BMRB Entry 16260
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16260
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: NMR assignments of FK506 binding domain from Plasmodium vivax PubMed: 19774494
Deposition date: 2009-04-19 Original release date: 2009-10-16
Authors: Alag, Reema; Yoon, Ho Sup; Shin, Joon
Citation: Alag, Reema; Shin, Joon; Yoon, Ho Sup. "NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax" Biomol. NMR Assignments 3, 243-245 (2009).
Assembly members:
PvFKBD, polymer, 126 residues, 13971.799 Da.
Natural source: Common Name: malaria parasite Taxonomy ID: not available Superkingdom: Eukaryota Kingdom: Alveolata Genus/species: Plasmodium vivax
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PvFKBD: MEQETLEQVHLTEDGGVVKT
ILRKGEGGEENAPKKGNEVT
VHYVGKLESSGKVFDSSRER
NVPFKFHLGQGEVIKGWDIC
VASMTKNEKCSVRLDSKYGY
GEEGCGESIPGNSVLIFEIE
LISFRE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 497 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 850 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Domain | 1 |
Entities:
Entity 1, Domain 126 residues - 13971.799 Da.
| 1 | MET | GLU | GLN | GLU | THR | LEU | GLU | GLN | VAL | HIS | ||||
| 2 | LEU | THR | GLU | ASP | GLY | GLY | VAL | VAL | LYS | THR | ||||
| 3 | ILE | LEU | ARG | LYS | GLY | GLU | GLY | GLY | GLU | GLU | ||||
| 4 | ASN | ALA | PRO | LYS | LYS | GLY | ASN | GLU | VAL | THR | ||||
| 5 | VAL | HIS | TYR | VAL | GLY | LYS | LEU | GLU | SER | SER | ||||
| 6 | GLY | LYS | VAL | PHE | ASP | SER | SER | ARG | GLU | ARG | ||||
| 7 | ASN | VAL | PRO | PHE | LYS | PHE | HIS | LEU | GLY | GLN | ||||
| 8 | GLY | GLU | VAL | ILE | LYS | GLY | TRP | ASP | ILE | CYS | ||||
| 9 | VAL | ALA | SER | MET | THR | LYS | ASN | GLU | LYS | CYS | ||||
| 10 | SER | VAL | ARG | LEU | ASP | SER | LYS | TYR | GLY | TYR | ||||
| 11 | GLY | GLU | GLU | GLY | CYS | GLY | GLU | SER | ILE | PRO | ||||
| 12 | GLY | ASN | SER | VAL | LEU | ILE | PHE | GLU | ILE | GLU | ||||
| 13 | LEU | ILE | SER | PHE | ARG | GLU |
Samples:
sample_1: PvFKBD, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%; H2O 90%; D2O 10%
sample_2: PvFKBD, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%; D2O 100%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts