BMRB Entry 25852
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25852
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Title: Structure and 15N relaxation data of Calmodulin bound to the endothelial Nitric Oxide Synthase Calmodulin Binding Domain Peptide at Physiological Calcium Concentration
Deposition date: 2015-10-16 Original release date: 2016-10-06
Authors: Piazza, Michael; Guillemette, Guy; Dieckmann, Thorsten
Citation: Piazza, Michael; Guillemette, Guy; Dieckmann, Thorsten. "Structure of Calmodulin bound to the endothelial Nitric Oxide Synthase Calmodulin Binding Domain Peptide at Physiological Calcium Concentration" Biochem. Biophys. Res. Commun. ., .-..
Assembly members:
CaM, polymer, 148 residues, 16721.465 Da.
eNOS, polymer, 22 residues, 2385.864 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: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
eNOS: TRKKTFKEVANAVKISASLM
GT
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
| Data type | Count |
| 13C chemical shifts | 415 |
| 15N chemical shifts | 144 |
| 1H chemical shifts | 966 |
| T1 relaxation values | 134 |
| T2 relaxation values | 135 |
| heteronuclear NOE values | 146 |
| order parameters | 125 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CaM | 1 |
| 2 | eNOS | 2 |
Entities:
Entity 1, CaM 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, eNOS 22 residues - 2385.864 Da.
| 1 | THR | ARG | LYS | LYS | THR | PHE | LYS | GLU | VAL | ALA | ||||
| 2 | ASN | ALA | VAL | LYS | ILE | SER | ALA | SER | LEU | MET | ||||
| 3 | GLY | THR |
Samples:
sample_1: CaM, [U-99% 13C; U-99% 15N], 1 mM; eNOS 1 mM; potassium chloride 100 mM; MOPS 30 mM; EGTA 4 mM; CaEGTA 6 mM
sample_conditions_1: ionic strength: 0.150 M; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H edited filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts