BMRB Entry 34537

Name: TFIIS N-terminal domain (TND) from human LEDGF/p75
Published: 2021-11-28

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PDB ID: 6zv0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34537
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:

TFIIS N-terminal domain (TND) from human LEDGF/p75

Deposition date:

2020-07-23

Original release date:

2021-11-28

Authors:

Veverka, V.

Citation:

Citation: Cermakova, Katerina; Demeulemeester, Jonas; Lux, Vanda; Nedomova, Monika; Goldman, Seth; Smith, Eric; Srb, Pavel; Hexnerova, Rozalie; Fabry, Milan; Madlikova, Marcela; Horejsi, Magdalena; De Rijck, Jan; Debyser, Zeger; Adelman, Karen; Hodges, H Courtney; Veverka, Vaclav. "A ubiquitous disordered protein interaction module orchestrates transcription elongation" Science 374, 1113-1121 (2021).
PubMed: 34822292

Assembly members:

Assembly members:
entity_1, polymer, 92 residues, 10648.392 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 YNKFKNMFLVGE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	97
1H chemical shifts	687

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 92 residues - 10648.392 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

Samples:

sample_1: LEDGF/p75, [U-13C; U-15N], 0.6 mM; TRIS, [U-2H], 25 mM; sodium chloride 200 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 225 mM; pH: 7.4; 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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

Sparky, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, YASARA - refinement

NMR spectrometers:

Bruker AVANCE III HD 850 MHz

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