BMRB Entry 7068
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7068
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Title: Solution structure and intermolecular interactions of the Copper form of third metal-binding domain of ATP7A, the menkes disease protein PubMed: 16873374
Deposition date: 2006-04-10 Original release date: 2008-07-07
Authors: Banci, L.; Bertini, I.; Cantini, F.; DellaMalva, N.; Rosato, A.; Herrmann, T.; Wuthrich, K.
Citation: Banci, L.; Bertini, I.; Cantini, F.; DellaMalva, N.; Herrmann, T.; Rosato, A.; Wuthrich, K.. "Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein" J. Biol. Chem. 281, 29141-29147 (2006).
Assembly members:
Copper-transporting ATPase 1, polymer, 90 residues, Formula weight is not available
CU1, non-polymer, 63.546 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Copper-transporting ATPase 1: NDSTATFIIDGMHCKSCVSN
IESTLSALQYVSSIVVSLEN
RSAIVVYNASSVTPESLRKA
IEAVSPGLYRVSITSEVEIE
GRLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 243 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 536 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Copper-transporting ATPase 1 | 1 |
| 2 | COPPER (I) ION | 2 |
Entities:
Entity 1, Copper-transporting ATPase 1 90 residues - Formula weight is not available
| 1 | ASN | ASP | SER | THR | ALA | THR | PHE | ILE | ILE | ASP | |
| 2 | GLY | MET | HIS | CYS | LYS | SER | CYS | VAL | SER | ASN | |
| 3 | ILE | GLU | SER | THR | LEU | SER | ALA | LEU | GLN | TYR | |
| 4 | VAL | SER | SER | ILE | VAL | VAL | SER | LEU | GLU | ASN | |
| 5 | ARG | SER | ALA | ILE | VAL | VAL | TYR | ASN | ALA | SER | |
| 6 | SER | VAL | THR | PRO | GLU | SER | LEU | ARG | LYS | ALA | |
| 7 | ILE | GLU | ALA | VAL | SER | PRO | GLY | LEU | TYR | ARG | |
| 8 | VAL | SER | ILE | THR | SER | GLU | VAL | GLU | ILE | GLU | |
| 9 | GLY | ARG | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Entity 2, COPPER (I) ION - Cu - 63.546 Da.
| 1 | CU1 |
Samples:
sample_1: Copper-transporting ATPase 1 1 mM; phosphate_buffer 100 mM; H2O 90%; D2O 10%
sample_2: Copper-transporting ATPase 1, [U-15N], 0.5 mM; phosphate_buffer 100 mM; H2O 90%; D2O 10%
sample_3: Copper-transporting ATPase 1, [U-15N; U-13C], 0.5 mM; phosphate_buffer 100 mM; H2O 90%; D2O 10%
sample_cond_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | sample_cond_1 |
| 2D TOCSY | not available | not available | sample_cond_1 |
| 3D 15N-separated NOESY | not available | not available | sample_cond_1 |
| CBCACONH | not available | not available | sample_cond_1 |
| CBCANH | not available | not available | sample_cond_1 |
| h(CCH)-TOCSY | not available | not available | sample_cond_1 |
| 3D 13C-separated NOESY | not available | not available | sample_cond_1 |
| 15N-HSQC | not available | not available | sample_cond_1 |
Software:
xwinnmr v1.3 - collection
XEASY v1.3 - data analysis
CARA v1.5 - data analysis
CYANA v2.1 - structure solution
AMBER v8.0 - refinement
NMR spectrometers:
- Bruker AVANCE 800 MHz
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
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