BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18689

Title: Backbone 1H, 13C, and 15N backbone resonance assignments of the TPR2A domain of mouse STI1   PubMed: 23070844

Deposition date: 2012-08-30 Original release date: 2014-02-19

Authors: Maciejewski, Andrzej; Choy, Wing-Yiu

Citation: Maciejewski, Andrzej; Prado, Marco; Choy, Wing-Yiu. "(1)H, (15)N and (13)C backbone resonance assignments of the TPR1 and TPR2A domains of mouse STI1."  Biomol. NMR Assignments 7, 305-310 (2013).

Assembly members:
tpr2a, polymer, 137 residues, Formula weight is not available

Natural source:   Common Name: House mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST17

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts132
1H chemical shifts132

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1tpr2a1

Entities:

Entity 1, tpr2a 137 residues - Formula weight is not available

Residue 216 is a non-native glycine result of cleavage of the affinity tag by TEV protease

1   GLYASPLEUPROGLUASNLYSLYSGLNALA
2   LEULYSGLULYSGLULEUGLYASNASPALA
3   TYRLYSLYSLYSASPPHEASPLYSALALEU
4   LYSHISTYRASPARGALALYSGLULEUASP
5   PROTHRASNMETTHRTYRILETHRASNGLN
6   ALAALAVALHISPHEGLULYSGLYASPTYR
7   ASNLYSCYSARGGLULEUCYSGLULYSALA
8   ILEGLUVALGLYARGGLUASNARGGLUASP
9   TYRARGGLNILEALALYSALATYRALAARG
10   ILEGLYASNSERTYRPHELYSGLUGLULYS
11   TYRLYSASPALAILEHISPHETYRASNLYS
12   SERLEUALAGLUHISARGTHRPROASPVAL
13   LEULYSLYSCYSGLNGLNALAGLULYSILE
14   LEULYSGLUGLNGLUARGLEU

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM; DSS 100 uM; tpr2a, [U-13C; U-15N], 0.5 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts