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 18177

Title: Backbone chemical shift assignments for the reduced form of cVIMP-Cys   PubMed: 22700979

Deposition date: 2012-01-04 Original release date: 2012-06-18

Authors: Christensen, Lea Cecilie; Teilum, Kaare; Ellgaard, Lars

Citation: Christensen, Lea Cecilie; Jensen, Njal Winther; Vala, Andrea; Kamarauskaite, Jurate; Johansson, Linda; Winther, Jakob Rahr; Hofmann, Kay; Teilum, Kaare; Ellgaard, Lars. "The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region."  J. Biol. Chem. 287, 26388-26399 (2012).

Assembly members:
cVIMP-Cys_red, polymer, 142 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):
cVIMP-Cys_red: MQKLSARLRALRQRQLDRAA AAVEPDVVVKRQEALAAARL KMQEELNAQVEKHKEKLKQL EEEKRRQKIEMWDSMQEGKS YKGNAKKPQEEDSPGPSTSS VLKRKSDRKPLRGGGYNPLS GEGGGACSWRPGRRGPSSGG CG

Data sets:
Data typeCount
13C chemical shifts241
15N chemical shifts81
1H chemical shifts81

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cVIMP-Cys1

Entities:

Entity 1, cVIMP-Cys 142 residues - Formula weight is not available

Residues 2-142 in the sequence represent residues 49-189 in human VIMP (SelS)

1   METGLNLYSLEUSERALAARGLEUARGALA
2   LEUARGGLNARGGLNLEUASPARGALAALA
3   ALAALAVALGLUPROASPVALVALVALLYS
4   ARGGLNGLUALALEUALAALAALAARGLEU
5   LYSMETGLNGLUGLULEUASNALAGLNVAL
6   GLULYSHISLYSGLULYSLEULYSGLNLEU
7   GLUGLUGLULYSARGARGGLNLYSILEGLU
8   METTRPASPSERMETGLNGLUGLYLYSSER
9   TYRLYSGLYASNALALYSLYSPROGLNGLU
10   GLUASPSERPROGLYPROSERTHRSERSER
11   VALLEULYSARGLYSSERASPARGLYSPRO
12   LEUARGGLYGLYGLYTYRASNPROLEUSER
13   GLYGLUGLYGLYGLYALACYSSERTRPARG
14   PROGLYARGARGGLYPROSERSERGLYGLY
15   CYSGLY

Samples:

cVIMP-Cys_red_sample: D2O 10%; DSS 1%; sodium phosphate 50 mM; EDTA 1 mM; sodium chloride 150 mM; cVIMP-Cys, [U-100% 13C; U-100% 15N], 265 uM; TCEP 10 mM; sodium azide 1%; H2O 90%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCcVIMP-Cys_red_sampleisotropicsample_conditions_1
3D HNCOcVIMP-Cys_red_sampleisotropicsample_conditions_1
3D HNCAcVIMP-Cys_red_sampleisotropicsample_conditions_1
3D HNNcVIMP-Cys_red_sampleisotropicsample_conditions_1
3D HNCACBcVIMP-Cys_red_sampleisotropicsample_conditions_1
3D CBCA(CO)NHcVIMP-Cys_red_sampleisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

CCPN-analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 750 MHz

Related Database Links:

BMRB 18176
GB AAF67483 AAH05840 AAI07775 AAK15708 AAP85541
REF NP_001108228 NP_001186934 NP_060915 NP_982298 XP_003281631
SP Q9BQE4

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts