BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26655

Title: 1H, 13C and 15N resonance assignments of the intrinsically disordered region of the nuclear envelope protein emerin   PubMed: 26725056

Authors: Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie

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).

Assembly members:
emerin_67-170, polymer, 105 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
emerin_67-170: GTRGDADMYDLPKKEDALLY QSKGYNDDYYEESYFTTRTY GEPESAGPSRAVRQSVTSFP DADAFHHQVHDDDLLSSSEE ECKDRERPMYGRDSAYQSIT HYRPV

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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

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