BMRB Entry 27915
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27915
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Title: NFkappaB p50DD homodimer PubMed: 31587407
Deposition date: 2019-05-16 Original release date: 2019-11-08
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
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 221 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 110 |
| T1 relaxation values | 90 |
| T2 relaxation values | 90 |
| heteronuclear NOE values | 86 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p50 DD, 1 | 1 |
| 2 | p50 DD, 2 | 1 |
Entities:
Entity 1, p50 DD, 1 121 residues - Formula weight is not available
residues 233-353 of mouse p50
| 1 | VAL | GLY | THR | GLY | SER | ASN | ASP | ASP | ASP | ASP | ||||
| 2 | LYS | ALA | PRO | ASN | ALA | SER | ASN | LEU | LYS | ILE | ||||
| 3 | VAL | ARG | MET | ASP | ARG | THR | ALA | GLY | CYS | VAL | ||||
| 4 | THR | GLY | GLY | GLU | GLU | ILE | TYR | LEU | LEU | CYS | ||||
| 5 | ASP | LYS | VAL | GLN | LYS | ASP | ASP | ILE | GLN | ILE | ||||
| 6 | ARG | PHE | TYR | GLU | GLU | GLU | GLU | ASN | GLY | GLY | ||||
| 7 | VAL | TRP | GLU | GLY | PHE | GLY | ASP | PHE | SER | PRO | ||||
| 8 | THR | ASP | VAL | HIS | ARG | GLN | PHE | ALA | ILE | VAL | ||||
| 9 | PHE | LYS | THR | PRO | LYS | TYR | LYS | ASP | VAL | ASN | ||||
| 10 | ILE | THR | LYS | PRO | ALA | SER | VAL | PHE | VAL | GLN | ||||
| 11 | LEU | ARG | ARG | LYS | SER | ASP | LEU | GLU | THR | SER | ||||
| 12 | GLU | PRO | LYS | PRO | PHE | LEU | TYR | TYR | PRO | GLU | ||||
| 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| T1, T2, NOE | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts