BMRB Entry 16279

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the yeast Hsp90 Middle Domain
Published: 2011-08-31

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16279

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the yeast Hsp90 Middle Domain

Deposition date:

2009-05-07

Original release date:

2011-08-31

Authors:

Hagn, Franz; Retzlaff, Marco; Rohrberg, Julia; Buchner, Johannes; Kessler, Horst

Citation:

Citation: Hagn, Franz; Lagleder, Stephan; Retzlaff, Marco; Rohrberg, Julia; Demmer, Oliver; Richter, Klaus; Buchner, Johannes; Kessler, Horst. "Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53." Nat. Struct. Mol. Biol. 18, 1086-1093 (2011).
PubMed: 21892170

Assembly members:

Assembly members:
Hsp90M, polymer, 260 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hsp90M: GSHMKTKPLWTRNPSDITQE EYNAFYKSISNDWEDPLYVK HFSVEGQLEFRAILFIPKRA PFDLFESKKKKNNIKLYVRR VFITDEAEDLIPEWLSFVKG VVDSEDLPLNLSREMLQQNK IMKVIRKNIVKKLIEAFNEI AEDSEQFEKFYSAFSKNIKL GVHEDTQNRAALAKLLRYNS TKSVDELTSLTDYVTRMPEH QKNIYYITGESLKAVEKSPF LDALKAKNFEVLFLTDPIDE YAFTQLKEFEGKTLVDITKD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	671
15N chemical shifts	201
1H chemical shifts	201

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hsp90 middle domain	1

Entities:

Entity 1, Hsp90 middle domain 260 residues - Formula weight is not available

residues 1-4 represent a clonig artifact after tag removal.

1	GLY	SER	HIS	MET	LYS	THR	LYS	PRO	LEU	TRP
2	THR	ARG	ASN	PRO	SER	ASP	ILE	THR	GLN	GLU
3	GLU	TYR	ASN	ALA	PHE	TYR	LYS	SER	ILE	SER
4	ASN	ASP	TRP	GLU	ASP	PRO	LEU	TYR	VAL	LYS
5	HIS	PHE	SER	VAL	GLU	GLY	GLN	LEU	GLU	PHE
6	ARG	ALA	ILE	LEU	PHE	ILE	PRO	LYS	ARG	ALA
7	PRO	PHE	ASP	LEU	PHE	GLU	SER	LYS	LYS	LYS
8	LYS	ASN	ASN	ILE	LYS	LEU	TYR	VAL	ARG	ARG
9	VAL	PHE	ILE	THR	ASP	GLU	ALA	GLU	ASP	LEU
10	ILE	PRO	GLU	TRP	LEU	SER	PHE	VAL	LYS	GLY
11	VAL	VAL	ASP	SER	GLU	ASP	LEU	PRO	LEU	ASN
12	LEU	SER	ARG	GLU	MET	LEU	GLN	GLN	ASN	LYS
13	ILE	MET	LYS	VAL	ILE	ARG	LYS	ASN	ILE	VAL
14	LYS	LYS	LEU	ILE	GLU	ALA	PHE	ASN	GLU	ILE
15	ALA	GLU	ASP	SER	GLU	GLN	PHE	GLU	LYS	PHE
16	TYR	SER	ALA	PHE	SER	LYS	ASN	ILE	LYS	LEU
17	GLY	VAL	HIS	GLU	ASP	THR	GLN	ASN	ARG	ALA
18	ALA	LEU	ALA	LYS	LEU	LEU	ARG	TYR	ASN	SER
19	THR	LYS	SER	VAL	ASP	GLU	LEU	THR	SER	LEU
20	THR	ASP	TYR	VAL	THR	ARG	MET	PRO	GLU	HIS
21	GLN	LYS	ASN	ILE	TYR	TYR	ILE	THR	GLY	GLU
22	SER	LEU	LYS	ALA	VAL	GLU	LYS	SER	PRO	PHE
23	LEU	ASP	ALA	LEU	LYS	ALA	LYS	ASN	PHE	GLU
24	VAL	LEU	PHE	LEU	THR	ASP	PRO	ILE	ASP	GLU
25	TYR	ALA	PHE	THR	GLN	LEU	LYS	GLU	PHE	GLU
26	GLY	LYS	THR	LEU	VAL	ASP	ILE	THR	LYS	ASP

Samples:

sample_1: Hsp90M, [U-99% 13C; U-99% 15N; U-95% 2H], 1.2 ± 0.2 mM; potassium phosphate 50 mM; potassium chloride 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

SPARKY v2, Goddard - data analysis, peak picking

PASTA v0.1, Kessler - chemical shift assignment

NMR spectrometers:

Bruker DMX 750 MHz

PIR	HHBY90
PDB	1HK7 1USU 1USV 2CG9 2CGE
DBJ	GAA25634 GAA26739
EMBL	CAA89919 CAA91604 CAA97961 CAY82016 CAY86720
GB	AAA02743 AAA02813 AHY76639 AHY77944 AJP40879
REF	NP_013911 NP_015084
SP	P02829 P15108
TPG	DAA10084 DAA11197
AlphaFold	P15108 P02829

