BMRB Entry 7102
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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/BMR7102
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Title: High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design PubMed: 17196978
Deposition date: 2006-05-05 Original release date: 2007-04-16
Authors: Reichow, S.
Citation: Dantas, G.; Corrent, C.; Reichow, S.; Havranek, J.; Eletr, Z.; Isern, N.; Kuhlman, B.; Varani, G.; Merritt, E.; Baker, D.. "High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design" J. Mol. Biol. 366, 1209-1221 (2007).
Assembly members:
Designed Protein AYE, polymer, 78 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 AYE: HHHHHHGSKTIFVIVPTNEE
QVAFLEALAKQDELNFDWQN
PPTEPGQPVVILIPSDMVEW
FLEMLKAKGIPFTVYVEE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 234 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 542 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DESIGNED PROTEIN AYE, chain 1 | 1 |
| 2 | DESIGNED PROTEIN AYE, chain 2 | 1 |
Entities:
Entity 1, DESIGNED PROTEIN AYE, chain 1 78 residues - Formula weight is not available
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | GLY | SER | LYS | THR | ||||
| 2 | ILE | PHE | VAL | ILE | VAL | PRO | THR | ASN | GLU | GLU | ||||
| 3 | GLN | VAL | ALA | PHE | LEU | GLU | ALA | LEU | ALA | LYS | ||||
| 4 | GLN | ASP | GLU | LEU | ASN | PHE | ASP | TRP | GLN | ASN | ||||
| 5 | PRO | PRO | THR | GLU | PRO | GLY | GLN | PRO | VAL | VAL | ||||
| 6 | ILE | LEU | ILE | PRO | SER | ASP | MET | VAL | GLU | TRP | ||||
| 7 | PHE | LEU | GLU | MET | LEU | LYS | ALA | LYS | GLY | ILE | ||||
| 8 | PRO | PHE | THR | VAL | TYR | VAL | GLU | GLU |
Samples:
sample_1: Designed Protein AYE 1 mM; phosphate buffer 50 mM; KCl 100 mM; H2O 90%; D2O 10%
sample_2: Designed Protein AYE 1 mM; phosphate buffer 50 mM; KCl 100 mM; D2O 100%
sample_3: Designed Protein AYE, [U-15N], 1 mM; phosphate buffer 50 mM; KCl 100 mM; H2O 90%; D2O 10%
sample_4: Designed Protein AYE, [U-13C; U-15N], 1 mM; phosphate buffer 50 mM; KCl 100 mM; H2O 90%; D2O 10%
sample_cond_1: ionic strength: 150 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 v2.1 - 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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