BMRB Entry 6022
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6022
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Title: Second Metal Binding Domain of the Menkes ATPase PubMed: 14572476
Deposition date: 2003-11-27 Original release date: 2004-02-13
Authors: Jones, C.; Daly, N.; Cobine, P.; Craik, D.; Dameron, C.
Citation: Jones, C.; Daly, N.; Cobine, P.; Craik, D.; Dameron, C.. "Structure and Metal Binding Studies of the Second Copper Binding Domain of the Menkes ATPase" J. Struct. Biol. 143, 209-218 (2003).
Assembly members:
Menkes ATPase subdomain2, polymer, 84 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):
Menkes ATPase subdomain2: GSMAQAGEVVLKMKVEGMTC
HSCTSTIEGKIGKLQGVQRI
KVSLDNQEATIVYQPHLISV
EEMKKQIEAMGFPAFVKKQP
KYLK
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 67 |
1H chemical shifts | 515 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Menkes ATPase subdomian2 | 1 |
Entities:
Entity 1, Menkes ATPase subdomian2 84 residues - Formula weight is not available
1 | GLY | SER | MET | ALA | GLN | ALA | GLY | GLU | VAL | VAL | ||||
2 | LEU | LYS | MET | LYS | VAL | GLU | GLY | MET | THR | CYS | ||||
3 | HIS | SER | CYS | THR | SER | THR | ILE | GLU | GLY | LYS | ||||
4 | ILE | GLY | LYS | LEU | GLN | GLY | VAL | GLN | ARG | ILE | ||||
5 | LYS | VAL | SER | LEU | ASP | ASN | GLN | GLU | ALA | THR | ||||
6 | ILE | VAL | TYR | GLN | PRO | HIS | LEU | ILE | SER | VAL | ||||
7 | GLU | GLU | MET | LYS | LYS | GLN | ILE | GLU | ALA | MET | ||||
8 | GLY | PHE | PRO | ALA | PHE | VAL | LYS | LYS | GLN | PRO | ||||
9 | LYS | TYR | LEU | LYS |
Samples:
sample_1: Menkes ATPase subdomain2, [U-15N], 0.5 mM; potassium phosphate 20 mM; sodium chloride 10 mM; H2O 90%; D2O 10%
sample_2: Menkes ATPase subdomain2, [U-90% 15N], 0.5 mM; potassium phosphate 20 mM; sodium chloride 10 mM; H2O 90%; D2O 10%
sample_cond_1: ionic strength: 30 mM; pH: 6.5; 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 |
DQF-COSY | not available | not available | not available |
3D 15N-seperated TOCSY | not available | not available | not available |
Software:
X-PLOR v3.851 - refinement
DYANA v1.5 - structure solution
XEASY v3.2 - data analysis
NMR spectrometers:
- Bruker DMX 750 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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