BMRB Entry 7101
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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/BMR7101
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Title: Mistranslation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering. PubMed: 16949611
Deposition date: 2006-05-05 Original release date: 2006-11-17
Authors: Dantas, G.
Citation: Dantas, G.; Watters, A.; Lunde, B.; Eletr, Z.; Isern, N.; Roseman, T.; Lipfert, J.; Doniach, S.; Tompa, M.; Kuhlman, B.; Stoddard, B.; Varani, G.; Baker, D.. "Mis-translation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering." J. Mol. Biol. 362, 1004-1024 (2006).
Assembly members:
Designed protein TOP7, polymer, 62 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Designed protein TOP7: MERVRISITARTKKEAEKFA
AILIKVFAELGYNDINVTWD
GDTVTVEGQLEGGSLEHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 223 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 390 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DESIGNED PROTEIN TOP7, chain 1 | 1 |
| 2 | DESIGNED PROTEIN TOP7, chain 2 | 1 |
Entities:
Entity 1, DESIGNED PROTEIN TOP7, chain 1 62 residues - Formula weight is not available
| 1 | MET | GLU | ARG | VAL | ARG | ILE | SER | ILE | THR | ALA | ||||
| 2 | ARG | THR | LYS | LYS | GLU | ALA | GLU | LYS | PHE | ALA | ||||
| 3 | ALA | ILE | LEU | ILE | LYS | VAL | PHE | ALA | GLU | LEU | ||||
| 4 | GLY | TYR | ASN | ASP | ILE | ASN | VAL | THR | TRP | ASP | ||||
| 5 | GLY | ASP | THR | VAL | THR | VAL | GLU | GLY | GLN | LEU | ||||
| 6 | GLU | GLY | GLY | SER | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 7 | HIS | HIS |
Samples:
sample_1: Designed protein TOP7 1 mM; phosphate buffer 25 mM; H2O 90%; D2O 10%
sample_2: Designed protein TOP7 1 mM; phosphate buffer 25 mM; D2O 100%
sample_3: Designed protein TOP7, [U-15N; U-13C], 1 mM; phosphate buffer 25 mM; H2O 90%; D2O 10%
sample_4: Designed protein TOP7, [U-15N], 1 mM; phosphate buffer 25 mM; H2O 90%; D2O 10%
sample_cond_1: ionic strength: 25 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | sample_cond_1 |
| 3D 13C-separated NOESY | not available | not available | sample_cond_1 |
| 3D 15N-separated NOESY | not available | not available | sample_cond_1 |
| 3D 13C-filtered NOESY | not available | not available | sample_cond_1 |
Software:
CYANA v2.0 - refinement, structure solution
TALOS - data analysis
NMRPipe v2.3 - processing
SPARKY v3.112 - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB |
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