BMRB Entry 27017
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27017
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Citation: Fowler, C.; Nunez Hernandez, Maria; O'Donnell, Susan; Yu, Liping; Shea, Madeline. "Backbone and side-chain resonance assignments of (Ca2+)4-calmodulin bound to beta calcineurin A CaMBD peptide" Biomol. NMR Assign. 11, 275-280 (2017).
PubMed: 28815458
Assembly members:
calmodulin, polymer, 148 residues, Formula weight is not available
beta_calcineurin_A_peptide, polymer, 34 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.
Natural source: Common Name: Paramecium tetraurelia Taxonomy ID: 5888 Superkingdom: Eukaryota Kingdom: not available Genus/species: Paramecium tetraurelia
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PT7-7
Entity Sequences (FASTA):
calmodulin: AEQLTEEQIAEFKEAFALFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLSLMARKMKEQD
SEEELIEAFKVFDRDGNGLI
SAAELRHVMTNLGEKLTDDE
VDEMIREADIDGDGHINYEE
FVRMMVSK
beta_calcineurin_A_peptide: GPGSSAAARKEIIRNKIRAI
GKMARVFSVLREES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 798 |
| 15N chemical shifts | 199 |
| 1H chemical shifts | 1231 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | calmodulin | 1 |
| 2 | beta calcineurin | 2 |
| 3 | calcium | 3 |
Entities:
Entity 1, calmodulin 148 residues - Formula weight is not available
| 1 | ALA | GLU | GLN | LEU | THR | GLU | GLU | GLN | ILE | ALA | ||||
| 2 | GLU | PHE | LYS | GLU | ALA | PHE | ALA | 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 | SER | ||||
| 8 | LEU | MET | ALA | ARG | LYS | MET | LYS | GLU | GLN | ASP | ||||
| 9 | SER | GLU | GLU | GLU | LEU | ILE | GLU | ALA | PHE | LYS | ||||
| 10 | VAL | PHE | ASP | ARG | ASP | GLY | ASN | GLY | LEU | ILE | ||||
| 11 | SER | ALA | ALA | GLU | LEU | ARG | HIS | VAL | MET | THR | ||||
| 12 | ASN | LEU | GLY | GLU | LYS | LEU | THR | ASP | ASP | GLU | ||||
| 13 | VAL | ASP | GLU | MET | ILE | ARG | GLU | ALA | ASP | ILE | ||||
| 14 | ASP | GLY | ASP | GLY | HIS | ILE | ASN | TYR | GLU | GLU | ||||
| 15 | PHE | VAL | ARG | MET | MET | VAL | SER | LYS |
Entity 2, beta calcineurin 34 residues - Formula weight is not available
First four residues (GPGS, -4 to -1) are part of a 3C protease cleavage site; beta calcineurin residue S397 is residue 5 of the peptide.
| 1 | GLY | PRO | GLY | SER | SER | ALA | ALA | ALA | ARG | LYS | ||||
| 2 | GLU | ILE | ILE | ARG | ASN | LYS | ILE | ARG | ALA | ILE | ||||
| 3 | GLY | LYS | MET | ALA | ARG | VAL | PHE | SER | VAL | LEU | ||||
| 4 | ARG | GLU | GLU | SER |
Entity 3, calcium - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; beta calcineurin A peptide, [U-99% 13C; U-99% 15N], 0.85 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%
sample_2: calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; beta calcineurin A peptide, [U-99% 13C; U-99% 15N], 0.85 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%
sample_3: calmodulin, [U-99% 15N], 0.78 mM; beta calcineurin A peptide, [U-99% 15N], 0.78 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%
sample_4: calmodulin 0.9 mM; beta calcineurin A peptide 0.9 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_2 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCDCE)HE | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H gCOSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis, CCPN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks