BMRB Entry 17663

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17663

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Title:
HVS ORF57 56-140 backbone assignment
Deposition date:
2011-05-25
Original release date:
2011-09-01
Authors:
Tunnicliffe, Richard; Hautbergue, Guillaume; Wilson, Stuart; Golovanov, Alexander
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, .-. (2011).
PubMed: 21253573

Assembly members:

Assembly members:
HVS_ORF57, polymer, 107 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Herpesvirus saimiri   Taxonomy ID: 10381   Superkingdom: Viruses   Kingdom: not available   Genus/species: Herpesvirus saimiri

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HVS_ORF57: MASMTGGQQMGRDPSTSNLK RERQRSPITWEHQSPLSRVY RSPSPMRFGKRPRISSNSTS RSCKTSWADRVREAAAQRRP SRPFRKPYSHPRNGPLRNGL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts229
15N chemical shifts73
1H chemical shifts224

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ORF57 56-1401

Entities:

Entity 1, ORF57 56-140 107 residues - Formula weight is not available

N-terminal sequence masmtggqqmgrdp and C-terminal sequence lehhhhhh are non-native from cloning

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGASPPROSERTHRSERASNLEULYS
3   ARGGLUARGGLNARGSERPROILETHRTRP
4   GLUHISGLNSERPROLEUSERARGVALTYR
5   ARGSERPROSERPROMETARGPHEGLYLYS
6   ARGPROARGILESERSERASNSERTHRSER
7   ARGSERCYSLYSTHRSERTRPALAASPARG
8   VALARGGLUALAALAALAGLNARGARGPRO
9   SERARGPROPHEARGLYSPROTYRSERHIS
10   PROARGASNGLYPROLEUARGASNGLYLEU
11   GLUHISHISHISHISHISHIS

Samples:

sample_1: HVS ORF57, [U-95% 13C; U-95% 15N], 1.0 ± 0.05 mM; H2O 90%; D2O 10%; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 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