BMRB Entry 18445

Name: NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explain how Hsp90 recognizes the R2TP complex
Published: 2013-05-20

Click here to enlarge.

PDB ID: 2lsu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18445
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explain how Hsp90 recognizes the R2TP complex PubMed: 24012479

Deposition date: 2012-05-07 Original release date: 2013-05-20

Authors: BACK, Regis; DOMINGUEZ, Cyril; ROTHE, Benjamin; BOBO, Claude; BEAUFILS, Chrystel; MORERA, Solange; MEYER, Philippe; CHARPENTIER, Bruno; BRANLANT, Christiane; ALLAIN, Frederic H.-T.; MANIVAL, Xavier

Citation: Back, Regis; Dominguez, Cyril; Rothe, Benjamin; Bobo, Claude; Beaufils, Chrystel; Morera, Solange; Meyer, Philippe; Charpentier, Bruno; Branlant, Christiane; Allain, Frederic H-T; Manival, Xavier. "High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex." Structure 21, 1834-1847 (2013).

Assembly members:
entity, polymer, 110 residues, 12393.052 Da.

Natural source: Common Name: bakers yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: SQFEKQKEQGNSLFKQGLYR EAVHCYDQLITAQPQNPVGY SNKAMALIKLGEYTQAIQMC QQGLRYTSTAEHVAIRSKLQ YRLELAQGAVGSVQIPVVEV DELPEGYDRS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	327
1H chemical shifts	760

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

BMRB	17312 18447
PDB	2L6J 2LSU 2LSV 4CGQ 4CGU
DBJ	GAA21965
EMBL	CAA42288 CAY78265
GB	AAS56477 AHN96120 AHV79323 AHY79733 AJP37484
REF	NP_009986
SP	P25638
TPG	DAA07534

Biological Magnetic Resonance Data Bank

BMRB Entry 18445

Title: NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explain how Hsp90 recognizes the R2TP complex PubMed: 24012479

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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