BMRB Entry 18517
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18517
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Title: Solution structure of EDK-delta-Bd37 from Babesia divergens PubMed: 22899250
Deposition date: 2012-06-12 Original release date: 2012-08-29
Authors: Murciano, Brice; Barthe, Philippe; Delbecq, Stephane; Roumestand, Christian
Citation: Barthe, Philippe; Murciano, Brice; Schetters, Theo; Gorenflot, Andre; Delbecq, Stephane; Roumestand, Christian. "1H, 15N and 13C Backbone resonance assignments of a conformational mutant of the adhesion protein delta-Bd37 from Babesia divergens." Biomol. NMR Assignments 7, 241-244 (2013).
Assembly members:
EDK-delta-Bd37, polymer, 224 residues, 24575.496 Da.
Natural source: Common Name: Apicomplexans Taxonomy ID: 32595 Superkingdom: Eukaryota Kingdom: not available Genus/species: Babesia divergens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
EDK-delta-Bd37: VKTLDVLRGELRGQREAFLS
EIIKSDGPFTILQLVGYLRV
VDTDLLLKVDSTKVDEAGKK
VKAYLEKIGIRGDSVEAALD
NLMIKVYEITKGTVESSAQG
TDSEELKTLLLKFSEDLKAE
QELHSEAKGGEALLSSMKTQ
HDELLKKFAALTPTFLTSED
ISGYLTVPEYGAPMNAAKWA
KVEGMIHGKLESSEVPANLK
ALVAELIELRAQMMALLYGP
IGHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 693 |
| 15N chemical shifts | 208 |
| 1H chemical shifts | 1510 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EDK-delta-Bd37 | 1 |
Entities:
Entity 1, EDK-delta-Bd37 224 residues - 24575.496 Da.
| 1 | VAL | LYS | THR | LEU | ASP | VAL | LEU | ARG | GLY | GLU | ||||
| 2 | LEU | ARG | GLY | GLN | ARG | GLU | ALA | PHE | LEU | SER | ||||
| 3 | GLU | ILE | ILE | LYS | SER | ASP | GLY | PRO | PHE | THR | ||||
| 4 | ILE | LEU | GLN | LEU | VAL | GLY | TYR | LEU | ARG | VAL | ||||
| 5 | VAL | ASP | THR | ASP | LEU | LEU | LEU | LYS | VAL | ASP | ||||
| 6 | SER | THR | LYS | VAL | ASP | GLU | ALA | GLY | LYS | LYS | ||||
| 7 | VAL | LYS | ALA | TYR | LEU | GLU | LYS | ILE | GLY | ILE | ||||
| 8 | ARG | GLY | ASP | SER | VAL | GLU | ALA | ALA | LEU | ASP | ||||
| 9 | ASN | LEU | MET | ILE | LYS | VAL | TYR | GLU | ILE | THR | ||||
| 10 | LYS | GLY | THR | VAL | GLU | SER | SER | ALA | GLN | GLY | ||||
| 11 | THR | ASP | SER | GLU | GLU | LEU | LYS | THR | LEU | LEU | ||||
| 12 | LEU | LYS | PHE | SER | GLU | ASP | LEU | LYS | ALA | GLU | ||||
| 13 | GLN | GLU | LEU | HIS | SER | GLU | ALA | LYS | GLY | GLY | ||||
| 14 | GLU | ALA | LEU | LEU | SER | SER | MET | LYS | THR | GLN | ||||
| 15 | HIS | ASP | GLU | LEU | LEU | LYS | LYS | PHE | ALA | ALA | ||||
| 16 | LEU | THR | PRO | THR | PHE | LEU | THR | SER | GLU | ASP | ||||
| 17 | ILE | SER | GLY | TYR | LEU | THR | VAL | PRO | GLU | TYR | ||||
| 18 | GLY | ALA | PRO | MET | ASN | ALA | ALA | LYS | TRP | ALA | ||||
| 19 | LYS | VAL | GLU | GLY | MET | ILE | HIS | GLY | LYS | LEU | ||||
| 20 | GLU | SER | SER | GLU | VAL | PRO | ALA | ASN | LEU | LYS | ||||
| 21 | ALA | LEU | VAL | ALA | GLU | LEU | ILE | GLU | LEU | ARG | ||||
| 22 | ALA | GLN | MET | MET | ALA | LEU | LEU | TYR | GLY | PRO | ||||
| 23 | ILE | GLY | HIS | HIS |
Samples:
sample_1: EDK-delta-Bd37, [U-100% 15N], 0.45 ± 0.01 mM; H2O, [U-100% 15N], 90%; D2O, [U-100% 15N], 10%
sample_2: EDK-delta-Bd37, [U-100% 13C; U-100% 15N], 0.38 ± 0.01 mM; H2O, [U-100% 15N], 90%; D2O, [U-100% 15N], 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.9; 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 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 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
Software:
GIFA v4.44, Delsuc - processing
CINDY v1.8, Padilla - data analysis
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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts