BMRB Entry 34765
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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/BMR34765
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Title: Solution structure of human apo/Calmodulin G113R (G114R)
Deposition date: 2022-10-25 Original release date: 2023-10-20
Authors: Wimmer, R.; Holler, C.; Petersson, N.; Brohus, M.; Niemelae, M.; Overgaard, M.; Iwai, H.
Citation: Petersson, N.; Holler, C.; Brohus, M.; Niemelae, M.; Overgaard, M.; Iwai, H.; Wimmer, R.. "Building the Case against Calmodulin G113 - Circumstantial Evidence from Structure and Dynamics" .
Assembly members:
entity_1, polymer, 148 residues, 16821.492 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):
entity_1: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLREKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 285 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 417 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 148 residues - 16821.492 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 | ARG | 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 G113R, [aa 81-148: U-13C; U-15N], 1.2 mM; EDTA 5 mM; potassium chloride 100 mM; NaN3 2 mM; HEPES 20 mM; TSP-d4 0.1 mM
sample_conditions_1: ionic strength: 128 mM; pH: 6.64 pH*; 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_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| COCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 |
| (HB)CB(CGCDCE)HE | sample_1 | isotropic | sample_conditions_1 |
| (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
Software:
YASARA v21.12.19, YASARA Biosciences - refinement
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment
TopSpin v3.6.6, Bruker Biospin - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts