Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15366
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Citation: Mantsyzov, Alexey; Ivanova, Elena; Birdsall, Berry; Kolosov, Petr; Kisselev, Lev; Polshakov, Vladimir. "NMR assignments of the C-terminal domain of human polypeptide release factor eRF1" Biomol. NMR Assignments 1, 183-185 (2007).
PubMed: 19636860
Assembly members:
C-domain_of_human_polypeptide_release_factor_eRF1, polymer, 171 residues, Formula weight is not available
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 Vector: pET23b(+)
Entity Sequences (FASTA):
C-domain_of_human_polypeptide_release_factor_eRF1: MSNVKFIQEKKLIGRYFDEI
SQDTGKYCFGVEDTLKALEM
GAVEILIVYENLDIMRYVLH
CQGTEEEKILYLTPEQEKDK
SHFTDKETGQEHELIESMPL
LEWFANNYKKFGATLEIVTD
KSQEGSQFVKGFGGIGGILR
YRVDFQGMEYQGGDDEFFDL
DDYLEHHHHHH
| Data type | Count |
| 13C chemical shifts | 315 |
| 15N chemical shifts | 160 |
| 1H chemical shifts | 160 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Human eRF1 C-domain | 1 |
Entity 1, Human eRF1 C-domain 171 residues - Formula weight is not available
| 1 | MET | SER | ASN | VAL | LYS | PHE | ILE | GLN | GLU | LYS | ||||
| 2 | LYS | LEU | ILE | GLY | ARG | TYR | PHE | ASP | GLU | ILE | ||||
| 3 | SER | GLN | ASP | THR | GLY | LYS | TYR | CYS | PHE | GLY | ||||
| 4 | VAL | GLU | ASP | THR | LEU | LYS | ALA | LEU | GLU | MET | ||||
| 5 | GLY | ALA | VAL | GLU | ILE | LEU | ILE | VAL | TYR | GLU | ||||
| 6 | ASN | LEU | ASP | ILE | MET | ARG | TYR | VAL | LEU | HIS | ||||
| 7 | CYS | GLN | GLY | THR | GLU | GLU | GLU | LYS | ILE | LEU | ||||
| 8 | TYR | LEU | THR | PRO | GLU | GLN | GLU | LYS | ASP | LYS | ||||
| 9 | SER | HIS | PHE | THR | ASP | LYS | GLU | THR | GLY | GLN | ||||
| 10 | GLU | HIS | GLU | LEU | ILE | GLU | SER | MET | PRO | LEU | ||||
| 11 | LEU | GLU | TRP | PHE | ALA | ASN | ASN | TYR | LYS | LYS | ||||
| 12 | PHE | GLY | ALA | THR | LEU | GLU | ILE | VAL | THR | ASP | ||||
| 13 | LYS | SER | GLN | GLU | GLY | SER | GLN | PHE | VAL | LYS | ||||
| 14 | GLY | PHE | GLY | GLY | ILE | GLY | GLY | ILE | LEU | ARG | ||||
| 15 | TYR | ARG | VAL | ASP | PHE | GLN | GLY | MET | GLU | TYR | ||||
| 16 | GLN | GLY | GLY | ASP | ASP | GLU | PHE | PHE | ASP | LEU | ||||
| 17 | ASP | ASP | TYR | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 18 | HIS |
sample_1: C-domain of human polypeptide release factor eRF1 1 mM; potassium phosphate 10 mM; potassium chloride 50 mM
sample_2: C-domain of human polypeptide release factor eRF1, [U-99% 15N], 1.1 mM; potassium phosphate 10 mM; potassium chloride 20 mM
sample_3: C-domain of human polypeptide release factor eRF1, [U-99% 13C; U-99% 15N], 0.8 mM; potassium phosphate 10 mM; potassium chloride 20 mM
sample_conditions_1: ionic strength: 0.08 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
VNMR, Varian - collection
xwinnmr, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
Pence, Wishart and Sykes - data analysis
| BMRB | 19506 |
| PDB | |
| DBJ | BAA13439 BAA85489 BAC33839 BAE31210 BAE31619 |
| EMBL | CAA57281 CAA57282 CAH93389 |
| GB | AAB49726 AAD43966 AAH13717 AAH14269 AAH85902 |
| REF | NP_001008345 NP_001069722 NP_001076236 NP_001126989 NP_001239075 |
| SP | P62495 P62496 P62497 Q0VCX5 Q5R4C7 |
| TPG | DAA27419 |
| AlphaFold | P62495 P62496 P62497 Q0VCX5 Q5R4C7 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks