BMRB Entry 17664

Name: HVS ORF57 103-120 backbone assignment
Published: 2011-09-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17664

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

HVS ORF57 103-120 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, 23 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: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HVS_ORF57: GPLGSSCKTSWADRVREAAA QRR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	85
15N chemical shifts	23
1H chemical shifts	120

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ORF57 103-120	1

Entities:

Entity 1, ORF57 103-120 23 residues - Formula weight is not available

N-terminal sequence GPLGS is non-native from cloning

1

GLY

PRO

LEU

GLY

SER

CYS

LYS

THR

SER

2

TRP

ALA

ASP

ARG

VAL

ARG

GLU

ALA

3

GLN

ARG

Samples:

sample_1: HVS ORF57, [U-95% 13C; U-95% 15N], 1.0 ± 0.05 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.05 M; 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_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.113, Goddard - data analysis

NMR spectrometers:

Bruker DRX 600 MHz

BMRB	16698 17663
PDB	2YKA
EMBL	CAA45680 CAC84353 CAC84354
GB	AAA46125 AAA66558
PIR	WMBEHA
REF	NP_040259
SP	P13199
AlphaFold	P13199