BMRB Entry 19167
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19167
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Title: Structural determination of the Citrus sinensis Poly(A)-Binding Protein CsPABP1
Deposition date: 2013-04-16 Original release date: 2014-04-14
Authors: Sforca, Mauricio; Domingues, Mariane; Zeri, Ana; Benedetti, Celso
Citation: Sforca, Mauricio; Domingues, Mariane; Zeri, Ana; Benedetti, Celso. "Structural determination of the Citrus sinensis Poly(A)-Binding Protein CsPABP1" To be Published ., .-..
Assembly members:
CsPABP1, polymer, 155 residues, 17187.258 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CsPABP1: MGSSHHHHHHSSGLVPRGSH
MGSDLEDMKKRLKEIEEEAG
ALREMQAKVEKEMGAVQDSS
STSATQAEKEEVDSRSIYVG
NVDYACTPEEVQQHFQSCGT
VNRVTILTDKFGQPKGFAYV
EFVEIDAVQNALLLNETELH
GRQLKVSAKRTNIPG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 447 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 626 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CsPABP1 | 1 |
Entities:
Entity 1, CsPABP1 155 residues - 17187.258 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | GLY | SER | ASP | LEU | GLU | ASP | MET | LYS | LYS | ||||
| 4 | ARG | LEU | LYS | GLU | ILE | GLU | GLU | GLU | ALA | GLY | ||||
| 5 | ALA | LEU | ARG | GLU | MET | GLN | ALA | LYS | VAL | GLU | ||||
| 6 | LYS | GLU | MET | GLY | ALA | VAL | GLN | ASP | SER | SER | ||||
| 7 | SER | THR | SER | ALA | THR | GLN | ALA | GLU | LYS | GLU | ||||
| 8 | GLU | VAL | ASP | SER | ARG | SER | ILE | TYR | VAL | GLY | ||||
| 9 | ASN | VAL | ASP | TYR | ALA | CYS | THR | PRO | GLU | GLU | ||||
| 10 | VAL | GLN | GLN | HIS | PHE | GLN | SER | CYS | GLY | THR | ||||
| 11 | VAL | ASN | ARG | VAL | THR | ILE | LEU | THR | ASP | LYS | ||||
| 12 | PHE | GLY | GLN | PRO | LYS | GLY | PHE | ALA | TYR | VAL | ||||
| 13 | GLU | PHE | VAL | GLU | ILE | ASP | ALA | VAL | GLN | ASN | ||||
| 14 | ALA | LEU | LEU | LEU | ASN | GLU | THR | GLU | LEU | HIS | ||||
| 15 | GLY | ARG | GLN | LEU | LYS | VAL | SER | ALA | LYS | ARG | ||||
| 16 | THR | ASN | ILE | PRO | GLY |
Samples:
sample_1: CsPABP1, [U-98% 15N], 0.6 mM; sodium phosphate 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%
sample_2: CsPABP1, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 50 mM; sodium chloride 20 mM; D2O 100%
sample_3: CsPABP1, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.70 M; pH: 6.4; 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-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAN77560 |
| GB | EEF51643 EOY22721 ESR50273 ESR50274 KDO57709 |
| REF | XP_002511041 XP_006437033 XP_006437034 XP_006485035 XP_007038220 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts