BMRB Entry 34376
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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/BMR34376
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Title: The N-terminal domain of rhomboid protease YqgP PubMed: 31930742
Deposition date: 2019-03-13 Original release date: 2020-01-06
Authors: Began, J.; Strisovsky, K.; Veverka, V.
Citation: Began, Jakub; Cordier, Baptiste; Brezinova, Jana; Delisle, Jordan; Hexnerova, Rozalie; Srb, Pavel; Rampirova, Petra; Kozisek, Milan; Baudet, Mathieu; Coute, Yohann; Galinier, Anne; Veverka, Vaclav; Doan, Thierry; Strisovsky, Kvido. "Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease" Embo J. 39, e102935-e102935 (2020).
Assembly members:
entity_1, polymer, 185 residues, 21836.576 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MFLLEYTYWKIAAHLVNSGY
GVIQAGESDEIWLEAPDKSS
HDLVRLYKHDLDFRQEMVRD
IEEQAERVERVRHQLGRRRM
KLLNVFFSTEAPVDDWEEIA
KKTFEKGTVSVEPAIVRGTM
LRDDLQAVFPSFRTEDCSEE
HASFENAQMARERFLSLVLK
QEEQRKTEAAVFQNGKLERE
NLYFQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 773 |
| 15N chemical shifts | 192 |
| 1H chemical shifts | 1279 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 185 residues - 21836.576 Da.
| 1 | MET | PHE | LEU | LEU | GLU | TYR | THR | TYR | TRP | LYS | ||||
| 2 | ILE | ALA | ALA | HIS | LEU | VAL | ASN | SER | GLY | TYR | ||||
| 3 | GLY | VAL | ILE | GLN | ALA | GLY | GLU | SER | ASP | GLU | ||||
| 4 | ILE | TRP | LEU | GLU | ALA | PRO | ASP | LYS | SER | SER | ||||
| 5 | HIS | ASP | LEU | VAL | ARG | LEU | TYR | LYS | HIS | ASP | ||||
| 6 | LEU | ASP | PHE | ARG | GLN | GLU | MET | VAL | ARG | ASP | ||||
| 7 | ILE | GLU | GLU | GLN | ALA | GLU | ARG | VAL | GLU | ARG | ||||
| 8 | VAL | ARG | HIS | GLN | LEU | GLY | ARG | ARG | ARG | MET | ||||
| 9 | LYS | LEU | LEU | ASN | VAL | PHE | PHE | SER | THR | GLU | ||||
| 10 | ALA | PRO | VAL | ASP | ASP | TRP | GLU | GLU | ILE | ALA | ||||
| 11 | LYS | LYS | THR | PHE | GLU | LYS | GLY | THR | VAL | SER | ||||
| 12 | VAL | GLU | PRO | ALA | ILE | VAL | ARG | GLY | THR | MET | ||||
| 13 | LEU | ARG | ASP | ASP | LEU | GLN | ALA | VAL | PHE | PRO | ||||
| 14 | SER | PHE | ARG | THR | GLU | ASP | CYS | SER | GLU | GLU | ||||
| 15 | HIS | ALA | SER | PHE | GLU | ASN | ALA | GLN | MET | ALA | ||||
| 16 | ARG | GLU | ARG | PHE | LEU | SER | LEU | VAL | LEU | LYS | ||||
| 17 | GLN | GLU | GLU | GLN | ARG | LYS | THR | GLU | ALA | ALA | ||||
| 18 | VAL | PHE | GLN | ASN | GLY | LYS | LEU | GLU | ARG | GLU | ||||
| 19 | ASN | LEU | TYR | PHE | GLN |
Samples:
sample_1: YqgP, [U-13C; U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 25 mM
sample_conditions_1: ionic strength: 175 mM; pH: 6.5; pressure: 1 atm; temperature: 298 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 |
| 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 |
Software:
TopSpin, Bruker Biospin - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
Sparky, Goddard - chemical shift assignment
YASARA, YASARA - refinement
NMR spectrometers:
- Bruker AVANCE III 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts