BMRB Entry 4089
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4089
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: DARDEL, F.; RAGUSA, S.; LAZENNEC, C.; BLANQUET, S.; MEINNEL, T.. "Solution Structure of Nickel-peptide Deformylase" J. Mol. Biol. 280, 501-513 (1998).
Assembly members:
peptide deformylase, polymer, 147 residues, Formula weight is not available
NI, non-polymer, 58.693 Da.
Natural source: Common Name: not available Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: ESCHERICHIA COLI
Experimental source: Production method: recombinant technology Host organism: PUC18 (IPTG-INDUCIBLE LAC PROMOTURCE 5 EXPRESSION_SYSTEM_PLASMID: PDEF-EC1-147
Entity Sequences (FASTA):
peptide deformylase: AVLQVLHIPDERLRKVAKPV
EEVNAEIQRIVDDMFETMYA
EEGIGLAATQVDIHQRIIVI
DVSENRDERLVLINPELLEK
SGETGIEEGCLSIPEQRALV
PRAEKVKIRALDRDGKPFEL
EADGLLAICIQHEMDHLVGK
LFMDYLS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 487 |
| 15N chemical shifts | 160 |
| 1H chemical shifts | 1110 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | peptide deformylase | 1 |
| 2 | Ni | 2 |
Entities:
Entity 1, peptide deformylase 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 |
Entity 2, Ni - Ni - 58.693 Da.
| 1 | NI |
Samples:
sample_1: data not available
sample_cond_1: ionic strength: 20 mM; pH: 7.2 na; pressure: 1 atm; temperature: 318 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY | sample_1 | not available | sample_cond_1 |
| DQF-COSY | sample_1 | not available | sample_cond_1 |
| CT-HSQC | sample_1 | not available | sample_cond_1 |
| HNCA | sample_1 | not available | sample_cond_1 |
| NOESY-HMQC | sample_1 | not available | sample_cond_1 |
| HCCH-TOCSY | sample_1 | not available | sample_cond_1 |
| HMBC-HSQC,HNHB | sample_1 | not available | sample_cond_1 |
Software:
No software information available
NMR spectrometers:
- Bruker AMX 600 MHz
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB37575 BAE78005 BAG79085 BAH66202 BAI27558 |
| EMBL | CAA11508 CAA45206 CAA54367 CAA54826 CAD09179 |
| GB | AAA58084 AAC76312 AAF76758 AAG58408 AAL22269 |
| PIR | AB1010 |
| REF | NP_312179 NP_417745 NP_458493 NP_462310 NP_709074 |
| SP | A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1 |
| AlphaFold | A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks