BMRB Entry 34068
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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/BMR34068
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Title: RBM5 OCRE domain PubMed: 27894420
Deposition date: 2016-11-19 Original release date: 2016-12-05
Authors: Warner, L.; Mourao, A.; Soni, K.; Sattler, M.
Citation: Mourao, A.; Bonnal, S.; Soni, K.; Warner, L.; Bordonne, R.; Valcarcel, J.; Sattler, M.. "Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation." Elife 5, .-. (2016).
Assembly members:
entity_1, polymer, 64 residues, 7436.785 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GAMGTKYAVPDTSTYQYDES
SGYYYDPTTGLYYDPNSQYY
YNSLTQQYLYWDGEKETYVP
AAES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 282 |
| 15N chemical shifts | 65 |
| 1H chemical shifts | 397 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 64 residues - 7436.785 Da.
| 1 | GLY | ALA | MET | GLY | THR | LYS | TYR | ALA | VAL | PRO | ||||
| 2 | ASP | THR | SER | THR | TYR | GLN | TYR | ASP | GLU | SER | ||||
| 3 | SER | GLY | TYR | TYR | TYR | ASP | PRO | THR | THR | GLY | ||||
| 4 | LEU | TYR | TYR | ASP | PRO | ASN | SER | GLN | TYR | TYR | ||||
| 5 | TYR | ASN | SER | LEU | THR | GLN | GLN | TYR | LEU | TYR | ||||
| 6 | TRP | ASP | GLY | GLU | LYS | GLU | THR | TYR | VAL | PRO | ||||
| 7 | ALA | ALA | GLU | SER |
Samples:
sample_1: D2O 10%; H2O 90%; ocre5, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 70 mM; pH: 6.5 pD; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_2 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| HDCB Kay | sample_1 | isotropic | sample_conditions_2 |
| HECB Kay | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY | 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_2 |
Software:
Analysis, CCPN - chemical shift assignment, peak picking
CNS, Brunger A. T. et.al. - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts