BMRB Entry 16698

Title:
HVS ORF57 8-120 backbone assignment
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:
ORF57_8-120, polymer, 135 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: pET24b

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts229
1H chemical shifts515

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ORF57_8-1201

Entities:

Entity 1, ORF57_8-120 135 residues - 4268.970 Da.

The construct contains the following non-ORF57 sequence at N-termini: MASMTGGQQMGRDP (assigned residue numbers -4 to 7) Plus the following at C-termini: LEHHHHHH (assigned residue numbers 121 to 128)

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGASPPROGLYILESERSERASPASP
3   ASPPHEASPSERSERASPSERSERSERASP
4   GLUGLUGLUSERASPTHRSERPROGLNILE
5   METLYSSERASPVALTHRMETALASERPRO
6   PROSERTHRPROGLUPROSERPROASPVAL
7   SERALASERTHRSERASNLEULYSARGGLU
8   ARGGLNARGSERPROILETHRTRPGLUHIS
9   GLNSERPROLEUSERARGVALTYRARGSER
10   PROSERPROMETARGPHEGLYLYSARGPRO
11   ARGILESERSERASNSERTHRSERARGSER
12   CYSLYSTHRSERTRPALAASPARGVALARG
13   GLUALAALAALAGLNARGARGLEUGLUHIS
14   HISHISHISHISHIS

Samples:

sample_1: ORF57 8-120, [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_1: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 288 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
3D 1H-15N TOCSYsample_1isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CaCOsample_1isotropicsample_conditions_1
2D CbCaCOsample_1isotropicsample_conditions_1
2D CbCaCO(N)sample_1isotropicsample_conditions_1
3D CbCaCO(N)sample_1isotropicsample_conditions_1
3D CbCaNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY v2.1, Goddard - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance II+ 700 MHz

Related Database Links:

EMBL CAA45680 CAC84353 CAC84354
GB AAA46125 AAA66558
PIR WMBEHA
REF NP_040259
SP P13199
AlphaFold P13199

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