BMRB Entry 26655

Title:
1H, 13C and 15N resonance assignments of the intrinsically disordered region of the nuclear envelope protein emerin
Deposition date:
2015-09-11
Original release date:
2016-02-12
Authors:
Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie
Citation:

Citation: Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie. "1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin"  Biomol. NMR Assign. 10, 179-182 (2016).
PubMed: 26725056

Assembly members:

Assembly members:
emerin_67-170, polymer, 105 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: pETM-13

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts96
1H chemical shifts96

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1emerin 67-1701

Entities:

Entity 1, emerin 67-170 105 residues - Formula weight is not available

1   GLYTHRARGGLYASPALAASPMETTYRASP
2   LEUPROLYSLYSGLUASPALALEULEUTYR
3   GLNSERLYSGLYTYRASNASPASPTYRTYR
4   GLUGLUSERTYRPHETHRTHRARGTHRTYR
5   GLYGLUPROGLUSERALAGLYPROSERARG
6   ALAVALARGGLNSERVALTHRSERPHEPRO
7   ASPALAASPALAPHEHISHISGLNVALHIS
8   ASPASPASPLEULEUSERSERSERGLUGLU
9   GLUCYSLYSASPARGGLUARGPROMETTYR
10   GLYARGASPSERALATYRGLNSERILETHR
11   HISTYRARGPROVAL

Samples:

sample_1: emerin 67-170, [U-100% 13C; U-100% 15N], 500 uM; urea 8 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 30 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 750 MHz

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