BMRB Entry 5650
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5650
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Anders, Ahman; Rak, Alexey; Dontsova, Maria; Garber, Maria; Hard, Torleif. "NMR structure of the ribosomal protein L23 from Thermus Thermophilus" J. Biomol. NMR 26, 131-137 (2003).
Assembly members:
L23, polymer, 96 residues, 10737 Da.
Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Eubacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Echerichia coli Vector: pET11c
Entity Sequences (FASTA):
L23: MKTAYDVILAPVLSEKAYAG
FAEGKYTFWVHPKATKTEIK
NAVETAFKVKVVKVNTLHVR
GKKKRLGRYLGKRPDRKKAI
VQVAPGQKIEALEGLI
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 717 |
| 13C chemical shifts | 413 |
| 15N chemical shifts | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | L23 | 1 |
Entities:
Entity 1, L23 96 residues - 10737 Da.
| 1 | MET | LYS | THR | ALA | TYR | ASP | VAL | ILE | LEU | ALA | ||||
| 2 | PRO | VAL | LEU | SER | GLU | LYS | ALA | TYR | ALA | GLY | ||||
| 3 | PHE | ALA | GLU | GLY | LYS | TYR | THR | PHE | TRP | VAL | ||||
| 4 | HIS | PRO | LYS | ALA | THR | LYS | THR | GLU | ILE | LYS | ||||
| 5 | ASN | ALA | VAL | GLU | THR | ALA | PHE | LYS | VAL | LYS | ||||
| 6 | VAL | VAL | LYS | VAL | ASN | THR | LEU | HIS | VAL | ARG | ||||
| 7 | GLY | LYS | LYS | LYS | ARG | LEU | GLY | ARG | TYR | LEU | ||||
| 8 | GLY | LYS | ARG | PRO | ASP | ARG | LYS | LYS | ALA | ILE | ||||
| 9 | VAL | GLN | VAL | ALA | PRO | GLY | GLN | LYS | ILE | GLU | ||||
| 10 | ALA | LEU | GLU | GLY | LEU | ILE |
Samples:
Sample_1: L23, [U-13C; U-15N], 0.8 mM
Sample_2: L23, [U-15N], 0.8 mM
Condition_1: pH: 5.1 na; temperature: 308 K; ionic strength: 0.65 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 15N-HSQC | not available | not available | not available |
| 3D 15N-DIPSI-HSQC | not available | not available | not available |
| 3D 15N-NOESY-HSQC | not available | not available | not available |
| 3D CBCANH | not available | not available | not available |
| CBCA(CO)NH | not available | not available | not available |
| HNCO | not available | not available | not available |
| HNCA | not available | not available | not available |
| HN(CO)CA | not available | not available | not available |
| 3D C(CO)NH | not available | not available | not available |
| HC(CO)NH | not available | not available | not available |
| HCCH-COSY | not available | not available | not available |
| HCCH-TOCSY | not available | not available | not available |
| 3D 13C-edited NOESY | not available | not available | not available |
| 2D DQF-COSY | not available | not available | not available |
| clean-TOCSY | not available | not available | not available |
| NOESY | not available | not available | not available |
Software:
XWINNMR v2.6 - data collection, processing
NMRPipe v2.1 - processing
Ansig for Windows v1.02 - data analysis, assignment
Talos v1999.019.15.47 - data analysis
Aqua v3.2 - data analysis
XPLOR v3.851 - structure calculation, structure analysis
MOLMOL v2K.1 - data and structure analysis
NMR spectrometers:
- Bruker AVANCE 600 MHz
- Bruker AVANCE 500 MHz
- Varian INOVA 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAD71513 |
| GB | AAD55971 AAS81668 AEG34103 AFH38264 EIA38549 |
| REF | WP_008633421 YP_005295 YP_005641230 YP_006058050 YP_144956 |
| SP | Q5SHP0 Q72I06 Q9RA57 |
| AlphaFold | Q5SHP0 Q72I06 Q9RA57 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks