BMRB Entry 17948
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17948
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Title: NMR structure of Hsp12 in the presence of DPC PubMed: 21998307
Deposition date: 2011-09-20 Original release date: 2011-10-28
Authors: Singarapu, Kiran; Markley, John
Citation: Singarapu, Kiran; Tonelli, Marco; Chow, Darius; Frederick, Ronnie; Westler, William; Markley, John. "Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally -helical." J. Biol. Chem. 286, 43447-43453 (2011).
Assembly members:
Hsp12, polymer, 109 residues, 11712.830 Da.
Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Hsp12: MSDAGRKGFGEKASEALKPD
SQKSYAEQGKEYITDKADKV
AGKVQPEDNKGVFQGVHDSA
EKGKDNAEGQGESLADQARD
YMGAAKSKLNDAVEYVSGRV
HGEEDPTKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 223 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 537 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hsp12 | 1 |
Entities:
Entity 1, Hsp12 109 residues - 11712.830 Da.
| 1 | MET | SER | ASP | ALA | GLY | ARG | LYS | GLY | PHE | GLY | ||||
| 2 | GLU | LYS | ALA | SER | GLU | ALA | LEU | LYS | PRO | ASP | ||||
| 3 | SER | GLN | LYS | SER | TYR | ALA | GLU | GLN | GLY | LYS | ||||
| 4 | GLU | TYR | ILE | THR | ASP | LYS | ALA | ASP | LYS | VAL | ||||
| 5 | ALA | GLY | LYS | VAL | GLN | PRO | GLU | ASP | ASN | LYS | ||||
| 6 | GLY | VAL | PHE | GLN | GLY | VAL | HIS | ASP | SER | ALA | ||||
| 7 | GLU | LYS | GLY | LYS | ASP | ASN | ALA | GLU | GLY | GLN | ||||
| 8 | GLY | GLU | SER | LEU | ALA | ASP | GLN | ALA | ARG | ASP | ||||
| 9 | TYR | MET | GLY | ALA | ALA | LYS | SER | LYS | LEU | ASN | ||||
| 10 | ASP | ALA | VAL | GLU | TYR | VAL | SER | GLY | ARG | VAL | ||||
| 11 | HIS | GLY | GLU | GLU | ASP | PRO | THR | LYS | LYS |
Samples:
sample_1: Hsp12, [U-13C; U-15N], 0.7 mM; DPC 200 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.9; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
VNMR, Varian - collection
XEASY, Bartels et al. - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 17482 17483 18523 |
| PDB | |
| DBJ | BAA09224 BAA14033 GAA23069 |
| EMBL | CAA39306 CAA86349 CAY79436 |
| GB | AAA34647 AAL06077 AAS56790 AHY75775 AJP38487 |
| REF | NP_116640 |
| SP | P22943 |
| TPG | DAA12425 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
or all simulated shifts