Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15180
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Citation: Kelker, Matthew; Dancheck, Barbara; Ju, Tingting; Kessler, Rene; Hudak, Jebecka; Nairn, Angus; Peti, Wolfgang. "Structural basis for spinophilin-neurabin receptor interaction" Biochemistry 46, 2333-2344 (2007).
PubMed: 17279777
Assembly members:
Spinophilin_PP1_binding_domain, polymer, 81 residues, 9231 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-TEV
Entity Sequences (FASTA):
Spinophilin_PP1_binding_domain: GHMDEEDGEPPYEPESGCVE
IPGLSEEEDPAPSRKIHFST
APIQVFSTYSNEDYDRRNED
VDPMAASAEYELEKRVERLE
L
Data type | Count |
13C chemical shifts | 302 |
15N chemical shifts | 68 |
1H chemical shifts | 388 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Spinophilin PP1 binding domain | 1 |
Entity 1, Spinophilin PP1 binding domain 81 residues - 9231 Da.
Residues 1 - 3 (G H M) are cloning artifacts. Residues 4 - 81 are spinophilin PP1 binding domain residues 417 - 494.
1 | GLY | HIS | MET | ASP | GLU | GLU | ASP | GLY | GLU | PRO | ||||
2 | PRO | TYR | GLU | PRO | GLU | SER | GLY | CYS | VAL | GLU | ||||
3 | ILE | PRO | GLY | LEU | SER | GLU | GLU | GLU | ASP | PRO | ||||
4 | ALA | PRO | SER | ARG | LYS | ILE | HIS | PHE | SER | THR | ||||
5 | ALA | PRO | ILE | GLN | VAL | PHE | SER | THR | TYR | SER | ||||
6 | ASN | GLU | ASP | TYR | ASP | ARG | ARG | ASN | GLU | ASP | ||||
7 | VAL | ASP | PRO | MET | ALA | ALA | SER | ALA | GLU | TYR | ||||
8 | GLU | LEU | GLU | LYS | ARG | VAL | GLU | ARG | LEU | GLU | ||||
9 | LEU |
PDB | 3EGG 3EGH |
EMBL | CAC37685 CAD28455 |
GB | AAB72005 AAC05183 AAI60878 AAR91608 EAW94636 |
REF | NP_115984 NP_445926 NP_758465 XP_003131641 XP_003466916 |
SP | O35274 Q6R891 Q96SB3 |
AlphaFold | O35274 Q6R891 Q96SB3 |
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