BMRB Entry 16118
Click here to enlarge.
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/BMR16118
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of PFE0790c, a putative bolA-like protein from the protozoan parasite Plasmodium falciparum: A Structural Genomics Center for Infectious Disease (SSGCID) community request.
Deposition date: 2009-01-12 Original release date: 2009-03-05
Authors: Buchko, Garry; Yee, Adelinda; Semesi, Anthony; Hui, Raymond; Arrowsmith, Cheryl
Citation: Buchko, Garry; Yee, Adelinda; Semesi, Anthony; Arrowsmith, Cheryl; Hui, Raymond. "Structural characterization of PFE0790c, a putative bolA-like protein from Plasmodium falciparum, the protozoan parasite responsible for malaria." Not known ., .-..
Assembly members:
PFE0790c, polymer, 108 residues, 12328.188 Da.
Natural source: Common Name: Plasmodium falciparum Taxonomy ID: 36329 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PFE0790c: MGSSHHHHHHSSGRENLYFQ
GHMCIQKVIEDKLSSALKPT
FLELVDKSCGCGTSFDAVIV
SNNFEDKKLLDRHRLVNTIL
KEELQNIHAFSMKCHTPLEY
DKLKSKGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 391 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 607 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PFE0790c | 1 |
Entities:
Entity 1, PFE0790c 108 residues - 12328.188 Da.
N-terminal residues 1-22 and C-terminal residues 107-108 are not native. The first residue in the native sequence of PFE0790c is M23.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | ARG | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 3 | GLY | HIS | MET | CYS | ILE | GLN | LYS | VAL | ILE | GLU | ||||
| 4 | ASP | LYS | LEU | SER | SER | ALA | LEU | LYS | PRO | THR | ||||
| 5 | PHE | LEU | GLU | LEU | VAL | ASP | LYS | SER | CYS | GLY | ||||
| 6 | CYS | GLY | THR | SER | PHE | ASP | ALA | VAL | ILE | VAL | ||||
| 7 | SER | ASN | ASN | PHE | GLU | ASP | LYS | LYS | LEU | LEU | ||||
| 8 | ASP | ARG | HIS | ARG | LEU | VAL | ASN | THR | ILE | LEU | ||||
| 9 | LYS | GLU | GLU | LEU | GLN | ASN | ILE | HIS | ALA | PHE | ||||
| 10 | SER | MET | LYS | CYS | HIS | THR | PRO | LEU | GLU | TYR | ||||
| 11 | ASP | LYS | LEU | LYS | SER | LYS | GLY | SER |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 1.5 ± 0.5 mM; sodium phosphate 10 ± 1 mM; sodium chloride 200 ± 5 mM; DTT 10 ± 1 mM; sodium azide 0.01 ± 0.002 %; benzamidine 1 ± 0.01 mM; H2O 93%; D2O 7%
sample_2: entity, [U-7% 13C; U-99% 15N], 1.5 ± 0.5 mM; sodium phosphate 10 ± 1 mM; sodium chloride 200 ± 5 mM; DTT 10 ± 1 mM; sodium azide 0.01 ± 0.002 %; benzamidine 1 ± 0.01 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
SPARKY v3.110, Goddard - data analysis, peak picking
FELIX v2007, Accelrys Software Inc. - processing
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
PSVS v1.3, Bhattacharya and Montelione - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts