BMRB Entry 18302
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18302
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Title: Solution structure of the calcium-bound CaM N-terminal domain in a complex. PubMed: 22518098
Deposition date: 2012-02-29 Original release date: 2012-06-04
Authors: Liu, Zhihong
Citation: Liu, Zhihong; Vogel, Hans. "Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca(2+)-calmodulin." Front. Mol. Neurosci. 5, 38-38 (2012).
Assembly members:
CaM N-terminal domain, polymer, 77 residues, 8583.593 Da.
NSCaTE peptide, polymer, 24 residues, Formula weight is not available
entity_CA, 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
Entity Sequences (FASTA):
CaM N-terminal domain: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMK
NSCaTE peptide: GTGAALSWQAAIDAARQAKL
MGSA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 364 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 447 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CaM N-terminal domain | 1 |
| 2 | NSCaTE peptide | 2 |
| 3 | Calcium ion, 1 | 3 |
| 4 | Calcium ion, 2 | 3 |
Entities:
Entity 1, CaM N-terminal domain 77 residues - 8583.593 Da.
| 1 | ALA | ASP | GLN | LEU | THR | GLU | GLU | GLN | ILE | ALA | ||||
| 2 | GLU | PHE | LYS | GLU | ALA | PHE | SER | LEU | PHE | ASP | ||||
| 3 | LYS | ASP | GLY | ASP | GLY | THR | ILE | THR | THR | LYS | ||||
| 4 | GLU | LEU | GLY | THR | VAL | MET | ARG | SER | LEU | GLY | ||||
| 5 | GLN | ASN | PRO | THR | GLU | ALA | GLU | LEU | GLN | ASP | ||||
| 6 | MET | ILE | ASN | GLU | VAL | ASP | ALA | ASP | GLY | ASN | ||||
| 7 | GLY | THR | ILE | ASP | PHE | PRO | GLU | PHE | LEU | THR | ||||
| 8 | MET | MET | ALA | ARG | LYS | MET | LYS |
Entity 2, NSCaTE peptide 24 residues - Formula weight is not available
| 1 | GLY | THR | GLY | ALA | ALA | LEU | SER | TRP | GLN | ALA | ||||
| 2 | ALA | ILE | ASP | ALA | ALA | ARG | GLN | ALA | LYS | LEU | ||||
| 3 | MET | GLY | SER | ALA |
Entity 3, Calcium ion, 1 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: calmodulin, [U-100% 13C; U-100% 15N], 1 mM; NSCaTE peptide 2 mM; H2O 55 M; D2O, [U-99% 2H], 5 M; DTT 10 mM; TRIS 20 mM
sample_2: NSCaTE peptide, [U-100% 13C; U-100% 15N], 1 mM; calmodulin 0.5 mM; H2O 55 M; D2O, [U-99% 2H], 5 M; DTT 10 mM; TRIS 20 mM
sample_3: calmodulin, [U-100% 13C; U-100% 15N], 1 mM; NSCaTE peptide 2 mM; Pf1 phage 7.5 mg
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | anisotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
TALOS, Cornilescu, Delaglio and Bax - data analysis
xwinnmr, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 500 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts