BMRB Entry 17729

Assembly:

Entities:

Entity 1, CT-Ler 57 residues - 6703.430 Da.

Entity 2, LeeH_A 15 residues - 6703.430 Da.

Entity 3, LeeH_B 15 residues - 6703.430 Da.

Samples:

sample_1: CT-Ler, [U-100% 13C; U-100% 15N], 1 mM; LeeH_A 2 mM; LeeH_B 2 mM; sodium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01 %(w/v); EDTA 0.2 mM; H2O 90%; D2O 10%

sample_2: CT-Ler, [U-100% 13C; U-100% 15N], 1 mM; LeeH_A 2 mM; LeeH_B 2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.01 %(w/v); EDTA 0.2 mM; D2O 100%

sample_3: CT-Ler, [U-10% 13C; U-100% 15N], 1 mM; LeeH_A 2 mM; LeeH_B 2 mM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.01 % (w/v); EDTA 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

Software:

NMRPipe, Delaglio, Zhengrong and Bax - Processing

TOPSPIN, Bruker Biospin - NMR spectra acquisition

CYANA, Guntert, Mumenthaler and Wuthrich - Structure Calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - Energy water refinement

CARA, Keller and Wuthrich - Chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - Prediction of Protein Phi and Psi Angles Using a Chemical Shift Database

CRYSOL, Svergun D.I., Barberato C. and Koch M.H.J. - Fitting to experimental scattering curves

HADDOCK, Alexandre Bonvin - Data-driven docking using CNS as structure calculation engine

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - molecular dynamics refinement

Procheck, Laskowski and MacArthur - Quality assessment

NMR spectrometers:

• Bruker Avance 600 MHz
• Bruker Avance 700 MHz
• Bruker Avance 800 MHz
• Bruker Avance 900 MHz