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 19858

Title: NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions

Authors: Bacot-Davis, Valjean; Porter, Frederick; Palmenberg, Ann

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:
entity_1, polymer, 71 residues, 8139.810 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:   Common Name: encephalomyocarditisvirus   Taxonomy ID: 12107   Superkingdom: Viruses   Kingdom: not available   Genus/species: Cardiovirus Mengovirus

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

Entity Sequences (FASTA):
entity_1: GSTAMATTMEQEICAHSMTF EECPKCSALQYRNGFYLLKY DEEWYPEELLXDGEDDVFDP DLDMEVVFETQ

Data sets:
Data typeCount
13C chemical shifts161
15N chemical shifts69
1H chemical shifts208

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION2

Entities:

Entity 1, entity_1 71 residues - 8139.810 Da.

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

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: L MENGO 1P, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 20 mM; potassium chloride 100 mM; magnesium chloride 2 mM; DTT 2 mM; sodium azide 0.04%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 102 mM; pH: 7.4; 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 HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
31-Psample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARTA+, Shen and Bax - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY, Goddard - chemical shift assignment

CARA, Kurt W. Thrich, Swiss Federal Institute of Technology ETH - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19084 19855 19857
PDB
EMBL CAE84564 CAE84565 CAE84566
GB AAA46547 AAB59755 ABB97066
SP P12296 P32540