BMRB Entry 16536
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16536
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Title: Structure of the E1064A mutant of the N-domain of Wilson Disease Associated Protein
Deposition date: 2009-10-03 Original release date: 2012-08-03
Authors: Dmitriev, Oleg
Citation: Dmitriev, Oleg; Lutsenko, Svetlana; Uhelmann, Eva-Maria. "The structure of the E1064A mutant reveals ATP-dependent conformational changes in the ATP7B N-domain." Biochemistry ., .-..
Assembly members:
E1064A mutant, polymer, 141 residues, 14752.269 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):
E1064A mutant: AGHMVPRVMRVLLLGDVATL
PLRKVLAVVGTAAASSEHPL
GVAVTKYCKEELGTETLGYC
TDFQAVPGCGIGCKVSNVEG
ILAAVPQTFSVLIGNREWLR
RNGLTISSDVSDAMTDHEMK
GQTAILVAIDGVLCGMIAIA
D
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 523 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 865 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E1064A mutant | 1 |
Entities:
Entity 1, E1064A mutant 141 residues - 14752.269 Da.
| 1 | ALA | GLY | HIS | MET | VAL | PRO | ARG | VAL | MET | ARG | ||||
| 2 | VAL | LEU | LEU | LEU | GLY | ASP | VAL | ALA | THR | LEU | ||||
| 3 | PRO | LEU | ARG | LYS | VAL | LEU | ALA | VAL | VAL | GLY | ||||
| 4 | THR | ALA | ALA | ALA | SER | SER | GLU | HIS | PRO | LEU | ||||
| 5 | GLY | VAL | ALA | VAL | THR | LYS | TYR | CYS | LYS | GLU | ||||
| 6 | GLU | LEU | GLY | THR | GLU | THR | LEU | GLY | TYR | CYS | ||||
| 7 | THR | ASP | PHE | GLN | ALA | VAL | PRO | GLY | CYS | GLY | ||||
| 8 | ILE | GLY | CYS | LYS | VAL | SER | ASN | VAL | GLU | GLY | ||||
| 9 | ILE | LEU | ALA | ALA | VAL | PRO | GLN | THR | PHE | SER | ||||
| 10 | VAL | LEU | ILE | GLY | ASN | ARG | GLU | TRP | LEU | ARG | ||||
| 11 | ARG | ASN | GLY | LEU | THR | ILE | SER | SER | ASP | VAL | ||||
| 12 | SER | ASP | ALA | MET | THR | ASP | HIS | GLU | MET | LYS | ||||
| 13 | GLY | GLN | THR | ALA | ILE | LEU | VAL | ALA | ILE | ASP | ||||
| 14 | GLY | VAL | LEU | CYS | GLY | MET | ILE | ALA | ILE | ALA | ||||
| 15 | ASP |
Samples:
sample_1: sodium phosphate 50 mM; DTT 5 mM; DSS 0.3 mM; H2O 95%; D2O 5%; protein, [13C; 15N], 0.8 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 300 K
Experiments:
| 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
FELIX v2007, Accelrys Software Inc. - peak picking
TALOS, Cornilescu, Delaglio and Bax - refinement
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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