BMRBj - BMREntryMaster

Found 1 Document (1.357 seconds)

BMRB: 34201

6F0Y

Rtt109 peptide bound to Asf1

Authors

Lercher, L., Kirkpatrick, J.P., Carlomagno, T.

Assembly

Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48)

Entity

1. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 1 (polymer), 172 monomers, 19310.49 Da Detail

GAMGSIVSLL GIKVLNNPAK FTDPYEFEIT FECLESLKHD LEWKLTYVGS SRSLDHDQEL DSILVGPVPV GVNKFVFSAD PPSAELIPAS ELVSVTVILL SCSYDGREFV RVGYYVNNEY DEEELRENPP AKVQVDHIVR NILAEKPRVT RFNIVWDNEN EGDLYPPEQP GV

2. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 2 (polymer, Thiol state: not present), 15 monomers, 1682.166 Da Detail

LAITMLKPRK KAKAL

Total weight

20992.656 Da

Max. entity weight

19310.49 Da

Source organism

Saccharomyces cerevisiae S288C

Exptl. method

solution NMR

Refine. method

simulated annealingtorsion angle dynamicsmolecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 92.7 %, Completeness (bb): 91.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.7 % (2036 of 2197)	96.7 % (1103 of 1141)	87.6 % (760 of 868)	92.0 % (173 of 188)
Backbone	91.2 % (998 of 1094)	95.7 % (354 of 370)	88.2 % (486 of 551)	91.3 % (158 of 173)
Sidechain	93.4 % (1196 of 1280)	97.1 % (749 of 771)	87.4 % (432 of 494)	100.0 % (15 of 15)
Aromatic	95.1 % (154 of 162)	97.5 % (79 of 81)	92.4 % (73 of 79)	100.0 % (2 of 2)
Methyl	93.1 % (216 of 232)	97.4 % (113 of 116)	88.8 % (103 of 116)

1. entity 1

GAMGSIVSLL GIKVLNNPAK FTDPYEFEIT FECLESLKHD LEWKLTYVGS SRSLDHDQEL DSILVGPVPV GVNKFVFSAD PPSAELIPAS ELVSVTVILL SCSYDGREFV RVGYYVNNEY DEEELRENPP AKVQVDHIVR NILAEKPRVT RFNIVWDNEN EGDLYPPEQP GV

2. entity 2

LAITMLKPRK KAKAL

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.5 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 3 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.15 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 0.5 mM histone acetyltransferase Rtt109 C-terminus, 100% D2O

#	Name	Isotope labeling	Type	Concentration
3	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.15 mM
4	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.5 mM

Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.5 mM [U-99% 13C; U-99% 15N; U-99% 2D] Histone chaperone ASF1, 0.15 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.15 mM
6	Histone chaperone ASF1	[U-99% 13C; U-99% 15N; U-99% 2D]		0.5 mM

Chem. Shift Complete2

Sequence coverage: 32.6 %, Completeness: 57.9 %, Completeness (bb): 57.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	57.9 % (2546 of 4394)	61.3 % (1400 of 2282)	53.4 % (927 of 1736)	58.2 % (219 of 376)
Backbone	57.9 % (1267 of 2188)	62.3 % (461 of 740)	55.0 % (606 of 1102)	57.8 % (200 of 346)
Sidechain	57.6 % (1474 of 2560)	60.9 % (939 of 1542)	52.2 % (516 of 988)	63.3 % (19 of 30)
Aromatic	51.9 % (168 of 324)	53.1 % (86 of 162)	50.6 % (80 of 158)	50.0 % (2 of 4)
Methyl	58.2 % (270 of 464)	62.9 % (146 of 232)	53.4 % (124 of 232)

1. entity 1

GAMGSIVSLL GIKVLNNPAK FTDPYEFEIT FECLESLKHD LEWKLTYVGS SRSLDHDQEL DSILVGPVPV GVNKFVFSAD PPSAELIPAS ELVSVTVILL SCSYDGREFV RVGYYVNNEY DEEELRENPP AKVQVDHIVR NILAEKPRVT RFNIVWDNEN EGDLYPPEQP GV

2. entity 2

LAITMLKPRK KAKAL

Show sample condition

Sample #1

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

Sample #2

#	Name	Isotope labeling	Type	Concentration
3	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.15 mM
4	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.5 mM

Sample #3

#	Name	Isotope labeling	Type	Concentration
5	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.15 mM
6	Histone chaperone ASF1	[U-99% 13C; U-99% 15N; U-99% 2D]		0.5 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 6F0Y, Strand ID: A, B Detail

Release date

2017-12-17

Citation

Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation
Lercher, L., Danilenko, N., Kirkpatrick, J., Carlomagno, T.
Nucleic Acids Res. (2018), 46, 2279-2289, PubMed 29300933 , DOI 10.1093/nar/gkx1283 , Abstract

Related entities 1. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 1, : 1 : 28 entities Detail

Related entities 2. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 2, : 1 : 9 entities Detail

Interaction partners 2. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 2, : 12 interactors Detail

More details for 12 interactors identified by 3 citations

Experiments performed 13 experiments Detail

1 3D HNCO

Instrument

Bruker Avance III HD - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.5 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 3 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

