BMRB Entry 18869

Assembly:

Entities:

Entity 1, HR8910C_1 69 residues - 7644.846 Da.

Protein is a dimer, residues 58-60 are part of N-terminal tag.

Samples:

sample_4: HR8910C.005, [U-5% 13C; U-100% 15N], 5.0 mg/mL; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%

sample_1: HR8910C.003, [U-100% 13C; U-100% 15N], 5.0 mg/mL; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%

sample_2: HR8910C, [U-100% 13C; U-100% 15N], 5.0 mg/mL; HR8910C 15.0 mg/mL; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%; Proteinase Inhibitors 1 x

sample_3: HR8910C, [U-100% 15N], 0.3 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 5%; Proteinase Inhibitors 1 x; PEG 4.2%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

CYANA v3.02, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

NMRPipe v2.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.112, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

NMR spectrometers:

• Bruker Avance 800 MHz