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/BMR16263
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: de Sa Pinheiro, Anderson; Ehart, Angela; Ebner, Nina; Proell, Martina; Schwarzenbacher, Robert; Peti, Wolfgang. "Backbone and sidechain (1)H, (15)N and (13)C assignments of the NLRP7 pyrin domain." Biomol. NMR Assignments 3, 207-209 (2009).
PubMed: 19888692
Assembly members:
NLRP7_Pyd, polymer, 106 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: pHis parallel
Entity Sequences (FASTA):
NLRP7_Pyd: GHMTSPQLEWTLQTLLEQLN
EDELKSFKSLLWAFPLEDVL
QKTPWSEVEEADGKKLAEIL
VNTSSENWIRNATVNILEEM
NLTELCKMAKAEMMEDGQLE
HHHHHH
Data type | Count |
13C chemical shifts | 417 |
15N chemical shifts | 101 |
1H chemical shifts | 713 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | subunit_1 | 1 |
Entity 1, subunit_1 106 residues - Formula weight is not available
Residues 1 and 2 (GH) are part of the protease cleavage site used to cleave off the solubility tag used in the expression of this protein. Residues 101-106 comprise a His6-tag used for purification.
1 | GLY | HIS | MET | THR | SER | PRO | GLN | LEU | GLU | TRP | ||||
2 | THR | LEU | GLN | THR | LEU | LEU | GLU | GLN | LEU | ASN | ||||
3 | GLU | ASP | GLU | LEU | LYS | SER | PHE | LYS | SER | LEU | ||||
4 | LEU | TRP | ALA | PHE | PRO | LEU | GLU | ASP | VAL | LEU | ||||
5 | GLN | LYS | THR | PRO | TRP | SER | GLU | VAL | GLU | GLU | ||||
6 | ALA | ASP | GLY | LYS | LYS | LEU | ALA | GLU | ILE | LEU | ||||
7 | VAL | ASN | THR | SER | SER | GLU | ASN | TRP | ILE | ARG | ||||
8 | ASN | ALA | THR | VAL | ASN | ILE | LEU | GLU | GLU | MET | ||||
9 | ASN | LEU | THR | GLU | LEU | CYS | LYS | MET | ALA | LYS | ||||
10 | ALA | GLU | MET | MET | GLU | ASP | GLY | GLN | LEU | GLU | ||||
11 | HIS | HIS | HIS | HIS | HIS | HIS |
sample_1: NLRP7 Pyd, [U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.25 mM; H2O 90%; D2O 10%
sample_2: NLRP7 Pyd, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.25 mM; H2O 90%; D2O 10%
sample_3: NLRP7 Pyd 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.25 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; 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 HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCACO | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
2D DQF-COSY | sample_3 | isotropic | sample_conditions_1 |
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
PDB | |
DBJ | BAG63894 |
GB | AAI09125 AAI09126 AAL69963 AAO18158 AIC57936 |
REF | NP_001120727 NP_631915 NP_996611 XP_004061498 XP_006723138 |
SP | Q8WX94 |
TPG | DAA01246 |
AlphaFold | Q8WX94 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks