BMRB Entry 17777
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17777
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Title: Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG PubMed: 21733840
Deposition date: 2011-07-11 Original release date: 2011-08-03
Authors: McDowell, Melanie; Johnson, S.; Deane, J.; Mcdonnell, J.; Lea, S.
Citation: McDowell, Melanie; Johnson, Steven; Deane, Janet; Cheung, Martin; Roehrich, A. Dorothea; Blocker, Ariel; McDonnell, James; Lea, Susan. "Structural and functional studies on the N-terminal domain of the Shigella type III secretion protein MxiG." J. Biol. Chem. 286, 30606-30614 (2011).
Assembly members:
PROTEIN_MXIG, polymer, 107 residues, 12147.3457 Da.
Natural source: Common Name: Shigella flexneri Taxonomy ID: 623 Superkingdom: Bacteria Kingdom: not available Genus/species: Shigella flexneri
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PROTEIN_MXIG: NSNLAPFRLLVKLTNGVGDE
FPLYYGNNLIVLGRTIETLE
FGNDNFPENIIPVTDSKSDG
IIYLTISKDNICQFSDEKGE
QIDINSQFNSFEYDGISFHL
KNMREDK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 148 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 588 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PROTEIN MXIG | 1 |
Entities:
Entity 1, PROTEIN MXIG 107 residues - 12147.3457 Da.
| 1 | ASN | SER | ASN | LEU | ALA | PRO | PHE | ARG | LEU | LEU | ||||
| 2 | VAL | LYS | LEU | THR | ASN | GLY | VAL | GLY | ASP | GLU | ||||
| 3 | PHE | PRO | LEU | TYR | TYR | GLY | ASN | ASN | LEU | ILE | ||||
| 4 | VAL | LEU | GLY | ARG | THR | ILE | GLU | THR | LEU | GLU | ||||
| 5 | PHE | GLY | ASN | ASP | ASN | PHE | PRO | GLU | ASN | ILE | ||||
| 6 | ILE | PRO | VAL | THR | ASP | SER | LYS | SER | ASP | GLY | ||||
| 7 | ILE | ILE | TYR | LEU | THR | ILE | SER | LYS | ASP | ASN | ||||
| 8 | ILE | CYS | GLN | PHE | SER | ASP | GLU | LYS | GLY | GLU | ||||
| 9 | GLN | ILE | ASP | ILE | ASN | SER | GLN | PHE | ASN | SER | ||||
| 10 | PHE | GLU | TYR | ASP | GLY | ILE | SER | PHE | HIS | LEU | ||||
| 11 | LYS | ASN | MET | ARG | GLU | ASP | LYS |
Samples:
sample_1: PROTEIN MXIG, [U-13C; U-15N], 5.4 mM; NaPi 25 mM; DTT 1 mM
sample_conditions_1: ionic strength: 25 mM; pH: 6.800; pressure: 1 atm; temperature: 298.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HN(CO)CA | sample_1 | solution | sample_conditions_1 |
| CBCA(CO)NH | sample_1 | solution | sample_conditions_1 |
| CBCANH | sample_1 | solution | sample_conditions_1 |
| HNCO | sample_1 | solution | sample_conditions_1 |
| CC(CO)NH | sample_1 | solution | sample_conditions_1 |
| H(CCCO)NH | sample_1 | solution | sample_conditions_1 |
| 15N-NOESY-HSQC | sample_1 | solution | sample_conditions_1 |
| 13C-NOESY | sample_1 | solution | sample_conditions_1 |
| CLEANEX-PM | sample_1 | solution | sample_conditions_1 |
| long-range HNCO | sample_1 | solution | sample_conditions_1 |
| HNHA | sample_1 | solution | sample_conditions_1 |
Software:
AutoDep v4.3, PDBE - collection
DYANA-1.5 vany, P. Guntert, C. Mumenthaler, K. Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts