BMRB Entry 26022
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26022
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Title: Solution structure of translation initiation factor IF1 from wolbachia endosymbiont strain TRS of Brugia malayi
Deposition date: 2016-03-31 Original release date: 2017-03-30
Authors: Kabra, Ashish; Nag, Jitendra; Arora, Ashish; Bhattacharya, Shailja
Citation: Kabra, Ashish; Nag, Jitendra; Arora, Ashish; Bhattacharya, Shailja. "Solution structure of translation initiation factor IF1 from wolbachia endosymbiont strain TRS of Brugia malayi" Not known ., .-..
Assembly members:
IF1, polymer, 87 residues, 9956.837 Da.
Natural source: Common Name: a-proteobacteria Taxonomy ID: 953 Superkingdom: Bacteria Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
IF1: MVKDEKSKTLFEVEGAVTAL
LPAAEFRVKLDNEHEIICHV
SGKVRRSKIRIIIGDRVLVE
MSIYDRNAKKGRIIRRLKGT
SDRTISK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 376 |
15N chemical shifts | 83 |
1H chemical shifts | 619 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | translation initiation factor IF1 | 1 |
Entities:
Entity 1, translation initiation factor IF1 87 residues - 9956.837 Da.
Sequence does not contain the purification tag.
1 | MET | VAL | LYS | ASP | GLU | LYS | SER | LYS | THR | LEU | ||||
2 | PHE | GLU | VAL | GLU | GLY | ALA | VAL | THR | ALA | LEU | ||||
3 | LEU | PRO | ALA | ALA | GLU | PHE | ARG | VAL | LYS | LEU | ||||
4 | ASP | ASN | GLU | HIS | GLU | ILE | ILE | CYS | HIS | VAL | ||||
5 | SER | GLY | LYS | VAL | ARG | ARG | SER | LYS | ILE | ARG | ||||
6 | ILE | ILE | ILE | GLY | ASP | ARG | VAL | LEU | VAL | GLU | ||||
7 | MET | SER | ILE | TYR | ASP | ARG | ASN | ALA | LYS | LYS | ||||
8 | GLY | ARG | ILE | ILE | ARG | ARG | LEU | LYS | GLY | THR | ||||
9 | SER | ASP | ARG | THR | ILE | SER | LYS |
Samples:
sample_1: IF1, [U-100% 15N], 0.5 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.1%; PMSF 2 mM
sample_2: IF1, [U-100% 13C; U-100% 15N], 0.8 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.1%; PMSF 2 mM
sample_3: IF1, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.1%; PMSF 2 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
PSVS, Bhattacharya and Montelione - Validation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts