BMRB Entry 27916

Title:
p50 heterodimer
Deposition date:
2019-05-16
Original release date:
2019-11-08
Authors:
Kohl, Bastian; Granitzka, Vanessa; Singh, Amrinder; Quintas, Pedro; Xiromeriti, Elli; Mortel, Fabian; Wright, Peter; Kroon, Gerard; Dyson, Jane; Stoll, Raphael
Citation:

Citation: Kohl, Bastian; Granitzka, Vanessa; Singh, Amrinder; Quintas, Pedro; Xiromeriti, Elli; Mortel, Fabian; Wright, Peter; Kroon, Gerard; Dyson, Jane; Stoll, Raphael. "Comparison of backbone dynamics of the p50 dimerization domain of NFkB in the homodimeric transcription factor NFkB1 and in its heterodimeric complex with RelA (p65)"  Protein Sci. 28, 2064-2072 (2019).
PubMed: 31587407

Assembly members:

Assembly members:
p50_heterodimer, polymer, 121 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-45b(+)

Data sets:
Data typeCount
13C chemical shifts212
15N chemical shifts108
1H chemical shifts108
T1 relaxation values87
T2 relaxation values87
heteronuclear NOE values87

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p50 heterodimer, 11
2p50 heterodimer, 21

Entities:

Entity 1, p50 heterodimer, 1 121 residues - Formula weight is not available

p50 dimerization domain in complex with p65 DD

1   VALGLYTHRGLYSERASNASPASPASPASP
2   LYSALAPROASNALASERASNLEULYSILE
3   VALARGMETASPARGTHRALAGLYCYSVAL
4   THRGLYGLYGLUGLUILETYRLEULEUCYS
5   ASPLYSVALGLNLYSASPASPILEGLNILE
6   ARGPHETYRGLUGLUGLUGLUASNGLYGLY
7   VALTRPGLUGLYPHEGLYASPPHESERPRO
8   THRASPVALHISARGGLNPHEALAILEVAL
9   PHELYSTHRPROLYSTYRLYSASPVALASN
10   ILETHRLYSPROALASERVALPHEVALGLN
11   LEUARGARGLYSSERASPLEUGLUTHRSER
12   GLUPROLYSPROPHELEUTYRTYRPROGLU
13   ILE

Samples:

sample_1: p50 DD, [U-13C; U-15N; U-2H], 1.25 mM; p65 DD 1.25 mM; HEPES 50 mM; DTT 150 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CCPNMR v2.7, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView vJ, Johnson, One Moon Scientific - chemical shift assignment

TOPSPIN, Bruker Biospin - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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