BMRB Entry 30134
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30134
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Title: Recognition and targeting mechanisms by chaperones in flagella assembly and operation PubMed: 27528687
Deposition date: 2016-07-07 Original release date: 2016-08-11
Authors: Khanra, N.; Rossi, P.; Economou, A.; Kalodimos, C.
Citation: Khanra, N.; Rossi, P.; Economou, A.; Kalodimos, C.. "Recognition and targeting mechanisms by chaperones in flagellum assembly and operation" Proc. Natl. Acad. Sci. U. S. A. 113, 9798-9803 (2016).
Assembly members:
entity_1, polymer, 155 residues, 17387.732 Da.
Natural source: Common Name: Salmonella enterica Taxonomy ID: 99287 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MTSTVEFINRWQRIALLSQS
LLELAQRGEWDLLLQQEVSY
LQSIETVMEKQTPPGITRSI
QDMVAGYIKQTLDNEQLLKG
LLQQRLDELSSLIGQVLFQG
PSAGLVPRGSGGIEGSIDET
VARYKAQFTQLDTMMSKLNN
TSSYLTQQFTAMNKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 528 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 766 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 155 residues - 17387.732 Da.
| 1 | MET | THR | SER | THR | VAL | GLU | PHE | ILE | ASN | ARG | ||||
| 2 | TRP | GLN | ARG | ILE | ALA | LEU | LEU | SER | GLN | SER | ||||
| 3 | LEU | LEU | GLU | LEU | ALA | GLN | ARG | GLY | GLU | TRP | ||||
| 4 | ASP | LEU | LEU | LEU | GLN | GLN | GLU | VAL | SER | TYR | ||||
| 5 | LEU | GLN | SER | ILE | GLU | THR | VAL | MET | GLU | LYS | ||||
| 6 | GLN | THR | PRO | PRO | GLY | ILE | THR | ARG | SER | ILE | ||||
| 7 | GLN | ASP | MET | VAL | ALA | GLY | TYR | ILE | LYS | GLN | ||||
| 8 | THR | LEU | ASP | ASN | GLU | GLN | LEU | LEU | LYS | GLY | ||||
| 9 | LEU | LEU | GLN | GLN | ARG | LEU | ASP | GLU | LEU | SER | ||||
| 10 | SER | LEU | ILE | GLY | GLN | VAL | LEU | PHE | GLN | GLY | ||||
| 11 | PRO | SER | ALA | GLY | LEU | VAL | PRO | ARG | GLY | SER | ||||
| 12 | GLY | GLY | ILE | GLU | GLY | SER | ILE | ASP | GLU | THR | ||||
| 13 | VAL | ALA | ARG | TYR | LYS | ALA | GLN | PHE | THR | GLN | ||||
| 14 | LEU | ASP | THR | MET | MET | SER | LYS | LEU | ASN | ASN | ||||
| 15 | THR | SER | SER | TYR | LEU | THR | GLN | GLN | PHE | THR | ||||
| 16 | ALA | MET | ASN | LYS | SER |
Samples:
sample_1: EDTA 0.5 mM; FliT-FliD_fusion, [U-99% 13C; U-99% 15N; U-99% 2H], 1 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05%
sample_2: EDTA 0.5 mM; FliT-FliD_fusion, U[15N,2H] 1H-13C-ILVMAT-methyl, 1 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05%
sample_3: EDTA 0.5 mM; FliT-FliD_fusion, [U-99% 13C; U-99% 15N], 1 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05%
sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
PSVS, Bhattacharya and Montelione - data analysis
SPARKY, Goddard - data analysis
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN v3.1, Bruker Biospin - collection
pdbstat v1.5, tejero and montelione - data analysis
NMR spectrometers:
- Bruker AvanceIII 700 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts