BMRB Entry 15524
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15524
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Fenwick, R Bryn; Prasannan, Sunil; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "Resonance assignments for the RLIP76 Ral binding domain in its free form and in complex with the small G protein RalB" Biomol. NMR Assignments 2, 191-194 (2008).
PubMed: 19636902
Assembly members:
RLIP76, polymer, 56 residues, Formula weight is not available
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 Vector: pGEX-2T
Entity Sequences (FASTA):
RLIP76: GSETQAGIKEEIRRQEFLLN
SLHRDLQGGIKDLSKEERLW
EVQRILTALKRKLREA
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 419 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RLIP76 | 1 |
Entities:
Entity 1, RLIP76 56 residues - Formula weight is not available
The first two residues are a tag remnant. The protein starts at E393 and ends at A446
| 1 | GLY | SER | GLU | THR | GLN | ALA | GLY | ILE | LYS | GLU | ||||
| 2 | GLU | ILE | ARG | ARG | GLN | GLU | PHE | LEU | LEU | ASN | ||||
| 3 | SER | LEU | HIS | ARG | ASP | LEU | GLN | GLY | GLY | ILE | ||||
| 4 | LYS | ASP | LEU | SER | LYS | GLU | GLU | ARG | LEU | TRP | ||||
| 5 | GLU | VAL | GLN | ARG | ILE | LEU | THR | ALA | LEU | LYS | ||||
| 6 | ARG | LYS | LEU | ARG | GLU | ALA |
Samples:
sample_1: RLIP76, [U-98% 15N], 0.8 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 10 mM; magnesium chloride 1 mM
sample_conditions_1: pH: 6.3; 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-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AZARA, Boucher - processing
Analysis, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides and Laue - chemical shift assignment
NMR spectrometers:
- Bruker DRX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks