BMRB Entry 17633
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/BMR17633
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 structure of BC28.1 PubMed: 22294693
Deposition date: 2011-05-09 Original release date: 2012-02-03
Authors: Roumestand, Christian; Delbecq, Stephane; Yang, Yin-Shan
Citation: Yang, Yin-Shan; Murciano, Brice; Moubri, Karina; Cibrelus, Prisca; Schetters, Theo; Gorenflot, Andre; Delbecq, Stephane; Roumestand, Christian. "Structural and Functional Characterization of Bc28.1, Major Erythrocyte-binding Protein from Babesia canis Merozoite Surface." J. Biol. Chem. 287, 9495-9508 (2012).
Assembly members:
BC28.1, polymer, 223 residues, 24947.393 Da.
Natural source: Common Name: Babesia canis Taxonomy ID: 5867 Superkingdom: Eukaryota Kingdom: not available Genus/species: Babesia canis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BC28.1: SSGIEGCTEDEKRDSVVEGA
TSVEASLKEQIDWLAERYSA
DLTNKDTSKWNTDEKVKELL
NEKAVGIESRLLAIAKEFHK
LKSVLCTGVNETPAHVANRV
SPGDAISMLYVLSITHRELS
SLKNKIDEWKKVKASEDGTK
VIQNIKDDRTNTWFVAHGFK
VAELNDVTLEKLATVVNELV
SHKDMIYINDAMKQNVDKWT
KEESERLAMMAEQGISGAKG
KKD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 671 |
| 15N chemical shifts | 224 |
| 1H chemical shifts | 1457 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BC28.1 | 1 |
Entities:
Entity 1, BC28.1 223 residues - 24947.393 Da.
| 1 | SER | SER | GLY | ILE | GLU | GLY | CYS | THR | GLU | ASP | ||||
| 2 | GLU | LYS | ARG | ASP | SER | VAL | VAL | GLU | GLY | ALA | ||||
| 3 | THR | SER | VAL | GLU | ALA | SER | LEU | LYS | GLU | GLN | ||||
| 4 | ILE | ASP | TRP | LEU | ALA | GLU | ARG | TYR | SER | ALA | ||||
| 5 | ASP | LEU | THR | ASN | LYS | ASP | THR | SER | LYS | TRP | ||||
| 6 | ASN | THR | ASP | GLU | LYS | VAL | LYS | GLU | LEU | LEU | ||||
| 7 | ASN | GLU | LYS | ALA | VAL | GLY | ILE | GLU | SER | ARG | ||||
| 8 | LEU | LEU | ALA | ILE | ALA | LYS | GLU | PHE | HIS | LYS | ||||
| 9 | LEU | LYS | SER | VAL | LEU | CYS | THR | GLY | VAL | ASN | ||||
| 10 | GLU | THR | PRO | ALA | HIS | VAL | ALA | ASN | ARG | VAL | ||||
| 11 | SER | PRO | GLY | ASP | ALA | ILE | SER | MET | LEU | TYR | ||||
| 12 | VAL | LEU | SER | ILE | THR | HIS | ARG | GLU | LEU | SER | ||||
| 13 | SER | LEU | LYS | ASN | LYS | ILE | ASP | GLU | TRP | LYS | ||||
| 14 | LYS | VAL | LYS | ALA | SER | GLU | ASP | GLY | THR | LYS | ||||
| 15 | VAL | ILE | GLN | ASN | ILE | LYS | ASP | ASP | ARG | THR | ||||
| 16 | ASN | THR | TRP | PHE | VAL | ALA | HIS | GLY | PHE | LYS | ||||
| 17 | VAL | ALA | GLU | LEU | ASN | ASP | VAL | THR | LEU | GLU | ||||
| 18 | LYS | LEU | ALA | THR | VAL | VAL | ASN | GLU | LEU | VAL | ||||
| 19 | SER | HIS | LYS | ASP | MET | ILE | TYR | ILE | ASN | ASP | ||||
| 20 | ALA | MET | LYS | GLN | ASN | VAL | ASP | LYS | TRP | THR | ||||
| 21 | LYS | GLU | GLU | SER | GLU | ARG | LEU | ALA | MET | MET | ||||
| 22 | ALA | GLU | GLN | GLY | ILE | SER | GLY | ALA | LYS | GLY | ||||
| 23 | LYS | LYS | ASP |
Samples:
sample_1: BC28.1, [U-15N], 0.5 ± 0.02 mM; H2O 90%; D2O 10%; Sodium phosphate 10 mM; NaCl 50 mM
sample_2: BC28.1, [U-13C; U-15N], 0.5 ± 0.02 mM; H2O 90%; D2O 10%; Sodium phosphate 10 mM; NaCl 50 mM
sample_3: BC28.1 0.1 ± 0.005 mM; D2O 100%; sodium phosphate 10 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
GIFA v4.4, Delsuc - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz
- Bruker Avance 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts