BMRB Entry 51187
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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/BMR51187
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Title: Backbone and sidechain NMR assignments of the J-domain of co-chaperone Sis1 in complex with EEVD peptide of HSP70 PubMed: 37589820
Deposition date: 2021-11-23 Original release date: 2022-11-23
Authors: Matos, Carolina; Pinheiro, Glaucia; Ramos, Carlos; Almeida, Fabio
Citation: Matos, Carolina; Pinheiro, Glaucia; Ramos, Carlos; Almeida, Fabio. "Backbone and sidechain NMR assignments of residues 1-81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide" Biomol. NMR Assign. 17, 239-242 (2023).
Assembly members:
entity_1, polymer, 84 residues, Formula weight is not available
entity_2, polymer, 8 residues, Formula weight is not available
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pEt32a
Entity Sequences (FASTA):
entity_1: GMTSVKETKLYDLLGVSPSA
NEQELKKGYRKAALKYHPDK
PTGDTEKFKEISEAFEILND
PQKREIYDQYGLEAARSGGP
SFGP
entity_2: GPTIEEVD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 355 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 548 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | J-domain of Sis1 | 1 |
| 2 | HSP70 C-terminal tail octapeptide | 2 |
Entities:
Entity 1, J-domain of Sis1 84 residues - Formula weight is not available
| 1 | GLY | MET | THR | SER | VAL | LYS | GLU | THR | LYS | LEU | ||||
| 2 | TYR | ASP | LEU | LEU | GLY | VAL | SER | PRO | SER | ALA | ||||
| 3 | ASN | GLU | GLN | GLU | LEU | LYS | LYS | GLY | TYR | ARG | ||||
| 4 | LYS | ALA | ALA | LEU | LYS | TYR | HIS | PRO | ASP | LYS | ||||
| 5 | PRO | THR | GLY | ASP | THR | GLU | LYS | PHE | LYS | GLU | ||||
| 6 | ILE | SER | GLU | ALA | PHE | GLU | ILE | LEU | ASN | ASP | ||||
| 7 | PRO | GLN | LYS | ARG | GLU | ILE | TYR | ASP | GLN | TYR | ||||
| 8 | GLY | LEU | GLU | ALA | ALA | ARG | SER | GLY | GLY | PRO | ||||
| 9 | SER | PHE | GLY | PRO |
Entity 2, HSP70 C-terminal tail octapeptide 8 residues - Formula weight is not available
| 1 | GLY | PRO | THR | ILE | GLU | GLU | VAL | ASP |
Samples:
sample_1: Sis1 J-domain, [U-95% 13C; U-95% 15N], 1 mM; GPTIEEVD 4 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; 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_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS - chemical shift assignment, chemical shift calculation, data analysis
NMR spectrometers:
- Bruker AVANCE III 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts