BMRB Entry 25434
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25434
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Title: Solution NMR Structure of the OCRE Domain of RBM10 PubMed: 26712279
Deposition date: 2015-01-20 Original release date: 2015-03-30
Authors: Martin, B.; Geralt, M.; Serrano, P.; Wuthrich, K.
Citation: Martin, Bryan; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif" Structure 24, 158-164 (2016).
Assembly members:
OCRE, polymer, 92 residues, 10856.678 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):
OCRE: GHMQESYSQYPVPDVSTYQY
DETSGYYYDPQTGLYYDPNS
QYYYNAQSQQYLYWDGERRT
YVPALEQSADGHKETGAPSK
EGKEKKEKHKTK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 294 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 549 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OCRE | 1 |
Entities:
Entity 1, OCRE 92 residues - 10856.678 Da.
| 1 | GLY | HIS | MET | GLN | GLU | SER | TYR | SER | GLN | TYR | ||||
| 2 | PRO | VAL | PRO | ASP | VAL | SER | THR | TYR | GLN | TYR | ||||
| 3 | ASP | GLU | THR | SER | GLY | TYR | TYR | TYR | ASP | PRO | ||||
| 4 | GLN | THR | GLY | LEU | TYR | TYR | ASP | PRO | ASN | SER | ||||
| 5 | GLN | TYR | TYR | TYR | ASN | ALA | GLN | SER | GLN | GLN | ||||
| 6 | TYR | LEU | TYR | TRP | ASP | GLY | GLU | ARG | ARG | THR | ||||
| 7 | TYR | VAL | PRO | ALA | LEU | GLU | GLN | SER | ALA | ASP | ||||
| 8 | GLY | HIS | LYS | GLU | THR | GLY | ALA | PRO | SER | LYS | ||||
| 9 | GLU | GLY | LYS | GLU | LYS | LYS | GLU | LYS | HIS | LYS | ||||
| 10 | THR | LYS |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM
sample_conditions_1: ionic strength: 0.240 M; pH: 6.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Bruker Biospin, Guntert, Mumenthaler and Wuthrich - collection, data analysis, processing, structure solution
UNIO vv2010, (UNIO) Hermann and Wuthrich - chemical shift assignment, peak picking, structure solution
CARA, (CARA) Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts