Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50256
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NMR-STAR v3 text file.
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Citation: Ramirez de Mingo, Daniel; Pantoja-Uceda, David; Carrion-Vazquez, Mariano; Laurents, Douglas. "Human CPEB3's Prion-Like Domain: Preferred Conformations and Implications for Memory Consolidation" Mol. Cell ., .-..
Assembly members:
entity_1, polymer, 450 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: pLL3.7-syn
| Data type | Count |
| 13C chemical shifts | 1416 |
| 15N chemical shifts | 441 |
| 1H chemical shifts | 384 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entity 1, entity_1 450 residues - Formula weight is not available
| 1 | MET | GLN | ASP | ASP | LEU | LEU | MET | ASP | LYS | SER | |
| 2 | LYS | THR | GLN | PRO | GLN | PRO | GLN | GLN | GLN | GLN | |
| 3 | ARG | GLN | GLN | GLN | GLN | PRO | GLN | PRO | GLU | SER | |
| 4 | SER | VAL | SER | GLU | ALA | PRO | SER | THR | PRO | LEU | |
| 5 | SER | SER | GLU | THR | PRO | LYS | PRO | GLU | GLU | ASN | |
| 6 | SER | ALA | VAL | PRO | ALA | LEU | SER | PRO | ALA | ALA | |
| 7 | ALA | PRO | PRO | ALA | PRO | ASN | GLY | PRO | ASP | LYS | |
| 8 | MET | GLN | MET | GLU | SER | PRO | LEU | LEU | PRO | GLY | |
| 9 | LEU | SER | PHE | HIS | GLN | PRO | PRO | GLN | GLN | PRO | |
| 10 | PRO | PRO | PRO | GLN | GLU | PRO | ALA | ALA | PRO | GLY | |
| 11 | ALA | SER | LEU | SER | PRO | SER | PHE | GLY | SER | THR | |
| 12 | TRP | SER | THR | GLY | THR | THR | ASN | ALA | VAL | GLU | |
| 13 | ASP | SER | PHE | PHE | GLN | GLY | ILE | THR | PRO | VAL | |
| 14 | ASN | GLY | THR | MET | LEU | PHE | GLN | ASN | PHE | PRO | |
| 15 | HIS | HIS | VAL | ASN | PRO | VAL | PHE | GLY | GLY | THR | |
| 16 | PHE | SER | PRO | GLN | ILE | GLY | LEU | ALA | GLN | THR | |
| 17 | GLN | HIS | HIS | GLN | GLN | PRO | PRO | PRO | PRO | ALA | |
| 18 | PRO | ALA | PRO | GLN | PRO | ALA | GLN | PRO | ALA | GLN | |
| 19 | PRO | PRO | GLN | ALA | GLN | PRO | PRO | GLN | GLN | ARG | |
| 20 | ARG | SER | PRO | ALA | SER | PRO | SER | GLN | ALA | PRO | |
| 21 | TYR | ALA | GLN | ARG | SER | ALA | ALA | ALA | ALA | TYR | |
| 22 | GLY | HIS | GLN | PRO | ILE | MET | THR | SER | LYS | PRO | |
| 23 | SER | SER | SER | SER | ALA | VAL | ALA | ALA | ALA | ALA | |
| 24 | ALA | ALA | ALA | ALA | ALA | SER | SER | ALA | SER | SER | |
| 25 | SER | TRP | ASN | THR | HIS | GLN | SER | VAL | ASN | ALA | |
| 26 | ALA | TRP | SER | ALA | PRO | SER | ASN | PRO | TRP | GLY | |
| 27 | GLY | LEU | GLN | ALA | GLY | ARG | ASP | PRO | ARG | ARG | |
| 28 | ALA | VAL | GLY | VAL | GLY | VAL | GLY | VAL | GLY | VAL | |
| 29 | GLY | VAL | PRO | SER | PRO | LEU | ASN | PRO | ILE | SER | |
| 30 | PRO | LEU | LYS | LYS | PRO | PHE | SER | SER | ASN | VAL | |
| 31 | ILE | ALA | PRO | PRO | LYS | PHE | PRO | ARG | ALA | ALA | |
| 32 | PRO | LEU | THR | SER | LYS | SER | TRP | MET | GLU | ASP | |
| 33 | ASN | ALA | PHE | ARG | THR | ASP | ASN | GLY | ASN | ASN | |
| 34 | LEU | LEU | PRO | PHE | GLN | ASP | ARG | SER | ARG | PRO | |
| 35 | TYR | ASP | THR | PHE | ASN | LEU | HIS | SER | LEU | GLU | |
| 36 | ASN | SER | LEU | MET | ASP | MET | ILE | ARG | THR | ASP | |
| 37 | HIS | GLU | PRO | LEU | LYS | GLY | ARG | MET | GLY | ILE | |
| 38 | ASN | PHE | HIS | HIS | PRO | GLY | THR | ASP | ASN | ILE | |
| 39 | MET | ALA | LEU | ASN | SER | ARG | SER | SER | LEU | PHE | |
| 40 | PRO | PHE | GLU | ASP | ALA | PHE | LEU | ASP | ASP | SER | |
| 41 | HIS | GLY | ASP | GLN | ALA | LEU | SER | SER | GLY | LEU | |
| 42 | SER | SER | PRO | THR | ARG | CYS | GLN | ASN | GLY | GLU | |
| 43 | ARG | VAL | GLU | ARG | TYR | SER | ARG | LYS | VAL | PHE | |
| 44 | VAL | GLY | GLY | LEU | PRO | PRO | ASP | ILE | ASP | GLU | |
| 45 | ASP | GLU | ILE | THR | ALA | SER | PHE | ARG | ARG | PHE |
sample_1: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM
sample_2: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 0.4 ± 0.1 mM
sample_3: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM
sample_4: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM
sample_5: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM
sample_6: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 0.6 ± 0.1 mM
sample_7: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 0.6 ± 0.1 mM
sample_conditions_1: ionic strength: 0.0010 M; pH: 4.0; pressure: 0.93 atm; temperature: 298.2 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_1 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_1 | isotropic | sample_conditions_1 |
| 1D 1H | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_2 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_2 | isotropic | sample_conditions_1 |
| 1D 1H | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_3 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_3 | isotropic | sample_conditions_1 |
| 1D 1H | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_4 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_4 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_4 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_4 | isotropic | sample_conditions_1 |
| 1D 1H | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_5 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_5 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_5 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_5 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_5 | isotropic | sample_conditions_1 |
| 1D 1H | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_6 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_6 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_6 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_6 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_6 | isotropic | sample_conditions_1 |
| 1D 1H | sample_7 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_7 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_7 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_7 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_7 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_7 | isotropic | sample_conditions_1 |
SPARKY v3.12 - chemical shift assignment
TOPSPIN v2.1 - collection
NMRPipe - data analysis
TALOS+ - structure solution
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks