BMRB Entry 25656
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25656
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Title: NMR Assignments and structure of Translation initiation factor IF-1 from Burkholderia thailandensis E264.
Deposition date: 2015-06-09 Original release date: 2015-06-23
Authors: Barnwal, Ravi Pratap; Varani, Gabriele
Citation: Barnwal, Ravi Pratap; Varani, Gabriele. "NMR Assignments and structure of Translation initiation factor IF-1 from Burkholderia thailandensis E264." To be Published ., .-..
Assembly members:
entity, polymer, 72 residues, 8231.756 Da.
Natural source: Common Name: Burkholderia thailandensis Taxonomy ID: 57975 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia thailandensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MAKDDVIQMQGEVIENLPNA
TFRVKLENGHVVLGHISGKM
RMHYIRILPGDKVTVELTPY
DLSRARIVFRAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 368 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Translation initiation factor IF-1 | 1 |
Entities:
Entity 1, Translation initiation factor IF-1 72 residues - 8231.756 Da.
| 1 | MET | ALA | LYS | ASP | ASP | VAL | ILE | GLN | MET | GLN | ||||
| 2 | GLY | GLU | VAL | ILE | GLU | ASN | LEU | PRO | ASN | ALA | ||||
| 3 | THR | PHE | ARG | VAL | LYS | LEU | GLU | ASN | GLY | HIS | ||||
| 4 | VAL | VAL | LEU | GLY | HIS | ILE | SER | GLY | LYS | MET | ||||
| 5 | ARG | MET | HIS | TYR | ILE | ARG | ILE | LEU | PRO | GLY | ||||
| 6 | ASP | LYS | VAL | THR | VAL | GLU | LEU | THR | PRO | TYR | ||||
| 7 | ASP | LEU | SER | ARG | ALA | ARG | ILE | VAL | PHE | ARG | ||||
| 8 | ALA | LYS |
Samples:
sample_1: Translation initiation factor IF-1, [U-95% 13C; U-95% 15N], 1.2 mM
sample_conditions_1: 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 |
| 2D 1H-13C HSQC | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 - collection, processing
CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAG44869 BAO87561 |
| EMBL | CAD16707 CAH37203 CAR50566 CBJ36605 CBJ41758 |
| GB | AAU47849 ABA49847 ABB07070 ABC39541 ABD71909 |
| REF | WP_003264140 WP_003273618 WP_004185257 WP_004521905 WP_006577442 |
| SP | A0K3P6 A1V882 A2S7J7 A3MRX5 A3NEF8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts