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 5401

Title: Conservation of chemical shift and secondary structure of the PNT/SAM domains from the Ets family of transcription factors   PubMed: 12449421

Deposition date: 2002-06-17 Original release date: 2004-08-19

Authors: Mackereth, Cameron; Schaerpf, Manuela; Gentile, Lisa; McIntosh, Lawrence

Citation: Mackereth, Cameron; Scharpf, Manuela; Gentile, Lisa; McIntosh, Lawrence. "Chemical Shift and Secondary Structure Conservation of the PNT/SAM Domains from the ets Family of Transcription Factors"  J. Biomol. NMR 24, 71-72 (2002).

Assembly members:
GABPalpha Pointed Domain, polymer, 87 residues, 10339 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):
GABPalpha Pointed Domain: AALEGYRKEQERLGIPYDPI HWSTDQVLHWVVWVMKEFSM TDIDLTTLNISGRELCSLNQ EDFFQRVPRGEILWSHLELL RKYVLAS

Data sets:
Data typeCount
1H chemical shifts635
13C chemical shifts412
15N chemical shifts99

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GABPalpha Pointed domain1

Entities:

Entity 1, GABPalpha Pointed domain 87 residues - 10339 Da.

1   ALAALALEUGLUGLYTYRARGLYSGLUGLN
2   GLUARGLEUGLYILEPROTYRASPPROILE
3   HISTRPSERTHRASPGLNVALLEUHISTRP
4   VALVALTRPVALMETLYSGLUPHESERMET
5   THRASPILEASPLEUTHRTHRLEUASNILE
6   SERGLYARGGLULEUCYSSERLEUASNGLN
7   GLUASPPHEPHEGLNARGVALPROARGGLY
8   GLUILELEUTRPSERHISLEUGLULEULEU
9   ARGLYSTYRVALLEUALASER

Samples:

15N_GABPa_PNT: GABPalpha Pointed Domain, [U-99% 15N], 0.5 – 2.5 mM

13C-15N_GABPalpha_PNT: GABPalpha Pointed Domain, [U-99% 13C; U-99% 15N], 1.5 mM

10_13C-15N_GABPalpha_PNT: GABPalpha Pointed Domain, [N-10% 13C; U-99% 15N], 1.5 mM

sample_conditions: pH: 7.2; temperature: 303 K; ionic strength: 0.02 M

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
1H-13C HSQCnot availablenot availablenot available
HNCACBnot availablenot availablenot available
HBCBCACONHnot availablenot availablenot available
HNCOnot availablenot availablenot available
H(CCO)NH-TOCSYnot availablenot availablenot available
C(CO)NH-TOCSYnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available

Software:

FELIX v95.0 - processing spectra, assignment

NMR spectrometers:

  • Varian UNITY 500 MHz

Related Database Links:

BMRB 6287
PDB
DBJ BAA02575 BAD96884 BAE24181 BAE26442 BAE26687
GB AAA53030 AAA65706 AAH13562 AAH35031 AAH52448
REF NP_001068905 NP_001102311 NP_001184226 NP_001253514 NP_002031
SP Q00422 Q06546
TPG DAA33658
AlphaFold Q00422 Q06546

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