Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50867
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Citation: Appling, Francis; Berlow, Rebecca; Stanfield, Robyn; Dyson, H Jane; Wright, Peter. "The molecular basis of allostery in a facilitated dissociation process" Structure 29, 1327-1338 (2021).
PubMed: 34520739
Assembly members:
entity_1, polymer, 100 residues, Formula weight is not available
entity_2, polymer, 67 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
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 Vector: pET21d
Entity Sequences (FASTA):
entity_1: ATGPTADPEKRKLIQQQLVL
LLHAHKCQRREQANGEVRAC
SLPHCRTMKNVLNHMTHCQA
GKACQVAHCASSRQIISHWK
NCTRHDCPVCLPLKNASDKR
entity_2: GSHMSNVIDTDFIDEEVLMS
LVIEMGLDRIKELPELTSYD
CEVNAPIQGSRNLLQGEELL
RAADQVN
Data type | Count |
13C chemical shifts | 412 |
15N chemical shifts | 140 |
1H chemical shifts | 205 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | TAZ1 | 1 |
2 | CITED2-HIF1alpha fusion peptide (L63A) | 2 |
3 | zinc1 | 3 |
4 | zinc2 | 3 |
5 | zinc3 | 3 |
Entity 1, TAZ1 100 residues - Formula weight is not available
1 | ALA | THR | GLY | PRO | THR | ALA | ASP | PRO | GLU | LYS | |
2 | ARG | LYS | LEU | ILE | GLN | GLN | GLN | LEU | VAL | LEU | |
3 | LEU | LEU | HIS | ALA | HIS | LYS | CYS | GLN | ARG | ARG | |
4 | GLU | GLN | ALA | ASN | GLY | GLU | VAL | ARG | ALA | CYS | |
5 | SER | LEU | PRO | HIS | CYS | ARG | THR | MET | LYS | ASN | |
6 | VAL | LEU | ASN | HIS | MET | THR | HIS | CYS | GLN | ALA | |
7 | GLY | LYS | ALA | CYS | GLN | VAL | ALA | HIS | CYS | ALA | |
8 | SER | SER | ARG | GLN | ILE | ILE | SER | HIS | TRP | LYS | |
9 | ASN | CYS | THR | ARG | HIS | ASP | CYS | PRO | VAL | CYS | |
10 | LEU | PRO | LEU | LYS | ASN | ALA | SER | ASP | LYS | ARG |
Entity 2, CITED2-HIF1alpha fusion peptide (L63A) 67 residues - Formula weight is not available
1 | GLY | SER | HIS | MET | SER | ASN | VAL | ILE | ASP | THR | ||||
2 | ASP | PHE | ILE | ASP | GLU | GLU | VAL | LEU | MET | SER | ||||
3 | LEU | VAL | ILE | GLU | MET | GLY | LEU | ASP | ARG | ILE | ||||
4 | LYS | GLU | LEU | PRO | GLU | LEU | THR | SER | TYR | ASP | ||||
5 | CYS | GLU | VAL | ASN | ALA | PRO | ILE | GLN | GLY | SER | ||||
6 | ARG | ASN | LEU | LEU | GLN | GLY | GLU | GLU | LEU | LEU | ||||
7 | ARG | ALA | ALA | ASP | GLN | VAL | ASN |
Entity 3, zinc1 - Zn - 65.409 Da.
1 | ZN |
sample_1: CBP TAZ1 domain, [U-100% 13C; U-100% 15N], 300 uM; CITED2-HIF-1alpha fusion peptide (L63A) 360 uM; NaCl 50 mM; DTT 2 mM; TRIS 20 mM
sample_2: CBP TAZ1 domain 570 uM; CITED2-HIF-1alpha fusion peptide (L63A), [U-100% 13C; U-100% 15N], 300 uM; NaCl 50 mM; DTT 2 mM; TRIS 20 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
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