Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10275
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: Sato, M.; Tochio, N.; Koshiba, S.; Watanabe, M.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structures of the PAAD_DAPIN domain of mus musculus
interferon-activatable protein 205" .
Assembly members:
Interferon-activable protein 205, polymer, 94 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: cell free synthesis Vector: P051212-10
Entity Sequences (FASTA):
Interferon-activable protein 205: GSSGSSGIVLLRGLECINKH
YFSLFKSLLARDLNLERDNQ
EQYTTIQIANMMEEKFPADS
GLGKLIEFCEEVPALRKRAE
ILKKERSESGPSSG
Data type | Count |
13C chemical shifts | 381 |
15N chemical shifts | 90 |
1H chemical shifts | 645 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Interferon-activable protein 205 | 1 |
Entity 1, Interferon-activable protein 205 94 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | ILE | VAL | LEU | ||||
2 | LEU | ARG | GLY | LEU | GLU | CYS | ILE | ASN | LYS | HIS | ||||
3 | TYR | PHE | SER | LEU | PHE | LYS | SER | LEU | LEU | ALA | ||||
4 | ARG | ASP | LEU | ASN | LEU | GLU | ARG | ASP | ASN | GLN | ||||
5 | GLU | GLN | TYR | THR | THR | ILE | GLN | ILE | ALA | ASN | ||||
6 | MET | MET | GLU | GLU | LYS | PHE | PRO | ALA | ASP | SER | ||||
7 | GLY | LEU | GLY | LYS | LEU | ILE | GLU | PHE | CYS | GLU | ||||
8 | GLU | VAL | PRO | ALA | LEU | ARG | LYS | ARG | ALA | GLU | ||||
9 | ILE | LEU | LYS | LYS | GLU | ARG | SER | GLU | SER | GLY | ||||
10 | PRO | SER | SER | GLY |
sample_1: Interferon-activable protein 205, [U-13C; U-15N], 0.5 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
xwinnmr v3.5, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.9820, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - refinement, structure solution
PDB | |
DBJ | BAC37930 BAE29634 BAE31415 BAE31495 BAE38635 |
EMBL | CAJ18559 |
GB | AAA39313 AAB26880 AAH10546 AAI32315 AAI32317 |
PIR | I56329 |
REF | NP_001028622 NP_001288674 NP_032355 XP_006496738 |
SP | P15092 Q08619 |
AlphaFold | P15092 Q08619 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks