BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27483

Title: Backbone assignment of ICP27 1-138

Deposition date: 2018-05-15 Original release date: 2018-09-24

Authors: Tunnicliffe, Richard; Tian, Xiaochen; Storer, Joanna; Sandri-Goldin, Rozanne; Golovanov, Alexander

Citation: Tunnicliffe, Richard; Tian, Xiaochen; Storer, Joanna; 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:
ICP27, polymer, 156 residues, Formula weight is not available

Natural source:   Common Name: Herpes simplex virus 1   Taxonomy ID: 10298   Superkingdom: Viruses   Kingdom: not available   Genus/species: Simplexvirus Herpes simplex virus 1

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

Entity Sequences (FASTA):
ICP27: MATDIDMLIDLGLDLSDSDL DEDPPEPAESRRDDLESDSN GECSSSDEDMEDPHGEDGPE PILDAARPAVRPSRPEDPGV PSTQTPRPTERQGPNDPQPA PHSVWSRLGARRPSCSPERH GGKVARLQPPPTKAQPARKL LEVLFQGPLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts140
1H chemical shifts118

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ICP27 1-1381

Entities:

Entity 1, ICP27 1-138 156 residues - Formula weight is not available

Residues 139-156 are not wild-type and introduced during cloning

1   METALATHRASPILEASPMETLEUILEASP
2   LEUGLYLEUASPLEUSERASPSERASPLEU
3   ASPGLUASPPROPROGLUPROALAGLUSER
4   ARGARGASPASPLEUGLUSERASPSERASN
5   GLYGLUCYSSERSERSERASPGLUASPMET
6   GLUASPPROHISGLYGLUASPGLYPROGLU
7   PROILELEUASPALAALAARGPROALAVAL
8   ARGPROSERARGPROGLUASPPROGLYVAL
9   PROSERTHRGLNTHRPROARGPROTHRGLU
10   ARGGLNGLYPROASNASPPROGLNPROALA
11   PROHISSERVALTRPSERARGLEUGLYALA
12   ARGARGPROSERCYSSERPROGLUARGHIS
13   GLYGLYLYSVALALAARGLEUGLNPROPRO
14   PROTHRLYSALAGLNPROALAARGLYSLEU
15   LEUGLUVALLEUPHEGLNGLYPROLEUGLU
16   HISHISHISHISHISHIS

Samples:

sample_1: ICP27, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; L-Arginine 50 mM; L-Glutamate 50 mM; EDTA 1 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.17 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 HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY v3.12, Goddard - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9J0X9

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts