BMRB Entry 19136
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19136
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NMR-STAR v3 text file.
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Citation: Regan, Michael; Horanyi, Peter; Pryor, Edward; Sarver, Jessica; Cafiso, David; Bushweller, John. "Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited." Proc. Natl. Acad. Sci. U.S.A. 110, 13374-13379 (2013).
PubMed: 23898196
Assembly members:
ERGu, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHis-Parallel2
Entity Sequences (FASTA):
ERGu: GAMGPGSGQIQLWQFLLELL
SDSSNSSCITWEGTNGEFKM
TDPDEVARRWGERKSKPNMN
YDKLSRALRYYYDKNIMTKV
HGKRYAYKFDFHGI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 250 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 164 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ERGu | 1 |
Entities:
Entity 1, ERGu 94 residues - Formula weight is not available
| 1 | GLY | ALA | MET | GLY | PRO | GLY | SER | GLY | GLN | ILE | ||||
| 2 | GLN | LEU | TRP | GLN | PHE | LEU | LEU | GLU | LEU | LEU | ||||
| 3 | SER | ASP | SER | SER | ASN | SER | SER | CYS | ILE | THR | ||||
| 4 | TRP | GLU | GLY | THR | ASN | GLY | GLU | PHE | LYS | MET | ||||
| 5 | THR | ASP | PRO | ASP | GLU | VAL | ALA | ARG | ARG | TRP | ||||
| 6 | GLY | GLU | ARG | LYS | SER | LYS | PRO | ASN | MET | ASN | ||||
| 7 | TYR | ASP | LYS | LEU | SER | ARG | ALA | LEU | ARG | TYR | ||||
| 8 | TYR | TYR | ASP | LYS | ASN | ILE | MET | THR | LYS | VAL | ||||
| 9 | HIS | GLY | LYS | ARG | TYR | ALA | TYR | LYS | PHE | ASP | ||||
| 10 | PHE | HIS | GLY | ILE |
Samples:
sample_1: ERGu, [U-98% 13C; U-98% 15N], 0.5 mM; H2O 95%; D2O 5%; MgSO4 0.2 M; KPI 0.02 M; DTT 0.005 M; NaN3 0.1%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 19137 19138 |
| PDB | |
| DBJ | BAB62744 BAB69948 BAB69949 BAB69950 BAC29518 |
| EMBL | CAA42055 CAA47389 CAA47399 CAA54404 CAA75077 |
| GB | AAA35811 AAA35812 AAA52398 AAB28525 AAB31417 |
| REF | NP_001008616 NP_001017381 NP_001026079 NP_001039763 NP_001079309 |
| SP | P11308 P26323 P41157 P81270 Q01543 |
| TPG | DAA13871 DAA32951 |
| AlphaFold | P11308 P26323 P41157 P81270 Q01543 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks