BMRB Entry 36259

Name: Complex of SUMO2 with Phosphorylated viral SIM IE2
Published: 2025-09-27

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PDB ID: 6k5r
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36259
MolProbity Validation Chart

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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:

Complex of SUMO2 with Phosphorylated viral SIM IE2

Deposition date:

2019-05-30

Original release date:

2025-09-27

Authors:

Chatterjee, K.; Das, R.

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 3, polymer, 77 residues, 8892.013 Da.
ASP-THR-ALA-GLY-CYS-ILE-VAL-ILE-SEP-ASP-SEP-GLU, 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 3: DHINLKVAGQDGSVVQFKIK RHTPLSKLMKAYCERQGLSM RQIRFRFDGQPINETDTPAQ LEMEDEDTIDVFQQQTG
ASP-THR-ALA-GLY-CYS-ILE-VAL-ILE-SEP-ASP-SEP-GLU: 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
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Assembly:

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

Entities:

Entity 1, entity_1 77 residues - 8892.013 Da.

1

ASP

HIS

ILE

ASN

LEU

LYS

VAL

ALA

GLY

GLN

2

ASP

GLY

SER

VAL

GLN

PHE

LYS

ILE

LYS

3

ARG

HIS

THR

PRO

LEU

SER

LYS

LEU

MET

LYS

4

ALA

TYR

CYS

GLU

ARG

GLN

GLY

LEU

SER

MET

5

ARG

GLN

ILE

ARG

PHE

ARG

PHE

ASP

GLY

GLN

6

PRO

ILE

ASN

GLU

THR

ASP

THR

PRO

ALA

GLN

7

LEU

GLU

MET

GLU

ASP

GLU

ASP

THR

ILE

ASP

8

VAL

PHE

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

13C15N_sample: 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