BMRB Entry 15180
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15180
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Title: Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation. PubMed: 17279777
Deposition date: 2007-03-16 Original release date: 2007-10-26
Authors: Dancheck, Barbara; Peti, Wolfgang
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).
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
Entity Sequences (FASTA):
Spinophilin_PP1_binding_domain: GHMDEEDGEPPYEPESGCVE
IPGLSEEEDPAPSRKIHFST
APIQVFSTYSNEDYDRRNED
VDPMAASAEYELEKRVERLE
L
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 302 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 388 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Spinophilin PP1 binding domain | 1 |
Entities:
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 |
Samples:
sample_1: Spinophilin PP1 binding domain, [U-99% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%
sample_2: Spinophilin PP1 binding domain, [U-99% 13C; U-99% 15N], 670 uM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%
sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
XEASY v1.5, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| EMBL | CAC37685 CAD28455 |
| GB | AAB72005 AAC05183 AAI60878 AAR91608 EAW94636 |
| REF | NP_115984 NP_445926 NP_758465 XP_003131641 XP_003466916 |
| SP | O35274 Q6R891 Q96SB3 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts