BMRB Entry 15554

Assembly:

Entities:

Entity 1, EH2 100 residues - 10985.906 Da.

residues 1-5 (GPLGS) in NMR structure calculations originate from the expression vector

Entity 2, Stonin 45 residues - 4998.502 Da.

residues 101-105 in NMR structure calculations originate from the expression vector

Entity 3, CA - Ca - 40.078 Da.

Samples:

sample_1: EH2, [U-99% 13C; U-99% 15N], 0.5-1 mM; Stonin peptide 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_2: EH2 0.5-1 mM; Stonin peptide, [U-99% 13C; U-99% 15N], 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_3: EH2, [U-99% 13C; U-99% 15N], 0.5-1 mM; Stonin peptide 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_4: EH2 0.5-1 mM; Stonin peptide, [U-99% 13C; U-99% 15N], 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_5: EH2 0.6 mM; Stonin peptide 0.6 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 295 K

Experiments:

Software:

NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - collection

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA v1.2, Linge, O, . - structure solution

NMR spectrometers:

• Bruker DRX 500 MHz
• Bruker Avance 800 MHz
• Bruker Avance 900 MHz