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 6287

Title: Diversity in structure and function of the Ets family pointed domains

Deposition date: 2004-08-10 Original release date: 2004-09-01

Authors: Mackereth, Cameron; Schaerpf, Manuela; Gentile, Lisa; MacIntosh, Scott; Slupsky, Carolin; Gentile, Lisa; McIntosh, Lawrence

Citation: Mackereth, Cameron; Schaerpf, Manuela; Gentile, Lisa; MacIntosh, Scott; Slupsky, Carolin; Gentile, Lisa; McIntosh, Lawrence. "Diversity in structure and function of the Ets family pointed domains"  J. Mol. Biol. ., .-..

Assembly members:
GABPalpha pointed domain, polymer, 91 residues, 10320 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli' 'E. coli

Entity Sequences (FASTA):
GABPalpha pointed domain: GSHMAALEGYRKEQERLGIP YDPIHWSTDQVLHWVVWVMK EFSMTDIDLTTLNISGRELC SLNQEDFFQRVPRGEILWSH LELLRKYVLAS

Data sets:
Data typeCount
1H chemical shifts663
13C chemical shifts414
15N chemical shifts86

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1GABPalpha pointed domain1

Entities:

Entity 1, GABPalpha pointed domain 91 residues - 10320 Da.

1   GLYSERHISMETALAALALEUGLUGLYTYR
2   ARGLYSGLUGLNGLUARGLEUGLYILEPRO
3   TYRASPPROILEHISTRPSERTHRASPGLN
4   VALLEUHISTRPVALVALTRPVALMETLYS
5   GLUPHESERMETTHRASPILEASPLEUTHR
6   THRLEUASNILESERGLYARGGLULEUCYS
7   SERLEUASNGLNGLUASPPHEPHEGLNARG
8   VALPROARGGLYGLUILELEUTRPSERHIS
9   LEUGLULEULEUARGLYSTYRVALLEUALA
10   SER

Samples:

sample_1: GABPalpha pointed domain' '[U-99% 15N] 0.5; .; .

sample_2: GABPalpha pointed domain' '[U-99% 13C; U-99% 15N]; .; .

sample_3: GABPalpha pointed domain' '[U-10% 13C; U-99% 15N]; .; .

generell_exp_condition: pH: 7.2; temperature: 303 K; ionic strength: 0.4 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 v2000 - processing

NMRPipe-Draw - processing

SPARKY v3 - assignment

NMR spectrometers:

  • Varian Inova 600 MHz
  • Varian Unity 500 MHz

Related Database Links:

BMRB 5401
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

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