BMRB Entry 50391
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50391
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Title: DedD PubMed: 33144379
Deposition date: 2020-07-16 Original release date: 2020-11-18
Authors: Simorre, Jean-pierre; Kenward, Calem; Laguri, Cedric; Caveney, Nathanael; Strynadka, Natalie
Citation: Pazos, Manuel; Peters, Katharina; Boes, Adrien; Safaei, Yalda; Kenward, Calem; Caveney, Nathanael; Laguri, Cedric; Breukink, Eefjan; Strynadka, Natalie; Simorre, Jean-Pierre; Terrak, Mohammed; Vollmer, Waldemar. "SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli" mBio 11, e02796-e02796 (2020).
Assembly members:
entity_1, polymer, 193 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: dedD
Entity Sequences (FASTA):
entity_1: DGQKKHYQDEFAAIPLVPKA
GDRDEPDMMPAATQALPTQP
PEGAAEEVRAGDAAAPSLDP
ATIAANNTEFEPEPAPVAPP
KPKPVEPLKPKVEAPPAPKP
EPKPVVEEKAAPTGKAYVVQ
LGALKNADKVNEIVGKLRGA
GYRVYTSPSTPVQGKITRIL
VGPDASKEKLKGSLGELKQL
SGLSGVVMGYTPN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 477 |
| 15N chemical shifts | 150 |
| 1H chemical shifts | 839 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DedD | 1 |
Entities:
Entity 1, DedD 193 residues - Formula weight is not available
| 1 | ASP | GLY | GLN | LYS | LYS | HIS | TYR | GLN | ASP | GLU | ||||
| 2 | PHE | ALA | ALA | ILE | PRO | LEU | VAL | PRO | LYS | ALA | ||||
| 3 | GLY | ASP | ARG | ASP | GLU | PRO | ASP | MET | MET | PRO | ||||
| 4 | ALA | ALA | THR | GLN | ALA | LEU | PRO | THR | GLN | PRO | ||||
| 5 | PRO | GLU | GLY | ALA | ALA | GLU | GLU | VAL | ARG | ALA | ||||
| 6 | GLY | ASP | ALA | ALA | ALA | PRO | SER | LEU | ASP | PRO | ||||
| 7 | ALA | THR | ILE | ALA | ALA | ASN | ASN | THR | GLU | PHE | ||||
| 8 | GLU | PRO | GLU | PRO | ALA | PRO | VAL | ALA | PRO | PRO | ||||
| 9 | LYS | PRO | LYS | PRO | VAL | GLU | PRO | LEU | LYS | PRO | ||||
| 10 | LYS | VAL | GLU | ALA | PRO | PRO | ALA | PRO | LYS | PRO | ||||
| 11 | GLU | PRO | LYS | PRO | VAL | VAL | GLU | GLU | LYS | ALA | ||||
| 12 | ALA | PRO | THR | GLY | LYS | ALA | TYR | VAL | VAL | GLN | ||||
| 13 | LEU | GLY | ALA | LEU | LYS | ASN | ALA | ASP | LYS | VAL | ||||
| 14 | ASN | GLU | ILE | VAL | GLY | LYS | LEU | ARG | GLY | ALA | ||||
| 15 | GLY | TYR | ARG | VAL | TYR | THR | SER | PRO | SER | THR | ||||
| 16 | PRO | VAL | GLN | GLY | LYS | ILE | THR | ARG | ILE | LEU | ||||
| 17 | VAL | GLY | PRO | ASP | ALA | SER | LYS | GLU | LYS | LEU | ||||
| 18 | LYS | GLY | SER | LEU | GLY | GLU | LEU | LYS | GLN | LEU | ||||
| 19 | SER | GLY | LEU | SER | GLY | VAL | VAL | MET | GLY | TYR | ||||
| 20 | THR | PRO | ASN |
Samples:
sample_1: DedD, [U-99% 13C; U-99% 15N], 1.08 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.2 - chemical shift assignment
TOPSPIN - processing
NMR spectrometers:
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts