BMRB Entry 17264
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17264
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Title: Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel NaV1.5 PubMed: 21167176
Deposition date: 2010-10-24 Original release date: 2010-12-22
Authors: Chagot, Benjamin; Chazin, Walter
Citation: Chagot, Benjamin; Chazin, Walter. "Solution NMR Structure of Apo-Calmodulin in Complex with the IQ Motif of Human Cardiac Sodium Channel NaV1.5." J. Mol. Biol. 406, 106-119 (2011).
Assembly members:
calmodulin, polymer, 148 residues, 16721.465 Da.
IQ_motif, polymer, 31 residues, 3529.137 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):
calmodulin: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
IQ_motif: GPGSEEVSAMVIQRAFRRHL
LQRSLKHASFL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 713 |
| 15N chemical shifts | 193 |
| 1H chemical shifts | 1236 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | calmodulin | 1 |
| 2 | IQ_motif | 2 |
Entities:
Entity 1, calmodulin 148 residues - 16721.465 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 | ASP | THR | ASP | ||||
| 9 | SER | GLU | GLU | GLU | ILE | ARG | GLU | ALA | PHE | ARG | ||||
| 10 | VAL | PHE | ASP | LYS | ASP | GLY | ASN | GLY | TYR | ILE | ||||
| 11 | SER | ALA | ALA | GLU | LEU | ARG | HIS | VAL | MET | THR | ||||
| 12 | ASN | LEU | GLY | GLU | LYS | LEU | THR | ASP | GLU | GLU | ||||
| 13 | VAL | ASP | GLU | MET | ILE | ARG | GLU | ALA | ASP | ILE | ||||
| 14 | ASP | GLY | ASP | GLY | GLN | VAL | ASN | TYR | GLU | GLU | ||||
| 15 | PHE | VAL | GLN | MET | MET | THR | ALA | LYS |
Entity 2, IQ_motif 31 residues - 3529.137 Da.
first 4 are cloning artefacts
| 1 | GLY | PRO | GLY | SER | GLU | GLU | VAL | SER | ALA | MET | ||||
| 2 | VAL | ILE | GLN | ARG | ALA | PHE | ARG | ARG | HIS | LEU | ||||
| 3 | LEU | GLN | ARG | SER | LEU | LYS | HIS | ALA | SER | PHE | ||||
| 4 | LEU |
Samples:
sample_1: calmodulin, [U-99% 13C; U-99% 15N], 1 mM; IQ_motif, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%; KCl 100 mM
sample_2: calmodulin 1 mM; IQ_motif 1 mM; H2O 95%; D2O 5%; KCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
SPARKY, Goddard - chemical shift assignment, data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
Related Database Links:
| BMRB | 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 16465 1648 16764 17360 17771 17807 18027 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310 |
| PDB | |
| DBJ | BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAD12084 BAD12085 BAD92103 |
| EMBL | CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 |
| GB | AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA58644 AAI40814 AAI44622 AAK74065 AAN61120 |
| PIR | JC1305 MCON |
| PRF | 0409298A 0608335A |
| REF | NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_000326 NP_001092874 NP_001092875 NP_001153632 NP_001153633 |
| SP | O02367 O16305 O96081 P02594 P05932 Q14524 |
| TPG | DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts