BMRB Entry 4395
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4395
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Title: RIBOSOMAL PROTEIN L25 FROM ESCHERICHIA COLI, NMR,
Deposition date: 1999-09-09 Original release date: 2000-03-08
Authors: Stoldt, M.; Wohnert, J.; Gorlach, M.; Brown, L.
Citation: Stoldt, M.; Wohnert, J.; Gorlach, M.; Brown, L.. "The NMR Structure of Escherichia coli Ribosomal Protein L25 shows Homology to General Stress Proteins and Glutaminyl-tRNA Synthetases" EMBO J. 17, 6377-6384 (1998).
Assembly members:
RIBOSOMAL PROTEIN L25, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: natural source Host organism: Escherichia coli
Entity Sequences (FASTA):
RIBOSOMAL PROTEIN L25: MFTINAEVRKEQGKGASRRL
RAANKFPAIIYGGKEAPLAI
ELDHDKVMNMQAKAEFYSEV
LTIVVDGKEIKVKAQDVQRH
PYKPKLQHIDFVRA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 410 |
15N chemical shifts | 93 |
1H chemical shifts | 675 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | L25 monomer | 1 |
Entities:
Entity 1, L25 monomer 94 residues - Formula weight is not available
1 | MET | PHE | THR | ILE | ASN | ALA | GLU | VAL | ARG | LYS | ||||
2 | GLU | GLN | GLY | LYS | GLY | ALA | SER | ARG | ARG | LEU | ||||
3 | ARG | ALA | ALA | ASN | LYS | PHE | PRO | ALA | ILE | ILE | ||||
4 | TYR | GLY | GLY | LYS | GLU | ALA | PRO | LEU | ALA | ILE | ||||
5 | GLU | LEU | ASP | HIS | ASP | LYS | VAL | MET | ASN | MET | ||||
6 | GLN | ALA | LYS | ALA | GLU | PHE | TYR | SER | GLU | VAL | ||||
7 | LEU | THR | ILE | VAL | VAL | ASP | GLY | LYS | GLU | ILE | ||||
8 | LYS | VAL | LYS | ALA | GLN | ASP | VAL | GLN | ARG | HIS | ||||
9 | PRO | TYR | LYS | PRO | LYS | LEU | GLN | HIS | ILE | ASP | ||||
10 | PHE | VAL | ARG | ALA |
Samples:
sample_1: RIBOSOMAL PROTEIN L25, [U-13C; U-15N], 1.4 mM; KCl 100 mM
sample_2: RIBOSOMAL PROTEIN L25, [U-15N], 1.4 mM; KCl 100 mM
sample_cond_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
not available | not available | not available | sample_cond_1 |
Software:
DYANA v1.5 - structure calculation
NMR spectrometers:
- Varian UNITY-INOVA 750 MHz
Related Database Links:
PDB | |
DBJ | BAA02585 BAB36500 BAE76650 BAG77978 BAI26310 |
EMBL | CAQ32591 CAQ99112 CAU98309 CBJ01826 CCJ44681 |
GB | AAA16413 AAC75246 AAG57323 AAN43791 AAP17608 |
PRF | 1712317A 754714A |
REF | NP_311104 NP_416690 NP_708084 WP_000494178 WP_000494179 |
SP | A7ZP09 A8A248 B1IY84 B1X883 B2TV63 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts