BMRB Entry 36260

Name: Complex of SUMO1 and phosphorylated hcmv protein IE2
Published: 2025-09-27

Click here to enlarge.

PDB ID: 6k5t
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36260
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Complex of SUMO1 and phosphorylated hcmv protein IE2

Deposition date:

2019-05-31

Original release date:

2025-09-27

Authors:

Tripathi, V.; Chatterjee, K.

Citation:

Citation: Tripathi, Vasvi; Chatterjee, Kiran; Das, Ranabir. "Casein kinase-2-mediated phosphorylation increases the SUMO-dependent activity of the cytomegalovirus transactivator IE2." J. Biol. Chem. 294, 14546-14561 (2019).
PubMed: 31371453

Assembly members:

Assembly members:
Small ubiquitin-related modifier 1, polymer, 77 residues, 8970.248 Da.
12-mer from Viral transcription factor IE2, polymer, 12 residues, 1369.241 Da.

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Small ubiquitin-related modifier 1: YIKLKVIGQDSSEIHFKVKM TTHLKKLKESYCQRQGVPMN SLRFLFEGQRIADNHTPKEL GMEEEDVIEVYQEQTGG
12-mer from Viral transcription factor IE2: DTAGCIVIXDXE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	71
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 77 residues - 8970.248 Da.

1

TYR

ILE

LYS

LEU

LYS

VAL

ILE

GLY

GLN

ASP

2

SER

GLU

ILE

HIS

PHE

LYS

VAL

LYS

MET

3

THR

HIS

LEU

LYS

LEU

LYS

GLU

SER

4

TYR

CYS

GLN

ARG

GLN

GLY

VAL

PRO

MET

ASN

5

SER

LEU

ARG

PHE

LEU

PHE

GLU

GLY

GLN

ARG

6

ILE

ALA

ASP

ASN

HIS

THR

PRO

LYS

GLU

LEU

7

GLY

MET

GLU

ASP

VAL

ILE

GLU

VAL

8

TYR

GLN

GLU

GLN

THR

GLY

Entity 2, entity_2 12 residues - 1369.241 Da.

1

ASP

THR

ALA

GLY

CYS

ILE

VAL

ILE

SEP

ASP

2

SEP

GLU

Samples:

15N_sample: SUMO1, [U-13C; U-15N], 0.3 mM; Phosphorylated SIM from viral protein IE2 3 mM; H2O 90%; D2O, [U-2H], 10%

13C15N_sample: SUMO1, [U-13C; U-15N], 1 mM; Phosphorylated SIM from viral protein IE2 1.5 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: Phosphorylated SIM from viral protein IE2 3 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 162.7 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	13C15N_sample	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D half filtered NOESY	13C15N_sample	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - data analysis

HADDOCK, Bonvin - structure calculation

NMR spectrometers:

Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks