BMRB Entry 34535

Name: Human TFIIS N-terminal domain (TND)
Published: 2021-11-28

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PDB ID: 6zuy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34535
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:

Human TFIIS N-terminal domain (TND)

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, 81 residues, 9064.700 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: MEDEVVRFAKKMDKMVQKKN AAGALDLLKELKNIPMTLEL LQSTRIGMSVNAIRKQSTDE EVTSLAKSLIKSWKKLLDGG S

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	357
15N chemical shifts	83
1H chemical shifts	609

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 81 residues - 9064.700 Da.

1

MET

GLU

ASP

GLU

VAL

ARG

PHE

ALA

LYS

2

LYS

MET

ASP

LYS

MET

VAL

GLN

LYS

ASN

3

ALA

GLY

ALA

LEU

ASP

LEU

LYS

GLU

4

LEU

LYS

ASN

ILE

PRO

MET

THR

LEU

GLU

LEU

5

LEU

GLN

SER

THR

ARG

ILE

GLY

MET

SER

VAL

6

ASN

ALA

ILE

ARG

LYS

GLN

SER

THR

ASP

GLU

7

GLU

VAL

THR

SER

LEU

ALA

LYS

SER

LEU

ILE

8

LYS

SER

TRP

LYS

LEU

ASP

GLY

9

SER

Samples:

sample_1: TFIIS, [U-13C; U-15N], 0.5 mM; TRIS, deuterated, 25 mM; sodium phospate 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
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 HBHA(CO)NH	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:

TopSpin, Bruker Biospin - processing

Sparky, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, Yasara - refinement

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