BMRB Entry 19855

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19855
MolProbity Validation Chart

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Title:
Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Deposition date:
2014-03-15
Original release date:
2014-10-07
Authors:
Bacot-Davis, Valjean; Cornilescu, Claudia; Markley, John; Palmenberg, Ann
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:
entity_1, polymer, 71 residues, 8262.100 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41B

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts159
15N chemical shifts70
1H chemical shifts212

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION2

Entities:

Entity 1, entity_1 71 residues - 8262.100 Da.

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

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: L MENGO, [U-100% 13C; U-100% 15N], 0.5 mM; RAN GTPASE 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

SPARKY, Goddard - chemical shift assignment

SPARTA+, Shen and Bax - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19084 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