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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/BMR18242
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Citation: Su, Ming-Yuan; Chang, Chung-I; Chang, Chi-Fon. "1H, 13C and 15N resonance assignments of the pyrin domain from human PYNOD." Biomol. NMR Assignments 7, 141-143 (2013).
PubMed: 22618865
Assembly members:
PYNOD_PYD, polymer, 102 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: pETM11
Entity Sequences (FASTA):
PYNOD_PYD: GAMAMAKARKPREALLWALS
DLEENDFKKLKFYLRDMTLS
EGQPPLARGELEGLIPVDLA
ELLISKYGEKEAVKVVLKGL
KVMNLLELVDQLSHICLHDY
RE
Data type | Count |
13C chemical shifts | 428 |
15N chemical shifts | 93 |
1H chemical shifts | 719 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PYNOD PYD | 1 |
Entity 1, PYNOD PYD 102 residues - Formula weight is not available
1 | GLY | ALA | MET | ALA | MET | ALA | LYS | ALA | ARG | LYS | ||||
2 | PRO | ARG | GLU | ALA | LEU | LEU | TRP | ALA | LEU | SER | ||||
3 | ASP | LEU | GLU | GLU | ASN | ASP | PHE | LYS | LYS | LEU | ||||
4 | LYS | PHE | TYR | LEU | ARG | ASP | MET | THR | LEU | SER | ||||
5 | GLU | GLY | GLN | PRO | PRO | LEU | ALA | ARG | GLY | GLU | ||||
6 | LEU | GLU | GLY | LEU | ILE | PRO | VAL | ASP | LEU | ALA | ||||
7 | GLU | LEU | LEU | ILE | SER | LYS | TYR | GLY | GLU | LYS | ||||
8 | GLU | ALA | VAL | LYS | VAL | VAL | LEU | LYS | GLY | LEU | ||||
9 | LYS | VAL | MET | ASN | LEU | LEU | GLU | LEU | VAL | ASP | ||||
10 | GLN | LEU | SER | HIS | ILE | CYS | LEU | HIS | ASP | TYR | ||||
11 | ARG | GLU |
sample_1: PYNOD PYD, [U-13C; U-15N], 0.2 mM
sample_conditions_1: ionic strength: 140 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | 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 |
CARA, Keller and Wuthrich - chemical shift assignment
PDB | |
GB | AAI04958 AAO18161 AAS67384 AIC53619 EAW68640 |
REF | NP_789791 XP_003254944 XP_003313013 XP_003818292 XP_004050717 |
SP | Q86W26 |
TPG | DAA01243 |
AlphaFold | Q86W26 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
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