BMRB Entry 27847

Name: Backbone resonance assignments and secondary structures of Ebola Nucleoprotein 600-739 construct.
Published: 2019-05-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27847

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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:

Backbone resonance assignments and secondary structures of Ebola Nucleoprotein 600-739 construct.

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:

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).
PubMed: 31076990

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: His6-MBP-Parallel1

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	129
1H chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	eNP-CTD	1

Entities:

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

1	ARG	THR	PRO	THR	VAL	ALA	PRO	PRO	ALA	PRO
2	VAL	TYR	ARG	ASP	HIS	SER	GLU	LYS	LYS	GLU
3	LEU	PRO	GLN	ASP	GLU	GLN	GLN	ASP	GLN	ASP
4	HIS	THR	GLN	GLU	ALA	ARG	ASN	GLN	ASP	SER
5	ASP	ASN	THR	GLN	SER	GLU	HIS	SER	PHE	GLU
6	GLU	MET	TYR	ARG	HIS	ILE	LEU	ARG	SER	GLN
7	GLY	PRO	PHE	ASP	ALA	VAL	LEU	TYR	TYR	HIS
8	MET	MET	LYS	ASP	GLU	PRO	VAL	VAL	PHE	SER
9	THR	SER	ASP	GLY	LYS	GLU	TYR	THR	TYR	PRO
10	ASP	SER	LEU	GLU	GLU	GLU	TYR	PRO	PRO	TRP
11	LEU	THR	GLU	LYS	GLU	ALA	MET	ASN	GLU	GLU
12	ASN	ARG	PHE	VAL	THR	LEU	ASP	GLY	GLN	GLN
13	PHE	TYR	TRP	PRO	VAL	MET	ASN	HIS	LYS	ASN
14	LYS	PHE	MET	ALA	ILE	LEU	GLN	HIS	HIS	GLN

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:

Name	Sample	Sample state	Sample conditions
2D 1H,15N TROSY-HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CB	sample_1	isotropic	sample_conditions_1
3D NOESY 15N-TROSY-HSQC	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

1	ARG	THR	PRO	THR	VAL	ALA	PRO	PRO	ALA	PRO
2	VAL	TYR	ARG	ASP	HIS	SER	GLU	LYS	LYS	GLU
3	LEU	PRO	GLN	ASP	GLU	GLN	GLN	ASP	GLN	ASP
4	HIS	THR	GLN	GLU	ALA	ARG	ASN	GLN	ASP	SER
5	ASP	ASN	THR	GLN	SER	GLU	HIS	SER	PHE	GLU
6	GLU	MET	TYR	ARG	HIS	ILE	LEU	ARG	SER	GLN
7	GLY	PRO	PHE	ASP	ALA	VAL	LEU	TYR	TYR	HIS
8	MET	MET	LYS	ASP	GLU	PRO	VAL	VAL	PHE	SER
9	THR	SER	ASP	GLY	LYS	GLU	TYR	THR	TYR	PRO
10	ASP	SER	LEU	GLU	GLU	GLU	TYR	PRO	PRO	TRP
11	LEU	THR	GLU	LYS	GLU	ALA	MET	ASN	GLU	GLU
12	ASN	ARG	PHE	VAL	THR	LEU	ASP	GLY	GLN	GLN
13	PHE	TYR	TRP	PRO	VAL	MET	ASN	HIS	LYS	ASN
14	LYS	PHE	MET	ALA	ILE	LEU	GLN	HIS	HIS	GLN

1	ARG	THR	PRO	THR	VAL	ALA	PRO	PRO	ALA	PRO
2	VAL	TYR	ARG	ASP	HIS	SER	GLU	LYS	LYS	GLU
3	LEU	PRO	GLN	ASP	GLU	GLN	GLN	ASP	GLN	ASP
4	HIS	THR	GLN	GLU	ALA	ARG	ASN	GLN	ASP	SER
5	ASP	ASN	THR	GLN	SER	GLU	HIS	SER	PHE	GLU
6	GLU	MET	TYR	ARG	HIS	ILE	LEU	ARG	SER	GLN
7	GLY	PRO	PHE	ASP	ALA	VAL	LEU	TYR	TYR	HIS
8	MET	MET	LYS	ASP	GLU	PRO	VAL	VAL	PHE	SER
9	THR	SER	ASP	GLY	LYS	GLU	TYR	THR	TYR	PRO
10	ASP	SER	LEU	GLU	GLU	GLU	TYR	PRO	PRO	TRP
11	LEU	THR	GLU	LYS	GLU	ALA	MET	ASN	GLU	GLU
12	ASN	ARG	PHE	VAL	THR	LEU	ASP	GLY	GLN	GLN
13	PHE	TYR	TRP	PRO	VAL	MET	ASN	HIS	LYS	ASN
14	LYS	PHE	MET	ALA	ILE	LEU	GLN	HIS	HIS	GLN

1	ARG	THR	PRO	THR	VAL	ALA	PRO	PRO	ALA	PRO
2	VAL	TYR	ARG	ASP	HIS	SER	GLU	LYS	LYS	GLU
3	LEU	PRO	GLN	ASP	GLU	GLN	GLN	ASP	GLN	ASP
4	HIS	THR	GLN	GLU	ALA	ARG	ASN	GLN	ASP	SER
5	ASP	ASN	THR	GLN	SER	GLU	HIS	SER	PHE	GLU
6	GLU	MET	TYR	ARG	HIS	ILE	LEU	ARG	SER	GLN
7	GLY	PRO	PHE	ASP	ALA	VAL	LEU	TYR	TYR	HIS
8	MET	MET	LYS	ASP	GLU	PRO	VAL	VAL	PHE	SER
9	THR	SER	ASP	GLY	LYS	GLU	TYR	THR	TYR	PRO
10	ASP	SER	LEU	GLU	GLU	GLU	TYR	PRO	PRO	TRP
11	LEU	THR	GLU	LYS	GLU	ALA	MET	ASN	GLU	GLU
12	ASN	ARG	PHE	VAL	THR	LEU	ASP	GLY	GLN	GLN
13	PHE	TYR	TRP	PRO	VAL	MET	ASN	HIS	LYS	ASN
14	LYS	PHE	MET	ALA	ILE	LEU	GLN	HIS	HIS	GLN