1L2Z

CD2BP2-GYF domain in complex with proline-rich CD2 tail segment peptide


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY1 mM GYF domain U-deuterated, U-15N, 1mM Peptide, 50 mM phosphate buffer, pH 6.3100% D2O50 mM NaPo46.31 atm298
22D NOESY1 mM GYF domain U-deuterated, U-15N, 1mM Peptide, 50 mM phosphate buffer, pH 6.3100% D2O50 mM NaPo46.31 atm298
32D TOCSY1 mM GYF domain U-deuterated, U-15N, 1mM Peptide, 50 mM phosphate buffer, pH 6.3100% D2O50 mM NaPo46.31 atm298
43D 15N edited TOCSY1 mM GYF domain U-deuterated, U-15N, 1mM Peptide, 50 mM phosphate buffer, pH 6.3100% D2O50 mM NaPo46.31 atm298
515N HSQC1 mM GYF domain U-deuterated, U-15N, 1mM Peptide, 50 mM phosphate buffer, pH 6.3100% D2O50 mM NaPo46.31 atm298
62D NOESY1 mM GYF domain, aromatic amino acids protonated only, 1 mM Peptide protonated100% D2O50 mM NaPo46.31 atm298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX600
2VarianUNITY750
NMR Refinement
MethodDetailsSoftware
simulated annealing1000K, force constant NOE 50 kcal mol-1A-2, force constant dihedral angles 200 kcal mol-1 rad-2, 1000 steps minimization, intermolecular NOEs 33, intramolecular NOEs (peptide) 49, intramolecular NOEs (GYF domain) 754X-PLOR
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number100
Conformers Submitted Total Number15
Representative Model1 (lowest energy)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1refinementX-PLOR3.1Brunger, A.
2data analysisXEASY
3processingPROSA