BMRB Entry 34539

Name: TFIIS N-terminal domain (TND) from human PPP1R10
Published: 2021-11-28

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PDB ID: 6zv2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34539
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 PPP1R10

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, 154 residues, 17221.992 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: SNAASMGSGPIDPKELLKGL DSFLNRDGEVKSVDGISKIF SLMKEARKMVSRCTYLNILL QTRSPEILVKFIDVGGYKLL NNWLTYSKTTNNIPLLQQIL LTLQHLPLTVDHLKQNNTAK LVKQLSKSSEDEELRKLASV LVSDWMAVIRSQGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	669
15N chemical shifts	154
1H chemical shifts	1120

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_1 154 residues - 17221.992 Da.

1

SER

ASN

ALA

SER

MET

GLY

SER

GLY

PRO

2

ILE

ASP

PRO

LYS

GLU

LEU

LYS

GLY

LEU

3

ASP

SER

PHE

LEU

ASN

ARG

ASP

GLY

GLU

VAL

4

LYS

SER

VAL

ASP

GLY

ILE

SER

LYS

ILE

PHE

5

SER

LEU

MET

LYS

GLU

ALA

ARG

LYS

MET

VAL

6

SER

ARG

CYS

THR

TYR

LEU

ASN

ILE

LEU

7

GLN

THR

ARG

SER

PRO

GLU

ILE

LEU

VAL

LYS

8

PHE

ILE

ASP

VAL

GLY

TYR

LYS

LEU

9

ASN

TRP

LEU

THR

TYR

SER

LYS

THR

10

ASN

ILE

PRO

LEU

GLN

ILE

LEU

11

LEU

THR

LEU

GLN

HIS

LEU

PRO

LEU

THR

VAL

12

ASP

HIS

LEU

LYS

GLN

ASN

THR

ALA

LYS

13

LEU

VAL

LYS

GLN

LEU

SER

LYS

SER

GLU

14

ASP

GLU

LEU

ARG

LYS

LEU

ALA

SER

VAL

15

LEU

VAL

SER

ASP

TRP

MET

ALA

VAL

ILE

ARG

16

SER

GLN

GLY

SER

Samples:

sample_1: PPP1R10, [U-13C; U-15N], 0.7 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-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N 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