BMRB Entry 6099

Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the activation domain of the transcriptional activator VP16
Deposition date:
2004-02-13
Original release date:
2004-09-28
Authors:
Jonker, Henry; Folkers, Gert; Wechselberger, Rainer; Boelens, Rolf; Kaptein, Rob
Citation:

Citation: Jonker, Henry. "Structural and functional studies on transcriptional activation - Interactions of the cofactor PC4 and activator VP16"  Thesis Utrecht University (2003).

Assembly members:

Assembly members:
herpes simplex virion protein 16, polymer, 80 residues, 8394 Da.

Natural source:

Natural source:   Common Name: Herpes Simplex Virus   Taxonomy ID: 10298   Superkingdom: Viruses   Kingdom: not available   Genus/species: Herpes simplex

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

Experimental source:

Natural source:   Common Name: Herpes Simplex Virus   Taxonomy ID: 10298   Superkingdom: Viruses   Kingdom: not available   Genus/species: Herpes simplex

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
herpes simplex virion protein 16: STAPPTDVSLGDELHLDGED VAMAHADALDDFDLDMLGDG DSPGPGFTPHDSAPYGALDT ADFEFEQMFTDALGIDEYGG

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts73
1H chemical shifts294

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VP16 activation domain1

Entities:

Entity 1, VP16 activation domain 80 residues - 8394 Da.

1   SERTHRALAPROPROTHRASPVALSERLEU
2   GLYASPGLULEUHISLEUASPGLYGLUASP
3   VALALAMETALAHISALAASPALALEUASP
4   ASPPHEASPLEUASPMETLEUGLYASPGLY
5   ASPSERPROGLYPROGLYPHETHRPROHIS
6   ASPSERALAPROTYRGLYALALEUASPTHR
7   ALAASPPHEGLUPHEGLUGLNMETPHETHR
8   ASPALALEUGLYILEASPGLUTYRGLYGLY

Samples:

sample_VP16_298K_LS: herpes simplex virion protein 16, [U-13C; U-15N], 0.5 – 1 mM; KCl 50 mM; KHxPO4 50 mM; D5-Glycin 2 M; Protease Inhibitor cocktail mM

condition_VP16_298K_LS: pH: 5.6; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
Spectrometer was locked on deuterated glycine.sample_VP16_298K_LSnot availablecondition_VP16_298K_LS
Triple resonance probes.sample_VP16_298K_LSnot availablecondition_VP16_298K_LS

Software:

NMRPipe - processing

SPARKY v3 - analyses, assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Varian Inova 500 MHz
  • Varian Inova 750 MHz

Related Database Links:

DBJ BAL03259 BAM21067 BAM21069 BAM21071 BAM21075
EMBL CAA26913 CAA32298 CAI26306 CAQ68373
GB AAA45766 AAB72093 AAF89185 AAG02187 AAG36984
REF NP_044650
SP P04486 P06492

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