BMRB Entry 16065

Assembly:

Entities:

Entity 1, subunit A 98 residues - 11336.2 Da.

Residues 1-3 represent a non-native cloning artifact from the affinity tag.

Entity 2, subunit B 36 residues - 4128.7 Da.

Residues 1-3 represent a cloning artifact from the affinity tag.

Samples:

sample_1: RelE, [U-13C; U-15N], 0.5 ± 0.2 mM; RelBc 0.5 ± 0.2 mM; sodium phosphate 25 ± 0 mM; sodium chloride 500 ± 0 mM; DTT 1 ± 0 mM; sodium azide 0.5 ± 0 mM

sample_2: RelE 0.5 ± 0.1 mM; RelBc, [U-13C; U-15N], 0.5 ± 0.1 mM; sodium phosphate 25 ± 2.5 mM; sodium chloride 500 ± 50 mM; DTT 1 ± 0.1 mM; sodium azide 0.5 ± 0.1 mM

sample_3: RelE, [U-13C; U-15N], 0.5 ± 0.1 mM; RelBc 0.5 ± 0.1 mM; sodium phosphate 25 ± 2.5 mM; sodium chloride 500 ± 50 mM; DTT 1 ± 0.1 mM; sodium azide 0.5 ± 0.1 mM

sample_4: RelE 0.5 ± 0.1 mM; RelBc, [U-13C; U-15N], 0.5 ± 0.1 mM; sodium phosphate 25 ± 2.5 mM; sodium chloride 500 ± 50 mM; DTT 1 ± 0.1 mM; sodium azide 0.5 ± 0.1 mM

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 296.5 K

Experiments:

Software:

TOPSPIN v2.0, Bruker Biospin - collection

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - automated NOE peak assignments, structure calculation

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

Molmol, Koradi, Billeter and Wuthrich - Structure analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

VNMR, Varian - collection

NMR spectrometers:

• Bruker Avance 800 MHz
• Bruker Avance 600 MHz
• Varian INOVA 500 MHz