BMRB Entry 18735
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18735
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Title: Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2, Northeast Structural Genomics Consortium (NESG) Target HR3520O
Deposition date: 2012-09-22 Original release date: 2012-11-21
Authors: Eletsky, Alexander; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2, Northeast Structural Genomics Consortium (NESG) Target HR3520O" To be published ., .-..
Assembly members:
HR3520O, polymer, 90 residues, 10667.535 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HR3520O: MGHHHHHHSHMKHSSRLEAH
LTRDELRAKALHIPFPVEKI
INLPVVDFNEMMSKEQFNEA
QLALIRDIRRRGKNKVAAQN
CRKRKLENIV
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 358 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 589 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR3520O | 1 |
Entities:
Entity 1, HR3520O 90 residues - 10667.535 Da.
Residues 12-90 correspond to residues 445-523 of the native protein. Residues 1-11 represent a non-native affinity tag
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | |
| 2 | MET | LYS | HIS | SER | SER | ARG | LEU | GLU | ALA | HIS | |
| 3 | LEU | THR | ARG | ASP | GLU | LEU | ARG | ALA | LYS | ALA | |
| 4 | LEU | HIS | ILE | PRO | PHE | PRO | VAL | GLU | LYS | ILE | |
| 5 | ILE | ASN | LEU | PRO | VAL | VAL | ASP | PHE | ASN | GLU | |
| 6 | MET | MET | SER | LYS | GLU | GLN | PHE | ASN | GLU | ALA | |
| 7 | GLN | LEU | ALA | LEU | ILE | ARG | ASP | ILE | ARG | ARG | |
| 8 | ARG | GLY | LYS | ASN | LYS | VAL | ALA | ALA | GLN | ASN | |
| 9 | CYS | ARG | LYS | ARG | LYS | LEU | GLU | ASN | ILE | VAL |
Samples:
NC: HR3520O, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; sodium azide 0.02%; Arginine 50 mM; DTT 10 mM; ammonium acetate 50 mM
NC5: HR3520O, [5% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; sodium azide 0.02%; Arginine 50 mM; DTT 10 mM; ammonium acetate 50 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC methyl | NC5 | isotropic | sample_conditions_1 |
| 1D 15N T1 | NC | isotropic | sample_conditions_1 |
| 1D 15N T2 | NC | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
AS-DP v1.0, Huang, Tejero, Powers and Montelione - refinement
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
VNMRJ v2.2D, Varian - collection
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS v1.4, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts