BMRB Entry 25481
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25481
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Citation: Yagi, Hiromasa; Conroy, Paul; Leung, Eleanor; Law, Ruby; Whisstock, James; Norton, Raymond. "Structural Basis for Ca2+-mediated Interaction of the Perforin C2 Domain with Lipid Membranes" J. Biol. Chem. 290, 25213-25226 (2015).
PubMed: 26306037
Assembly members:
perforin_C2_domain, polymer, 125 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: recombinant technology Host organism: Escherichia coli Vector: pComb3X
Entity Sequences (FASTA):
perforin_C2_domain: AQRGLAHLVVSNFRAEHLAG
DATTATDAYLKVFFGGQEFR
TGVVWNNNNPRWTDKMDFEN
VLLSTGGPLRVQVWDADAGA
DDDLLGSCDRSPHSGFHEVT
CELNHGRVKFSYHAKSLPGH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 211 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 108 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | perforin C2 quad mutant | 1 |
Entities:
Entity 1, perforin C2 quad mutant 125 residues - Formula weight is not available
An extra Alanine is remained at N-terminal as a result of cleavage of the signal sequence. Gly + His6 tag are attached at C-terminal.
| 1 | ALA | GLN | ARG | GLY | LEU | ALA | HIS | LEU | VAL | VAL | ||||
| 2 | SER | ASN | PHE | ARG | ALA | GLU | HIS | LEU | ALA | GLY | ||||
| 3 | ASP | ALA | THR | THR | ALA | THR | ASP | ALA | TYR | LEU | ||||
| 4 | LYS | VAL | PHE | PHE | GLY | GLY | GLN | GLU | PHE | ARG | ||||
| 5 | THR | GLY | VAL | VAL | TRP | ASN | ASN | ASN | ASN | PRO | ||||
| 6 | ARG | TRP | THR | ASP | LYS | MET | ASP | PHE | GLU | ASN | ||||
| 7 | VAL | LEU | LEU | SER | THR | GLY | GLY | PRO | LEU | ARG | ||||
| 8 | VAL | GLN | VAL | TRP | ASP | ALA | ASP | ALA | GLY | ALA | ||||
| 9 | ASP | ASP | ASP | LEU | LEU | GLY | SER | CYS | ASP | ARG | ||||
| 10 | SER | PRO | HIS | SER | GLY | PHE | HIS | GLU | VAL | THR | ||||
| 11 | CYS | GLU | LEU | ASN | HIS | GLY | ARG | VAL | LYS | PHE | ||||
| 12 | SER | TYR | HIS | ALA | LYS | SER | LEU | PRO | GLY | HIS | ||||
| 13 | HIS | HIS | HIS | HIS | HIS |
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