BMRB Entry 50141

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50141

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone chemical shift assignments of the APO Fowlpox virus resolvase (APO Fpr)
Deposition date:
2019-12-24
Original release date:
2020-02-05
Authors:
Rao, Timsi; Aihara, Hideki; Li, Na
Citation:

Citation: Li, Na; Shi, Ke; Rao, Timsi; Banerjee, Surajit; Aihara, Hideki. "Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase"  Sci. Rep. 10, 393-393 (2020).
PubMed: 31941902

Assembly members:

Assembly members:
Fowlpox virus resolvase protein, D135N, C-terminal 6 residues deleted, polymer, 150 residues, 17478.07 Da.

Natural source:

Natural source:   Common Name: Avipoxvirus Fowlpox virus   Taxonomy ID: 10261   Superkingdom: Virus   Kingdom: not available   Genus/species: Avipoxvirus fowlpox

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fowlpox virus resolvase protein, D135N, C-terminal 6 residues deleted: MIICSVDIGIKNPAYAIFNY DNTSNTIKLIAIEKSDWTKN WERSVARDLTRYNPDVVILE KQGFKSPNSKIIYFIKGFFY NSNTKVIVRNPTFKGGSYRN RKKQSIDVFIQKISEYTDYK NDILNKYTKLDDIANSFNLG LSYMESLLKK

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts132
1H chemical shifts132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Polypeptide1

Entities:

Entity 1, Polypeptide 150 residues - 17478.07 Da.

1   METILEILECYSSERVALASPILEGLYILE
2   LYSASNPROALATYRALAILEPHEASNTYR
3   ASPASNTHRSERASNTHRILELYSLEUILE
4   ALAILEGLULYSSERASPTRPTHRLYSASN
5   TRPGLUARGSERVALALAARGASPLEUTHR
6   ARGTYRASNPROASPVALVALILELEUGLU
7   LYSGLNGLYPHELYSSERPROASNSERLYS
8   ILEILETYRPHEILELYSGLYPHEPHETYR
9   ASNSERASNTHRLYSVALILEVALARGASN
10   PROTHRPHELYSGLYGLYSERTYRARGASN
11   ARGLYSLYSGLNSERILEASPVALPHEILE
12   GLNLYSILESERGLUTYRTHRASPTYRLYS
13   ASNASPILELEUASNLYSTYRTHRLYSLEU
14   ASPASPILEALAASNSERPHEASNLEUGLY
15   LEUSERTYRMETGLUSERLEULEULYSLYS

Samples:

sample_1: Fpr C151Stop D135N, [U-2H; U-15N; U-13C], ; L-Arginine 25 mM; L-Glutamine 25 mM; DSS 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4, Bahrami, Markley, Assadi, and Eghbalnia, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

UNP Q9J546.1
AlphaFold Q9J546

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