BMRB Entry 26338
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26338
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Walinda, Erik; Motosugi, Ryo; Kim, Taehee; Morimoto, Daichi; Sakata, Eri. "Molecular basis for a Ca2+ binding hierarchy in the EF-hand motifs of CaBP2
" J. Biol. Chem. ., .-..
Assembly members:
Calcium-binding protein 2, polymer, . residues, Formula weight is not available
CALCIUM ION, non-polymer, 40.078 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 BL21(DE3) Vector: pET28
Entity Sequences (FASTA):
Calcium-binding protein 2: GSHMQLDRELRPEEIEELQV
AFQEFDRDRDGYIGCRELGA
CMRTLGYMPTEMELIEISQQ
ISGGKVDFEDFVELMGPKLL
AETADMIGVRELRDAFREFD
TNGDGRISVGELRAALKALL
GERLSQREVDEILQDVDLNG
DGLVDFEEFVRMMSR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 426 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 150 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CaBP2 | 1 |
| 2 | Ca2+ | 2 |
Entities:
Entity 1, CaBP2 - Formula weight is not available
The first four residues (Gly-Ser-His-Met) are plasmid-derived and are not part of human CaBP2 protein. The sequence QLDRELRPEEIEELQVAFQEFDRDRDGYIGCRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGRISVGELRAALKALLGERLSQREVDEILQDVDLNGDGLVDFEEFVRMMSR corresponds to CaBP2 residues 70-220. See https://web.expasy.org/cgi-bin/protparam/protparam1?Q9NPB3@noft@ for details.
| 1 | GLY | SER | HIS | MET | GLN | LEU | ASP | ARG | GLU | LEU | ||||
| 2 | ARG | PRO | GLU | GLU | ILE | GLU | GLU | LEU | GLN | VAL | ||||
| 3 | ALA | PHE | GLN | GLU | PHE | ASP | ARG | ASP | ARG | ASP | ||||
| 4 | GLY | TYR | ILE | GLY | CYS | ARG | GLU | LEU | GLY | ALA | ||||
| 5 | CYS | MET | ARG | THR | LEU | GLY | TYR | MET | PRO | THR | ||||
| 6 | GLU | MET | GLU | LEU | ILE | GLU | ILE | SER | GLN | GLN | ||||
| 7 | ILE | SER | GLY | GLY | LYS | VAL | ASP | PHE | GLU | ASP | ||||
| 8 | PHE | VAL | GLU | LEU | MET | GLY | PRO | LYS | LEU | LEU | ||||
| 9 | ALA | GLU | THR | ALA | ASP | MET | ILE | GLY | VAL | ARG | ||||
| 10 | GLU | LEU | ARG | ASP | ALA | PHE | ARG | GLU | PHE | ASP | ||||
| 11 | THR | ASN | GLY | ASP | GLY | ARG | ILE | SER | VAL | GLY | ||||
| 12 | GLU | LEU | ARG | ALA | ALA | LEU | LYS | ALA | LEU | LEU | ||||
| 13 | GLY | GLU | ARG | LEU | SER | GLN | ARG | GLU | VAL | ASP | ||||
| 14 | GLU | ILE | LEU | GLN | ASP | VAL | ASP | LEU | ASN | GLY | ||||
| 15 | ASP | GLY | LEU | VAL | ASP | PHE | GLU | GLU | PHE | VAL | ||||
| 16 | ARG | MET | MET | SER | ARG |
Entity 2, Ca2+ - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: Calcium-binding protein 2, [U-13C; U-15N], 0.6 mM; TCEP 1 mM; sodium chloride 150 mM; calcium chloride 15 mM; HEPES 25 mM; DSS 0.2 mM; H2O 96%; D2O, [U-2H], 4%
sample_conditions_1: ionic strength: 0.1875 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.1875 M; pH: 6.2; 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-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_2 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 1D 1H | sample_1 | isotropic | sample_conditions_2 |
Software:
CcpNmr Analysis v2.5 - chemical shift assignment, data analysis, peak picking, refinement
TOPSPIN v3.1 - Acquisition
CYANA v3 - chemical shift assignment
NMRPipe - processing
NMR spectrometers:
- Bruker AVANCE II 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks