BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27847

Title: Backbone resonance assignments and secondary structures of Ebola Nucleoprotein 600-739 construct.   PubMed: 31076990

Deposition date: 2019-03-20 Original release date: 2019-05-22

Authors: Lee, Woonghee; Tonelli, Marco; Wu, Chao; Aceti, David; Amarasinghe, Gaya; Markley, John

Citation: Lee, Woonghee; Tonelli, Marco; Wu, Chao; Aceti, David; Amarasinghe, Gaya; Markley, John. "Backbone resonance assignments and secondary structure of Ebola nucleoprotein 600-739 construct"  Biomol. NMR Assignments 3, 315-319 (2019).

Assembly members:
eNP-CTD, polymer, 140 residues, Formula weight is not available

Natural source:   Common Name: Ebola virus   Taxonomy ID: 1570291   Superkingdom: Viruses   Kingdom: not available   Genus/species: Ebolavirus Ebola virus

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

Entity Sequences (FASTA):
eNP-CTD: RTPTVAPPAPVYRDHSEKKE LPQDEQQDQDHTQEARNQDS DNTQSEHSFEEMYRHILRSQ GPFDAVLYYHMMKDEPVVFS TSDGKEYTYPDSLEEEYPPW LTEKEAMNEENRFVTLDGQQ FYWPVMNHKNKFMAILQHHQ

Data sets:
Data typeCount
13C chemical shifts405
15N chemical shifts129
1H chemical shifts129

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1eNP-CTD1

Entities:

Entity 1, eNP-CTD 140 residues - Formula weight is not available

1   ARGTHRPROTHRVALALAPROPROALAPRO
2   VALTYRARGASPHISSERGLULYSLYSGLU
3   LEUPROGLNASPGLUGLNGLNASPGLNASP
4   HISTHRGLNGLUALAARGASNGLNASPSER
5   ASPASNTHRGLNSERGLUHISSERPHEGLU
6   GLUMETTYRARGHISILELEUARGSERGLN
7   GLYPROPHEASPALAVALLEUTYRTYRHIS
8   METMETLYSASPGLUPROVALVALPHESER
9   THRSERASPGLYLYSGLUTYRTHRTYRPRO
10   ASPSERLEUGLUGLUGLUTYRPROPROTRP
11   LEUTHRGLULYSGLUALAMETASNGLUGLU
12   ASNARGPHEVALTHRLEUASPGLYGLNGLN
13   PHETYRTRPPROVALMETASNHISLYSASN
14   LYSPHEMETALAILELEUGLNHISHISGLN

Samples:

sample_1: eNP-CTD, [U-100% 13C; U-100% 15N], 1.3 mM; HEPES buffer 10 mM; sodium chloride 150 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H,15N TROSY-HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D NOESY 15N-TROSY-HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Ying et al. - processing

SPARKY vNMRFAM-SPARKY, Lee, W et al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Bruker Avance 800 MHz

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