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.
Deposition date:
2007-03-16
Original release date:
2007-10-26
Authors:
Dancheck, Barbara; Peti, Wolfgang
Citation:

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:

Assembly members:
Spinophilin_PP1_binding_domain, polymer, 81 residues, 9231 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Spinophilin_PP1_binding_domain: GHMDEEDGEPPYEPESGCVE IPGLSEEEDPAPSRKIHFST APIQVFSTYSNEDYDRRNED VDPMAASAEYELEKRVERLE L

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts68
1H chemical shifts388

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Spinophilin PP1 binding domain1

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   GLYHISMETASPGLUGLUASPGLYGLUPRO
2   PROTYRGLUPROGLUSERGLYCYSVALGLU
3   ILEPROGLYLEUSERGLUGLUGLUASPPRO
4   ALAPROSERARGLYSILEHISPHESERTHR
5   ALAPROILEGLNVALPHESERTHRTYRSER
6   ASNGLUASPTYRASPARGARGASNGLUASP
7   VALASPPROMETALAALASERALAGLUTYR
8   GLULEUGLULYSARGVALGLUARGLEUGLU
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_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
AlphaFold O35274 Q6R891 Q96SB3

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks