BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18421

Title: Capsid protein from Equine Infectious Anemia Virus   PubMed: 23184932

Deposition date: 2012-04-24 Original release date: 2012-09-14

Authors: Chen, Kang; Tjandra, Nico

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).

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

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:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts588
15N chemical shifts185
1H chemical shifts188

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1eiavCA1

Entities:

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

1   PROILEMETILEASPGLYALAGLYASNARG
2   ASNPHEARGPROLEUTHRPROARGGLYTYR
3   THRTHRTRPVALASNTHRILEGLNTHRASN
4   GLYLEULEUASNGLUALASERGLNASNLEU
5   PHEGLYILELEUSERVALASPCYSTHRSER
6   GLUGLUMETASNALAPHELEUASPVALVAL
7   PROGLYGLNALAGLYGLNLYSGLNILELEU
8   LEUASPALAILEASPLYSILEALAASPASP
9   TRPASPASNARGHISPROLEUPROASNALA
10   PROLEUVALALAPROPROGLNGLYPROILE
11   PROMETTHRALAARGPHEILEARGGLYLEU
12   GLYVALPROARGGLUARGGLNMETGLUPRO
13   ALAPHEASPGLNPHEARGGLNTHRTYRARG
14   GLNTRPILEILEGLUALAMETSERGLUGLY
15   ILELYSVALMETILEGLYLYSPROLYSALA
16   GLNASNILEARGGLNGLYALALYSGLUPRO
17   TYRPROGLUPHEVALASPARGLEULEUSER
18   GLNILELYSSERGLUGLYHISPROGLNGLU
19   ILESERLYSPHELEUTHRASPTHRLEUTHR
20   ILEGLNASNALAASNGLUGLUCYSARGASN
21   ALAMETARGHISLEUARGPROGLUASPTHR
22   LEUGLUGLULYSMETTYRALACYSARGASP
23   ILEGLYTHRTHRLYSGLNLYSMETMETLEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HMQC-NOE-HSQCsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

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

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