Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53475
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Citation: Reichheld, Sean; Muiznieks, Lisa; Liu, Zi Hao; Payliss, Brandon; Keeley, Fred; Sharpe, Simon. "A free energy landscape screen reveals the disordered conformational ensemble of tropoelastin" .
Assembly members:
entity_1, polymer, 228 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: pet32b
| Data type | Count |
| 13C chemical shifts | 589 |
| 15N chemical shifts | 199 |
| 1H chemical shifts | 430 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hTE_18-26 | 1 |
Entity 1, hTE_18-26 228 residues - Formula weight is not available
| 1 | ALA | GLY | VAL | PRO | GLY | VAL | GLY | VAL | PRO | GLY | ||||
| 2 | ALA | GLY | ILE | PRO | VAL | VAL | PRO | GLY | ALA | GLY | ||||
| 3 | ILE | PRO | GLY | ALA | ALA | VAL | PRO | GLY | VAL | VAL | ||||
| 4 | SER | PRO | GLU | ALA | ALA | ALA | LYS | ALA | ALA | ALA | ||||
| 5 | LYS | ALA | ALA | LYS | TYR | GLY | ALA | ARG | PRO | GLY | ||||
| 6 | VAL | GLY | VAL | GLY | GLY | ILE | PRO | THR | TYR | GLY | ||||
| 7 | VAL | GLY | ALA | GLY | GLY | PHE | PRO | GLY | PHE | GLY | ||||
| 8 | VAL | GLY | VAL | GLY | GLY | ILE | PRO | GLY | VAL | ALA | ||||
| 9 | GLY | VAL | PRO | GLY | VAL | GLY | GLY | VAL | PRO | GLY | ||||
| 10 | VAL | GLY | GLY | VAL | PRO | GLY | VAL | GLY | ILE | SER | ||||
| 11 | PRO | GLU | ALA | GLN | ALA | ALA | ALA | ALA | ALA | LYS | ||||
| 12 | ALA | ALA | LYS | TYR | GLY | VAL | GLY | THR | PRO | ALA | ||||
| 13 | ALA | ALA | ALA | ALA | LYS | ALA | ALA | ALA | LYS | ALA | ||||
| 14 | ALA | GLN | PHE | GLY | LEU | VAL | PRO | GLY | VAL | GLY | ||||
| 15 | VAL | ALA | PRO | GLY | VAL | GLY | VAL | ALA | PRO | GLY | ||||
| 16 | VAL | GLY | VAL | ALA | PRO | GLY | VAL | GLY | LEU | ALA | ||||
| 17 | PRO | GLY | VAL | GLY | VAL | ALA | PRO | GLY | VAL | GLY | ||||
| 18 | VAL | ALA | PRO | GLY | VAL | GLY | VAL | ALA | PRO | GLY | ||||
| 19 | ILE | GLY | PRO | GLY | GLY | VAL | ALA | ALA | ALA | ALA | ||||
| 20 | LYS | SER | ALA | ALA | LYS | VAL | ALA | ALA | LYS | ALA | ||||
| 21 | GLN | LEU | ARG | ALA | ALA | ALA | GLY | LEU | GLY | ALA | ||||
| 22 | GLY | ILE | PRO | GLY | LEU | GLY | VAL | GLY | VAL | GLY | ||||
| 23 | VAL | PRO | GLY | LEU | GLY | VAL | GLY | ALA |
sample_1: hTE fragment domains 18-26 monomer, [U-100% 13C; U-100% 15N], 1.3 mM; sodium phosphate 50 mM; sodium chloride 200 mM
sample_conditions_1: ionic strength: 0.25 M; pH: 7.0; pressure: 1 atm; temperature: 283 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HSQC-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCAN | sample_1 | isotropic | sample_conditions_1 |
| 3D HNN | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)N | sample_1 | isotropic | sample_conditions_1 |
TOPSPIN - collection
CcpNMR - chemical shift assignment
NMRPipe - processing
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks