BMRB Entry 17878
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17878
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for La(4-325) PubMed: 22009680
Deposition date: 2011-08-22 Original release date: 2011-12-09
Authors: Martino, Luigi; Kelly, Geoff; Curry, Stephen; Conte, Maria
Citation: Martino, Luigi; Pennell, Simon; Kelly, Geoff; Bui, Tam; Kotik-Kogan, Olga; Smerdon, Stephen; Drake, Alex; Curry, Stephen; Conte, Maria. "Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein." Nucleic Acids Res. 40, 1381-1394 (2012).
Assembly members:
human_La_protein, polymer, 322 residues, 37441.7 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
human_La_protein: NGDNEKMAALEAKICHQIEY
YFGDFNLPRDKFLKEQIKLD
EGWVPLEIMIKFNRLNRLTT
DFNVIVEALSKSKAELMEIS
EDKTKIRRSPSKPLPEVTDE
YKNDVKNRSVYIKGFPTDAT
LDDIKEWLEDKGQVLNIQMR
RTLHKAFKGSIFVVFDSIES
AKKFVETPGQKYKETDLLIL
FKDDYFAKKNEERKQNKVEA
KLRAKQEQEAKQKLEEDAEM
KSLEEKIGCLLKFSGDLDDQ
TCREDLHILFSNHGEIKWID
FVRGAKEGIILFKEKAKEAL
GKAKDANNGNLQLRNKEVTW
EVLEGEVEKEALKKIIEDQQ
ES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 687 |
| 15N chemical shifts | 260 |
| 1H chemical shifts | 260 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | La(4-325) | 1 |
Entities:
Entity 1, La(4-325) 322 residues - 37441.7 Da.
| 1 | ASN | GLY | ASP | ASN | GLU | LYS | MET | ALA | ALA | LEU | ||||
| 2 | GLU | ALA | LYS | ILE | CYS | HIS | GLN | ILE | GLU | TYR | ||||
| 3 | TYR | PHE | GLY | ASP | PHE | ASN | LEU | PRO | ARG | ASP | ||||
| 4 | LYS | PHE | LEU | LYS | GLU | GLN | ILE | LYS | LEU | ASP | ||||
| 5 | GLU | GLY | TRP | VAL | PRO | LEU | GLU | ILE | MET | ILE | ||||
| 6 | LYS | PHE | ASN | ARG | LEU | ASN | ARG | LEU | THR | THR | ||||
| 7 | ASP | PHE | ASN | VAL | ILE | VAL | GLU | ALA | LEU | SER | ||||
| 8 | LYS | SER | LYS | ALA | GLU | LEU | MET | GLU | ILE | SER | ||||
| 9 | GLU | ASP | LYS | THR | LYS | ILE | ARG | ARG | SER | PRO | ||||
| 10 | SER | LYS | PRO | LEU | PRO | GLU | VAL | THR | ASP | GLU | ||||
| 11 | TYR | LYS | ASN | ASP | VAL | LYS | ASN | ARG | SER | VAL | ||||
| 12 | TYR | ILE | LYS | GLY | PHE | PRO | THR | ASP | ALA | THR | ||||
| 13 | LEU | ASP | ASP | ILE | LYS | GLU | TRP | LEU | GLU | ASP | ||||
| 14 | LYS | GLY | GLN | VAL | LEU | ASN | ILE | GLN | MET | ARG | ||||
| 15 | ARG | THR | LEU | HIS | LYS | ALA | PHE | LYS | GLY | SER | ||||
| 16 | ILE | PHE | VAL | VAL | PHE | ASP | SER | ILE | GLU | SER | ||||
| 17 | ALA | LYS | LYS | PHE | VAL | GLU | THR | PRO | GLY | GLN | ||||
| 18 | LYS | TYR | LYS | GLU | THR | ASP | LEU | LEU | ILE | LEU | ||||
| 19 | PHE | LYS | ASP | ASP | TYR | PHE | ALA | LYS | LYS | ASN | ||||
| 20 | GLU | GLU | ARG | LYS | GLN | ASN | LYS | VAL | GLU | ALA | ||||
| 21 | LYS | LEU | ARG | ALA | LYS | GLN | GLU | GLN | GLU | ALA | ||||
| 22 | LYS | GLN | LYS | LEU | GLU | GLU | ASP | ALA | GLU | MET | ||||
| 23 | LYS | SER | LEU | GLU | GLU | LYS | ILE | GLY | CYS | LEU | ||||
| 24 | LEU | LYS | PHE | SER | GLY | ASP | LEU | ASP | ASP | GLN | ||||
| 25 | THR | CYS | ARG | GLU | ASP | LEU | HIS | ILE | LEU | PHE | ||||
| 26 | SER | ASN | HIS | GLY | GLU | ILE | LYS | TRP | ILE | ASP | ||||
| 27 | PHE | VAL | ARG | GLY | ALA | LYS | GLU | GLY | ILE | ILE | ||||
| 28 | LEU | PHE | LYS | GLU | LYS | ALA | LYS | GLU | ALA | LEU | ||||
| 29 | GLY | LYS | ALA | LYS | ASP | ALA | ASN | ASN | GLY | ASN | ||||
| 30 | LEU | GLN | LEU | ARG | ASN | LYS | GLU | VAL | THR | TRP | ||||
| 31 | GLU | VAL | LEU | GLU | GLY | GLU | VAL | GLU | LYS | GLU | ||||
| 32 | ALA | LEU | LYS | LYS | ILE | ILE | GLU | ASP | GLN | GLN | ||||
| 33 | GLU | SER |
Samples:
sample_La(4-325): La(4-325), [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; Tris 20 mM; KCl 100 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.25; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY-HSQC | sample_La(4-325) | isotropic | sample_conditions_1 |
| 3D TROSY-HNCA | sample_La(4-325) | isotropic | sample_conditions_1 |
| 3D TROSY-HNCACB | sample_La(4-325) | isotropic | sample_conditions_1 |
| 3D TROSY-HN(COCA)CB | sample_La(4-325) | isotropic | sample_conditions_1 |
| 3D TROSY-HNCO | sample_La(4-325) | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| BMRB | 15726 15727 |
| PDB | |
| DBJ | BAE87871 BAE87890 BAG70042 BAG70165 BAI45822 |
| EMBL | CAA31985 CAA32815 |
| GB | AAA36577 AAA51885 AAH01289 AAH20818 AAP88864 |
| REF | NP_001267347 NP_001270975 NP_001281074 NP_001296114 NP_003133 |
| SP | P05455 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts