BMRB Entry 34188
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34188
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Jemth, Per; Karlsson, Elin; Vogeli, Beat; Guzovsky, Brenda; Andersson, Eva; Hultqvist, Greta; Dogan, Jakob; Guntert, Peter; Riek, Roland; Chi, Celestine. "Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins" Sci. Adv. 4, eaau4130-eaau4130 (2018).
PubMed: 30397651
Assembly members:
entity_1, polymer, 45 residues, 4823.197 Da.
entity_2, polymer, 50 residues, 5594.450 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):
entity_1: GSESQNDEKALLDQLDSLLS
STDEMELAEIDRALGIDKLV
SQQGG
entity_2: GSIPPNALQDLLRTLRSPSS
PQQQQQVLNILKSNPQLMAA
FIKQRAAKYQ
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 221 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 588 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 45 residues - 4823.197 Da.
| 1 | GLY | SER | GLU | SER | GLN | ASN | ASP | GLU | LYS | ALA | ||||
| 2 | LEU | LEU | ASP | GLN | LEU | ASP | SER | LEU | LEU | SER | ||||
| 3 | SER | THR | ASP | GLU | MET | GLU | LEU | ALA | GLU | ILE | ||||
| 4 | ASP | ARG | ALA | LEU | GLY | ILE | ASP | LYS | LEU | VAL | ||||
| 5 | SER | GLN | GLN | GLY | GLY |
Entity 2, entity_2 50 residues - 5594.450 Da.
| 1 | GLY | SER | ILE | PRO | PRO | ASN | ALA | LEU | GLN | ASP | |
| 2 | LEU | LEU | ARG | THR | LEU | ARG | SER | PRO | SER | SER | |
| 3 | PRO | GLN | GLN | GLN | GLN | GLN | VAL | LEU | ASN | ILE | |
| 4 | LEU | LYS | SER | ASN | PRO | GLN | LEU | MET | ALA | ALA | |
| 5 | PHE | ILE | LYS | GLN | ARG | ALA | ALA | LYS | TYR | GLN |
Samples:
sample_1: entity_1, [U-99% 15N; U-13C], 100 uM; entity_2, [U-99% 15N; U-13C], 100 uM
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 Pa; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2J HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | anisotropic | sample_conditions_1 |
| filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker AvanceII 700 MHz
- Bruker AvanceIII 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks