BMRB Entry 34497
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34497
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Title: Ca2+-free Calmodulin mutant N53I PubMed: 32317284
Deposition date: 2020-03-06 Original release date: 2020-04-27
Authors: Holt, C.; Hamborg, L.; Lau, K.; Brohus, M.; Sorensen, A.; Larsen, K.; Sommer, C.; Petegem, F.; Overgaard, M.; Wimmer, R.
Citation: Holt, C.; Hamborg, L.; Lau, K.; Brohus, M.; Sorensen, A.; Larsen, K.; Sommer, C.; Petegem, F.; Overgaard, M.; Wimmer, R.. "The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-domain, altering its interaction with the cardiac ryanodine receptor" J. Biol. Chem. ., .-. (2020).
Assembly members:
entity_1, polymer, 148 residues, 16720.404 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMIIEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 611 |
| 15N chemical shifts | 146 |
| 1H chemical shifts | 983 |
| T1 relaxation values | 139 |
| T2 relaxation values | 139 |
| heteronuclear NOE values | 139 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 148 residues - 16720.404 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 | ILE | 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 |
Samples:
sample_1: Calmodulin N53I, [U-99% 13C; U-99% 15N], 1.9 mM; HEPES 20 mM; potassium chloride 100 mM; EDTA 1 mM; sodium azide 2 mM; TSP 0.05 mM
sample_2: Calmodulin N53I, [U-99% 15N], 1.2 mM; HEPES 2 mM; potassium chloride 10 mM; EDTA 10 mM; sodium azide 2 mM; TSP 0.05 mM
sample_3: Calmodulin, [U-99% 13C; U-99% 15N], 1.2 mM; HEPES 2 mM; potassium chloride 10 mM; EDTA 10 mM; sodium azide 2 mM; TSP 0.05 mM
sample_conditions_1: ionic strength: 105 mM; pH: 6.3; pressure: 1 atm; temperature: 298.1 K
sample_conditions_2: ionic strength: 42 mM; pH: 6.56; pressure: 1 atm; temperature: 298.1 K
sample_conditions_3: ionic strength: 42 mM; pH: 6.53; pressure: 1 atm; temperature: 298.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | 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 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 15N-T2 | sample_2 | isotropic | sample_conditions_2 |
| 15N-T1 | sample_2 | isotropic | sample_conditions_2 |
| T2-relaxation dispersion | sample_2 | isotropic | sample_conditions_2 |
| {1H}-15N-NOE | sample_2 | isotropic | sample_conditions_2 |
| T2-relaxation dispersion | sample_3 | isotropic | sample_conditions_3 |
| {1H}-15N-NOE | sample_3 | isotropic | sample_conditions_3 |
| 15N-T2 | sample_3 | isotropic | sample_conditions_3 |
| 15N-T1 | sample_3 | isotropic | sample_conditions_3 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
YASARA v14.12.2, YASARA Biosciences GmbH - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
TALOS vTALOS+, Cornilescu, Delaglio and Bax - structure calculation
CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, peak picking
TopSpin v3.0, Bruker Biospin - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts