BMRB Entry 16683

Title:
RRM domain of mRNA export adaptor REF2-I bound to HSV-1 ICP27 peptide
Deposition date:
2010-01-18
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:
REF_54-155, polymer, 124 residues, 13596.237 Da.
ICP27_103-138, polymer, 40 residues, 4268.970 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24b

Data sets:
Data typeCount
13C chemical shifts627
15N chemical shifts159
1H chemical shifts1049

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1REF_54-1551
2ICP27_103-1382

Entities:

Entity 1, REF_54-155 124 residues - 13596.237 Da.

Construct contains the following non-REF sequences: N-terminal T7 tag: MASMTGGQQMGRDP (assigned residue numbers 40-53) C-terminal His tag: LEHHHHHH (assigned residue numbers 156-163)

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGASPPROASPLYSTRPGLNHISASP
3   LEUPHEASPSERGLYCYSGLYGLYGLYGLU
4   GLYVALGLUTHRGLYALALYSLEULEUVAL
5   SERASNLEUASPPHEGLYVALSERASPALA
6   ASPILEGLNGLULEUPHEALAGLUPHEGLY
7   THRLEULYSLYSALAALAVALASPTYRASP
8   ARGSERGLYARGSERLEUGLYTHRALAASP
9   VALHISPHEGLUARGARGALAASPALALEU
10   LYSALAMETLYSGLNTYRLYSGLYVALPRO
11   LEUASPGLYARGPROMETASPILEGLNLEU
12   VALALASERGLNILEASPLEUGLUHISHIS
13   HISHISHISHIS

Entity 2, 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: REF 54-155, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; ICP27 103-138 2 ± 0.05 mM; Na 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; H2O 90%; D2O 10%

sample_2: ICP27 103-138, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; REF 54-155 2 ± 0.05 mM; Na 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; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropicsample_conditions
3D 15N-separated NOESYsample_1isotropicsample_conditions
filtered 13C-NOESYsample_1isotropicsample_conditions
filtered 13C-NOESYsample_2isotropicsample_conditions
3D 13C-separated NOESYsample_2isotropicsample_conditions
3D 15N-separated NOESYsample_2isotropicsample_conditions
3D Standard triple-resonancesample_1isotropicsample_conditions
3d Standard triple-resonancesample_2isotropicsample_conditions

Software:

CYANA v2.1, P.GUNTERT ET AL. - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance II+ 700 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16697 17693 16696
PDB
DBJ BAE44978 BAE44979 BAE44980 BAE44981 BAE44982
EMBL CAA32290
GB AAF43147 ACM62278 ACU57136 ADD60047 ADD60124
REF NP_044657
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