BMRB Entry 17005

Assembly:

Entities:

Entity 1, trPRAI 134 residues - 14308.270 Da.

Residue 132-134 are cloning artifacts from the plasmid display selection and not part of the original sequence of PRAI from E.coli

Samples:

sample_1: trPRAI 0.8 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%

sample_2: trPRAI, [U-99% 15N], .6 – 1 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%

sample_3: trPRAI, [U-98% 13C; U-98% 15N], .6 – .8 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%

sample_4: trPRAI, [U-98% 13C; U-98% 15N], 0.7 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - automated NOE peak assignments, NOE peaks calibration

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

TALOS vTALOS+, Cornilescu, Delaglio and Bax - prediction of protein backbone torsion angles from NMR chemical shifts

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution, water refinement

ProcheckNMR v3.5.3, Laskowski and MacArthur - data analysis

NMR spectrometers:

• Bruker Avance 800 MHz
• Bruker Avance 600 MHz