BMRB Entry 4589
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4589
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Title: NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum
Deposition date: 2000-05-05 Original release date: 2001-03-08
Authors: Mosbah, A.; Belaich, A.; Bornet, O.; Belaich, J.; Henrissat, B.; Darbon, H.
Citation: Mosbah, A.; Belaich, A.; Bornet, O.; Belaich, J.; Henrissat, B.; Darbon, H.. "NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum" J. Mol. Biol. 304, 201-217 (2000).
Assembly members:
scaffoldin protein, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: Clostridium cellulolyticum Taxonomy ID: 1521 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium cellulolyticum
Experimental source: Production method: .
Entity Sequences (FASTA):
scaffoldin protein: MQDPTINPTSISAKAGSFAD
TKITLTPNGNTFNGISELQS
SQYTKGTNEVTLLASYLNTL
PENTTKTLTFDFGVGTKNPK
LTITVLPKDIPGLE
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 525 |
| coupling constants | 77 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | scaffoldin protein | 1 |
Entities:
Entity 1, scaffoldin protein 94 residues - Formula weight is not available
| 1 | MET | GLN | ASP | PRO | THR | ILE | ASN | PRO | THR | SER | ||||
| 2 | ILE | SER | ALA | LYS | ALA | GLY | SER | PHE | ALA | ASP | ||||
| 3 | THR | LYS | ILE | THR | LEU | THR | PRO | ASN | GLY | ASN | ||||
| 4 | THR | PHE | ASN | GLY | ILE | SER | GLU | LEU | GLN | SER | ||||
| 5 | SER | GLN | TYR | THR | LYS | GLY | THR | ASN | GLU | VAL | ||||
| 6 | THR | LEU | LEU | ALA | SER | TYR | LEU | ASN | THR | LEU | ||||
| 7 | PRO | GLU | ASN | THR | THR | LYS | THR | LEU | THR | PHE | ||||
| 8 | ASP | PHE | GLY | VAL | GLY | THR | LYS | ASN | PRO | LYS | ||||
| 9 | LEU | THR | ILE | THR | VAL | LEU | PRO | LYS | ASP | ILE | ||||
| 10 | PRO | GLY | LEU | GLU |
Samples:
sample_1: scaffoldin protein, [U-15N], 25 mM; sodium acetate buffer 20 mM; H2O 90%; D2O 10%
sample_cond_1: pH: 5.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_1 | not available | sample_cond_1 |
| 3D 15N-separated_NOESY | sample_1 | not available | sample_cond_1 |
| DQF-COSY | sample_1 | not available | sample_cond_1 |
| 2D 15N HSQC | sample_1 | not available | sample_cond_1 |
| 2D 15N HSQC_NOESY | sample_1 | not available | sample_cond_1 |
| 2D 15N HSQC_TOCSY | sample_1 | not available | sample_cond_1 |
Software:
xwinnmr v2.1 - processing
XEASY v1.2 - data analysis
DIANA v2.8 - structure solution
CNS v1.0 - refinement
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts