BMRB Entry 34201

Name: Rtt109 peptide bound to Asf1
Published: 2017-12-21

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PDB ID: 6f0y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34201
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Rtt109 peptide bound to Asf1

Deposition date:

2017-11-21

Original release date:

2017-12-21

Authors:

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

Citation:

Citation: Lercher, Lukas; Danilenko, Nataliya; Kirkpatrick, John; Carlomagno, Teresa. "Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation" Nucleic Acids Res. 46, 2279-2289 (2018).
PubMed: 29300933

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, 19327.652 Da.
entity_2, polymer, 15 residues, 1687.207 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGSIVSLLGIKVLNNPAK FTDPYEFEITFECLESLKHD LEWKLTYVGSSRSLDHDQEL DSILVGPVPVGVNKFVFSAD PPSAELIPASELVSVTVILL SCSYDGREFVRVGYYVNNEY DEEELRENPPAKVQVDHIVR NILAEKPRVTRFNIVWDNEN EGDLYPPEQPGV
entity_2: LAITMLKPRKKAKAL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	750
15N chemical shifts	176
1H chemical shifts	1494

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_1 172 residues - 19327.652 Da.

1

GLY

ALA

MET

GLY

SER

ILE

VAL

SER

LEU

2

GLY

ILE

LYS

VAL

LEU

ASN

PRO

ALA

LYS

3

PHE

THR

ASP

PRO

TYR

GLU

PHE

GLU

ILE

THR

4

PHE

GLU

CYS

LEU

GLU

SER

LEU

LYS

HIS

ASP

5

LEU

GLU

TRP

LYS

LEU

THR

TYR

VAL

GLY

SER

6

SER

ARG

SER

LEU

ASP

HIS

ASP

GLN

GLU

LEU

7

ASP

SER

ILE

LEU

VAL

GLY

PRO

VAL

PRO

VAL

8

GLY

VAL

ASN

LYS

PHE

VAL

PHE

SER

ALA

ASP

9

PRO

SER

ALA

GLU

LEU

ILE

PRO

ALA

SER

10

GLU

LEU

VAL

SER

VAL

THR

VAL

ILE

LEU

11

SER

CYS

SER

TYR

ASP

GLY

ARG

GLU

PHE

VAL

12

ARG

VAL

GLY

TYR

VAL

ASN

GLU

TYR

13

ASP

GLU

LEU

ARG

GLU

ASN

PRO

14

ALA

LYS

VAL

GLN

VAL

ASP

HIS

ILE

VAL

ARG

15

ASN

ILE

LEU

ALA

GLU

LYS

PRO

ARG

VAL

THR

16

ARG

PHE

ASN

ILE

VAL

TRP

ASP

ASN

GLU

ASN

17

GLU

GLY

ASP

LEU

TYR

PRO

GLU

GLN

PRO

18

GLY

VAL

Entity 2, entity_2 15 residues - 1687.207 Da.

1

LEU

ALA

ILE

THR

MET

LEU

LYS

PRO

ARG

LYS

2

LYS

ALA

LYS

ALA

LEU

Samples:

sample_1: Histone chaperone Asf1, [U-99% 13C; U-99% 15N], 0.5 mM; histone acetyltransferase Rtt109 C-terminus 3 mM

sample_2: Histone chaperone Asf1, [U-99% 13C; U-99% 15N], 0.15 mM; histone acetyltransferase Rtt109 C-terminus 0.5 mM

sample_3: histone acetyltransferase Rtt109 C-terminus 0.15 mM; Histone chaperone ASF1, [U-99% 13C; U-99% 15N; U-99% 2D], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
(HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 13C,15N filtered 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY-HSQC	sample_1	anisotropic	sample_conditions_2
2D 1H-15N TROSY-HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

CNS v1.21, Brunger, Adams, Clore, Delano, Gros, Grosse-Kunstleve, Jiang, Kuszewski, Nilges, Pannu, Read, Rice, Simonson, Warren - structure calculation

ARIA v2.3, W. Rieping, M. Habeck, B. Bardiaux, A. Bernard, T.E. Malliavin, M. Nilges - structure calculation

PALES, M. Zweckstetter - data analysis

TALOS-N, Y. Shen, A. Bax - data analysis

NMR spectrometers:

Bruker Avance III HD 850 MHz
Bruker Avance III HD 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks