BMRB Entry 30559
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30559
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Title: Solution structure of the Tudor domain of PSHCP
Deposition date: 2019-01-14 Original release date: 2019-08-16
Authors: Bauer, Katherine; Pelligrini, M.; Ragusa, Michael
Citation: Bauer, Katherine; Dicovitsky, R.; Pellegrini, M.; Zhaxybayeva, O.; Ragusa, Michael. "The structure of a highly conserved picocyanobacterial hypothetical protein reveals a Tudor domain with a novel tRNA binding function" . ., .-..
Assembly members:
PSHCP, polymer, 59 residues, 6471.392 Da.
Natural source: Common Name: Prochlorococcus marinus (strain MIT 9303) Taxonomy ID: 59922 Superkingdom: Bacteria Kingdom: not available Genus/species: Prochlorococcus Prochlorococcus marinus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PSHCP: SNAMELDLQPGDVVKVLESA
ALGWVRARVIRVKSGGRVVV
QSDQGREFTARGNQVRLIE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 409 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 59 residues - 6471.392 Da.
| 1 | SER | ASN | ALA | MET | GLU | LEU | ASP | LEU | GLN | PRO | ||||
| 2 | GLY | ASP | VAL | VAL | LYS | VAL | LEU | GLU | SER | ALA | ||||
| 3 | ALA | LEU | GLY | TRP | VAL | ARG | ALA | ARG | VAL | ILE | ||||
| 4 | ARG | VAL | LYS | SER | GLY | GLY | ARG | VAL | VAL | VAL | ||||
| 5 | GLN | SER | ASP | GLN | GLY | ARG | GLU | PHE | THR | ALA | ||||
| 6 | ARG | GLY | ASN | GLN | VAL | ARG | LEU | ILE | GLU |
Samples:
sample_1: PSHCP, [U-15N], 1.4 mM; sodium phosphate 20 mM; sodium chloride 200 mM; TCEP 0.2 mM
sample_2: PSHCP, [U-15N, -13C], 1.6 mM; sodium phosphate 20 mM; sodium chloride 200 mM; TCEP 0.2 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D_NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - processing
CNS, Brunger A. T. et.al. - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts