BMRB Entry 17553
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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/BMR17553
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Title: Solution structure of acyl CoA binding protein from Babesia bovis T2Bo. Seattle Structure Genomics Center for Infectious Disease (SSGCID)
Deposition date: 2011-03-29 Original release date: 2011-04-11
Authors: Yang, Fan; Barnwal, Ravi; Varani, Gabriele
Citation: Yang, Fan; Barnwal, Ravi; Varani, Gabriele. "Solution structure of acyl CoA binding protein from Babesia bovis T2Bo" Not known ., .-..
Assembly members:
entity, polymer, 88 residues, 10086.520 Da.
Natural source: Common Name: Babesia bovis T2Bo Taxonomy ID: 484906 Superkingdom: Eukaryota Kingdom: Chromalveolata Genus/species: Babesia bovis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MSADDFDAAVKYVSNTTTMM
ASNDDKLCFYKYYKQATVGD
CNKPKPGMLQLQEKYKWEAW
NALRGMSTESAKEAYVKLLD
TLAPSWRN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 367 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 547 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | acyl CoA binding protein | 1 |
Entities:
Entity 1, acyl CoA binding protein 88 residues - 10086.520 Da.
| 1 | MET | SER | ALA | ASP | ASP | PHE | ASP | ALA | ALA | VAL | ||||
| 2 | LYS | TYR | VAL | SER | ASN | THR | THR | THR | MET | MET | ||||
| 3 | ALA | SER | ASN | ASP | ASP | LYS | LEU | CYS | PHE | TYR | ||||
| 4 | LYS | TYR | TYR | LYS | GLN | ALA | THR | VAL | GLY | ASP | ||||
| 5 | CYS | ASN | LYS | PRO | LYS | PRO | GLY | MET | LEU | GLN | ||||
| 6 | LEU | GLN | GLU | LYS | TYR | LYS | TRP | GLU | ALA | TRP | ||||
| 7 | ASN | ALA | LEU | ARG | GLY | MET | SER | THR | GLU | SER | ||||
| 8 | ALA | LYS | GLU | ALA | TYR | VAL | LYS | LEU | LEU | ASP | ||||
| 9 | THR | LEU | ALA | PRO | SER | TRP | ARG | ASN |
Samples:
sample_1: entity, [U-95% 15N], 0.8 mM; BIS-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; EDTA 2 mM
sample_2: entity, [U-95% 13C; U-95% 15N], 0.8 mM; BIS-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; EDTA 2 mM
sample_3: entity 1 mM; BIS-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; EDTA 2 mM
sample_conditions_1: pH: 6.5; 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_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol, Koradi, Billeter and Wuthrich - structure display
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - data analysis
CcpNMR, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts