BMRB Entry 6142
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6142
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Title: 1H 13C and 15N resonance assignments for peptide deformylase-actinonin complex PubMed: 17201406
Deposition date: 2004-03-05 Original release date: 2008-07-01
Authors: LARUE, Valery; BOULAROT, Adrien; ARTAUD, Isabelle; MEINNEL, Thierry; DARDEL, Frederic
Citation: Boularot, Adrien; Giglione, Carmela; Petit, Sylvain; Duroc, Yann; de Sousa, Rodolphe; Larue, Valery; Cresteil, Thierry; Dardel, Frederic; Artaud, Isabelle; Meinnel, Thierry. "Discovery and Refinement of a New Structural Class of Potent Peptide Deformylase Inhibitors" J. Med. Chem. 50, 10-20 (2007).
Assembly members:
Peptide Deformylase-actinonin complex, polymer, 147 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Peptide Deformylase-actinonin complex: AVLQVLHIPDERLRKVAKPV
EEVNAEIQRIVDDMFETMYA
EEGIGLAATQVDIHQRIIVI
DVSENRDERLVLINPELLEK
SGETGIEEGCLSIPEQRALV
PRAEKVKIRALDRDGKPFEL
EADGLLAICIQHEMDHLVGK
LFMDYLS
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 903 |
| 13C chemical shifts | 421 |
| 15N chemical shifts | 135 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Deformylase complex | 1 |
Entities:
Entity 1, Deformylase complex 147 residues - Formula weight is not available
| 1 | ALA | VAL | LEU | GLN | VAL | LEU | HIS | ILE | PRO | ASP | ||||
| 2 | GLU | ARG | LEU | ARG | LYS | VAL | ALA | LYS | PRO | VAL | ||||
| 3 | GLU | GLU | VAL | ASN | ALA | GLU | ILE | GLN | ARG | ILE | ||||
| 4 | VAL | ASP | ASP | MET | PHE | GLU | THR | MET | TYR | ALA | ||||
| 5 | GLU | GLU | GLY | ILE | GLY | LEU | ALA | ALA | THR | GLN | ||||
| 6 | VAL | ASP | ILE | HIS | GLN | ARG | ILE | ILE | VAL | ILE | ||||
| 7 | ASP | VAL | SER | GLU | ASN | ARG | ASP | GLU | ARG | LEU | ||||
| 8 | VAL | LEU | ILE | ASN | PRO | GLU | LEU | LEU | GLU | LYS | ||||
| 9 | SER | GLY | GLU | THR | GLY | ILE | GLU | GLU | GLY | CYS | ||||
| 10 | LEU | SER | ILE | PRO | GLU | GLN | ARG | ALA | LEU | VAL | ||||
| 11 | PRO | ARG | ALA | GLU | LYS | VAL | LYS | ILE | ARG | ALA | ||||
| 12 | LEU | ASP | ARG | ASP | GLY | LYS | PRO | PHE | GLU | LEU | ||||
| 13 | GLU | ALA | ASP | GLY | LEU | LEU | ALA | ILE | CYS | ILE | ||||
| 14 | GLN | HIS | GLU | MET | ASP | HIS | LEU | VAL | GLY | LYS | ||||
| 15 | LEU | PHE | MET | ASP | TYR | LEU | SER |
Samples:
sample_1: Peptide Deformylase-actinonin complex, [U-13C; U-15N], 0.001 M; Actinonin 0.001 M
Ex-cond_1: pH: 7; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HSQC | sample_1 | not available | Ex-cond_1 |
| HNCA | sample_1 | not available | Ex-cond_1 |
| HNCACB | sample_1 | not available | Ex-cond_1 |
| CBCACONH | sample_1 | not available | Ex-cond_1 |
| TOCSYHSQC | sample_1 | not available | Ex-cond_1 |
| HCCH-TOCSY | sample_1 | not available | Ex-cond_1 |
| NOESYHSQC | sample_1 | not available | Ex-cond_1 |
Software:
No software information available
NMR spectrometers:
- BRUKER ADVANCE 600 MHz
Related Database Links:
| BMRB | 4089 5404 |
| PDB | |
| DBJ | BAB37575 BAE78005 BAG79085 BAH66202 BAI27558 |
| EMBL | CAA11508 CAA45206 CAA54367 CAA54826 CAD09179 |
| GB | AAA58084 AAC76312 AAF76758 AAG58408 AAL22269 |
| PIR | AB1010 |
| REF | NP_289848 NP_312179 NP_417745 NP_458493 NP_462310 |
| SP | A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts