BMRB Entry 17629

Assembly:

Entities:

Entity 1, Nbp2_SH3 73 residues - 7562.403 Da.

Residues 1-2 and 66-67 represent non-native residues obtained from cloning. Residues 68-73 represent His tag.

Entity 2, Ste20_peptide 16 residues - 1639.933 Da.

Samples:

sample_1: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 1.4 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%%; D2O 5%%; H2O 95%%

sample_2: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 1.4 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 100%

sample_3: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 0.7 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 5%; H2O 95%

sample_4: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 0.7 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, data analysis, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

• Bruker INOVA 500 MHz
• Bruker INOVA 800 MHz