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PDB ID: 2kko
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16368
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Citation: Ramelot, Theresa; Cort, John; Wang, D.; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the homodimeric winged helix-turn-helix DNA-binding
domain (fragment 1-100) Mb0332 from Mycobacterium bovis, a possible ArsR-family
transcriptional regulator. Northeast Structural Genomics Consortium Target
MbR242E." .
Assembly members:
Mb0332, polymer, 109 residues, 11700 Da.
Natural source: Common Name: Mycobacterium bovis Taxonomy ID: 1765 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium bovis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21-23C
Entity Sequences (FASTA):
Mb0332: XMAGQSDRKAALLDQVARVG
KALANGRRLQILDLLAQGER
AVEAIATATGMNLTTASANL
QALKSGGLVEARREGTRQYY
RIAGEDVARLFALVQVVADE
HLEHHHHHH
Data type | Count |
13C chemical shifts | 431 |
15N chemical shifts | 116 |
1H chemical shifts | 720 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Mb0332, chain A | 1 |
2 | Mb0332, chain B | 1 |
Entity 1, Mb0332, chain A 109 residues - 11700 Da.
8 non-native residues at C-terminus (LEHHHHHH)
1 | ACE | MET | ALA | GLY | GLN | SER | ASP | ARG | LYS | ALA | ||||
2 | ALA | LEU | LEU | ASP | GLN | VAL | ALA | ARG | VAL | GLY | ||||
3 | LYS | ALA | LEU | ALA | ASN | GLY | ARG | ARG | LEU | GLN | ||||
4 | ILE | LEU | ASP | LEU | LEU | ALA | GLN | GLY | GLU | ARG | ||||
5 | ALA | VAL | GLU | ALA | ILE | ALA | THR | ALA | THR | GLY | ||||
6 | MET | ASN | LEU | THR | THR | ALA | SER | ALA | ASN | LEU | ||||
7 | GLN | ALA | LEU | LYS | SER | GLY | GLY | LEU | VAL | GLU | ||||
8 | ALA | ARG | ARG | GLU | GLY | THR | ARG | GLN | TYR | TYR | ||||
9 | ARG | ILE | ALA | GLY | GLU | ASP | VAL | ALA | ARG | LEU | ||||
10 | PHE | ALA | LEU | VAL | GLN | VAL | VAL | ALA | ASP | GLU | ||||
11 | HIS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
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