BMRB Entry 15176

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15176

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Title:
Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation.
Deposition date:
2007-03-15
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:
Darpp-32, polymer, 120 residues, Formula weight is not available

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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Darpp-32: GHMDPKGRKKIQFSVPAPPS QLDPRQVEMIRRRRPTPALL FRVSEHSSPEEESSPHQRTS GEGHHPKSKRPNPSAYTPPS LKAVQRIAESHLQTISNLSE NQASEEEDELGELRELGYPQ

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts102
1H chemical shifts689

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Darpp-321

Entities:

Entity 1, Darpp-32 120 residues - Formula weight is not available

Residues 1 - 2 (G H) are cloning artifacts. Residues 3 - 120 are Darpp-32 residues 1 - 118.

1   GLYHISMETASPPROLYSGLYARGLYSLYS
2   ILEGLNPHESERVALPROALAPROPROSER
3   GLNLEUASPPROARGGLNVALGLUMETILE
4   ARGARGARGARGPROTHRPROALALEULEU
5   PHEARGVALSERGLUHISSERSERPROGLU
6   GLUGLUSERSERPROHISGLNARGTHRSER
7   GLYGLUGLYHISHISPROLYSSERLYSARG
8   PROASNPROSERALATYRTHRPROPROSER
9   LEULYSALAVALGLNARGILEALAGLUSER
10   HISLEUGLNTHRILESERASNLEUSERGLU
11   ASNGLNALASERGLUGLUGLUASPGLULEU
12   GLYGLULEUARGGLULEUGLYTYRPROGLN

Samples:

sample_1: Darpp-32, [U-99% 13C; U-99% 15N], 750 uM; sodium phosphate 50 mM; sodium chloride 50 mM; PMSF 250 uM; D2O 10%

sample_2: Darpp-32, [U-99% 15N], 750 uM; sodium phosphate 50 mM; sodium chloride 50 mM; PMSF 250 uM; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_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:

BMRB 15865
GB AAH78954 AAT11858 EDM05918 EDM05919
REF NP_612530
SP Q6J4I0
AlphaFold Q6J4I0

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