BMRB Entry 18877
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18877
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Title: 1H,13C,15N chemical shift assignment of Ca2+_bound CaBP4 PubMed: 23925854
Deposition date: 2012-12-05 Original release date: 2014-02-14
Authors: Ames, James
Citation: Park, Saebomi; Li, Congmin; Ames, James. "(1)H, (15)N, and (13)C chemical shift assignments of murine calcium-binding protein 4." Biomol. NMR Assignments ., .-. (2013).
Assembly members:
CaBP4, polymer, 271 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CaBP4: MATEHNVQLVPGSQKIPKGV
VSPRSAAEGPALTRRRSKKE
SWHPGSQKASSGDQSSSQGS
EASGSSKHPPRTKVGQEEPS
SAPARPASHRHSHRHRSDPQ
QDAAQRTYGPLLNRMFGKDR
ELGPEELEELQAAFEEFDTD
QDGYIGYRELGDCMRTLGYM
PTEMELLEVSQHVKMRMGGF
VDFEEFVELISPKLREETAH
MLGVRELRIAFREFDKDRDG
RITVAELRQAAPALLGEPLE
GTELDEMLREMDLNGDGTID
FDEFVMMLSTG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 159 |
| 1H chemical shifts | 761 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CaBP4 polypeptide | 1 |
Entities:
Entity 1, CaBP4 polypeptide 271 residues - Formula weight is not available
| 1 | MET | ALA | THR | GLU | HIS | ASN | VAL | GLN | LEU | VAL | ||||
| 2 | PRO | GLY | SER | GLN | LYS | ILE | PRO | LYS | GLY | VAL | ||||
| 3 | VAL | SER | PRO | ARG | SER | ALA | ALA | GLU | GLY | PRO | ||||
| 4 | ALA | LEU | THR | ARG | ARG | ARG | SER | LYS | LYS | GLU | ||||
| 5 | SER | TRP | HIS | PRO | GLY | SER | GLN | LYS | ALA | SER | ||||
| 6 | SER | GLY | ASP | GLN | SER | SER | SER | GLN | GLY | SER | ||||
| 7 | GLU | ALA | SER | GLY | SER | SER | LYS | HIS | PRO | PRO | ||||
| 8 | ARG | THR | LYS | VAL | GLY | GLN | GLU | GLU | PRO | SER | ||||
| 9 | SER | ALA | PRO | ALA | ARG | PRO | ALA | SER | HIS | ARG | ||||
| 10 | HIS | SER | HIS | ARG | HIS | ARG | SER | ASP | PRO | GLN | ||||
| 11 | GLN | ASP | ALA | ALA | GLN | ARG | THR | TYR | GLY | PRO | ||||
| 12 | LEU | LEU | ASN | ARG | MET | PHE | GLY | LYS | ASP | ARG | ||||
| 13 | GLU | LEU | GLY | PRO | GLU | GLU | LEU | GLU | GLU | LEU | ||||
| 14 | GLN | ALA | ALA | PHE | GLU | GLU | PHE | ASP | THR | ASP | ||||
| 15 | GLN | ASP | GLY | TYR | ILE | GLY | TYR | ARG | GLU | LEU | ||||
| 16 | GLY | ASP | CYS | MET | ARG | THR | LEU | GLY | TYR | MET | ||||
| 17 | PRO | THR | GLU | MET | GLU | LEU | LEU | GLU | VAL | SER | ||||
| 18 | GLN | HIS | VAL | LYS | MET | ARG | MET | GLY | GLY | PHE | ||||
| 19 | VAL | ASP | PHE | GLU | GLU | PHE | VAL | GLU | LEU | ILE | ||||
| 20 | SER | PRO | LYS | LEU | ARG | GLU | GLU | THR | ALA | HIS | ||||
| 21 | MET | LEU | GLY | VAL | ARG | GLU | LEU | ARG | ILE | ALA | ||||
| 22 | PHE | ARG | GLU | PHE | ASP | LYS | ASP | ARG | ASP | GLY | ||||
| 23 | ARG | ILE | THR | VAL | ALA | GLU | LEU | ARG | GLN | ALA | ||||
| 24 | ALA | PRO | ALA | LEU | LEU | GLY | GLU | PRO | LEU | GLU | ||||
| 25 | GLY | THR | GLU | LEU | ASP | GLU | MET | LEU | ARG | GLU | ||||
| 26 | MET | ASP | LEU | ASN | GLY | ASP | GLY | THR | ILE | ASP | ||||
| 27 | PHE | ASP | GLU | PHE | VAL | MET | MET | LEU | SER | THR | ||||
| 28 | GLY |
Samples:
sample_1: CaBP4, [U-13C; U-15N; U-2H], 0.5 mM
sample_2: CaBP4, [U-15N], 0.5 mM
sample_3: CaBP4, [U-13C; U-15N], 0.5 mM
sample_4: CaBP4 0.5 mM
sample_5: CaBP4, [U-10% 13C; U-99% 15N], 0.5 mM
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 310 K
sample_conditions_2: pH: 7.4; pressure: 1 atm; temperature: 310 K
sample_conditions_3: pH: 7.4; pressure: 1 atm; temperature: 310 K
sample_conditions_4: pH: 7.4; pressure: 1 atm; temperature: 310 K
sample_conditions_5: pH: 7.4; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_3 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_3 |
| Trosy HNCACB | sample_1 | isotropic | sample_conditions_1 |
| Trosy HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_2 |
| 2D 1H-1H COSY | sample_4 | isotropic | sample_conditions_4 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_4 |
| 13C CT-HSQC | sample_5 | isotropic | sample_conditions_5 |
Software:
SPARKY, Goddard - processing
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| GB | AAH49263 AAK83463 EDL33015 EDL33016 |
| REF | NP_653115 XP_006531910 XP_006531911 XP_006531912 XP_006544976 |
| SP | Q8VHC5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts