1m3a Experiments and Validation

Solution NMR

Entry percentile scores
Source organism: Mus musculus
Refinement method: Simulated annealing combined with torsion angle dynamics
Number of deposited models: 20 models
Backbone RMSD for the largest domain: 0.3 Å

Sample information

Author description:
Solution structure of a circular form of the truncated N-terminal SH3 domain from oncogene protein c-Crk.
Source organism: Mus musculus
Expression system: Escherichia coli

Validation information

 
Structure ensemble information
Refinement method: Simulated annealing combined with torsion angle dynamics
Number of calculated models: 200
Number of deposited models: 20 (structures with the lowest target function)
Well-defined residues: A:135-A:143, A:151-A:189
Backbone RMSD for the largest domain: 0.3 Å
Representative model: 10 (medoid: most similar to other models)
 
Experimental NMR data

Experimental information

Sample 1
Contents: 1mM SH3 NA, 20mM sodium phosphate, 20 mM DTT-d10, 100 mM NaCl, 0.1% (w/v) NaN3 Recorded spectra: 2D NOESY, 2D TOCSY, DQF-COSY

Sample 2
Contents: 1mM SH3 U-15N, 20mM sodium phosphate, 20 mM DTT-d10, 100 mM NaCl, 0.1% (w/v) NaN3 Recorded spectra: 2D HSQC, 2D TOCSY

Samples and spectra
NMR spectrometers used
Bruker DMX 500 MHz, Bruker DMX 600 MHz, Bruker DRX 600 MHz