BMRB Entry 7069
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7069
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure and intermolecular interactions of the apo 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 (E.C.3.6.3.4), polymer, 90 residues, Formula weight is not available
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 (E.C.3.6.3.4): NDSTATFIIDGMHCKSCVSN
IESTLSALQYVSSIVVSLEN
RSAIVVYNASSVTPESLRKA
IEAVSPGLYRVSITSEVEIE
GRLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 248 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 546 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Copper-transporting ATPase 1 | 1 |
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 |
Samples:
sample_1: Copper-transporting ATPase 1 (E.C.3.6.3.4) 1 mM; phosphate_buffer 100 mM; H2O 90%; D2O 10%
sample_2: Copper-transporting ATPase 1 (E.C.3.6.3.4), [U-15N], 1 mM; phosphate_buffer 100 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_3: Copper-transporting ATPase 1 (E.C.3.6.3.4), [U-15N; U-13C], 1 mM; phosphate_buffer 100 mM; DTT 1 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 | not available |
| 2D TOCSY | not available | not available | not available |
| 3D 15N-separated NOESY | not available | not available | not available |
| (H)CCH-TOCSY | not available | not available | not available |
| CBCA(CO)NH | not available | not available | not available |
| CBCANH | not available | not available | not available |
| 3D 13C-separated NOESY | not available | not available | not available |
Software:
xwinnmr - collection
XEASY v1.3 - data analysis
CARA - data analysis
ATHNOS-CANDID v1.0 - structure solution
AMBER v8.0 - refinement
NMR spectrometers:
- Bruker AVANCE 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts