BMRB Entry 18421

Name: Capsid protein from Equine Infectious Anemia Virus
Published: 2012-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18421

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Capsid protein from Equine Infectious Anemia Virus

Deposition date:

2012-04-24

Original release date:

2012-09-14

Authors:

Chen, Kang; Tjandra, Nico

Citation:

Citation: Chen, Kang; Piszczek, Grzegorz; Carter, Carol; Tjandra, Nico. "The maturational refolding of the -hairpin motif of equine infectious anemia virus capsid protein extends its helix 1 at capsid assembly locus." J. Biol. Chem. 288, 1511-1520 (2013).
PubMed: 23184932

Assembly members:

Assembly members:
eiavCA, polymer, 230 residues, Formula weight is not available

Natural source:

Natural source: Common Name: equine infectious anemia virus Taxonomy ID: 11665 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus equine infectious anemia virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
eiavCA: PIMIDGAGNRNFRPLTPRGY TTWVNTIQTNGLLNEASQNL FGILSVDCTSEEMNAFLDVV PGQAGQKQILLDAIDKIADD WDNRHPLPNAPLVAPPQGPI PMTARFIRGLGVPRERQMEP AFDQFRQTYRQWIIEAMSEG IKVMIGKPKAQNIRQGAKEP YPEFVDRLLSQIKSEGHPQE ISKFLTDTLTIQNANEECRN AMRHLRPEDTLEEKMYACRD IGTTKQKMML

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	588
15N chemical shifts	185
1H chemical shifts	188

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	eiavCA	1

Entities:

Entity 1, eiavCA 230 residues - Formula weight is not available

1	PRO	ILE	MET	ILE	ASP	GLY	ALA	GLY	ASN	ARG
2	ASN	PHE	ARG	PRO	LEU	THR	PRO	ARG	GLY	TYR
3	THR	THR	TRP	VAL	ASN	THR	ILE	GLN	THR	ASN
4	GLY	LEU	LEU	ASN	GLU	ALA	SER	GLN	ASN	LEU
5	PHE	GLY	ILE	LEU	SER	VAL	ASP	CYS	THR	SER
6	GLU	GLU	MET	ASN	ALA	PHE	LEU	ASP	VAL	VAL
7	PRO	GLY	GLN	ALA	GLY	GLN	LYS	GLN	ILE	LEU
8	LEU	ASP	ALA	ILE	ASP	LYS	ILE	ALA	ASP	ASP
9	TRP	ASP	ASN	ARG	HIS	PRO	LEU	PRO	ASN	ALA
10	PRO	LEU	VAL	ALA	PRO	PRO	GLN	GLY	PRO	ILE
11	PRO	MET	THR	ALA	ARG	PHE	ILE	ARG	GLY	LEU
12	GLY	VAL	PRO	ARG	GLU	ARG	GLN	MET	GLU	PRO
13	ALA	PHE	ASP	GLN	PHE	ARG	GLN	THR	TYR	ARG
14	GLN	TRP	ILE	ILE	GLU	ALA	MET	SER	GLU	GLY
15	ILE	LYS	VAL	MET	ILE	GLY	LYS	PRO	LYS	ALA
16	GLN	ASN	ILE	ARG	GLN	GLY	ALA	LYS	GLU	PRO
17	TYR	PRO	GLU	PHE	VAL	ASP	ARG	LEU	LEU	SER
18	GLN	ILE	LYS	SER	GLU	GLY	HIS	PRO	GLN	GLU
19	ILE	SER	LYS	PHE	LEU	THR	ASP	THR	LEU	THR
20	ILE	GLN	ASN	ALA	ASN	GLU	GLU	CYS	ARG	ASN
21	ALA	MET	ARG	HIS	LEU	ARG	PRO	GLU	ASP	THR
22	LEU	GLU	GLU	LYS	MET	TYR	ALA	CYS	ARG	ASP
23	ILE	GLY	THR	THR	LYS	GLN	LYS	MET	MET	LEU

Samples:

sample_1: eiavCA, [U-13C; U-15N; U-2H], 0.15 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.7; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HMQC-NOE-HSQC	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz

BMRB	18815
PDB	1EIA 2EIA
DBJ	BAB12103 BAB12109
GB	AAA43003 AAA43010 AAA43011 AAB59861 AAC03760
REF	NP_056901
SP	P69730 P69731 P69732
AlphaFold	P69730 P69731 P69732

