BMRB Entry 36101

Name: Solution structure of the complex between UVSSA acidic region and TFIIH p62 PH domain
Published: 2018-07-11

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PDB ID: 5xv8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36101
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:

Solution structure of the complex between UVSSA acidic region and TFIIH p62 PH domain

Deposition date:

2017-06-27

Original release date:

2018-07-11

Authors:

Okuda, M.; Nishimura, Y.

Citation:

Citation: Okuda, M.; Nakazawa, Y.; Guo, C.; Ogi, T.; Nishimura, Y.. "Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways" Nucleic Acids Res. 45, 13043-13055 (2017).
PubMed: 29069470

Assembly members:

Assembly members:
entity_1, polymer, 48 residues, 5507.810 Da.
entity_2, polymer, 110 residues, 12450.445 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: GSMRRRTEALGDAEEDEDDE DFVEVPEKEGYEPHIPDHLR PEYGLEAA
entity_2: GSMATSSEEVLLIVKKVRQK KQDGALYLMAERIAWAPEGK DRFTISHMYADIKCQKISPE GKAKIQLQLVLHAGDTTNFH FSNESTAVKERDAVKDLLQQ LLPKFKRKAN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	662
15N chemical shifts	156
1H chemical shifts	1018

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 48 residues - 5507.810 Da.

1

GLY

SER

MET

ARG

THR

GLU

ALA

LEU

2

GLY

ASP

ALA

GLU

ASP

GLU

ASP

GLU

3

ASP

PHE

VAL

GLU

VAL

PRO

GLU

LYS

GLU

GLY

4

TYR

GLU

PRO

HIS

ILE

PRO

ASP

HIS

LEU

ARG

5

PRO

GLU

TYR

GLY

LEU

GLU

ALA

Entity 2, entity_2 110 residues - 12450.445 Da.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HNHB	sample_3	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 36101

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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