BMRB Entry 25016
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25016
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Title: Solution structure of Y125F mutant of eRF1 N-domain
Deposition date: 2014-06-12 Original release date: 2015-06-15
Authors: Pillay, Shubhadra; Li, Yan; Wong, Leo E; Pervushin, Konstantin
Citation: Pillay, Shubhadra; Li, Yan; Wong, Leo E; Pervushin, Konstantin. "Structural insights of eRF1 mutants and their correlation with stop codon recognition" ACS chemical biology ., .-..
Assembly members:
entity, polymer, 142 residues, 15682.319 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):
entity: MADDPSAADRNVEIWKIKKL
IKSLEAARGNGTSMISLIIP
PKDQISRVAKMLADEFGTAS
NIKSRVNRLSVLGAITSVQQ
RLKLYNKVPPNGLVVYCGTI
VTEEGKEKKVNIDFEPFKPI
NTSLFLCDNKFHTEALTALL
SD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 441 |
| 15N chemical shifts | 146 |
| 1H chemical shifts | 975 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Y125F mutant of eRF1 N-domain | 1 |
Entities:
Entity 1, Y125F mutant of eRF1 N-domain 142 residues - 15682.319 Da.
| 1 | MET | ALA | ASP | ASP | PRO | SER | ALA | ALA | ASP | ARG | ||||
| 2 | ASN | VAL | GLU | ILE | TRP | LYS | ILE | LYS | LYS | LEU | ||||
| 3 | ILE | LYS | SER | LEU | GLU | ALA | ALA | ARG | GLY | ASN | ||||
| 4 | GLY | THR | SER | MET | ILE | SER | LEU | ILE | ILE | PRO | ||||
| 5 | PRO | LYS | ASP | GLN | ILE | SER | ARG | VAL | ALA | LYS | ||||
| 6 | MET | LEU | ALA | ASP | GLU | PHE | GLY | THR | ALA | SER | ||||
| 7 | ASN | ILE | LYS | SER | ARG | VAL | ASN | ARG | LEU | SER | ||||
| 8 | VAL | LEU | GLY | ALA | ILE | THR | SER | VAL | GLN | GLN | ||||
| 9 | ARG | LEU | LYS | LEU | TYR | ASN | LYS | VAL | PRO | PRO | ||||
| 10 | ASN | GLY | LEU | VAL | VAL | TYR | CYS | GLY | THR | ILE | ||||
| 11 | VAL | THR | GLU | GLU | GLY | LYS | GLU | LYS | LYS | VAL | ||||
| 12 | ASN | ILE | ASP | PHE | GLU | PRO | PHE | LYS | PRO | ILE | ||||
| 13 | ASN | THR | SER | LEU | PHE | LEU | CYS | ASP | ASN | LYS | ||||
| 14 | PHE | HIS | THR | GLU | ALA | LEU | THR | ALA | LEU | LEU | ||||
| 15 | SER | ASP |
Samples:
sample_1: Y125F mutant of eRF1 N-domain, [U-99% 15N], 1 mM; MES 20 mM; potassium chloride 100 mM; DTT 2 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Related Database Links:
| BMRB | 18092 19506 25020 |
| PDB | |
| DBJ | BAA85489 BAC33839 BAE31210 BAE31619 BAE37589 |
| EMBL | CAA37987 CAA57281 CAA57282 CAA78620 CAF90786 |
| GB | AAA36665 AAB49726 AAD43966 AAH13717 AAH14269 |
| REF | NP_001008345 NP_001069722 NP_001076236 NP_001084363 NP_001126989 |
| SP | P35615 P62495 P62496 P62497 P62498 |
| TPG | DAA27419 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts