BMRB Entry 5698
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5698
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Title: Backbone and Side-chain 1H, and 15N Chemical Shift Assignments for TcPABC PubMed: 12930992
Deposition date: 2003-02-17 Original release date: 2003-09-12
Authors: Siddiqui, Nadeem; Kozlov, Guennadi; D'Orso, Ivan; Trempe, Jean-Francois; Gehring, Kalle
Citation: Siddiqui, Nadeem; Kozlov, Guennadi; D'Orso, Ivan; Trempe, Jean-Francois; Gehring, Kalle. "Solution Structure of the C-terminal Domain from Poly(A)-binding Protein in Trypanosoma cruzi: A Vegetal PABC Domain " Protein Sci. 12, 1925-1933 (2003).
Assembly members:
C-terminal domain of PABP, polymer, 85 residues, 9090 Da.
Natural source: Common Name: Trypanosoma cruzi Taxonomy ID: 5693 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma cruzi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
C-terminal domain of PABP: GSSLASQGQNLSTVLANLTP
EQQKNVLGERLYNHIVAINP
AAAAKVTGMLLEMDNGEILN
LLDTPGLLDAKVQEALEVLN
RHMNV
- assigned_chemical_shifts
- coupling_constants
Data type | Count |
1H chemical shifts | 466 |
15N chemical shifts | 80 |
coupling constants | 74 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | C-term domain of PABP | 1 |
Entities:
Entity 1, C-term domain of PABP 85 residues - 9090 Da.
1 | GLY | SER | SER | LEU | ALA | SER | GLN | GLY | GLN | ASN | ||||
2 | LEU | SER | THR | VAL | LEU | ALA | ASN | LEU | THR | PRO | ||||
3 | GLU | GLN | GLN | LYS | ASN | VAL | LEU | GLY | GLU | ARG | ||||
4 | LEU | TYR | ASN | HIS | ILE | VAL | ALA | ILE | ASN | PRO | ||||
5 | ALA | ALA | ALA | ALA | LYS | VAL | THR | GLY | MET | LEU | ||||
6 | LEU | GLU | MET | ASP | ASN | GLY | GLU | ILE | LEU | ASN | ||||
7 | LEU | LEU | ASP | THR | PRO | GLY | LEU | LEU | ASP | ALA | ||||
8 | LYS | VAL | GLN | GLU | ALA | LEU | GLU | VAL | LEU | ASN | ||||
9 | ARG | HIS | MET | ASN | VAL |
Samples:
sample_1: C-terminal domain of PABP, [U-15N], 2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 1 mM
Ex-cond_1: pH: 6.3; temperature: 303 K; ionic strength: 0.20 M
Ex-cond_2: pH: 6.3; temperature: 303 K; ionic strength: 0.20 M
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
HNCACB | not available | not available | not available |
CBCACONH | not available | not available | not available |
HNHA | not available | not available | not available |
2D NOESY | not available | not available | not available |
3D-15N NOESY | not available | not available | not available |
IPAP-HSQC | not available | not available | not available |
Software:
XWINNMR v2.1 - Processing
GIFA v4.31 - Processing
CNS v1.1 - Refinement
XEASY v1.3 - data analysis
ARIA v1.1 - structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
- Varian UNITYplus 800 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