BMRB Entry 4352
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4352
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Citation: Whittaker, Sara; Czisch, Michael; Wechselberger, Rainer; Kaptein, Robert; Hemmings, Andrew; James, Richard; Kleanthous, Colin; Moore, Geoffrey. "Slow Conformational Dynamics of an Endonuclease Persist in its Complex
with its Natural Protein Inhibitor" Protein Sci. 9, 713-720 (2000).
Assembly members:
DNase domain of colicin E9, polymer, 134 residues, 15090 Da.
Immunity protein of colicin E9, polymer, 86 residues, 9582 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Eschericia coli Vector: pRJ353
Entity Sequences (FASTA):
DNase domain of colicin E9: MESKRNKPGKATGKGKPVGD
KWLDDAGKDSGAPIPDRIAD
KLRDKEFKSFDDFRKAVWEE
VSKDPELSKNLNPSNKSSVS
KGYSPFTPKNQQVGGRKVYE
LHHDKPISQGGEVYDMDNIR
VTTPKRHIDIHRGK
Immunity protein of colicin E9: MELKHSISDYTEAEFLQLVT
TICNADTSSEEELVKLVTHF
EEMTEHPSGSDLIYYPKEGD
DDSPSGIVNTVKQWRAANGK
SGFKQG
| Data type | Count |
| 13C chemical shifts | 420 |
| 15N chemical shifts | 156 |
| 1H chemical shifts | 472 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E9 DNase | 1 |
| 2 | Im9 | 2 |
Entities:
Entity 1, E9 DNase 134 residues - 15090 Da.
| 1 | MET | GLU | SER | LYS | ARG | ASN | LYS | PRO | GLY | LYS | ||||
| 2 | ALA | THR | GLY | LYS | GLY | LYS | PRO | VAL | GLY | ASP | ||||
| 3 | LYS | TRP | LEU | ASP | ASP | ALA | GLY | LYS | ASP | SER | ||||
| 4 | GLY | ALA | PRO | ILE | PRO | ASP | ARG | ILE | ALA | ASP | ||||
| 5 | LYS | LEU | ARG | ASP | LYS | GLU | PHE | LYS | SER | PHE | ||||
| 6 | ASP | ASP | PHE | ARG | LYS | ALA | VAL | TRP | GLU | GLU | ||||
| 7 | VAL | SER | LYS | ASP | PRO | GLU | LEU | SER | LYS | ASN | ||||
| 8 | LEU | ASN | PRO | SER | ASN | LYS | SER | SER | VAL | SER | ||||
| 9 | LYS | GLY | TYR | SER | PRO | PHE | THR | PRO | LYS | ASN | ||||
| 10 | GLN | GLN | VAL | GLY | GLY | ARG | LYS | VAL | TYR | GLU | ||||
| 11 | LEU | HIS | HIS | ASP | LYS | PRO | ILE | SER | GLN | GLY | ||||
| 12 | GLY | GLU | VAL | TYR | ASP | MET | ASP | ASN | ILE | ARG | ||||
| 13 | VAL | THR | THR | PRO | LYS | ARG | HIS | ILE | ASP | ILE | ||||
| 14 | HIS | ARG | GLY | LYS |
Entity 2, Im9 86 residues - 9582 Da.
| 1 | MET | GLU | LEU | LYS | HIS | SER | ILE | SER | ASP | TYR | ||||
| 2 | THR | GLU | ALA | GLU | PHE | LEU | GLN | LEU | VAL | THR | ||||
| 3 | THR | ILE | CYS | ASN | ALA | ASP | THR | SER | SER | GLU | ||||
| 4 | GLU | GLU | LEU | VAL | LYS | LEU | VAL | THR | HIS | PHE | ||||
| 5 | GLU | GLU | MET | THR | GLU | HIS | PRO | SER | GLY | SER | ||||
| 6 | ASP | LEU | ILE | TYR | TYR | PRO | LYS | GLU | GLY | ASP | ||||
| 7 | ASP | ASP | SER | PRO | SER | GLY | ILE | VAL | ASN | THR | ||||
| 8 | VAL | LYS | GLN | TRP | ARG | ALA | ALA | ASN | GLY | LYS | ||||
| 9 | SER | GLY | PHE | LYS | GLN | GLY |
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks