BMRB Entry 16045
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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/BMR16045
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Title: 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal EF-Hand domain of human cardiac sodium channel NaV1.5 PubMed: 19074138
Deposition date: 2008-11-28 Original release date: 2009-02-09
Authors: Chagot, Benjamin; Potet, Franck; Balser, Jeffrey; Chazin, Walter
Citation: Chagot, Benjamin; Potet, Franck; Balser, Jeffrey; Chazin, Walter. "Solution NMR structure of the C-terminal EF-Hand domain of human cardiac sodium channel NaV1.5" J. Biol. Chem. 284, 6436-6445 (2009).
Assembly members:
hH1, polymer, 97 residues, 10994.295 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
Entity Sequences (FASTA):
hH1: GPGSENFSVATEESTEPLSE
DDFDMFYEIWEKFDPEATQF
IEYSVLSDFADALSEPLRIA
KPNQISLINMDLPMVSGDRI
HCMDILFAFTKRVLGES
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 381 |
15N chemical shifts | 96 |
1H chemical shifts | 673 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | hH1 | 1 |
Entities:
Entity 1, hH1 97 residues - 10994.295 Da.
Residues 1-4 represent a non-native affinity tag
1 | GLY | PRO | GLY | SER | GLU | ASN | PHE | SER | VAL | ALA | ||||
2 | THR | GLU | GLU | SER | THR | GLU | PRO | LEU | SER | GLU | ||||
3 | ASP | ASP | PHE | ASP | MET | PHE | TYR | GLU | ILE | TRP | ||||
4 | GLU | LYS | PHE | ASP | PRO | GLU | ALA | THR | GLN | PHE | ||||
5 | ILE | GLU | TYR | SER | VAL | LEU | SER | ASP | PHE | ALA | ||||
6 | ASP | ALA | LEU | SER | GLU | PRO | LEU | ARG | ILE | ALA | ||||
7 | LYS | PRO | ASN | GLN | ILE | SER | LEU | ILE | ASN | MET | ||||
8 | ASP | LEU | PRO | MET | VAL | SER | GLY | ASP | ARG | ILE | ||||
9 | HIS | CYS | MET | ASP | ILE | LEU | PHE | ALA | PHE | THR | ||||
10 | LYS | ARG | VAL | LEU | GLY | GLU | SER |
Samples:
sample_1: hH1, [U-100% 13C; U-100% 15N], 1.2 mM; H2O 100%; phosphate 100 mM; NaCl 200 mM; beta-mercaptoethanol 5 mM; NaN3 0.01%
sample_2: hH1 1.2 mM; H2O 100%; phosphate 100 mM; NaCl 200 mM; beta-mercaptoethanol 5 mM; NaN3 0.01%
sample_conditions_1: pH: 6.5; 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 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.0, Bruker Biospin - collection, processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker AMX 600 MHz
Related Database Links:
BMRB | 16031 |
PDB | |
DBJ | BAD12084 BAD12085 BAD92103 BAE27800 BAE27966 |
EMBL | CAB70096 CAD88248 |
GB | AAA42114 AAA58644 AAI40814 AAI44622 AAI72643 |
REF | NP_000326 NP_001002994 NP_001092874 NP_001092875 NP_001153632 |
SP | P15389 Q14524 Q9JJV9 |
TPG | DAA34921 |
Download simulated HSQC data in one of the following formats:
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