BMRB Entry 19193
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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/BMR19193
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Title: NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1 PubMed: 23782698
Deposition date: 2013-04-25 Original release date: 2013-10-17
Authors: Chary, Kandala; Rout, Ashok; Patel, Sunita; Bhattacharya, Alok
Citation: Chary, Kandala; Rout, Ashok; Patel, Sunita; Bhattacharya, Alok. "Functional manipulation of a calcium binding protein from E. histolytica guided by paramagnetic NMR" J. Biol. Chem. ., .-..
Assembly members:
(Y81F)-EhCaBP1, polymer, 66 residues, 14742.640 Da.
Natural source: Common Name: Eukaryotes 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):
(Y81F)-EhCaBP1: MAEALFKEIDVNGDGAVSYE
EVKAFVSKKRAIKNEQLLQL
IFKSIDADGNGEIDQNEFAK
FYGSIQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 248 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 323 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | (Y81F)-EhCaBP1 | 1 |
Entities:
Entity 1, (Y81F)-EhCaBP1 66 residues - 14742.640 Da.
| 1 | MET | ALA | GLU | ALA | LEU | PHE | LYS | GLU | ILE | ASP | ||||
| 2 | VAL | ASN | GLY | ASP | GLY | ALA | VAL | SER | TYR | GLU | ||||
| 3 | GLU | VAL | LYS | ALA | PHE | VAL | SER | LYS | LYS | ARG | ||||
| 4 | ALA | ILE | LYS | ASN | GLU | GLN | LEU | LEU | GLN | LEU | ||||
| 5 | ILE | PHE | LYS | SER | ILE | ASP | ALA | ASP | GLY | ASN | ||||
| 6 | GLY | GLU | ILE | ASP | GLN | ASN | GLU | PHE | ALA | LYS | ||||
| 7 | PHE | TYR | GLY | SER | ILE | GLN |
Samples:
sample_1: (Y81F)-EhCaBP1, [U-99% 15N], 0.8 ± 0.1 mM; H2O 90%; D2O 10%
sample_2: (Y81F)-EhCaBP1, [U-99% 13C; U-99% 15N], 0.8 ± 0.1 mM; H2O 90%; D2O 10%
sample_3: (Y81F)-EhCaBP1, [U-99% 13C; U-99% 15N], 0.8 ± 0.1 mM; D2O 100%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; 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 | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
FELIX, Accelrys Software Inc. - processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection, processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts