BMRB Entry 7094
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7094
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Title: 1H and 15N Chemical Shift Assignments for the Acylphosphatase from Eschaerichia Coli PubMed: 17021943
Deposition date: 2006-05-03 Original release date: 2006-10-30
Authors: Pagano, Katiuscia; Corazza, Alessandra; Viglino, Paolo; Esposito, Gennaro
Citation: Pagano, K.; Ramazzotti, M.; Viglino, P.; Esposito, G.; Degl'innocenti, D.; Taddei, N.; Corazza, A.. "NMR solution structure of the acylphosphatase from Escherichia coli." J. Biomol. NMR 36, 199-204 (2006).
Assembly members:
Eschaerichia Coli Acylphosphatase, polymer, 92 residues, 10581 Da.
Natural source: Common Name: Eschaerichia Coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Eschaerichia coli
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Eschaerichia Coli Acylphosphatase: MSKVCIIAWVYGRVQGVGFR
YTTQYEAKRLGLTGYAKNLD
DGSVEVVACGEEGQVEKLMQ
WLKSGGPRSARVERVLSEPH
HPSGELTDFRIR
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 486 |
| coupling constants | 59 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EColi | 1 |
Entities:
Entity 1, EColi 92 residues - 10581 Da.
| 1 | MET | SER | LYS | VAL | CYS | ILE | ILE | ALA | TRP | VAL | ||||
| 2 | TYR | GLY | ARG | VAL | GLN | GLY | VAL | GLY | PHE | ARG | ||||
| 3 | TYR | THR | THR | GLN | TYR | GLU | ALA | LYS | ARG | LEU | ||||
| 4 | GLY | LEU | THR | GLY | TYR | ALA | LYS | ASN | LEU | ASP | ||||
| 5 | ASP | GLY | SER | VAL | GLU | VAL | VAL | ALA | CYS | GLY | ||||
| 6 | GLU | GLU | GLY | GLN | VAL | GLU | LYS | LEU | MET | GLN | ||||
| 7 | TRP | LEU | LYS | SER | GLY | GLY | PRO | ARG | SER | ALA | ||||
| 8 | ARG | VAL | GLU | ARG | VAL | LEU | SER | GLU | PRO | HIS | ||||
| 9 | HIS | PRO | SER | GLY | GLU | LEU | THR | ASP | PHE | ARG | ||||
| 10 | ILE | ARG |
Samples:
sample_1: Eschaerichia Coli Acylphosphatase 0.5 mM
sample_2: Eschaerichia Coli Acylphosphatase, [U-95% 15N], 0.5 mM
conditions_1: pH: 4.95; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H TOCSY | not available | not available | conditions_1 |
| 2D 1H NOESY | not available | not available | conditions_1 |
| 2D 1H DQF-COSY | not available | not available | conditions_1 |
| 2D 1H 15N HSQC | not available | not available | conditions_1 |
| 3D 1H 15N NOESY-HSQC | not available | not available | conditions_1 |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 500.1323 MHz
Related Database Links:
| PDB | |
| DBJ | BAA35733 BAB34475 BAI24411 BAI29861 BAI34990 |
| EMBL | CAQ31496 CAQ88634 CAQ97873 CAR12367 CAR18304 |
| GB | AAC74054 AAG55454 AAN42598 AAN79574 AAP16484 |
| REF | NP_286843 NP_309079 NP_415488 NP_706891 NP_753031 |
| SP | P0AB65 P0AB66 Q31YN1 Q83LL9 Q8FJ70 |
| AlphaFold | Q8FJ70 P0AB65 P0AB66 Q31YN1 Q83LL9 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts