BMRB Entry 19084

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19084
MolProbity Validation Chart

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Title:
The Mengovirus Leader protein
Deposition date:
2013-03-12
Original release date:
2013-04-17
Authors:
Cornilescu, Claudia; Porter, Frederick; Zao, Kate Qin; Davis, Valarie; Palmenberg, Ann; Markley, John
Citation:

Citation: Bacot-Davis, Valjean; Ciomperlik, J.; Basta, H.; Cornilescu, Claudia; Palmenberg, Ann. "Solution Structures of Mengovirus Leader Protein, its Phosphorylated Derivatives, and in Complex with Nuclear Transport Protein, RanGTPase"  Proc. Nat. Acad. Sci, U.S.A. ., .-. (2014).

Assembly members:

Assembly members:
full_length_mengoL, polymer, 71 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mengo virus   Taxonomy ID: 12104   Superkingdom: Viruses   Kingdom: not available   Genus/species: Cardiovirus Encephalomyocarditis virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
full_length_mengoL: GSTAMATTMEQEICAHSMTF EECPKCSALQYRNGFYLLKY DEEWYPEELLTDGEDDVFDP DLDMEVVFETQ

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts65
1H chemical shifts231

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1mengovirus1

Entities:

Entity 1, mengovirus 71 residues - Formula weight is not available

1   GLYSERTHRALAMETALATHRTHRMETGLU
2   GLNGLUILECYSALAHISSERMETTHRPHE
3   GLUGLUCYSPROLYSCYSSERALALEUGLN
4   TYRARGASNGLYPHETYRLEULEULYSTYR
5   ASPGLUGLUTRPTYRPROGLUGLULEULEU
6   THRASPGLYGLUASPASPVALPHEASPPRO
7   ASPLEUASPMETGLUVALVALPHEGLUTHR
8   GLN

Samples:

sample_1: full length mengoL, [U-13C; U-15N], 0.7 – 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D-(HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D-(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

No software information available

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

BMRB 19855 19857 19858
PDB
EMBL CAE84564 CAE84565 CAE84566 CAE84567
GB AAA46547 AAB59755 ABB97066 ABI15777
SP P12296 P32540
AlphaFold P12296 P32540

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