BMRB Entry 11594

Name: Solution structure of the complex between XPC acidic domain and TFIIH p62 PH domain
Published: 2016-02-15

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PDB ID: 2rvb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11594
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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 XPC acidic domain and TFIIH p62 PH domain

Deposition date:

2015-07-01

Original release date:

2016-02-15

Authors:

Okuda, Masahiko; Nishimura, Yoshifumi

Citation:

Citation: Okuda, Masahiko; Kinoshita, Minoru; Kakumu, Erina; Sugasawa, Kaoru; Nishimura, Yoshifumi. "Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC" Structure 23, 1827-1837 (2015).
PubMed: 26278177

Assembly members:

Assembly members:
XPC_acidic_domain, polymer, 52 residues, 5511.741 Da.
TFIIH_p62_PH_domain, polymer, 110 residues, 12306.429 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 Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
XPC_acidic_domain: GSHMAHHLKRGATMNEDSNE EEEESENDWEEVEELSEPVL GDVRESTAFSRS
TFIIH_p62_PH_domain: GSMATSSEEVLLIVKKVRQK KQDGALYLMAERIAWAPEGK DRFTISHMYADIKCQKISPE GKAKIQLQLVLHAGDTTNFH FSNESTAVKERDAVKDLLQQ LLPKFKRKAN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	680
15N chemical shifts	165
1H chemical shifts	1036

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	XPC acidic domain	1
2	TFIIH p62 PH domain	2

Entities:

Entity 1, XPC acidic domain 52 residues - 5511.741 Da.

1

GLY

SER

HIS

MET

ALA

HIS

LEU

LYS

ARG

2

GLY

ALA

THR

MET

ASN

GLU

ASP

SER

ASN

GLU

3

GLU

SER

GLU

ASN

ASP

TRP

GLU

4

GLU

VAL

GLU

LEU

SER

GLU

PRO

VAL

LEU

5

GLY

ASP

VAL

ARG

GLU

SER

THR

ALA

PHE

SER

6

ARG

SER

Entity 2, TFIIH p62 PH domain 110 residues - 12306.429 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
2D 1H-13C HSQC	sample_2	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_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_4	isotropic	sample_conditions_1
3D HNHB	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	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 11594

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