BMRBj - BMREntryMaster

Found 1 Document (2.086 seconds)

BMRB: 30576

Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.

Authors

Danilenko, N., Carlomagno, T., Kirkpatrick, J.P.

Assembly

Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate

Entity

1. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 1 (polymer), 264 monomers, 30614.71 × 2 Da Detail

MMSDQENENE HAKAFLGLAK CEEEVDAIER EVELYRLNKM KPVYEKRDAY IDEIAEFWKI VLSQHVSFAN YIRASDFKYI DTIDKIKVEW LALESEMYDT RDFSITFHFH GIEGDFKEQQ VTKVFQIKKG KDDQEDGILT SEPVPIEWPQ SYDSINPDLI KDKRSPEGKK KYRQGMKTIF GWFRWTGLKP GKEFPHGDSL ASLFSEEIYP FCVKYYAEAQ RDLEDEEGES GLSADGDSED DDGSLGEVDL PLSDEEPSSK KRKV

2. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 2 (polymer), 442 monomers, 50696.88 Da Detail

GMDPNSMSLN DFLSSVLPVS EQFEYLSLQS IPLETHAVVT PNKDDKRVPK STIKTQHFFS LFHQGKVFFS LEVYVYVTLW DEADAERLIF VSKADTNGYC NTRVSVRDIT KIILEFILSI DPNYYLQKVK PAIRSYKKIS PELISAASTP ARTLRILARR LKQSGSTVLK EIESPRFQQD LYLSFTCPRE ILTKICLFTR PASQYLFPDS SKNSKKHILN GEELMKWWGF ILDRLLIECF QNDTQAKLRI PGEDPARVRS YLRGMKYPLW QVGDIFTSKE NSLAVYNIPL FPDDPKARFI HQLAEEDRLL KVSLSSFWIE LQERQEFKLS VTSSVMGISG YSLATPSLFP SSADVIVPKS RKQFRAIKKY ITGEEYDTEE GAIEAFTNIR DFLLLRMATN LQSLTGKREH RERNQPVPAS NINTLAITML KPRKKAKALP KT

3. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 3 (polymer), 279 monomers, 31558.89 Da Detail

SSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS LDHDQELDSI LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDEE ELRENPPAKV QVDHIVRNIL AEKPRVTRFN IVWDNENEGD LYPPEQPGVD DEEEEDDEEE DDDEDDEDDE DDDQEDGEGE AEEAAEEEEE EEEKTEDNET NLEEEEEDIE NSDGDEEEGE EEVGSVDKNE DGNDKKRRKI EGGSTDIEST PKDAARSTN

4. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 4 (polymer), 136 monomers, 15387.83 Da Detail

MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA

5. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 5 (polymer), 103 monomers, 11367.20 Da Detail

MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG

Total weight

170240.22 Da

Max. entity weight

50696.88 Da

Source organism

Saccharomyces cerevisiae S288C , Xenopus laevis

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 7.4 %, Completeness: 3.0 %, Completeness (bb): 3.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	3.0 % (391 of 13209)	2.9 % (222 of 7589)	3.0 % (169 of 5620)
Backbone	3.0 % (179 of 6062)	3.5 % (85 of 2460)	2.6 % (94 of 3602)
Sidechain	2.9 % (237 of 8301)	2.6 % (134 of 5129)	3.2 % (103 of 3172)
Aromatic	1.2 % (12 of 1034)	1.5 % (8 of 523)	0.8 % (4 of 511)
Methyl	9.7 % (122 of 1264)	9.7 % (61 of 632)	9.7 % (61 of 632)

1. entity 1

2. entity 2

3. entity 3

4. entity 4

MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA

5. entity 5

MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG

Show sample condition

Sample #1

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3, 70 uM H4, 100% D2O

#	Name	Isotope labeling	Concentration
1	Vps75 (dimer)	ILV methyl labelled, perdeuterated	70 uM
2	Rtt109	natural abundance	70 uM
3	Asf1	natural abundance	70 uM
4	H3	natural abundance	70 uM
5	H4	natural abundance	70 uM

Sample #2

#	Name	Isotope labeling	Concentration
6	Vps75 (dimer)	ILV methyl labelled, perdeuterated	70 uM
7	Rtt109	natural abundance	70 uM
8	Asf1	natural abundance	70 uM
9	H4	natural abundance	70 uM
10	H3(110A,63C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	70 uM

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 90 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 90 uM Rtt109, 90 uM Asf1, 90 uM H3(110A,76C) mutant with a cysteine coupled to a paramagnetic tag, 90 uM H4, 100% D2O

#	Name	Isotope labeling	Concentration
11	Vps75 (dimer)	ILV methyl labelled, perdeuterated	90 uM
12	Rtt109	natural abundance	90 uM
13	Asf1	natural abundance	90 uM
14	H4	natural abundance	90 uM
15	H3(110A,76C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	90 uM

Sample #4

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(30C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O

#	Name	Isotope labeling	Concentration
16	Vps75 (dimer)	ILV methyl labelled, perdeuterated	30 uM
17	Rtt109	natural abundance	30 uM
18	Asf1	natural abundance	30 uM
19	H3	natural abundance	30 uM
20	H4(30C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	30 uM

Sample #5

#	Name	Isotope labeling	Concentration
21	Vps75 (dimer)	ILV methyl labelled, perdeuterated	70 uM
22	Rtt109	natural abundance	70 uM
23	Asf1	natural abundance	70 uM
24	H3	natural abundance	70 uM
25	H4(82C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	70 uM

