U2SNRNPCOMPONENTIST3 / INCREASED SODIUM TOLERANCE PROTEIN 3 / U2 SNRNP PROTEIN SNU17 / SNU17P
Mass: 10538.707 Da / Num. of mol.: 1 / Fragment: RRM, RESIDUES 25-113 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): PLYSS 24D / References: UniProt: P40565
#2: Protein/peptide
PRE-MRNA-SPLICINGFACTORCWC26 / BUD SITE SELECTION PROTEIN 13 / COMPLEXED WITH CEF1 PROTEIN 26 / SYNTHETIC LETHAL WITH CLF1 PROTEIN 7 / BUD13P
Mass: 4532.087 Da / Num. of mol.: 1 / Fragment: TRP-CONTAINING LIGAND, RESIDUES 222-256 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): PLYSS 24D / References: UniProt: P46947
Sequence details
FIRST FOUR RESIDUES OF THE PROTEIN SEQUENCE (GAMG) ARE COMING FROM THE TAG.
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
15N-EDITED 3D NOESY
1
2
1
13C- EDITED 3D NOESY (ALIPHATICS)
1
3
1
13C-EDITED 3D NOESY (AROMATICS)
1
4
1
13C- EDITED 3D NOESY (ALIPHATICSS) F1 15N/13C FILTERED
NMR details
Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON STOICHIOMETRIC COMPLEX SAMPLES WHERE ONLY SNU17P OR BUD13P WAS 13C, 15N-LABELED
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Sample preparation
Details
Contents: 93% WATER/7% D2O
Sample conditions
Ionic strength: 25 mM / pH: 6.3 / Pressure: 1.0 atm / Temperature: 298.0 K
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NMR measurement
NMR spectrometer
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz
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