Representative Model1 (lowest energy)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingXwinNMR2.6BRUKER, A.G.
2collectionXwinNMR2.6BRUKER, A.G.
3data analysisANSIG3.3Kraulis, P.J
4refinementX-PLOR3.1Brunger, A.