BMRB Entry 18301
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18301
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Title: Metal binding repeat 2 of the Wilson disease protein (ATP7B) PubMed: 23751120
Deposition date: 2012-02-28 Original release date: 2013-07-01
Authors: Nokhrin, Sergiy; Dolgova, Nataliya; Yu, Corey; Dmitriev, Oleg
Citation: Dolgova, Nataliya; Nokhrin, Sergiy; Yu, Corey; George, Graham; Dmitriev, Oleg. "Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification." Biochem. J. 454, 147-156 (2013).
Assembly members:
MBD2, polymer, 76 residues, 8427.775 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):
MBD2: AGHMQEAVVKLRVEGMTCQS
CVSSIEGKVRKLQGVVRVKV
SLSNQEAVITYQPYLIQPED
LRDHVNDMGFEAAIKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 413 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MBD2 | 1 |
Entities:
Entity 1, MBD2 76 residues - 8427.775 Da.
| 1 | ALA | GLY | HIS | MET | GLN | GLU | ALA | VAL | VAL | LYS | ||||
| 2 | LEU | ARG | VAL | GLU | GLY | MET | THR | CYS | GLN | SER | ||||
| 3 | CYS | VAL | SER | SER | ILE | GLU | GLY | LYS | VAL | ARG | ||||
| 4 | LYS | LEU | GLN | GLY | VAL | VAL | ARG | VAL | LYS | VAL | ||||
| 5 | SER | LEU | SER | ASN | GLN | GLU | ALA | VAL | ILE | THR | ||||
| 6 | TYR | GLN | PRO | TYR | LEU | ILE | GLN | PRO | GLU | ASP | ||||
| 7 | LEU | ARG | ASP | HIS | VAL | ASN | ASP | MET | GLY | PHE | ||||
| 8 | GLU | ALA | ALA | ILE | LYS | SER |
Samples:
sample_1: Tris-Cl, [U-2H], 50 mM; DSS 0.5 mM; sodium azide 0.05 mM; D2O, [U-2H], 5%; TCEP (tris(2-carboxyethyl)phosphine) 5 mM; H2O, [U-2H], 95%; MBD2, [U-2H], 0.9 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | not available |
| 3D HNCO | sample_1 | isotropic | not available |
| 3D HNCA | sample_1 | isotropic | not available |
| 3D HNCACB | sample_1 | isotropic | not available |
| 3D HN(CO)CACB | sample_1 | isotropic | not available |
| 3D C(CO)NH | sample_1 | isotropic | not available |
| 3D H(CCO)NH | sample_1 | isotropic | not available |
| 3D 1H-15N TOCSY | sample_1 | isotropic | not available |
| 3D 1H-15N NOESY | sample_1 | isotropic | not available |
| 3D 1H-13C NOESY | sample_1 | isotropic | not available |
| 3D HN(CA)CO | sample_1 | isotropic | not available |
Software:
CYANA_3.0, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CARA v1.9.0, F. Damberger, R. Keller - chemical shift assignment
FELIX, Accelrys Software Inc. - peak picking, processing
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
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