BMRB Entry 34541

Name: TFIIS N-terminal domain (TND) from human IWS1
Published: 2021-11-28

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PDB ID: 6zv4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34541
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 IWS1

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, 116 residues, 12600.160 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 SGSGSGSGSSGELSDKKNEE KDLFGSDSESGNEEEN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	447
15N chemical shifts	108
1H chemical shifts	749

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_1 116 residues - 12600.160 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

GLY

SER

GLY

SER

GLY

SER

GLY

SER

10

GLY

GLU

LEU

SER

ASP

LYS

ASN

GLU

11

LYS

ASP

LEU

PHE

GLY

SER

ASP

SER

GLU

SER

12

GLY

ASN

GLU

ASN

Samples:

sample_1: TFIIS-IWS1, [U-13C; U-15N], 0.35 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

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