BMRB Entry 15206
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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/BMR15206
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Title: Differences in the electrostatic surfaces of the type III secretion needle proteins PubMed: 17617421
Deposition date: 2007-04-06 Original release date: 2007-10-24
Authors: Wang, Yu; Ouellette, Andrew; Egan, Chet; De Guzman, Roberto
Citation: Wang, Yu; Ouellette, Andrew; Egana, Chet; Rathinavelana, Thenmalarchelvi; Ima, Wonpil; De Guzman, Roberto. "Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH." J. Mol. Biol. 371, 1304-1314 (2007).
Assembly members:
needle monomer, polymer, 83 residues, 9279.383 Da.
Natural source: Common Name: Salmonella typhimurium Taxonomy ID: 602 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
needle monomer: MATPWSGYLDDVSAKFDTGV
DNLQTQVTEALDKLAAKPSD
PALLAAYQSKLSEYNLYRNA
QSNTVKVFKDIDAAILEHHH
HHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 297 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 477 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | needle monomer | 1 |
Entities:
Entity 1, needle monomer 83 residues - 9279.383 Da.
| 1 | MET | ALA | THR | PRO | TRP | SER | GLY | TYR | LEU | ASP | ||||
| 2 | ASP | VAL | SER | ALA | LYS | PHE | ASP | THR | GLY | VAL | ||||
| 3 | ASP | ASN | LEU | GLN | THR | GLN | VAL | THR | GLU | ALA | ||||
| 4 | LEU | ASP | LYS | LEU | ALA | ALA | LYS | PRO | SER | ASP | ||||
| 5 | PRO | ALA | LEU | LEU | ALA | ALA | TYR | GLN | SER | LYS | ||||
| 6 | LEU | SER | GLU | TYR | ASN | LEU | TYR | ARG | ASN | ALA | ||||
| 7 | GLN | SER | ASN | THR | VAL | LYS | VAL | PHE | LYS | ASP | ||||
| 8 | ILE | ASP | ALA | ALA | ILE | LEU | GLU | HIS | HIS | HIS | ||||
| 9 | HIS | HIS | HIS |
Samples:
sample_1: entity 0.8 mM
sample_conditions_1: ionic strength: 70 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 |
Software:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts