BMRB Entry 19775
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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/BMR19775
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Title: Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in free state PubMed: 24990967
Deposition date: 2014-02-07 Original release date: 2014-07-21
Authors: Afroz, Tariq; Skrisovska, Lenka; Belloc, Eulalia; Boixet, Jordina; Mendez, Raul; Allain, Frederic
Citation: Afroz, Tariq; Skrisovska, Lenka; Belloc, Eulalia; Boixet, Jordina; Mendez, Raul; Allain, Frederic. "A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins" Genes Dev. 28, 1498-1514 (2014).
Assembly members:
CPEB1RRM12, polymer, 217 residues, 23817.588 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):
CPEB1RRM12: MTWSGQLPPRNYKNPIYSCK
VFLGGVPWDITEAGLVNTFR
VFGSLSVEWPGKDGKHPRCP
PKGYVYLVFELEKSVRSLLQ
ACSHDPLSPDGLSEYYFKMS
SRRMRCKEVQVIPWVLADSN
FVRSPSQRLDPSRTVFVGAL
HGMLNAEALAAILNDLFGGV
VYAGIDTDKHKYPIGSGRVT
FNNQRSYLKAVSAAFVEIKT
TKFTKKVQIDPYLEDSL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 563 |
| 15N chemical shifts | 212 |
| 1H chemical shifts | 1262 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CPEB1RRM12 | 1 |
Entities:
Entity 1, CPEB1RRM12 217 residues - 23817.588 Da.
| 1 | MET | THR | TRP | SER | GLY | GLN | LEU | PRO | PRO | ARG | ||||
| 2 | ASN | TYR | LYS | ASN | PRO | ILE | TYR | SER | CYS | LYS | ||||
| 3 | VAL | PHE | LEU | GLY | GLY | VAL | PRO | TRP | ASP | ILE | ||||
| 4 | THR | GLU | ALA | GLY | LEU | VAL | ASN | THR | PHE | ARG | ||||
| 5 | VAL | PHE | GLY | SER | LEU | SER | VAL | GLU | TRP | PRO | ||||
| 6 | GLY | LYS | ASP | GLY | LYS | HIS | PRO | ARG | CYS | PRO | ||||
| 7 | PRO | LYS | GLY | TYR | VAL | TYR | LEU | VAL | PHE | GLU | ||||
| 8 | LEU | GLU | LYS | SER | VAL | ARG | SER | LEU | LEU | GLN | ||||
| 9 | ALA | CYS | SER | HIS | ASP | PRO | LEU | SER | PRO | ASP | ||||
| 10 | GLY | LEU | SER | GLU | TYR | TYR | PHE | LYS | MET | SER | ||||
| 11 | SER | ARG | ARG | MET | ARG | CYS | LYS | GLU | VAL | GLN | ||||
| 12 | VAL | ILE | PRO | TRP | VAL | LEU | ALA | ASP | SER | ASN | ||||
| 13 | PHE | VAL | ARG | SER | PRO | SER | GLN | ARG | LEU | ASP | ||||
| 14 | PRO | SER | ARG | THR | VAL | PHE | VAL | GLY | ALA | LEU | ||||
| 15 | HIS | GLY | MET | LEU | ASN | ALA | GLU | ALA | LEU | ALA | ||||
| 16 | ALA | ILE | LEU | ASN | ASP | LEU | PHE | GLY | GLY | VAL | ||||
| 17 | VAL | TYR | ALA | GLY | ILE | ASP | THR | ASP | LYS | HIS | ||||
| 18 | LYS | TYR | PRO | ILE | GLY | SER | GLY | ARG | VAL | THR | ||||
| 19 | PHE | ASN | ASN | GLN | ARG | SER | TYR | LEU | LYS | ALA | ||||
| 20 | VAL | SER | ALA | ALA | PHE | VAL | GLU | ILE | LYS | THR | ||||
| 21 | THR | LYS | PHE | THR | LYS | LYS | VAL | GLN | ILE | ASP | ||||
| 22 | PRO | TYR | LEU | GLU | ASP | SER | LEU |
Samples:
sample_1: CPEB1RRM12, [U-100% 15N], 0.4 – 0.6 mM; sodium chloride 100 mM; DTT 1 mM; magnesium sulphate 1 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%
sample_2: CPEB1RRM12, [U-100% 13C; U-100% 15N], 0.4 – 0.6 mM; sodium chloride 100 mM; DTT 1 mM; magnesium sulphate 1 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%
sample_3: CPEB1RRM12, [U-100% 13C; U-100% 15N; U-100% 2H], 0.4 – 0.6 mM; sodium chloride 100 mM; DTT 1 mM; magnesium sulphate 1 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 303 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 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | 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 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
| BMRB | 19778 |
| PDB | |
| DBJ | BAB14496 BAB33089 BAE87429 BAG63194 BAH11723 |
| EMBL | CAH92427 |
| GB | AAH35348 AAH50629 AAK01239 AAK01240 ADQ32841 |
| REF | NP_001073001 NP_001073002 NP_001073003 NP_001126432 NP_001239455 |
| SP | Q5R733 Q9BZB8 |
| TPG | DAA17635 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts