BMRB Entry 26855

Title:
phosducin chemical shift
Deposition date:
2016-07-20
Original release date:
2017-08-23
Authors:
Kacirova, Miroslava; Novacek, Jiri; Man, Petr; Obsilova, Veronika; Obsil, Tomas
Citation:

Citation: Kacirova, Miroslava; Novacek, Jiri; Man, Petr; Obsilova, Veronika; Obsil, Tomas. "Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function"  Biophys. J. 112, 1339-1349 (2017).
PubMed: 28402877

Assembly members:

Assembly members:
PDC, polymer, 265 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15b

Data sets:
Data typeCount
13C chemical shifts402
15N chemical shifts155
1H chemical shifts197

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1phosducin1

Entities:

Entity 1, phosducin 265 residues - Formula weight is not available

1   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   GLUGLUALAALASERGLNSERLEUGLUGLU
4   ASPPHEGLUGLYGLNALATHRHISTHRGLY
5   PROLYSGLYVALILEASNASPTRPARGLYS
6   PHELYSLEUGLUSERGLUASPGLYASPSER
7   ILEPROPROSERLYSLYSGLUILELEUARG
8   LYSMETSERSERPROGLNSERARGASPASP
9   LYSASPSERLYSGLUARGMETSERARGLYS
10   METSERILEGLNGLUTYRGLULEUILEHIS
11   GLNASPLYSGLUASPGLUGLYCYSLEUARG
12   LYSTYRARGARGGLNCYSMETGLNASPMET
13   HISGLNLYSLEUSERPHEGLYPROARGTYR
14   GLYPHEVALTYRGLULEUGLUTHRGLYGLU
15   GLNPHELEUGLUTHRILEGLULYSGLUGLN
16   LYSVALTHRTHRILEVALVALASNILETYR
17   GLUASPGLYVALARGGLYCYSASPALALEU
18   ASNSERSERLEUGLUCYSLEUALAALAGLU
19   TYRPROMETVALLYSPHECYSLYSILEARG
20   ALASERASNTHRGLYALAGLYASPARGPHE
21   SERSERASPVALLEUPROTHRLEULEUVAL
22   TYRLYSGLYGLYGLULEUILESERASNPHE
23   ILESERVALALAGLUGLNPHEALAGLUASP
24   PHEPHEALAALAASPVALGLUSERPHELEU
25   ASNGLUTYRGLYLEULEUPROGLUARGGLU
26   ILEHISASPLEUGLYGLNTHRASNTHRGLU
27   ASPGLUASPILEGLU

Samples:

sample_1: PDC, [U-100% 13C; U-100% 15N], 0.2 mM; MES 50 mM; sodium chloride 100 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
5D HN(CA)CONHsample_1isotropicsample_conditions_1
5D HabCabCONHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz
  • Bruker Avance 950 MHz

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