BMRB Entry 34475

Name: LEDGF/p75 dimer (residues 345-467)
Published: 2020-09-07

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PDB ID: 6tvm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34475
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:

LEDGF/p75 dimer (residues 345-467)

Deposition date:

2020-01-10

Original release date:

2020-09-07

Authors:

Lux, V.; Veverka, V.

Citation:

Citation: Lux, Vanda; Brouns, Tine; Cermakova, Katerina; Srb, Pavel; Fabry, Milan; Madlikova, Marcela; Horejsi, Magdalena; Kukacka, Zdenek; Novak, Petr; Kugler, Michael; Brynda, Jiri; DeRijck, Jan; Christ, Frauke; Debyser, Zeger; Veverka, Vaclav. "Molecular Mechanism of LEDGF/p75 Dimerization" Structure ., .-. (2020).
PubMed: 32946742

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, 14644.854 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: SNAASETSMDSRLQRIHAEI KNSLKIDNLDVNRCIEALDE LASLQVTMQQAQKHTEMITT LKKIRRFKVSQVIMEKSTML YNKFKNMFLVGEGDSVITQV LNKSLAEQRQHEEANKTKDQ GKKGPNKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	549
15N chemical shifts	130
1H chemical shifts	882

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	1

Entities:

Entity 1, unit_1 128 residues - 14644.854 Da.

1

SER

ASN

ALA

SER

GLU

THR

SER

MET

ASP

2

SER

ARG

LEU

GLN

ARG

ILE

HIS

ALA

GLU

ILE

3

LYS

ASN

SER

LEU

LYS

ILE

ASP

ASN

LEU

ASP

4

VAL

ASN

ARG

CYS

ILE

GLU

ALA

LEU

ASP

GLU

5

LEU

ALA

SER

LEU

GLN

VAL

THR

MET

GLN

6

ALA

GLN

LYS

HIS

THR

GLU

MET

ILE

THR

7

LEU

LYS

ILE

ARG

PHE

LYS

VAL

SER

8

GLN

VAL

ILE

MET

GLU

LYS

SER

THR

MET

LEU

9

TYR

ASN

LYS

PHE

LYS

ASN

MET

PHE

LEU

VAL

10

GLY

GLU

GLY

ASP

SER

VAL

ILE

THR

GLN

VAL

11

LEU

ASN

LYS

SER

LEU

ALA

GLU

GLN

ARG

GLN

12

HIS

GLU

ALA

ASN

LYS

THR

LYS

ASP

GLN

13

GLY

LYS

GLY

PRO

ASN

LYS

Samples:

sample_1: LEDGF, [U-13C; U-15N], 0.5 mM; HEPES 20 mM; sodium chloride 100 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7; 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 HSQC	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 HCCH-TOCSY	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:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

Sparky, Goddard - data analysis

TopSpin, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AVANCE 850 MHz

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