BMRB Entry 16696

Name: HSV-1 ICP27 (REF-interation) peptide backbone assignment in free form
Published: 2011-01-25

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

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: HSV-1 ICP27 (REF-interation) peptide backbone assignment in free form PubMed: 21253573

Deposition date: 2010-01-29 Original release date: 2011-01-25

Authors: Tunnicliffe, Richard; Golovanov, Alexander; Wilson, Stuart; Hautbergue, Guillaume

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).

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

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	61
15N chemical shifts	33
1H chemical shifts	132

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ICP27_103-138	1

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	GLY	PRO	LEU	GLY	SER	VAL	TRP	SER	ARG	LEU
2	GLY	ALA	ARG	ARG	PRO	SER	CYS	SER	PRO	GLU
3	ARG	HIS	GLY	GLY	LYS	VAL	ALA	ARG	LEU	GLN
4	PRO	PRO	PRO	THR	LYS	ALA	GLN	PRO	ALA	ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions
3D HNCA	sample_1	isotropic	sample_conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions

Software:

SPARKY v3.1, Goddard - data analysis

NMR spectrometers:

Bruker DRX 600 MHz

PDB	2KT5
DBJ	BAE44978 BAE44979 BAE44980 BAE44981 BAE44982
EMBL	CAA32290
GB	AAF43147 ACM62278 ACU57136 ADD60047 ADD60124
REF	YP_009137130
SP	P10238 P36295

Biological Magnetic Resonance Data Bank