Sample #6

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 80 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 80 uM Rtt109, 80 uM Asf1, 80 uM H3, 80 uM H4(45C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O

#	Name	Isotope labeling	Concentration
26	Vps75 (dimer)	ILV methyl labelled, perdeuterated	80 uM
27	Rtt109	natural abundance	80 uM
28	Asf1	natural abundance	80 uM
29	H3	natural abundance	80 uM
30	H4(45C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	80 uM

Sample #7

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(93C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O

#	Name	Isotope labeling	Concentration
31	Vps75 (dimer)	ILV methyl labelled, perdeuterated	30 uM
32	Rtt109	natural abundance	30 uM
33	Asf1	natural abundance	30 uM
34	H3	natural abundance	30 uM
35	H4(93C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	30 uM

Protein Blocks Logo

Calculated from 1 models in PDB: 6O22, Strand ID: A, B, C, D, E, F Detail

Release date

2019-04-08

Citation

Histone chaperone exploits intrinsic disorder to switch acetylation specificity
Danilenko, N., Lercher, L., Kirkpatrick, J., Gabel, F., Codutti, L., Carlomagno, T.
Nat. Commun. (2019), 10, 3435-3435, PubMed 31387991 , DOI 10.1038/s41467-019-11410-7 , Abstract

Related entities 1. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 1, : 2 : 12 entities Detail

Related entities 2. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 2, : 2 entities Detail

Related entities 3. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 3, : 1 entities Detail

Related entities 4. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 4, : 5 : 2 : 4 : 83 entities Detail

Related entities 5. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 5, : 11 : 7 : 2 : 18 entities Detail

Interaction partners 1. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 1, : 17 : 1 interactors Detail

More details for 18 interactors identified by 3 citations

Interaction partners 2. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 2, : 11 : 1 interactors Detail

More details for 12 interactors identified by 3 citations

Experiments performed 7 experiments Detail

1 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3, 70 uM H4, 100% D2O

#	Name	Isotope labeling	Concentration
1	Vps75 (dimer)	ILV methyl labelled, perdeuterated	70 uM
2	Rtt109	natural abundance	70 uM
3	Asf1	natural abundance	70 uM
4	H3	natural abundance	70 uM
5	H4	natural abundance	70 uM

2 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
6	Vps75 (dimer)	ILV methyl labelled, perdeuterated	70 uM
7	Rtt109	natural abundance	70 uM
8	Asf1	natural abundance	70 uM
9	H4	natural abundance	70 uM
10	H3(110A,63C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	70 uM

3 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 90 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 90 uM Rtt109, 90 uM Asf1, 90 uM H3(110A,76C) mutant with a cysteine coupled to a paramagnetic tag, 90 uM H4, 100% D2O

#	Name	Isotope labeling	Concentration
11	Vps75 (dimer)	ILV methyl labelled, perdeuterated	90 uM
12	Rtt109	natural abundance	90 uM
13	Asf1	natural abundance	90 uM
14	H4	natural abundance	90 uM
15	H3(110A,76C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	90 uM

4 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(30C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O

#	Name	Isotope labeling	Concentration
16	Vps75 (dimer)	ILV methyl labelled, perdeuterated	30 uM
17	Rtt109	natural abundance	30 uM
18	Asf1	natural abundance	30 uM
19	H3	natural abundance	30 uM
20	H4(30C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	30 uM

5 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

#	Name	Isotope labeling	Concentration
21	Vps75 (dimer)	ILV methyl labelled, perdeuterated	70 uM
22	Rtt109	natural abundance	70 uM
23	Asf1	natural abundance	70 uM
24	H3	natural abundance	70 uM
25	H4(82C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	70 uM

6 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 80 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 80 uM Rtt109, 80 uM Asf1, 80 uM H3, 80 uM H4(45C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O

#	Name	Isotope labeling	Concentration
26	Vps75 (dimer)	ILV methyl labelled, perdeuterated	80 uM
27	Rtt109	natural abundance	80 uM
28	Asf1	natural abundance	80 uM
29	H3	natural abundance	80 uM
30	H4(45C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	80 uM

7 2D 1H-13C HSQC

Instrument

Bruker AvanceIII - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5, Details 30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(93C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O

#	Name	Isotope labeling	Concentration
31	Vps75 (dimer)	ILV methyl labelled, perdeuterated	30 uM
32	Rtt109	natural abundance	30 uM
33	Asf1	natural abundance	30 uM
34	H3	natural abundance	30 uM
35	H4(93C) mutant with a cysteine coupled to a paramagnetic tag	natural abundance	30 uM

Chemical shift validation 7 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30576_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: bmr30576_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	368		12.9 (chain: 1, length: 264)
1	Chemical shift references	chem_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 264, Sequence coverage: 12.9%
- Total number of assignments
  - ¹H chemical shifts: 276
  - ¹³C chemical shifts: 92
- Completeness of assignments
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts

Keywords Chaperone

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Found 1 Document (2.086 seconds)

BMRB: 30576

Sample #1

Sample #2

Sample #3

Sample #4

Sample #5

Sample #6

Sample #7

Related entities 1. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 1, : 2 : 12 entities Detail

Related entities 2. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 2, : 2 entities Detail

Related entities 3. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 3, : 1 entities Detail

Related entities 4. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 4, : 5 : 2 : 4 : 83 entities Detail

Related entities 5. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 5, : 11 : 7 : 2 : 18 entities Detail

Interaction partners 1. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 1, : 17 : 1 interactors Detail

Interaction partners 2. Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate, entity 2, : 11 : 1 interactors Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 7 contents Detail