BMRB Entry 6613
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6613
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Title: Structure and dynamics of coxsackievirus B4 2A proteinase, an enzyme involved in the aetiology of heart disease PubMed: 16415022
Deposition date: 2005-04-28 Original release date: 2006-04-10
Authors: Baxter, N.; Roetzer, A.; Liebig, H.; Sedelnikova, S.; Hounslow, A.; Skern, T.; Waltho, J.
Citation: Baxter, N.; Roetzer, A.; Liebig, H.; Sedelnikova, S.; Hounslow, A.; Skern, T.; Waltho, J.. "Structure and dynamics of coxsackievirus B4 2A proteinase, an enzyme involved in the etiology of heart disease " J. Virol. 80, 1451-1462 (2006).
Assembly members:
2A proteinase, polymer, 166 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Human enterovirus B Taxonomy ID: 138949 Superkingdom: Viruses Kingdom: not available Genus/species: Enterovirus Coxsackievirus B4
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
2A proteinase: MAHHHHHHERASLITTGPYG
HQSGAVYVGNYKVVNRHLAT
HVDWQNCVWEDYNRDLLVST
TTAHGCDTIARCQCTTGVYF
CASKSKHYPVSFEGPGLVEV
QESEYYPKRYQSHVLLATGF
SEPGDAGGILRCEHGVIGLV
TMGGEGVVGFADVRDLLWLE
DDAMEQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 848 |
| 13C chemical shifts | 573 |
| 15N chemical shifts | 125 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | 2A proteinase | 1 |
| 2 | ZINC (II) ION | 2 |
Entities:
Entity 1, 2A proteinase 166 residues - Formula weight is not available
| 1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | GLU | ARG | ||||
| 2 | ALA | SER | LEU | ILE | THR | THR | GLY | PRO | TYR | GLY | ||||
| 3 | HIS | GLN | SER | GLY | ALA | VAL | TYR | VAL | GLY | ASN | ||||
| 4 | TYR | LYS | VAL | VAL | ASN | ARG | HIS | LEU | ALA | THR | ||||
| 5 | HIS | VAL | ASP | TRP | GLN | ASN | CYS | VAL | TRP | GLU | ||||
| 6 | ASP | TYR | ASN | ARG | ASP | LEU | LEU | VAL | SER | THR | ||||
| 7 | THR | THR | ALA | HIS | GLY | CYS | ASP | THR | ILE | ALA | ||||
| 8 | ARG | CYS | GLN | CYS | THR | THR | GLY | VAL | TYR | PHE | ||||
| 9 | CYS | ALA | SER | LYS | SER | LYS | HIS | TYR | PRO | VAL | ||||
| 10 | SER | PHE | GLU | GLY | PRO | GLY | LEU | VAL | GLU | VAL | ||||
| 11 | GLN | GLU | SER | GLU | TYR | TYR | PRO | LYS | ARG | TYR | ||||
| 12 | GLN | SER | HIS | VAL | LEU | LEU | ALA | THR | GLY | PHE | ||||
| 13 | SER | GLU | PRO | GLY | ASP | ALA | GLY | GLY | ILE | LEU | ||||
| 14 | ARG | CYS | GLU | HIS | GLY | VAL | ILE | GLY | LEU | VAL | ||||
| 15 | THR | MET | GLY | GLY | GLU | GLY | VAL | VAL | GLY | PHE | ||||
| 16 | ALA | ASP | VAL | ARG | ASP | LEU | LEU | TRP | LEU | GLU | ||||
| 17 | ASP | ASP | ALA | MET | GLU | GLN |
Entity 2, ZINC (II) ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: 2A proteinase, [U-15N], 0.25 mM; potassium phosphate 50 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_2: 2A proteinase, [U-13C; U-15N], 0.25 mM; potassium phosphate 50 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_3: 2A proteinase, [U-13C; U-15N], 0.50 mM; potassium phosphate 50 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_4: 2A proteinase, [U-13C; U-15N], 0.25 mM; potassium phosphate 50 mM; DTT 10 mM; D2O 100%
sample_cond_1: pH: 7.6; temperature: 303 K; ionic strength: 50 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| simultaneously acquired 15N- and 13C-edited 3D NOESY | not available | not available | sample_cond_1 |
Software:
XWINNMR v3.5 - collection
FELIX v2000 - processing, data analysis
CNS v1.1 - structure solution, refinement
NMR spectrometers:
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts