BMRB Entry 34223

Name: NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP90 peptide DTSRMEEVD
Published: 2018-07-26

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PDB ID: 6fdp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34223
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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: NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP90 peptide DTSRMEEVD PubMed: 30033218

Deposition date: 2017-12-26 Original release date: 2018-07-26

Authors: Quinternet, M.; Chagot, M.; Manival, X.

Citation: Henri, Julien; Chagot, Marie-Eve; Bourguet, Maxime; Abel, Yoann; Terral, Guillaume; Maurizy, Chloe; Aigueperse, Christelle; Georgescauld, Florian; Vandermoere, Franck; Saint-Fort, Renette; Behm-Ansmant, Isabelle; Charpentier, Bruno; Pradet-Balade, Berengere; Verheggen, Celine; Bertrand, Edouard; Meyer, Philippe; Cianferani, Sarah; Manival, Xavier; Quinternet, Marc. "Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex" Structure 26, 1196-1209 (2018).

Assembly members:
entity_1, polymer, 120 residues, 13368.283 Da.
entity_2, polymer, 9 residues, 1082.120 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: GPHMQAISEKDRGNGFFKEG KYERAIECYTRGIAADGANA LLPANRAMAYLKIQKYEEAE KDCTQAILLDGSYSKAFARR GTARTFLGKLNEAKQDFETV LLLEPGNKQAVTELSKIKKK
entity_2: DTSRMEEVD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	527
15N chemical shifts	141
1H chemical shifts	920

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_1 120 residues - 13368.283 Da.

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

Entity 2, entity_2 9 residues - 1082.120 Da.

1

ASP

THR

SER

ARG

MET

GLU

VAL

ASP

Samples:

sample_1: RPAP3-TPR2, [U-13C; U-15N], 1 mM; HSP90-pep 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_2: RPAP3-TPR2, [U-13C; U-15N], 1 mM; HSP90-pep 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D X-halffiltered 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D X-half filtered 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D double X-half filtered 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D double X-half filtered 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS, Cornilescu, Delaglio and Bax - structure calculation

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts

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

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

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