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 30162

Title: Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity

Authors: Lee, J.; Nyenhuis, D.; Nelson, E.; Cafiso, D.; White, J.; Tamm, L.

Citation: Lee, J.; Nyenhuis, D.; Nelson, E.; Cafiso, D.; White, J.; Tamm, L.. "Ebola virus, membrane protein, protein-protein interaction, NMR, membrane fusion"  . ., .-..

Assembly members:
entity_1, polymer, 47 residues, 5134.819 Da.

Natural source:   Common Name: ZEBOV   Taxonomy ID: 128951   Superkingdom: Viruses   Kingdom: not available   Genus/species: Ebolavirus ZEBOV

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: GSDKTLPDQGDNDNWWTGWR QWIPAGIGVTGVVIAVIALF AIAKFVF

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts49
1H chemical shifts284

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 47 residues - 5134.819 Da.

1   GLYSERASPLYSTHRLEUPROASPGLNGLY
2   ASPASNASPASNTRPTRPTHRGLYTRPARG
3   GLNTRPILEPROALAGLYILEGLYVALTHR
4   GLYVALVALILEALAVALILEALALEUPHE
5   ALAILEALALYSPHEVALPHE

Samples:

sample_1: EBOV_MPER/TM, [U-99% 15N], 500 uM; Pi 30 mM; NaCl 100 mM

sample_2: EBOV_MPER/TM, [U-99% 13C; U-99% 15N], 500 uM; Pi 30 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 125 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
HCCCONHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - geometry optimization

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

ProcheckNMR, Laskowski and MacArthur - data analysis

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

Related Database Links: