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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/BMR18416
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Citation: Huang, Hsiao-Wen; Yu, Chin. "Backbone and side-chain resonance assignments (1H, 15N and 13C) of the ubiquitin homology domain of mouse BAG-1." Biomol. NMR Assignments 7, 235-239 (2013).
PubMed: 22903788
Assembly members:
ubiquitin_homology_domain_of_mouse_BAG-1, polymer, 97 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-1
Entity Sequences (FASTA):
ubiquitin_homology_domain_of_mouse_BAG-1: MAKTEEMVQTEEMETPRLSV
IVTHSNERYDLLVTPQQGNS
EPVVQDLAQLVEEATGVPLP
FQKLIFKGKSLKEMETPLSA
LGMQNGCRVMLIGEKSN
Data type | Count |
13C chemical shifts | 383 |
15N chemical shifts | 96 |
1H chemical shifts | 634 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ubiquitin homology of mouse BAG-1 | 1 |
Entity 1, ubiquitin homology of mouse BAG-1 97 residues - Formula weight is not available
1 | MET | ALA | LYS | THR | GLU | GLU | MET | VAL | GLN | THR | ||||
2 | GLU | GLU | MET | GLU | THR | PRO | ARG | LEU | SER | VAL | ||||
3 | ILE | VAL | THR | HIS | SER | ASN | GLU | ARG | TYR | ASP | ||||
4 | LEU | LEU | VAL | THR | PRO | GLN | GLN | GLY | ASN | SER | ||||
5 | GLU | PRO | VAL | VAL | GLN | ASP | LEU | ALA | GLN | LEU | ||||
6 | VAL | GLU | GLU | ALA | THR | GLY | VAL | PRO | LEU | PRO | ||||
7 | PHE | GLN | LYS | LEU | ILE | PHE | LYS | GLY | LYS | SER | ||||
8 | LEU | LYS | GLU | MET | GLU | THR | PRO | LEU | SER | ALA | ||||
9 | LEU | GLY | MET | GLN | ASN | GLY | CYS | ARG | VAL | MET | ||||
10 | LEU | ILE | GLY | GLU | LYS | SER | ASN |
sample_1: ubiquitin homology domain of mouse BAG-1, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
VNMR, Varian - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
PDB | |
DBJ | BAB26106 |
GB | AAC34259 AAH03722 AAH69918 AAH93509 EDL05422 |
REF | NP_001165210 NP_033866 |
SP | Q60739 |
AlphaFold | Q60739 Q60739 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks