BMRB Entry 27341

Title:
Backbone assignment of HSV-1 ICP27 103-155
Deposition date:
2017-12-15
Original release date:
2018-09-24
Authors:
Tunnicliffe, Richard; Levy, Colin; Mould, Paul; McKenzie, Edward; Sandri-Goldin, Rozanne; Golovanov, Alexander
Citation:

Citation: Tunnicliffe, Richard; Levy, Colin; Mould, Paul; McKenzie, Edward; Sandri-Goldin, Rozanne; Golovanov, Alexander. "Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIF"  Sci. Rep. 8, 15005-15005 (2018).

Assembly members:

Assembly members:
ICP27_103-155, polymer, 57 residues, 5977.83 Da.

Natural source:

Natural source:   Common Name: Human alphaherpesvirus 1   Taxonomy ID: 10298   Superkingdom: Viruses   Kingdom: not available   Genus/species: Simplexvirus Human alphaherpesvirus 1

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ICP27_103-155: GPLGSVWSRLGARRPSCSPE RHGGKVARLQPPPTKAQPAR GGRRGRRRGRGRGGPGA

Data sets:
Data typeCount
13C chemical shifts147
15N chemical shifts49
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ICP27 103-1551

Entities:

Entity 1, ICP27 103-155 57 residues - 5977.83 Da.

First 4 residues GPLG are non-native, remaining after HRV3C protease cleavage.

1   GLYPROLEUGLYSERVALTRPSERARGLEU
2   GLYALAARGARGPROSERCYSSERPROGLU
3   ARGHISGLYGLYLYSVALALAARGLEUGLN
4   PROPROPROTHRLYSALAGLNPROALAARG
5   GLYGLYARGARGGLYARGARGARGGLYARG
6   GLYARGGLYGLYPROGLYALA

Samples:

sample_1: ICP27 103-155, [U-99% 13C; U-99% 15N], 0.45 mM; phosphate buffer 20 mM; NaCl 50 mM; L-Arg 50 mM; L-Glu 50 mM; 2-mercaptoethanol 50 mM; EDTA 10 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.2; pressure: 1 atm; temperature: 298 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9J0X9
AlphaFold Q9J0X9

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