Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15690
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Citation: Banci, Lucia; Bertini, Ivano; Calderone, Vito; Della?Malva, Nunzia; Felli, Isabella; Neri, Sara; Pavelkova, Anna; Rosato, Antonio. "Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces." Biochem. J. 422, 37-42 (2009).
PubMed: 19453293
Assembly members:
MNK1, polymer, 73 residues, Formula weight is not available
HAH1, polymer, 68 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 Host organism: Escherichia coli Vector: pET20
Entity Sequences (FASTA):
MNK1: MGVNSVTISVEGMTCNSCVW
TIEQQIGKVNGVHHIKVSLE
EKNATIIYDPKLQTPKTLQE
AIDDMGFDAVIHN
HAH1: MPKHEFSVDMTCGGCAEAVS
RVLNKLGGVKYDIDLPNKKV
CIESEHSMDTLLATLKKTGK
TVSYLGLE
Data type | Count |
13C chemical shifts | 564 |
15N chemical shifts | 137 |
1H chemical shifts | 907 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | COPPER(I) ION | 3 |
2 | MNK1 | 1 |
3 | HAH1 | 2 |
Entity 3, COPPER(I) ION - Cu - 63.546 Da.
1 | CU1 |
Entity 1, MNK1 73 residues - Formula weight is not available
1 | MET | GLY | VAL | ASN | SER | VAL | THR | ILE | SER | VAL | ||||
2 | GLU | GLY | MET | THR | CYS | ASN | SER | CYS | VAL | TRP | ||||
3 | THR | ILE | GLU | GLN | GLN | ILE | GLY | LYS | VAL | ASN | ||||
4 | GLY | VAL | HIS | HIS | ILE | LYS | VAL | SER | LEU | GLU | ||||
5 | GLU | LYS | ASN | ALA | THR | ILE | ILE | TYR | ASP | PRO | ||||
6 | LYS | LEU | GLN | THR | PRO | LYS | THR | LEU | GLN | GLU | ||||
7 | ALA | ILE | ASP | ASP | MET | GLY | PHE | ASP | ALA | VAL | ||||
8 | ILE | HIS | ASN |
Entity 2, HAH1 68 residues - Formula weight is not available
1 | MET | PRO | LYS | HIS | GLU | PHE | SER | VAL | ASP | MET | ||||
2 | THR | CYS | GLY | GLY | CYS | ALA | GLU | ALA | VAL | SER | ||||
3 | ARG | VAL | LEU | ASN | LYS | LEU | GLY | GLY | VAL | LYS | ||||
4 | TYR | ASP | ILE | ASP | LEU | PRO | ASN | LYS | LYS | VAL | ||||
5 | CYS | ILE | GLU | SER | GLU | HIS | SER | MET | ASP | THR | ||||
6 | LEU | LEU | ALA | THR | LEU | LYS | LYS | THR | GLY | LYS | ||||
7 | THR | VAL | SER | TYR | LEU | GLY | LEU | GLU |
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