BMRB Entry 16770
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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/BMR16770
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Title: NMR solution structure of a soluble PrgI mutant from Salmonella Typhimurium PubMed: 20543831
Deposition date: 2010-03-09 Original release date: 2010-07-27
Authors: Schmidt, Holger; Poyraz, Oemer; Seidel, Karsten; Delissen, Friedmar; Ader, Christian; Tenenboim, Hezi; Goosmann, Christian; Laube, Britta; Thuenemann, Andreas; Zychlinski, Arturo; Baldus, Marc; Lange, Adam; Griesinger, Christian; Kolbe, Michael
Citation: Poyraz, Omer; Schmidt, Holger; Seidel, Karsten; Delissen, Friedmar; Ader, Christian; Tenenboim, Hezi; Goosmann, Christian; Laube, Britta; Thunemann, Andreas; Zychlinsky, Arturo; Baldus, Marc; Lange, Adam; Griesinger, Christian; Kolbe, Michael. "Protein refolding is required for assembly of the type three secretion needle." Nat. Struct. Mol. Biol. 17, 788-792 (2010).
Assembly members:
PrgI, polymer, 83 residues, 9091.127 Da.
Natural source: Common Name: Salmonella enterica Taxonomy ID: 28901 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PrgI: GSHMATPWSGYLDDVSAKFD
TGVDNLQTQVTEALDKLAAK
PSDPALLAAYQSKLSEYNLY
RNAQSNTAKAFKDIDAAIIQ
NFR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 335 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 568 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PrgI | 1 |
Entities:
Entity 1, PrgI 83 residues - 9091.127 Da.
Residues G1-H3 represent a non-native remainder of the cleavage of the affinity tag. A68 & A70 are mutated residues and correspond to valines in the wild type sequence.
| 1 | GLY | SER | HIS | MET | ALA | THR | PRO | TRP | SER | GLY | ||||
| 2 | TYR | LEU | ASP | ASP | VAL | SER | ALA | LYS | PHE | ASP | ||||
| 3 | THR | GLY | VAL | ASP | ASN | LEU | GLN | THR | GLN | VAL | ||||
| 4 | THR | GLU | ALA | LEU | ASP | LYS | LEU | ALA | ALA | LYS | ||||
| 5 | PRO | SER | ASP | PRO | ALA | LEU | LEU | ALA | ALA | TYR | ||||
| 6 | GLN | SER | LYS | LEU | SER | GLU | TYR | ASN | LEU | TYR | ||||
| 7 | ARG | ASN | ALA | GLN | SER | ASN | THR | ALA | LYS | ALA | ||||
| 8 | PHE | LYS | ASP | ILE | ASP | ALA | ALA | ILE | ILE | GLN | ||||
| 9 | ASN | PHE | ARG |
Samples:
sample_15N: PrgI*, [U-100% 15N], 0.3 mM; MES 20 mM; NaCl 20 mM
sample_15N13C: PrgI*, [U-100% 13C; U-100% 15N], 0.3 mM; MES 20 mM; NaCl 20 mM
sample_15Naniso: PrgI*, [U-100% 15N], 0.3 mM; MES 20 mM; NaCl 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_15N | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_15N13C | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_15N13C | isotropic | sample_conditions_1 |
| 3D HNCA | sample_15N13C | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_15N13C | isotropic | sample_conditions_1 |
| 3D HNCO | sample_15N13C | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_15N13C | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_15N13C | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_15N13C | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_15N | isotropic | sample_conditions_1 |
| 2D 1H-15N COCAINE | sample_15N | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_15Naniso | anisotropic | sample_conditions_1 |
| 2D 1H-15N COCAINE | sample_15Naniso | anisotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking
CARA, Keller and Wuthrich - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 18276 |
| PDB | |
| DBJ | BAJ37865 BAP08778 |
| EMBL | CAR34293 CAR38585 CBG25842 CBW18951 CCF89508 |
| GB | AAB60189 AAL21753 AAX49613 AAX66711 ACF64232 |
| REF | NP_461794 WP_000235228 YP_009073587 |
| SP | P41784 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts