BMRB Entry 19195
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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/BMR19195
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Title: alfa-actinin from parasite Entamoeba histolytica
Deposition date: 2013-04-26 Original release date: 2013-06-04
Authors: Persson, Cecilia; Mayzel, Maxim; Karlsson, Goran; Backman, Lars
Citation: Persson, Cecilia; Mayzel, Maxim; Karlsson, Goran; Backman, Lars. "alfa-actinin from parasite Entamoeba histolytica" Not known ., .-..
Assembly members:
entity, polymer, 144 residues, 15924.354 Da.
Natural source: Common Name: Entamoeba Histolytica Taxonomy ID: 5759 Superkingdom: Eukaryota Kingdom: not available Genus/species: Entamoeba Histolytica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSSSGVTAEQMQEFKQSFDA
FDGNHDGILDKLEFRSCLSS
MGLIDIDFTGGEDAQYDAIY
NNVTKGENGVSFDNYVQYMK
EKNDENPSPEQLNEIFSTIA
AGKDSITETDMQKAGMSAEQ
IEYVKANLPQKGDGYDYAAW
VKTN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 537 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 869 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alfa-actinin from parasite Entamoeba histolytica | 1 |
Entities:
Entity 1, alfa-actinin from parasite Entamoeba histolytica 144 residues - 15924.354 Da.
| 1 | GLY | SER | SER | SER | GLY | VAL | THR | ALA | GLU | GLN | ||||
| 2 | MET | GLN | GLU | PHE | LYS | GLN | SER | PHE | ASP | ALA | ||||
| 3 | PHE | ASP | GLY | ASN | HIS | ASP | GLY | ILE | LEU | ASP | ||||
| 4 | LYS | LEU | GLU | PHE | ARG | SER | CYS | LEU | SER | SER | ||||
| 5 | MET | GLY | LEU | ILE | ASP | ILE | ASP | PHE | THR | GLY | ||||
| 6 | GLY | GLU | ASP | ALA | GLN | TYR | ASP | ALA | ILE | TYR | ||||
| 7 | ASN | ASN | VAL | THR | LYS | GLY | GLU | ASN | GLY | VAL | ||||
| 8 | SER | PHE | ASP | ASN | TYR | VAL | GLN | TYR | MET | LYS | ||||
| 9 | GLU | LYS | ASN | ASP | GLU | ASN | PRO | SER | PRO | GLU | ||||
| 10 | GLN | LEU | ASN | GLU | ILE | PHE | SER | THR | ILE | ALA | ||||
| 11 | ALA | GLY | LYS | ASP | SER | ILE | THR | GLU | THR | ASP | ||||
| 12 | MET | GLN | LYS | ALA | GLY | MET | SER | ALA | GLU | GLN | ||||
| 13 | ILE | GLU | TYR | VAL | LYS | ALA | ASN | LEU | PRO | GLN | ||||
| 14 | LYS | GLY | ASP | GLY | TYR | ASP | TYR | ALA | ALA | TRP | ||||
| 15 | VAL | LYS | THR | ASN |
Samples:
sample_1: The protein, [U-100% 13C; U-100% 15N], 1.5 mM; sodium phosphate 25 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS v2.2, CCPN - assignment and data analysis
DANGLE v1.1 -
CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 900 MHz
Related Database Links:
| PDB | |
| GB | EAL47897 EKE40069 EMD43687 EMH76125 EMS12580 |
| REF | XP_008857596 XP_653283 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts