BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27915

Title: NFkappaB p50DD homodimer   PubMed: 31587407

Authors: Kohl, Bastian; Granitzka, Vanessa; Singh, Amrinder; Quintas, Pedro; Xiromeriti, Elli; Mortel, Fabian; Xiromeriti, Elli; Wright, Peter; Dyson, Jane; Stoll, Raphael

Citation: Kohl, Bastian; Granitzka, Vanessa; Singh, Amrinder; Quintas, Pedro; Xiromeriti, Elli; Mortel, Fabian; Kroon, Gerard; Wright, Peter; 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).

Assembly members:
p50_homodimer, polymer, 121 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
p50_homodimer: VGTGSNDDDDKAPNASNLKI VRMDRTAGCVTGGEEIYLLC DKVQKDDIQIRFYEEEENGG VWEGFGDFSPTDVHRQFAIV FKTPKYKDVNITKPASVFVQ LRRKSDLETSEPKPFLYYPE I

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts110
1H chemical shifts110
T1 relaxation values90
T2 relaxation values90
heteronuclear NOE values86

Additional metadata:

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

Assembly:

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

Entities:

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

residues 233-353 of mouse p50

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 homodimer, [U-13C; U-15N; U-2H], 1.5 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 HN(COCA)CBsample_1isotropicsample_conditions_1
T1, T2, NOEsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

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

CCPNMR v2.7, CCPN - chemical shift assignment

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

TOPSPIN v3.5, Bruker Biospin - data analysis

NMR spectrometers:

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

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