BMRB Entry 25870
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25870
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Title: Holo form of Calmodulin-Like Domain of Human Non-Muscle alpha-actinin 1 PubMed: 27272015
Deposition date: 2016-06-27 Original release date: 2016-06-27
Authors: Drmota Prebil, Sara; Slapsak, Urska; de Almeida Ribeiro, Euripedes; Pavsic, Miha; Ilc, Gregor; Zielinska, Karolina; Hartl, Markus; Backman, Lars; Plavec, Janez; Lenarcic, Brigita; Djinovic-Carugo, Kristina
Citation: Drmota Prebil, Sara; Slapsak, Urska; de Almeida Ribeiro, Euripedes; Pavsic, Miha; Ilc, Gregor; Zielinska, Karolina; Hartl, Markus; Backman, Lars; Plavec, Janez; Lenarcic, Brigita; Djinovic-Carugo, Kristina. "Structure and calcium-binding studies of calmodulin-like domain of human non-muscle alpha-actinin-1" Sci. Rep. 6, 27383-27383 (2016).
Assembly members:
Calmodulin-Like_Domain_of_alpha-actinin_1, polymer, 153 residues, 16986.877 Da.
CALCIUM ION, non-polymer, 40.078 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):
Calmodulin-Like_Domain_of_alpha-actinin_1: GSSISQEQMNEFRASFNHFD
RDHSGTLGPEEFKACLISLG
YDIGNDPQGEAEFARIMSIV
DPNRLGVVTFQAFIDFMSRE
TADTDTADQVMASFKILAGD
KNYITMDELRRELPPDQAEY
CIARMAPYTGPDSVPGALDY
MSFSTALYGESDL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 517 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 1022 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | Calcium ion | 2 |
Entities:
Entity 1, entity_1 153 residues - 16986.877 Da.
Residues 1-3 represent a non-native affinity tag This is the GSS linker.
| 1 | GLY | SER | SER | ILE | SER | GLN | GLU | GLN | MET | ASN | ||||
| 2 | GLU | PHE | ARG | ALA | SER | PHE | ASN | HIS | PHE | ASP | ||||
| 3 | ARG | ASP | HIS | SER | GLY | THR | LEU | GLY | PRO | GLU | ||||
| 4 | GLU | PHE | LYS | ALA | CYS | LEU | ILE | SER | LEU | GLY | ||||
| 5 | TYR | ASP | ILE | GLY | ASN | ASP | PRO | GLN | GLY | GLU | ||||
| 6 | ALA | GLU | PHE | ALA | ARG | ILE | MET | SER | ILE | VAL | ||||
| 7 | ASP | PRO | ASN | ARG | LEU | GLY | VAL | VAL | THR | PHE | ||||
| 8 | GLN | ALA | PHE | ILE | ASP | PHE | MET | SER | ARG | GLU | ||||
| 9 | THR | ALA | ASP | THR | ASP | THR | ALA | ASP | GLN | VAL | ||||
| 10 | MET | ALA | SER | PHE | LYS | ILE | LEU | ALA | GLY | ASP | ||||
| 11 | LYS | ASN | TYR | ILE | THR | MET | ASP | GLU | LEU | ARG | ||||
| 12 | ARG | GLU | LEU | PRO | PRO | ASP | GLN | ALA | GLU | TYR | ||||
| 13 | CYS | ILE | ALA | ARG | MET | ALA | PRO | TYR | THR | GLY | ||||
| 14 | PRO | ASP | SER | VAL | PRO | GLY | ALA | LEU | ASP | TYR | ||||
| 15 | MET | SER | PHE | SER | THR | ALA | LEU | TYR | GLY | GLU | ||||
| 16 | SER | ASP | LEU |
Entity 2, Calcium ion - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: Calmodulin-Like Domain of alpha-actinin 1, [U-100% 13C; U-100% 15N], 1 mM; HEPES 20 mM; Sodium chloride 100 mM; DTT 1.5 mM; EGTA 0.05 mM; Calcium chloride 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.6; pressure: 1 atm; temperature: 298 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 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
SPARKY, Cornilescu, Delaglio and Bax - peak picking
TALOS, Cornilescu, Delaglio and Bax - Prediction of Protein Backbone Torsion Angles
YASARA, Krieger, Koraimann, Vriend - refinement
NMR spectrometers:
- Varian VNMRS 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts