BMRB Entry 34538

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

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PDB ID: 6zv1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34538
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, 150 residues, 16737.436 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: SNAASGTFISDADDVVSAMI VKMNEAAEEDRQLNNQKKPA LKKLTLLPAVVMHLKKQDLK ETFIDSGVMSAIKEWLSPLP DRSLPALKIREELLKILQEL PSVSQETLKHSGIGRAVMYL YKHPKESRSNKDMAGKLINE WSRPIFGLGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	616
15N chemical shifts	140
1H chemical shifts	1019

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_1 150 residues - 16737.436 Da.

1	SER	ASN	ALA	ALA	SER	GLY	THR	PHE	ILE	SER
2	ASP	ALA	ASP	ASP	VAL	VAL	SER	ALA	MET	ILE
3	VAL	LYS	MET	ASN	GLU	ALA	ALA	GLU	GLU	ASP
4	ARG	GLN	LEU	ASN	ASN	GLN	LYS	LYS	PRO	ALA
5	LEU	LYS	LYS	LEU	THR	LEU	LEU	PRO	ALA	VAL
6	VAL	MET	HIS	LEU	LYS	LYS	GLN	ASP	LEU	LYS
7	GLU	THR	PHE	ILE	ASP	SER	GLY	VAL	MET	SER
8	ALA	ILE	LYS	GLU	TRP	LEU	SER	PRO	LEU	PRO
9	ASP	ARG	SER	LEU	PRO	ALA	LEU	LYS	ILE	ARG
10	GLU	GLU	LEU	LEU	LYS	ILE	LEU	GLN	GLU	LEU
11	PRO	SER	VAL	SER	GLN	GLU	THR	LEU	LYS	HIS
12	SER	GLY	ILE	GLY	ARG	ALA	VAL	MET	TYR	LEU
13	TYR	LYS	HIS	PRO	LYS	GLU	SER	ARG	SER	ASN
14	LYS	ASP	MET	ALA	GLY	LYS	LEU	ILE	ASN	GLU
15	TRP	SER	ARG	PRO	ILE	PHE	GLY	LEU	GLY	SER

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

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CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 34538

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	SER	ASN	ALA	ALA	SER	GLY	THR	PHE	ILE	SER
2	ASP	ALA	ASP	ASP	VAL	VAL	SER	ALA	MET	ILE
3	VAL	LYS	MET	ASN	GLU	ALA	ALA	GLU	GLU	ASP
4	ARG	GLN	LEU	ASN	ASN	GLN	LYS	LYS	PRO	ALA
5	LEU	LYS	LYS	LEU	THR	LEU	LEU	PRO	ALA	VAL
6	VAL	MET	HIS	LEU	LYS	LYS	GLN	ASP	LEU	LYS
7	GLU	THR	PHE	ILE	ASP	SER	GLY	VAL	MET	SER
8	ALA	ILE	LYS	GLU	TRP	LEU	SER	PRO	LEU	PRO
9	ASP	ARG	SER	LEU	PRO	ALA	LEU	LYS	ILE	ARG
10	GLU	GLU	LEU	LEU	LYS	ILE	LEU	GLN	GLU	LEU
11	PRO	SER	VAL	SER	GLN	GLU	THR	LEU	LYS	HIS
12	SER	GLY	ILE	GLY	ARG	ALA	VAL	MET	TYR	LEU
13	TYR	LYS	HIS	PRO	LYS	GLU	SER	ARG	SER	ASN
14	LYS	ASP	MET	ALA	GLY	LYS	LEU	ILE	ASN	GLU
15	TRP	SER	ARG	PRO	ILE	PHE	GLY	LEU	GLY	SER

1	SER	ASN	ALA	ALA	SER	GLY	THR	PHE	ILE	SER
2	ASP	ALA	ASP	ASP	VAL	VAL	SER	ALA	MET	ILE
3	VAL	LYS	MET	ASN	GLU	ALA	ALA	GLU	GLU	ASP
4	ARG	GLN	LEU	ASN	ASN	GLN	LYS	LYS	PRO	ALA
5	LEU	LYS	LYS	LEU	THR	LEU	LEU	PRO	ALA	VAL
6	VAL	MET	HIS	LEU	LYS	LYS	GLN	ASP	LEU	LYS
7	GLU	THR	PHE	ILE	ASP	SER	GLY	VAL	MET	SER
8	ALA	ILE	LYS	GLU	TRP	LEU	SER	PRO	LEU	PRO
9	ASP	ARG	SER	LEU	PRO	ALA	LEU	LYS	ILE	ARG
10	GLU	GLU	LEU	LEU	LYS	ILE	LEU	GLN	GLU	LEU
11	PRO	SER	VAL	SER	GLN	GLU	THR	LEU	LYS	HIS
12	SER	GLY	ILE	GLY	ARG	ALA	VAL	MET	TYR	LEU
13	TYR	LYS	HIS	PRO	LYS	GLU	SER	ARG	SER	ASN
14	LYS	ASP	MET	ALA	GLY	LYS	LEU	ILE	ASN	GLU
15	TRP	SER	ARG	PRO	ILE	PHE	GLY	LEU	GLY	SER

1	SER	ASN	ALA	ALA	SER	GLY	THR	PHE	ILE	SER
2	ASP	ALA	ASP	ASP	VAL	VAL	SER	ALA	MET	ILE
3	VAL	LYS	MET	ASN	GLU	ALA	ALA	GLU	GLU	ASP
4	ARG	GLN	LEU	ASN	ASN	GLN	LYS	LYS	PRO	ALA
5	LEU	LYS	LYS	LEU	THR	LEU	LEU	PRO	ALA	VAL
6	VAL	MET	HIS	LEU	LYS	LYS	GLN	ASP	LEU	LYS
7	GLU	THR	PHE	ILE	ASP	SER	GLY	VAL	MET	SER
8	ALA	ILE	LYS	GLU	TRP	LEU	SER	PRO	LEU	PRO
9	ASP	ARG	SER	LEU	PRO	ALA	LEU	LYS	ILE	ARG
10	GLU	GLU	LEU	LEU	LYS	ILE	LEU	GLN	GLU	LEU
11	PRO	SER	VAL	SER	GLN	GLU	THR	LEU	LYS	HIS
12	SER	GLY	ILE	GLY	ARG	ALA	VAL	MET	TYR	LEU
13	TYR	LYS	HIS	PRO	LYS	GLU	SER	ARG	SER	ASN
14	LYS	ASP	MET	ALA	GLY	LYS	LEU	ILE	ASN	GLU
15	TRP	SER	ARG	PRO	ILE	PHE	GLY	LEU	GLY	SER