BMRB Entry 16696

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16696

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Title:
HSV-1 ICP27 (REF-interation) peptide backbone assignment in free form
Deposition date:
2010-01-29
Original release date:
2011-01-25
Authors:
Tunnicliffe, Richard; Golovanov, Alexander; Wilson, Stuart; Hautbergue, Guillaume
Citation:

Citation: Tunnicliffe, Richard; Hautbergue, Guillaume; Kalra, Priti; Jackson, Brian; Whitehouse, Adrian; Wilson, Stuart; Golovanov, Alexander. "Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57."  PLoS Pathog. 7, e1001244-. (2011).
PubMed: 21253573

Assembly members:

Assembly members:
ICP27_103-138, polymer, 40 residues, 4268.970 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ICP27_103-138: GPLGSVWSRLGARRPSCSPE RHGGKVARLQPPPTKAQPAR

Data sets:
Data typeCount
13C chemical shifts61
15N chemical shifts33
1H chemical shifts132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ICP27_103-1381

Entities:

Entity 1, ICP27_103-138 40 residues - 4268.970 Da.

The construct contains the following non-ICP27 sequence remaining from protease cleavage site at N-termini: GPLG (assigned residue numbers 99-102)

1   GLYPROLEUGLYSERVALTRPSERARGLEU
2   GLYALAARGARGPROSERCYSSERPROGLU
3   ARGHISGLYGLYLYSVALALAARGLEUGLN
4   PROPROPROTHRLYSALAGLNPROALAARG

Samples:

sample_1: ICP27 103-138, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; phosphate buffer 20 mM; NaCl 50 mM; L-Arg 50 mM; L-Glu 50 mM; 2-mercaptoethanol 50 mM; DTT 10 mM; EDTA 10 mM

sample_conditions: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
3D HNCAsample_1isotropicsample_conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions
3D HBHA(CO)NHsample_1isotropicsample_conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions

Software:

SPARKY v3.1, Goddard - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAE44978 BAE44979 BAE44980 BAE44981 BAE44982
EMBL CAA32290
GB AAF43147 ACM62278 ACU57136 ADD60047 ADD60124
REF YP_009137130
SP P10238 P36295
AlphaFold P10238 P36295

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