BMRB Entry 34180

Name: Solution structure of the LEDGF/p75 IBD - POGZ (aa 1370-1404) complex
Published: 2018-07-20

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PDB ID: 6emp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34180
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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:

Solution structure of the LEDGF/p75 IBD - POGZ (aa 1370-1404) complex

Deposition date:

2017-10-03

Original release date:

2018-07-20

Authors:

Veverka, V.

Citation:

Citation: Sharma, S.; Cermakova, K.; De Rijck, J.; Demeulemeester, J.; Fabry, M.; El Ashkar, S.; Van Belle, S.; Lepsik, M.; Tesina, P.; Duchoslav, V.; Novak, P.; Hubalek, M.; Srb, P.; Christ, F.; Rezacova, P.; Hodges, H.; Debyser, Z.; Veverka, V.. "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation." Proc. Natl. Acad. Sci. U.S.A. 115, E7053-E7062 (2018).
PubMed: 29997176

Assembly members:

Assembly members:
entity_1, polymer, 139 residues, 16036.094 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):
entity_1: SNAASWETSMDSRLQRIHAE IKNSLKIDNLDVNRCIEALD ELASLQVTMQQAQKHTEMIT TLKKIRRFKVSQVIMEKSTM LYNKFKNMFLVGEGDSVITQ VLNKRPRSSPEETIEPESLH QLFEGESETESFYGFEEAD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	584
15N chemical shifts	133
1H chemical shifts	956

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 139 residues - 16036.094 Da.

1

SER

ASN

ALA

SER

TRP

GLU

THR

SER

MET

2

ASP

SER

ARG

LEU

GLN

ARG

ILE

HIS

ALA

GLU

3

ILE

LYS

ASN

SER

LEU

LYS

ILE

ASP

ASN

LEU

4

ASP

VAL

ASN

ARG

CYS

ILE

GLU

ALA

LEU

ASP

5

GLU

LEU

ALA

SER

LEU

GLN

VAL

THR

MET

GLN

6

GLN

ALA

GLN

LYS

HIS

THR

GLU

MET

ILE

THR

7

THR

LEU

LYS

ILE

ARG

PHE

LYS

VAL

8

SER

GLN

VAL

ILE

MET

GLU

LYS

SER

THR

MET

9

LEU

TYR

ASN

LYS

PHE

LYS

ASN

MET

PHE

LEU

10

VAL

GLY

GLU

GLY

ASP

SER

VAL

ILE

THR

GLN

11

VAL

LEU

ASN

LYS

ARG

PRO

ARG

SER

PRO

12

GLU

THR

ILE

GLU

PRO

GLU

SER

LEU

HIS

13

GLN

LEU

PHE

GLU

GLY

GLU

SER

GLU

THR

GLU

14

SER

PHE

TYR

GLY

PHE

GLU

ALA

ASP

Samples:

sample_1: LEDGF/p75 IBD-POGZ, [U-13C; U-15N], 0.5 mM; TRIS 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, Krieger - refinement

NMR spectrometers:

Bruker AvanceIII 850 MHz

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