BMRB Entry 30162

Name: Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity
Published: 2017-08-22

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PDB ID: 5t42
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30162
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2016-08-28

Original release date:

2017-08-22

Authors:

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

Citation:

Citation: Lee, J.; Nyenhuis, D.; Nelson, E.; Cafiso, D.; White, J.; Tamm, L.. "Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity" Proc. Natl. Acad. Sci. U. S. A. 114, E7987-E7996 (2017).
PubMed: 28874543

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDKTLPDQGDNDNWWTGWR QWIPAGIGVTGVVIAVIALF AIAKFVF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	187
15N chemical shifts	49
1H chemical shifts	284

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 47 residues - 5134.819 Da.

1

GLY

SER

ASP

LYS

THR

LEU

PRO

ASP

GLN

GLY

2

ASP

ASN

ASP

ASN

TRP

THR

GLY

TRP

ARG

3

GLN

TRP

ILE

PRO

ALA

GLY

ILE

GLY

VAL

THR

4

GLY

VAL

ILE

ALA

VAL

ILE

ALA

LEU

PHE

5

ALA

ILE

ALA

LYS

PHE

VAL

PHE

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1
HCCCONH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_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

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