BMRB Entry 18268
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18268
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Title: Unliganded (apo) C-terminal EF-hand domain from human polycystin-2 PubMed: 22474326
Deposition date: 2012-02-15 Original release date: 2012-05-08
Authors: Petri, Edward; Celic, Andjelka; Ehrlich, Barbara; Boggon, Titus; Hodsdon, Michael
Citation: Celic, Andjelka; Petri, Edward; Benbow, Jennifer; Hodsdon, Michael; Ehrlich, Barbara; Boggon, Titus. "Calcium-induced Conformational Changes in C-terminal Tail of Polycystin-2 Are Necessary for Channel Gating." J. Biol. Chem. 287, 17232-17240 (2012).
Assembly members:
EF-hand_domain_of_polycystin-2, polymer, 78 residues, Formula weight is not available
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
EF-hand_domain_of_polycystin-2: NTVDDISESLRQGGGKLNFD
ELRQDLKGKGHTDAEIEAIF
TKYDQDGDQELTEHEHQQMR
DDLEKEREDLDLDHSSLP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 145 |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 163 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EF-hand_domain_of_polycystin-2 | 1 |
Entities:
Entity 1, EF-hand_domain_of_polycystin-2 78 residues - Formula weight is not available
| 1 | ASN | THR | VAL | ASP | ASP | ILE | SER | GLU | SER | LEU | ||||
| 2 | ARG | GLN | GLY | GLY | GLY | LYS | LEU | ASN | PHE | ASP | ||||
| 3 | GLU | LEU | ARG | GLN | ASP | LEU | LYS | GLY | LYS | GLY | ||||
| 4 | HIS | THR | ASP | ALA | GLU | ILE | GLU | ALA | ILE | PHE | ||||
| 5 | THR | LYS | TYR | ASP | GLN | ASP | GLY | ASP | GLN | GLU | ||||
| 6 | LEU | THR | GLU | HIS | GLU | HIS | GLN | GLN | MET | ARG | ||||
| 7 | ASP | ASP | LEU | GLU | LYS | GLU | ARG | GLU | ASP | LEU | ||||
| 8 | ASP | LEU | ASP | HIS | SER | SER | LEU | PRO |
Samples:
sample_1: EF-hand_domain_of_polycystin-2, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 298 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.2c, Varian - collection
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 16191 16590 17621 |
| PDB | |
| DBJ | BAG56956 BAG57494 |
| EMBL | CAG31243 CAI38797 |
| GB | AAC16004 AAC50520 AAC50933 AAI11455 AAI12262 |
| REF | NP_000288 NP_001026311 NP_001039777 NP_001232908 XP_001099242 |
| SP | Q13563 Q4GZT3 |
| TPG | DAA28806 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts