BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34201

Title: Rtt109 peptide bound to Asf1   PubMed: 29300933

Deposition date: 2017-11-21 Original release date: 2017-12-21

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

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts750
15N chemical shifts176
1H chemical shifts1494

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 172 residues - 19327.652 Da.

1   GLYALAMETGLYSERILEVALSERLEULEU
2   GLYILELYSVALLEUASNASNPROALALYS
3   PHETHRASPPROTYRGLUPHEGLUILETHR
4   PHEGLUCYSLEUGLUSERLEULYSHISASP
5   LEUGLUTRPLYSLEUTHRTYRVALGLYSER
6   SERARGSERLEUASPHISASPGLNGLULEU
7   ASPSERILELEUVALGLYPROVALPROVAL
8   GLYVALASNLYSPHEVALPHESERALAASP
9   PROPROSERALAGLULEUILEPROALASER
10   GLULEUVALSERVALTHRVALILELEULEU
11   SERCYSSERTYRASPGLYARGGLUPHEVAL
12   ARGVALGLYTYRTYRVALASNASNGLUTYR
13   ASPGLUGLUGLULEUARGGLUASNPROPRO
14   ALALYSVALGLNVALASPHISILEVALARG
15   ASNILELEUALAGLULYSPROARGVALTHR
16   ARGPHEASNILEVALTRPASPASNGLUASN
17   GLUGLYASPLEUTYRPROPROGLUGLNPRO
18   GLYVAL

Entity 2, entity_2 15 residues - 1687.207 Da.

1   LEUALAILETHRMETLEULYSPROARGLYS
2   LYSALALYSALALEU

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:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 13C,15N filtered 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_1anisotropicsample_conditions_2
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts