BMRB Entry 27483

Name: Backbone assignment of ICP27 1-138
Published: 2018-09-24

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27483

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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:

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:

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:

Assembly members:
ICP27, polymer, 156 residues, Formula weight is not available

Natural source:

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:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24b

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	391
15N chemical shifts	140
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ICP27 1-138	1

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

MET

ALA

THR

ASP

ILE

ASP

MET

LEU

ILE

ASP

2

LEU

GLY

LEU

ASP

LEU

SER

ASP

SER

ASP

LEU

3

ASP

GLU

ASP

PRO

GLU

PRO

ALA

GLU

SER

4

ARG

ASP

LEU

GLU

SER

ASP

SER

ASN

5

GLY

GLU

CYS

SER

ASP

GLU

ASP

MET

6

GLU

ASP

PRO

HIS

GLY

GLU

ASP

GLY

PRO

GLU

7

PRO

ILE

LEU

ASP

ALA

ARG

PRO

ALA

VAL

8

ARG

PRO

SER

ARG

PRO

GLU

ASP

PRO

GLY

VAL

9

PRO

SER

THR

GLN

THR

PRO

ARG

PRO

THR

GLU

10

ARG

GLN

GLY

PRO

ASN

ASP

PRO

GLN

PRO

ALA

11

PRO

HIS

SER

VAL

TRP

SER

ARG

LEU

GLY

ALA

12

ARG

PRO

SER

CYS

SER

PRO

GLU

ARG

HIS

13

GLY

LYS

VAL

ALA

ARG

LEU

GLN

PRO

14

PRO

THR

LYS

ALA

GLN

PRO

ALA

ARG

LYS

LEU

15

LEU

GLU

VAL

LEU

PHE

GLN

GLY

PRO

LEU

GLU

16

HIS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.12, Goddard - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 800 MHz

UNP	Q9J0X9
AlphaFold	Q9J0X9