BMRB Entry 11578

Name: Solution structure of the complex between p53 transactivation domain 2 and TFIIH p62 PH domain
Published: 2017-08-11

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PDB ID: 2ruk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11578
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the complex between p53 transactivation domain 2 and TFIIH p62 PH domain

Deposition date:

2014-09-24

Original release date:

2017-08-11

Authors:

Okuda, Masahiko; Nishimura, Yoshifumi

Citation:

Citation: Okuda, Masahiko; Nishimura, Yoshifumi. "Extended String Binding Mode of the Phosphorylated Transactivation Domain of Tumor Suppressor p53" J. Am. Chem. Soc. ., 14143-14152 (2014).
PubMed: 25216154

Assembly members:

Assembly members:
p53_TAD2, polymer, 22 residues, 2724.623 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p53_TAD2: DDLMLXPDDIEQWFXEDPGP DE
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	497
15N chemical shifts	116
1H chemical shifts	911

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 22 residues - 2724.623 Da.

1

ASP

LEU

MET

LEU

SEP

PRO

ASP

ILE

2

GLU

GLN

TRP

PHE

TPO

GLU

ASP

PRO

GLY

PRO

3

ASP

GLU

Entity 2, entity_2 110 residues - 12306.429 Da.

Residues 1,2 represent a non-native remainder of an affinity tag

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
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	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-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

BMRB Entry 11578

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