Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11262
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Ubiquitin-like Domain in the 4931431F19Rik
Protein" .
Assembly members:
ubiquitin-like domain, polymer, 96 residues, Formula weight is not available
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P040705-07
Entity Sequences (FASTA):
ubiquitin-like domain: GSSGSSGVSGREPSSRIIRV
SVKTPQDCHEFFLAENSNVR
RFKKQISKYLHCNADRLVLI
FTGKILRDQDILSQRGILDG
STVHVVVRSHSGPSSG
Data type | Count |
13C chemical shifts | 373 |
15N chemical shifts | 85 |
1H chemical shifts | 600 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ubiquitin-like domain | 1 |
Entity 1, ubiquitin-like domain 96 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | VAL | SER | GLY | ||||
2 | ARG | GLU | PRO | SER | SER | ARG | ILE | ILE | ARG | VAL | ||||
3 | SER | VAL | LYS | THR | PRO | GLN | ASP | CYS | HIS | GLU | ||||
4 | PHE | PHE | LEU | ALA | GLU | ASN | SER | ASN | VAL | ARG | ||||
5 | ARG | PHE | LYS | LYS | GLN | ILE | SER | LYS | TYR | LEU | ||||
6 | HIS | CYS | ASN | ALA | ASP | ARG | LEU | VAL | LEU | ILE | ||||
7 | PHE | THR | GLY | LYS | ILE | LEU | ARG | ASP | GLN | ASP | ||||
8 | ILE | LEU | SER | GLN | ARG | GLY | ILE | LEU | ASP | GLY | ||||
9 | SER | THR | VAL | HIS | VAL | VAL | VAL | ARG | SER | HIS | ||||
10 | SER | GLY | PRO | SER | SER | GLY |
sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.51 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.0 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
xwinnmr v2.6, Bruker - collection
NMRPipe v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.921, Kobayashi, N. - data analysis
CYANA v1.0.8, Guntert, P. - refinement, structure solution
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks