BMRB Entry 18776
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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/BMR18776
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Title: 1H, 13C, 15N backbone NMR resonance assignments for N-terminal RNA recognition motif of HvRBP1 from Hordeum vulgare L. (barley) PubMed: 23417794
Deposition date: 2012-10-10 Original release date: 2013-01-22
Authors: Mason, Katelyn; Tripet, Brian; Fischer, Andreas; Copie, Valerie
Citation: Mason, Katelyn; Tripet, Brian; Parrott, David; Fischer, Andreas; Copie, Valerie. "(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence." Biomol. NMR Assignments ., .-. (2013).
Assembly members:
RBP1, polymer, 92 residues, Formula weight is not available
Natural source: Common Name: barley Taxonomy ID: 4513 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Hordeum Hordeum vulgare L.
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RBP1: MAESDGAEYRCFVGSLSWNT
DDRGLEAAFSSFGEILDAKI
INDRETGRSRGFGFVSFSNE
QAMQDAIEGMNGKELDGRSI
VVNEAQSRGYGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 248 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 443 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hordeum vulgare glycine rich- RNA binding protein 1 | 1 |
Entities:
Entity 1, Hordeum vulgare glycine rich- RNA binding protein 1 92 residues - Formula weight is not available
N-Terminal RNA recognition Domain of RBP1
| 1 | MET | ALA | GLU | SER | ASP | GLY | ALA | GLU | TYR | ARG | ||||
| 2 | CYS | PHE | VAL | GLY | SER | LEU | SER | TRP | ASN | THR | ||||
| 3 | ASP | ASP | ARG | GLY | LEU | GLU | ALA | ALA | PHE | SER | ||||
| 4 | SER | PHE | GLY | GLU | ILE | LEU | ASP | ALA | LYS | ILE | ||||
| 5 | ILE | ASN | ASP | ARG | GLU | THR | GLY | ARG | SER | ARG | ||||
| 6 | GLY | PHE | GLY | PHE | VAL | SER | PHE | SER | ASN | GLU | ||||
| 7 | GLN | ALA | MET | GLN | ASP | ALA | ILE | GLU | GLY | MET | ||||
| 8 | ASN | GLY | LYS | GLU | LEU | ASP | GLY | ARG | SER | ILE | ||||
| 9 | VAL | VAL | ASN | GLU | ALA | GLN | SER | ARG | GLY | TYR | ||||
| 10 | GLY | GLY |
Samples:
15N_13C_HvGR-RBP1: RBP1, [U-99% 13C; U-99% 15N], 15 mM; sodium azide 0.01%; potassium phosphate 50 mM; D2O 5%; EDTA 1 mM; sodium chloride 500 mM; PMSF 1 mM
15N_13C_HvGr_RBP1_conditions_1: ionic strength: 1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 2D 1H-13C HSQC | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D HCCH-TOCSY | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D H(CCO)NH | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D CBCA(CO)NH | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D C(CO)NH | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D HNCACB | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D HBHA(CO)NH | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D 1H-15N NOESY | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
| 3D 1H-13C NOESY | 15N_13C_HvGR-RBP1 | isotropic | 15N_13C_HvGr_RBP1_conditions_1 |
Software:
TOPSPIN v2.1, Bruker BioSpin - collection
SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking
NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift indexing, Spectrum processing
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts