BMRB Entry 25796
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR25796
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Title: NMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin PubMed: 27876793
Deposition date: 2015-09-04 Original release date: 2016-11-28
Authors: Wang, Xu; Putkey, John
Citation: Wang, Xu; Putkey, John. "PEP-19 Modulates Calcium Binding to Calmodulin by Electrostatic Steering" Nat. Commun. 7, 13583-13583 (2016).
Assembly members:
C-CaM, polymer, 73 residues, 8416.260 Da.
PEP-19, polymer, 62 residues, 6775.41 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):
C-CaM: MKDTDSEEEIREAFRVFDKD
GNGYISAAELRHVMTNLGEK
LTDEEVDEMIREADIDGDGQ
VNYEEFVQMMTAK
PEP-19: MAERQGAGATNGKDKTSGEN
DGQKKVQEEFDIDMDAPETE
RAAVAIQSQFRKFQKKKAGS
QS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 430 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 716 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 73 residues - 8416.260 Da.
Isolated C-domain of calmodulin from residue M76 to K148
| 1 | MET | LYS | ASP | THR | ASP | SER | GLU | GLU | GLU | ILE | ||||
| 2 | ARG | GLU | ALA | PHE | ARG | VAL | PHE | ASP | LYS | ASP | ||||
| 3 | GLY | ASN | GLY | TYR | ILE | SER | ALA | ALA | GLU | LEU | ||||
| 4 | ARG | HIS | VAL | MET | THR | ASN | LEU | GLY | GLU | LYS | ||||
| 5 | LEU | THR | ASP | GLU | GLU | VAL | ASP | GLU | MET | ILE | ||||
| 6 | ARG | GLU | ALA | ASP | ILE | ASP | GLY | ASP | GLY | GLN | ||||
| 7 | VAL | ASN | TYR | GLU | GLU | PHE | VAL | GLN | MET | MET | ||||
| 8 | THR | ALA | LYS |
Entity 2, entity_2 62 residues - 6775.41 Da.
| 1 | MET | ALA | GLU | ARG | GLN | GLY | ALA | GLY | ALA | THR | ||||
| 2 | ASN | GLY | LYS | ASP | LYS | THR | SER | GLY | GLU | ASN | ||||
| 3 | ASP | GLY | GLN | LYS | LYS | VAL | GLN | GLU | GLU | PHE | ||||
| 4 | ASP | ILE | ASP | MET | ASP | ALA | PRO | GLU | THR | GLU | ||||
| 5 | ARG | ALA | ALA | VAL | ALA | ILE | GLN | SER | GLN | PHE | ||||
| 6 | ARG | LYS | PHE | GLN | LYS | LYS | LYS | ALA | GLY | SER | ||||
| 7 | GLN | SER |
Samples:
sample_1: C-CaM, [U-100% 13C; U-100% 15N], 0.8 mM; PEP_19 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; H2O 95%; D2O 5%
sample_2: PEP_19, [U-100% 13C; U-100% 15N], 0.8 mM; C-CaM 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; H2O 95%; D2O 5%
sample_3: C-CaM, [U-100% 13C; U-100% 15N], 0.8 mM; PEP_19 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; D2O 100%
sample_4: PEP-19, [U-100% 13C; U-100% 15N], 0.8 mM; C-CaM 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; D2O 100%
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-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D F1--filtered, F3-edited NOESY-HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_4 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| D F1--filtered, F3-edited NOESY-HSQC | sample_4 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
Felix_2007, Accelrys Software Inc. - data analysis
TOPSPIN v2.1, Bruker Biospin - collection, data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts