BMRB Entry 34201

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

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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

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