1ri9 Experiments and Validation

Solution NMR

Source organism: Homo sapiens [9606]
Refinement method: torsion angle dynamics
Number of deposited models: 20 models
Chemical shifts: BMR5467  

Sample information

Author description:
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
Source organism: Homo sapiens [9606]
Expression system: Escherichia coli BL21 [511693]

Validation information

 
Structure ensemble information
Refinement method: torsion angle dynamics
Number of calculated models: 51
Number of deposited models: 20 (The submitted conformer models are the 20 structures with the lowest energy.)
Representative model: 1 (fewest violations,lowest energy)
 
Experimental NMR data
Chemical shifts: BMR5467  

Experimental information

Sample 1
Contents: 1.8mM ADAP-hSH3 domain "[U-95% 13C; U-90% 15N]" Recorded spectra: 2D NOESY, 2D TOCSY, 3D_13C-separated_NOESY, 3D_15N-separated_NOESY

Samples and spectra
NMR spectrometers used
Bruker DRX 600 MHz