BMRB Entry 15753
Click here to enlarge.
            
                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15753
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: Structure of a Glycosylphosphatidylinositol-anchored Domain from a Trypanosome Variant Surface Glycoprotein PubMed: 18003615
Deposition date: 2008-05-05 Original release date: 2008-11-12
Authors: Jones, Nicola; Nietlispach, Daniel; Sharma, Reuben; Burke, David; Eyres, Isobel; Mues, Marsilius; Mott, Helen; Carrington, Mark
Citation: Jones, Nicola; Nietlispach, Daniel; Sharma, Reuben; Burke, David; Eyres, Isobel; Mues, Marsilius; Mott, Helen; Carrington, Mark. "Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein" J. Biol. Chem. 283, 3584-3593 (2008).
Assembly members:
Variant_Surface_Glycoprotein_ILTat1.24, polymer, 46 residues,   5141.820 Da.
Natural source: Common Name: not available Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Variant_Surface_Glycoprotein_ILTat1.24: GKSPEAECNKITEEPKCSEE
KICSWHKEVKAGEKNCQFNS
TKASKS
- assigned_chemical_shifts
 
| Data type | Count | 
| 1H chemical shifts | 298 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | entity | 1 | 
Entities:
Entity 1, entity 46 residues - 5141.820 Da.
This is the first C-terminal subdomain of the Variant Surface Glycoprotein ILTat1.24
| 1 | GLY | LYS | SER | PRO | GLU | ALA | GLU | CYS | ASN | LYS | ||||
| 2 | ILE | THR | GLU | GLU | PRO | LYS | CYS | SER | GLU | GLU | ||||
| 3 | LYS | ILE | CYS | SER | TRP | HIS | LYS | GLU | VAL | LYS | ||||
| 4 | ALA | GLY | GLU | LYS | ASN | CYS | GLN | PHE | ASN | SER | ||||
| 5 | THR | LYS | ALA | SER | LYS | SER | 
Samples:
sample_1: ILTat1.24 C1-domain 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.05%; D2O 10%; H2O 90%
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 | 
Software:
AZARA, Boucher - processing
ANSIG, Kraulis - data analysis
ARIA, Linge, O, . - structure solution
NMR spectrometers:
- Bruker DRX 800 MHz