1	GLY	SER	HIS	MET	LYS	THR	LYS	PRO	LEU	TRP
2	THR	ARG	ASN	PRO	SER	ASP	ILE	THR	GLN	GLU
3	GLU	TYR	ASN	ALA	PHE	TYR	LYS	SER	ILE	SER
4	ASN	ASP	TRP	GLU	ASP	PRO	LEU	TYR	VAL	LYS
5	HIS	PHE	SER	VAL	GLU	GLY	GLN	LEU	GLU	PHE
6	ARG	ALA	ILE	LEU	PHE	ILE	PRO	LYS	ARG	ALA
7	PRO	PHE	ASP	LEU	PHE	GLU	SER	LYS	LYS	LYS
8	LYS	ASN	ASN	ILE	LYS	LEU	TYR	VAL	ARG	ARG
9	VAL	PHE	ILE	THR	ASP	GLU	ALA	GLU	ASP	LEU
10	ILE	PRO	GLU	TRP	LEU	SER	PHE	VAL	LYS	GLY
11	VAL	VAL	ASP	SER	GLU	ASP	LEU	PRO	LEU	ASN
12	LEU	SER	ARG	GLU	MET	LEU	GLN	GLN	ASN	LYS
13	ILE	MET	LYS	VAL	ILE	ARG	LYS	ASN	ILE	VAL
14	LYS	LYS	LEU	ILE	GLU	ALA	PHE	ASN	GLU	ILE
15	ALA	GLU	ASP	SER	GLU	GLN	PHE	GLU	LYS	PHE
16	TYR	SER	ALA	PHE	SER	LYS	ASN	ILE	LYS	LEU
17	GLY	VAL	HIS	GLU	ASP	THR	GLN	ASN	ARG	ALA
18	ALA	LEU	ALA	LYS	LEU	LEU	ARG	TYR	ASN	SER
19	THR	LYS	SER	VAL	ASP	GLU	LEU	THR	SER	LEU
20	THR	ASP	TYR	VAL	THR	ARG	MET	PRO	GLU	HIS
21	GLN	LYS	ASN	ILE	TYR	TYR	ILE	THR	GLY	GLU
22	SER	LEU	LYS	ALA	VAL	GLU	LYS	SER	PRO	PHE
23	LEU	ASP	ALA	LEU	LYS	ALA	LYS	ASN	PHE	GLU
24	VAL	LEU	PHE	LEU	THR	ASP	PRO	ILE	ASP	GLU
25	TYR	ALA	PHE	THR	GLN	LEU	LYS	GLU	PHE	GLU
26	GLY	LYS	THR	LEU	VAL	ASP	ILE	THR	LYS	ASP

1	GLY	SER	HIS	MET	LYS	THR	LYS	PRO	LEU	TRP
2	THR	ARG	ASN	PRO	SER	ASP	ILE	THR	GLN	GLU
3	GLU	TYR	ASN	ALA	PHE	TYR	LYS	SER	ILE	SER
4	ASN	ASP	TRP	GLU	ASP	PRO	LEU	TYR	VAL	LYS
5	HIS	PHE	SER	VAL	GLU	GLY	GLN	LEU	GLU	PHE
6	ARG	ALA	ILE	LEU	PHE	ILE	PRO	LYS	ARG	ALA
7	PRO	PHE	ASP	LEU	PHE	GLU	SER	LYS	LYS	LYS
8	LYS	ASN	ASN	ILE	LYS	LEU	TYR	VAL	ARG	ARG
9	VAL	PHE	ILE	THR	ASP	GLU	ALA	GLU	ASP	LEU
10	ILE	PRO	GLU	TRP	LEU	SER	PHE	VAL	LYS	GLY
11	VAL	VAL	ASP	SER	GLU	ASP	LEU	PRO	LEU	ASN
12	LEU	SER	ARG	GLU	MET	LEU	GLN	GLN	ASN	LYS
13	ILE	MET	LYS	VAL	ILE	ARG	LYS	ASN	ILE	VAL
14	LYS	LYS	LEU	ILE	GLU	ALA	PHE	ASN	GLU	ILE
15	ALA	GLU	ASP	SER	GLU	GLN	PHE	GLU	LYS	PHE
16	TYR	SER	ALA	PHE	SER	LYS	ASN	ILE	LYS	LEU
17	GLY	VAL	HIS	GLU	ASP	THR	GLN	ASN	ARG	ALA
18	ALA	LEU	ALA	LYS	LEU	LEU	ARG	TYR	ASN	SER
19	THR	LYS	SER	VAL	ASP	GLU	LEU	THR	SER	LEU
20	THR	ASP	TYR	VAL	THR	ARG	MET	PRO	GLU	HIS
21	GLN	LYS	ASN	ILE	TYR	TYR	ILE	THR	GLY	GLU
22	SER	LEU	LYS	ALA	VAL	GLU	LYS	SER	PRO	PHE
23	LEU	ASP	ALA	LEU	LYS	ALA	LYS	ASN	PHE	GLU
24	VAL	LEU	PHE	LEU	THR	ASP	PRO	ILE	ASP	GLU
25	TYR	ALA	PHE	THR	GLN	LEU	LYS	GLU	PHE	GLU
26	GLY	LYS	THR	LEU	VAL	ASP	ILE	THR	LYS	ASP