BMRB Entry 6098

Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the amino terminal domain of the transcriptional cofactor PC4
Deposition date:
2004-02-13
Original release date:
2004-06-25
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:
positive cofactor 4, polymer, 126 residues, 14264 Da.

Natural source:

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

Experimental source:

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

Data typeCount
13C chemical shifts492
1H chemical shifts217
15N chemical shifts159

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PC4ntd, 11
2PC4ctd, 21

Entities:

Entity 1, PC4ntd, 1 126 residues - 14264 Da.

1   PROLYSSERLYSGLULEUVALSERSERSER
2   SERSERGLYSERASPSERASPSERGLUVAL
3   ASPLYSLYSLEULYSARGLYSLYSGLNVAL
4   ALAPROGLULYSPROVALLYSLYSGLNLYS
5   THRGLYGLUTHRSERARGALALEUSERSER
6   SERLYSGLNSERSERSERSERARGASPASP
7   ASNMETPHEGLNILEGLYLYSMETARGTYR
8   VALSERVALARGASPPHELYSGLYLYSVAL
9   LEUILEASPILEARGGLUTYRTRPMETASP
10   PROGLUGLYGLUMETLYSPROGLYARGLYS
11   GLYILESERLEUASNPROGLUGLNTRPSER
12   GLNLEULYSGLUGLNILESERASPILEASP
13   ASPALAVALARGLYSLEU

Samples:

sample_PC4_298K_LS: positive cofactor 4, [U-13C; U-15N], 0.5 – 1 mM; KCl 50 mM; KHxPO4 50 mM; D5-Glycin 2 M; Protease Inhibitor cocktail mM

sample_PC4_305K_HS: positive cofactor 4, [U-13C; U-15N], 0.5 – 1 mM; KCl 400 mM; KHxPO4 50 mM; D5-Glycin 2 M; Protease Inhibitor cocktail mM

sample_PC4_P: positive cofactor 4, [U-13C; U-15N], 0.5 – 1 mM; KCl 400 mM; KHxPO4 50 mM; D5-Glycin 2 M; Protease Inhibitor cocktail mM

condition_PC4_298K_LS: pH: 5.6; temperature: 298 K

condition_PC4_305K_HS: pH: 5.6; temperature: 305 K

condition_PC4_P: pH: 5.6; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D (1H,15N)-HSQCnot availablenot availablenot available
3D NOESY (1H,15N) HSQCnot availablenot availablenot available
3D TOCSY (1H,15N) HSQCnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HN(CA)COnot availablenot availablenot available

Software:

NMRPipe - processing

SPARKY v3 - analyses, assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

Related Database Links:

PDB
DBJ BAD92522 BAE00374 BAE87869 BAE91489 BAG10763
EMBL CAA56200 CAG33183 CAH92686
GB AAA20980 AAH09610 AAH10537 AAH18189 AAH22339
REF NP_001098877 NP_001126574 NP_001248140 NP_001272042 NP_006704
SP P53999 Q4R947 Q5R6D0
TPG DAA17835
AlphaFold Q5R6D0

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