BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16045

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

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts96
1H chemical shifts673

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1hH11

Entities:

Entity 1, hH1 97 residues - 10994.295 Da.

Residues 1-4 represent a non-native affinity tag

1   GLYPROGLYSERGLUASNPHESERVALALA
2   THRGLUGLUSERTHRGLUPROLEUSERGLU
3   ASPASPPHEASPMETPHETYRGLUILETRP
4   GLULYSPHEASPPROGLUALATHRGLNPHE
5   ILEGLUTYRSERVALLEUSERASPPHEALA
6   ASPALALEUSERGLUPROLEUARGILEALA
7   LYSPROASNGLNILESERLEUILEASNMET
8   ASPLEUPROMETVALSERGLYASPARGILE
9   HISCYSMETASPILELEUPHEALAPHETHR
10   LYSARGVALLEUGLYGLUSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_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:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts