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 5399

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

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

Citation: Mackereth, Cameron; Scharpf, Manuela; Gentile, Lisa; McIntosh, Lawrence. "Letters to the Editor: New NMR assignments 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:
Erg Pointed Domain, polymer, 97 residues, 11381 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Erg Pointed Domain: GSHMEEKHMPPPNMTTNERR VIVPADPTLWSTDHVRQWLE WAVKEYGLPDVNILLFQNID GKELCKMTKDDFQRLTPSYN ADILLSHLHYLRETPLP

Data sets:
Data typeCount
1H chemical shifts671
13C chemical shifts432
15N chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Erg Pointed domain1

Entities:

Entity 1, Erg Pointed domain 97 residues - 11381 Da.

1   GLYSERHISMETGLUGLULYSHISMETPRO
2   PROPROASNMETTHRTHRASNGLUARGARG
3   VALILEVALPROALAASPPROTHRLEUTRP
4   SERTHRASPHISVALARGGLNTRPLEUGLU
5   TRPALAVALLYSGLUTYRGLYLEUPROASP
6   VALASNILELEULEUPHEGLNASNILEASP
7   GLYLYSGLULEUCYSLYSMETTHRLYSASP
8   ASPPHEGLNARGLEUTHRPROSERTYRASN
9   ALAASPILELEULEUSERHISLEUHISTYR
10   LEUARGGLUTHRPROLEUPRO

Samples:

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

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

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

sample_conditions: pH: 7.0; temperature: 303 K; ionic strength: 0.05 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
HACANnot availablenot availablenot available
H(CCO)NH-TOCSYnot availablenot availablenot available
C(CO)NH-TOCSYnot availablenot availablenot available
HHCH-TOCSYnot availablenot availablenot available

Software:

FELIX v2000 - processing spectra

Sparky v3 - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian Unity 500 MHz

Related Database Links:

PDB
DBJ BAG60145 BAG62127 BAG62837 BAG64546 BAH24130
EMBL CAA54404 CAL37450
GB AAA35811 AAA52398 AAH40168 AAI48055 AAP41719
REF NP_001095653 NP_001129626 NP_001129627 NP_001230357 NP_001230358
SP P11308 Q90837
TPG DAA32951