BMRB Entry 27880

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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/BMR27880
MolProbity Validation Chart

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Title:
1H, 13C, 15N Backbone chemical Shift Assignment of the RYMV-encoded viral supressor of RNA silencing P1 protein
Deposition date:
2019-04-17
Original release date:
2019-08-14
Authors:
Yang, Yinshan; Gillet, Francois-Xavier; Hoh, Francois; Brugidou, Christophe; Vignols, Florence
Citation:

Citation: Yang, Yinshan; Poignavent, Vianney; Gillet, Francois-Xavier; Hoh, Francois; Brugidou, Christophe; Vignols, Florence; Demene, Helene. "NMR chemical shift backbone assignment of the viral protein P1 encoded by the African Rice Yellow Mottle Virus"  Biomol. NMR Assignments 13, 345-348 (2019).
PubMed: 31346897

Assembly members:

Assembly members:
RYMV_P1, polymer, 157 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Sobemovirus   Taxonomy ID: 12137   Superkingdom: Viruses   Kingdom: not available   Genus/species: Sobemovirus not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RYMV_P1: MTRLEVLIRPTEQTAAKANA VGYTHALTWVWHSQTWDVDS VRDPSLRADFNPEKVGWVSV SFACTQCTAHYYTSEQVKYF TNIPPVHFDVVCADCERSVQ LDDEIDREHQERNAEISACN ARALSEGRPASLVYLSRDAC DIPEHSGRCRFVKYLNF

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts152
1H chemical shifts317

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RYMV P11
2ZINC ION, 12
3ZINC ION, 22

Entities:

Entity 1, RYMV P1 157 residues - Formula weight is not available

1   METTHRARGLEUGLUVALLEUILEARGPRO
2   THRGLUGLNTHRALAALALYSALAASNALA
3   VALGLYTYRTHRHISALALEUTHRTRPVAL
4   TRPHISSERGLNTHRTRPASPVALASPSER
5   VALARGASPPROSERLEUARGALAASPPHE
6   ASNPROGLULYSVALGLYTRPVALSERVAL
7   SERPHEALACYSTHRGLNCYSTHRALAHIS
8   TYRTYRTHRSERGLUGLNVALLYSTYRPHE
9   THRASNILEPROPROVALHISPHEASPVAL
10   VALCYSALAASPCYSGLUARGSERVALGLN
11   LEUASPASPGLUILEASPARGGLUHISGLN
12   GLUARGASNALAGLUILESERALACYSASN
13   ALAARGALALEUSERGLUGLYARGPROALA
14   SERLEUVALTYRLEUSERARGASPALACYS
15   ASPILEPROGLUHISSERGLYARGCYSARG
16   PHEVALLYSTYRLEUASNPHE

Entity 2, ZINC ION, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: RYMV P1, [U-99% 13C; U-99% 15N], 350 ± 50 uM; ZnSO4 350 uM; DSS 50 uM; sodium chloride 100 mM; Na2SO4 60 mM; TRIS 15 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 8; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

GIFA, Marc Andre Delsuc - processing

NMRview, Johnson Bruce A - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

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