BMRB Entry 26705

Title:
Backbone chemical shifts of the oligomerization inhibited mutant of the CASKIN2 SAM domain tandem
Deposition date:
2015-11-09
Original release date:
2016-06-29
Authors:
Donaldson, Logan
Citation:

Citation: Smirnova, Ekaterina; Kwan, Jamie; Siu, Ryan; Gao, Xin; Zoid, Georg; Demeler, Borries; Saridakis, Vivian; Donaldson, Logan. "A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein"  Cell Commun. Signal 14, 17-17 (2016).
PubMed: 27549312

Assembly members:

Assembly members:
CASKIN2, polymer, 171 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: pET28

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts114
1H chemical shifts114

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SAMSAM monomer1

Entities:

Entity 1, SAMSAM monomer 171 residues - Formula weight is not available

1   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERMETGLU
3   GLNLEULEUGLUGLYLYSASPALAGLNALA
4   ILEHISASNTRPLEUSERGLUPHEGLNLEU
5   GLUGLYTYRTHRALAHISPHELEUGLNALA
6   GLYTYRASPVALPROTHRILESERARGMET
7   THRPROGLUASPLEUTHRALAILEGLYVAL
8   THRLYSPROASPHISARGGLULYSILEALA
9   SERGLUILEALAGLNLEUSERILEALAGLU
10   TRPLEUPROSERTYRILEPROTHRASPLEU
11   LEUGLUTRPLEUCYSALALEUGLYLEUPRO
12   GLNTYRHISLYSGLNLEUVALSERSERGLY
13   TYRASPSERMETGLYLEUVALALAASPLEU
14   THRTRPGLUGLULEUGLNGLUILEGLYVAL
15   ASNLYSLEUGLYHISGLNLYSLYSLEUMET
16   LEUGLYVALLYSARGLEUALAGLULEUARG
17   ARGGLYLEULEUGLNGLYGLUALALEUSER
18   GLU

Samples:

sample_1: CASKIN2, [U-99% 13C; U-99% 15N], 0.8 mM; potassium chloride 20 mM; sodium azide 0.05 % w/v; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

Analysis v2.4, CCPN - chemical shift assignment

NMR spectrometers:

  • 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