BMRB Entry 25028
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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/BMR25028
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Title: NMR structure of the hypotheical protein Lreu_0056 from Lactobacillus reuteri
Deposition date: 2014-06-18 Original release date: 2014-09-02
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the hypotheical protein Lreu_0056 from Lactobacillus reuteri" Not known ., .-..
Assembly members:
entity, polymer, 119 residues, 13287.176 Da.
Natural source: Common Name: firmicutes Taxonomy ID: 1598 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactobacillus reuteri
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GHMKFTDQQIGVLAGLAISP
EWLKQNIAANQLVYGIVKPS
DTVPAGVDDYSYLVAADDQD
GTIIFFKAEGQTVIIKYTSQ
RNTKLKAKALTLSQLKKEFY
QTRSQKREVDDYVAGLRTE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 859 |
| 13C chemical shifts | 419 |
| 15N chemical shifts | 125 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 119 residues - 13287.176 Da.
| 1 | GLY | HIS | MET | LYS | PHE | THR | ASP | GLN | GLN | ILE | ||||
| 2 | GLY | VAL | LEU | ALA | GLY | LEU | ALA | ILE | SER | PRO | ||||
| 3 | GLU | TRP | LEU | LYS | GLN | ASN | ILE | ALA | ALA | ASN | ||||
| 4 | GLN | LEU | VAL | TYR | GLY | ILE | VAL | LYS | PRO | SER | ||||
| 5 | ASP | THR | VAL | PRO | ALA | GLY | VAL | ASP | ASP | TYR | ||||
| 6 | SER | TYR | LEU | VAL | ALA | ALA | ASP | ASP | GLN | ASP | ||||
| 7 | GLY | THR | ILE | ILE | PHE | PHE | LYS | ALA | GLU | GLY | ||||
| 8 | GLN | THR | VAL | ILE | ILE | LYS | TYR | THR | SER | GLN | ||||
| 9 | ARG | ASN | THR | LYS | LEU | LYS | ALA | LYS | ALA | LEU | ||||
| 10 | THR | LEU | SER | GLN | LEU | LYS | LYS | GLU | PHE | TYR | ||||
| 11 | GLN | THR | ARG | SER | GLN | LYS | ARG | GLU | VAL | ASP | ||||
| 12 | ASP | TYR | VAL | ALA | GLY | LEU | ARG | THR | GLU |
Samples:
sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%
sample_conditions_1: temperature: 308 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G ntert P., Luginbuhl, Guntert, Billeter and Wuthrich - structure solution, refinement
j-UNIO, Herrmann, Guntert and Wuthrich - peak picking, structure solution
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| UNP | A5VHK8_LACRD |
| PDB | |
| GB | ABQ82332 AKP00282 EEI09009 EGC14866 KRK50377 |
| REF | WP_003669575 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts