BMRB Entry 16698

Name: HVS ORF57 8-120 backbone assignment
Published: 2011-01-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16698

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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 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ORF57_8-120: MASMTGGQQMGRDPGISSDD DFDSSDSSSDEEESDTSPQI MKSDVTMASPPSTPEPSPDV SASTSNLKRERQRSPITWEH QSPLSRVYRSPSPMRFGKRP RISSNSTSRSCKTSWADRVR EAAAQRRLEHHHHHH

Data sets:

assigned_chemical_shifts
- Free_ORF57_288k
- Free_ORF57_303k

Data type	Count
13C chemical shifts	361
15N chemical shifts	229
1H chemical shifts	515

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ORF57_8-120	1

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

MET

ALA

SER

MET

THR

GLY

GLN

MET

2

GLY

ARG

ASP

PRO

GLY

ILE

SER

ASP

3

ASP

PHE

ASP

SER

ASP

SER

ASP

4

GLU

SER

ASP

THR

SER

PRO

GLN

ILE

5

MET

LYS

SER

ASP

VAL

THR

MET

ALA

SER

PRO

6

PRO

SER

THR

PRO

GLU

PRO

SER

PRO

ASP

VAL

7

SER

ALA

SER

THR

SER

ASN

LEU

LYS

ARG

GLU

8

ARG

GLN

ARG

SER

PRO

ILE

THR

TRP

GLU

HIS

9

GLN

SER

PRO

LEU

SER

ARG

VAL

TYR

ARG

SER

10

PRO

SER

PRO

MET

ARG

PHE

GLY

LYS

ARG

PRO

11

ARG

ILE

SER

ASN

SER

THR

SER

ARG

SER

12

CYS

LYS

THR

SER

TRP

ALA

ASP

ARG

VAL

ARG

13

GLU

ALA

GLN

ARG

LEU

GLU

HIS

14

HIS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_2
3D HNCO	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1
2D CaCO	sample_1	isotropic	sample_conditions_1
2D CbCaCO	sample_1	isotropic	sample_conditions_1
2D CbCaCO(N)	sample_1	isotropic	sample_conditions_1
3D CbCaCO(N)	sample_1	isotropic	sample_conditions_1
3D CbCaNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v2.1, Goddard - data analysis

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance II+ 700 MHz

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