BMRB Entry 34179

Name: Solution structure of the LEDGF/p75 IBD - JPO2 (aa 1-32) complex
Published: 2018-07-20

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PDB ID: 6emo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34179
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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 - JPO2 (aa 1-32) 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, 136 residues, 15694.933 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 VLNKMELATRYQIPKEVADI FNAPSDDEEFVGFRDD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	590
15N chemical shifts	145
1H chemical shifts	995

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_1 136 residues - 15694.933 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

MET

GLU

LEU

ALA

THR

ARG

12

TYR

GLN

ILE

PRO

LYS

GLU

VAL

ALA

ASP

ILE

13

PHE

ASN

ALA

PRO

SER

ASP

GLU

PHE

14

VAL

GLY

PHE

ARG

ASP

Samples:

sample_1: LEDGF/p75 IBD-JPO2 M1, [U-13C; U-15N], 0.5 mM; TRIS 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - structure solution

SPARKY - structure solution

CYANA - structure solution

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