BMRB Entry 34534
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34534
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
Title: Spor protein DedD PubMed: 33144379
Deposition date: 2020-07-20 Original release date: 2020-11-06
Authors: Pazos, M.; Peters, K.; Boes, A.; Safaei, Y.; Kenward, C.; Caveney, N.; Laguri, C.; Breukink, E.; Strynadka, N.; Simorre, J.; Terrak, M.; Vollmer, W.
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, e02796-20-e02796-20 (2020).
Assembly members:
entity_1, polymer, 193 residues, 20158.920 Da.
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
Entity Sequences (FASTA):
entity_1: DGQKKHYQDEFAAIPLVPKA
GDRDEPDMMPAATQALPTQP
PEGAAEEVRAGDAAAPSLDP
ATIAANNTEFEPEPAPVAPP
KPKPVEPPKPKVEAPPAPKP
EPKPVVEEKAAPTGKAYVVQ
LGALKNADKVNEIVGKLRGA
GYRVYTSPSTPVQGKITRIL
VGPDASKDKLKGSLGELKQL
SGLSGVVMGYTPN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 477 |
| 15N chemical shifts | 150 |
| 1H chemical shifts | 836 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 193 residues - 20158.920 Da.
| 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 | PRO | 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 | ASP | 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-13C; U-15N], 1.08 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 Pa; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | 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:
CNS, Brunger A. T. et.al. - refinement
ARIA, Linge, O'Donoghue and Nilges - structure calculation
CcpNmr Analysis, CCPN - chemical shift assignment, peak picking
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