1	PRO	ILE	MET	ILE	ASP	GLY	ALA	GLY	ASN	ARG
2	ASN	PHE	ARG	PRO	LEU	THR	PRO	ARG	GLY	TYR
3	THR	THR	TRP	VAL	ASN	THR	ILE	GLN	THR	ASN
4	GLY	LEU	LEU	ASN	GLU	ALA	SER	GLN	ASN	LEU
5	PHE	GLY	ILE	LEU	SER	VAL	ASP	CYS	THR	SER
6	GLU	GLU	MET	ASN	ALA	PHE	LEU	ASP	VAL	VAL
7	PRO	GLY	GLN	ALA	GLY	GLN	LYS	GLN	ILE	LEU
8	LEU	ASP	ALA	ILE	ASP	LYS	ILE	ALA	ASP	ASP
9	TRP	ASP	ASN	ARG	HIS	PRO	LEU	PRO	ASN	ALA
10	PRO	LEU	VAL	ALA	PRO	PRO	GLN	GLY	PRO	ILE
11	PRO	MET	THR	ALA	ARG	PHE	ILE	ARG	GLY	LEU
12	GLY	VAL	PRO	ARG	GLU	ARG	GLN	MET	GLU	PRO
13	ALA	PHE	ASP	GLN	PHE	ARG	GLN	THR	TYR	ARG
14	GLN	TRP	ILE	ILE	GLU	ALA	MET	SER	GLU	GLY
15	ILE	LYS	VAL	MET	ILE	GLY	LYS	PRO	LYS	ALA
16	GLN	ASN	ILE	ARG	GLN	GLY	ALA	LYS	GLU	PRO
17	TYR	PRO	GLU	PHE	VAL	ASP	ARG	LEU	LEU	SER
18	GLN	ILE	LYS	SER	GLU	GLY	HIS	PRO	GLN	GLU
19	ILE	SER	LYS	PHE	LEU	THR	ASP	THR	LEU	THR
20	ILE	GLN	ASN	ALA	ASN	GLU	GLU	CYS	ARG	ASN
21	ALA	MET	ARG	HIS	LEU	ARG	PRO	GLU	ASP	THR
22	LEU	GLU	GLU	LYS	MET	TYR	ALA	CYS	ARG	ASP
23	ILE	GLY	THR	THR	LYS	GLN	LYS	MET	MET	LEU

1	PRO	ILE	MET	ILE	ASP	GLY	ALA	GLY	ASN	ARG
2	ASN	PHE	ARG	PRO	LEU	THR	PRO	ARG	GLY	TYR
3	THR	THR	TRP	VAL	ASN	THR	ILE	GLN	THR	ASN
4	GLY	LEU	LEU	ASN	GLU	ALA	SER	GLN	ASN	LEU
5	PHE	GLY	ILE	LEU	SER	VAL	ASP	CYS	THR	SER
6	GLU	GLU	MET	ASN	ALA	PHE	LEU	ASP	VAL	VAL
7	PRO	GLY	GLN	ALA	GLY	GLN	LYS	GLN	ILE	LEU
8	LEU	ASP	ALA	ILE	ASP	LYS	ILE	ALA	ASP	ASP
9	TRP	ASP	ASN	ARG	HIS	PRO	LEU	PRO	ASN	ALA
10	PRO	LEU	VAL	ALA	PRO	PRO	GLN	GLY	PRO	ILE
11	PRO	MET	THR	ALA	ARG	PHE	ILE	ARG	GLY	LEU
12	GLY	VAL	PRO	ARG	GLU	ARG	GLN	MET	GLU	PRO
13	ALA	PHE	ASP	GLN	PHE	ARG	GLN	THR	TYR	ARG
14	GLN	TRP	ILE	ILE	GLU	ALA	MET	SER	GLU	GLY
15	ILE	LYS	VAL	MET	ILE	GLY	LYS	PRO	LYS	ALA
16	GLN	ASN	ILE	ARG	GLN	GLY	ALA	LYS	GLU	PRO
17	TYR	PRO	GLU	PHE	VAL	ASP	ARG	LEU	LEU	SER
18	GLN	ILE	LYS	SER	GLU	GLY	HIS	PRO	GLN	GLU
19	ILE	SER	LYS	PHE	LEU	THR	ASP	THR	LEU	THR
20	ILE	GLN	ASN	ALA	ASN	GLU	GLU	CYS	ARG	ASN
21	ALA	MET	ARG	HIS	LEU	ARG	PRO	GLU	ASP	THR
22	LEU	GLU	GLU	LYS	MET	TYR	ALA	CYS	ARG	ASP
23	ILE	GLY	THR	THR	LYS	GLN	LYS	MET	MET	LEU