BMRB Entry 18553
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18553
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Title: ZirS C-terminal Domain PubMed: 22810234
Deposition date: 2012-06-28 Original release date: 2012-08-21
Authors: Prehna, Gerd; Li, Yuling; Stoynov, Nikolay; Okon, Mark; Vukovic, Marija; McIntosh, Lawrence; Foster, Leonard; Finlay, B. Brett; Strynadka, Natalie
Citation: Prehna, Gerd; Li, Yuling; Stoynov, Nikolay; Okon, Mark; Vuckovic, Marija; McIntosh, Lawrence; Foster, Leonard; Finlay, B. Brett; Strynadka, Natalie. "The zinc regulated antivirulence pathway of Salmonella is a multiprotein immunoglobulin adhesion system." J. Biol. Chem. 287, 32324-32337 (2012).
Assembly members:
ZirS, polymer, 146 residues, 16105.249 Da.
Natural source: Common Name: Enterobacteria Taxonomy ID: 90371 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ZirS: GPLGSGSKIKLEIYNETDMA
SASGYTPVPSVSEFQYIETE
TISNTPSPDLTVMSIDKSVL
SPGESATITTIVKDIDGNPV
NEVHINKTVARENLKGLWDY
GPLKKENVPGKYTQVITYRG
HSNERIDISFKYAMSFTKEI
SIRGRL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 540 |
| 15N chemical shifts | 125 |
| 1H chemical shifts | 917 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ZirS C-terminal Domain | 1 |
Entities:
Entity 1, ZirS C-terminal Domain 146 residues - 16105.249 Da.
| 1 | GLY | PRO | LEU | GLY | SER | GLY | SER | LYS | ILE | LYS | ||||
| 2 | LEU | GLU | ILE | TYR | ASN | GLU | THR | ASP | MET | ALA | ||||
| 3 | SER | ALA | SER | GLY | TYR | THR | PRO | VAL | PRO | SER | ||||
| 4 | VAL | SER | GLU | PHE | GLN | TYR | ILE | GLU | THR | GLU | ||||
| 5 | THR | ILE | SER | ASN | THR | PRO | SER | PRO | ASP | LEU | ||||
| 6 | THR | VAL | MET | SER | ILE | ASP | LYS | SER | VAL | LEU | ||||
| 7 | SER | PRO | GLY | GLU | SER | ALA | THR | ILE | THR | THR | ||||
| 8 | ILE | VAL | LYS | ASP | ILE | ASP | GLY | ASN | PRO | VAL | ||||
| 9 | ASN | GLU | VAL | HIS | ILE | ASN | LYS | THR | VAL | ALA | ||||
| 10 | ARG | GLU | ASN | LEU | LYS | GLY | LEU | TRP | ASP | TYR | ||||
| 11 | GLY | PRO | LEU | LYS | LYS | GLU | ASN | VAL | PRO | GLY | ||||
| 12 | LYS | TYR | THR | GLN | VAL | ILE | THR | TYR | ARG | GLY | ||||
| 13 | HIS | SER | ASN | GLU | ARG | ILE | ASP | ILE | SER | PHE | ||||
| 14 | LYS | TYR | ALA | MET | SER | PHE | THR | LYS | GLU | ILE | ||||
| 15 | SER | ILE | ARG | GLY | ARG | LEU |
Samples:
sample_1: ZirS, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 50 mM; sodium chloride 50 mM; TCEP 0.1 mM; PMSF 0.1 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.1; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| CCC-TOCSY-NNH | sample_1 | isotropic | sample_conditions_1 |
| CT-HSQC | sample_1 | isotropic | sample_conditions_1 |
| (HB)CB(CGCD)HD_aromatic | sample_1 | isotropic | sample_conditions_1 |
| HBCBGCCC-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| HCC-TOCSY-NNH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian Unity 500 MHz
- Varian Unity 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAJ36633 BAP07530 |
| EMBL | CBG24675 CBW17693 CCF89381 CCR01301 CCR05077 |
| GB | AAL20585 AAX65569 ACH49127 ACN46197 ACY88485 |
| REF | NP_460626 WP_000033763 WP_000033764 WP_001242915 WP_001517944 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts