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Found 1 Document (5.827 seconds)

BMRB: 5355

1BGQ

Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone

Authors

Williams, M.A., Salek, R.M., Ladbury, J.E.

Assembly

Hsp90 N-terminal ATPase domain

Entity

1. Hsp90 N-terminal ATPase domain (polymer, Thiol state: not present), 218 monomers, 24708.83 Da Detail

MRGSHHHHHH GMASETFEFQ AEITQLMSLI INTVYSNKEI FLRELISNAS DALDKIRYKS LSDPKQLETE PDLFIRITPK PEQKVLEIRD SGIGMTKAEL INNLGTIAKS GTKAFMEALS AGADVSMIGQ FGVGFYSLFL VADRVQVISK SNDDEQYIWE SNAGGSFTVT LDEVNERIGR GTILRLFLKD DQLEYLEEKR IKEVIKRHSE FVAYPIQL

Formula weight

24708.83 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.6 %, Completeness: 48.8 %, Completeness (bb): 86.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	48.8 % (1261 of 2582)	35.7 % (479 of 1342)	58.7 % (592 of 1009)	82.3 % (190 of 231)
Backbone	86.6 % (1124 of 1298)	80.9 % (360 of 445)	89.8 % (575 of 640)	88.7 % (189 of 213)
Sidechain	21.5 % (320 of 1488)	13.3 % (119 of 897)	34.9 % (200 of 573)	5.6 % (1 of 18)
Aromatic	6.1 % (12 of 198)	11.1 % (11 of 99)	1.0 % (1 of 98)	0.0 % (0 of 1)
Methyl	16.8 % (43 of 256)	20.3 % (26 of 128)	13.3 % (17 of 128)

1. Heat shock protein 90 N-terminal domain

Show sample condition

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: 0.5 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: 0.5 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.17 ppm, Outliers: 3 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.36 ppm, Outliers: 1 Detail

Release date

2002-09-24

Citation 1

Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone
Salek, R.M., Williams, M.A., Prodromou, C., Pearl, L.H., Ladbury, J.E.
J. Biomol. NMR (2002), 23, 327-328, PubMed 12398355 , Abstract

Show more 2 citaions

Citation 2

Structure, function, and mechanism of the Hsp90 molecular chaperone
Pearl, L.H., Prodromou, C.
Adv. Protein Chem. (2001), 59, 157-186, PubMed 11868271 , DOI: , Abstract

Citation 3

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W., Pearl, L.H.
Cell (1997), 90, 65-75, PubMed 9230303 , DOI: , Abstract

Hide non-primary 2 citaions

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P02829 released on 1986-07-21
Title HSP82_YEAST Entity ATP-dependent molecular chaperone HSP82

Related entities 1. Hsp90 N-terminal ATPase domain, : 1 : 1 : 29 : 258 entities Detail

Interaction partners 1. Hsp90 N-terminal ATPase domain, : 1153 interactors Detail

More details for 1153 interactors identified by 24 citations

Experiments performed 10 experiments Detail

1 1H-15N HSQC

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

2 1H-13C HSQC

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

3 1H-15N NOESY-HSQC

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

4 1H-15N TOCSY-HSQC

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

5 HNCA

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

6 HN(CA)CB

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

7 HN(CO)CA

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

8 HN(COCA)CB

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

9 HNCO

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

10 HN(CA)CO

Instrument

#1 Model Varian UnityPlus (500 MHz)

#2 Model Varian UnityPlus (600 MHz)

#3 Model Varian INOVA (800 MHz)

Sample #1

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
1	Heat shock protein 90 N-terminal domain	[U-98% 13C; U-98% 15N; U-70% 2H]		0.5 mM
2	Tris			20 mM

Sample #2

Temperature 298 (±0.2) K

#	Name	Isotope labeling	Type	Concentration
3	Heat shock protein 90 N-terminal domain	[U-98% 15N]		0.5 mM
4	Tris			20.0 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5355_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr5355_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1158		91.7 (chain: 1, length: 218)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 218, Sequence coverage: 91.7%
- Total number of assignments
  - ¹³C chemical shifts: 572
  - ¹⁵N chemical shifts: 192
  - ¹H chemical shifts: 394
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	1009	572	56.7
¹⁵N chemical shifts	242	192	79.3
¹H chemical shifts	1342	370	27.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	436	390	89.4
¹⁵N chemical shifts	213	191	89.7
¹H chemical shifts	445	344	77.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	573	182	31.8
¹⁵N chemical shifts	29	1	3.4
¹H chemical shifts	897	26	2.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	134	11	8.2
¹H chemical shifts	134	12	9.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	98	0	0.0
¹⁵N chemical shifts	1	0	0.0
¹H chemical shifts	99	1	1.0

Keywords Hsp90, heat shock protein, Saccharomyces Cerevisiae, heteronuclear NMR, resonance assignments

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Found 1 Document (5.827 seconds)

BMRB: 5355

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Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles Swiss-Prot: 1 entries Detail

Related entities 1. Hsp90 N-terminal ATPase domain, : 1 : 1 : 29 : 258 entities Detail

Interaction partners 1. Hsp90 N-terminal ATPase domain, : 1153 interactors Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 3 contents Detail