2 3D HCCH-TOCSY

Instrument

Bruker Avance III HD - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

3 (HB)CB(CGCD)HD

Instrument

Bruker Avance III HD - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

4 3D 1H-15N NOESY

Instrument

Bruker Avance III HD - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

5 3D 1H-13C NOESY

Instrument

Bruker Avance III HD - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

6 3D 13C,15N filtered 1H-13C NOESY

Instrument

Bruker Avance III HD - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

7 2D 1H-15N HSQC

Instrument

Bruker Avance III HD - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.15 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 0.5 mM histone acetyltransferase Rtt109 C-terminus, 100% D2O

#	Name	Isotope labeling	Type	Concentration
3	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.15 mM
4	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.5 mM

8 2D 1H-15N HSQC

Instrument

Bruker Avance III HD - 600 MHz

Sample

State anisotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.5 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 3 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

9 2D 1H-15N HSQC

Instrument

Bruker Avance III HD - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

10 2D 1H-15N TROSY-HSQC

Instrument

Bruker Avance III HD - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

11 2D 1H-15N TROSY-HSQC

Instrument

Bruker Avance III HD - 600 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
1	Histone chaperone Asf1	[U-99% 13C; U-99% 15N]		0.5 mM
2	histone acetyltransferase Rtt109 C-terminus	natural abundance		3 mM

12 2D 1H-1H TOCSY

Instrument

Bruker Avance III HD - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.2, Details 0.5 mM [U-99% 13C; U-99% 15N; U-99% 2D] Histone chaperone ASF1, 0.15 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
5	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.15 mM
6	Histone chaperone ASF1	[U-99% 13C; U-99% 15N; U-99% 2D]		0.5 mM

13 2D 1H-1H NOESY

Instrument

Bruker Avance III HD - 850 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
5	histone acetyltransferase Rtt109 C-terminus	natural abundance		0.15 mM
6	Histone chaperone ASF1	[U-99% 13C; U-99% 15N; U-99% 2D]		0.5 mM

NMR combined restraints 7 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_34201_6f0y.nef
Input source #2: Coordindates	6f0y.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

-----------10--------20--------30--------40--------50--------60--------70--------80--------90-------
GAMGSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GAMGSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILL
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

100-------110-------120-------130-------140-------150-------160---------
SCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGV
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGV
-------110-------120-------130-------140-------150-------160-------170--

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

-420-----430---
LAITMLKPRKKAKAL
|||||||||||||||
LAITMLKPRKKAKAL
--------10-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	172	0	0	100.0
B	B	15	0	0	100.0

Content subtype: combined_34201_6f0y.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	2056		100.0 (chain: A, length: 172), 100.0 (chain: B, length: 15)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	102		100.0 (chain: B, length: 15)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	11149 (1)	noe	100.0 (chain: A, length: 172)
2	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	80 (1)	hbond	35.5 (chain: A, length: 172)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	270 (270)	.	90.1 (chain: A, length: 172)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_2	OK	61 (61)	.	35.5 (chain: A, length: 172)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 172, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 1130
  - ¹³C chemical shifts: 750
  - ¹⁵N chemical shifts: 176
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A
  - Chain_ID: B
Saveframe: assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 102
- Completeness of assignments
  - Entity_assemble_ID: B
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
30	CYS	HG	1.751
93	THR	HG1	5.183
99	CYS	HG	-0.179
111	TYR	HH	8.705
137	ARG	HH11	6.826
137	ARG	HH22	6.826

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1037	1022	98.6
¹³C chemical shifts	792	750	94.7
¹⁵N chemical shifts	181	176	97.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	341	335	98.2
¹³C chemical shifts	344	317	92.2
¹⁵N chemical shifts	159	154	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	696	687	98.7
¹³C chemical shifts	448	433	96.7
¹⁵N chemical shifts	22	22	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	105	105	100.0
¹³C chemical shifts	105	105	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	79	97.5
¹³C chemical shifts	79	72	91.1
¹⁵N chemical shifts	2	2	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	101	97.1
¹³C chemical shifts	76	0	0.0
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	29	27	93.1
¹³C chemical shifts	30	0	0.0
¹⁵N chemical shifts	14	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	75	74	98.7
¹³C chemical shifts	46	0	0.0
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0
¹³C chemical shifts	13	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	101	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	29	28	96.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	75	73	97.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 172, Sequence coverage: 100.0%
- Total number of restraints: 10919
- Weight of restraints: 1.0 (10919)
- Potential type of restraints: square-well-parabolic (10919)
- Range of distance target values: 1.23, 8.9 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_5
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 172, Sequence coverage: 35.5%
  - Total number of restraints: 80
  - Weight of restraints: 1.0 (80)
  - Potential type of restraints: square-well-parabolic (80)
  - Range of distance target values: 2.21, 3.62 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
      None
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 172, Sequence coverage: 90.1%
- Total number of restraints: 270
- Total number of restraints per polymer type: 270
- Weight of restraints: 1.0 (270)
- Potential type of restraints: square-well-parabolic (270)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 172, Sequence coverage: 35.5%
- Total number of restraints: 61
- Potential type of restraints: undefined (61)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue

Keywords acetyl transferase, histone chaperone, transferase

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.357 seconds)

BMRB: 34201

Sample #1

Sample #2

Sample #3

Sample #1

Sample #2

Sample #3

Related entities 1. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 1, : 1 : 28 entities Detail

Related entities 2. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 2, : 1 : 9 entities Detail

Interaction partners 2. Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (E.C.2.3.1.48), entity 2, : 12 interactors Detail

Experiments performed 13 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 7 contents Detail