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 30275

Title: Solution NMR structure of histone H2A-H2B mono-ubiquitylated at H2A Lys15 in complex with RNF169 (653-708)

Authors: Hu, Q.; Botuyan, M.; Cui, G.; Mer, G.

Citation: Hu, Q.; Botuyan, M.; Cui, G.; Zhao, D.; Mer, G.. "Mechanisms of ubiquitin-nucleosome recognition and regulation of 53BP1 chromatin recruitment by RNF168/169 and RAD18"  . ., .-..

Assembly members:
entity_1, polymer, 194 residues, 21658.943 Da.
entity_2, polymer, 76 residues, 8576.831 Da.
entity_3, polymer, 59 residues, 7016.938 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity_1: MHHHHHHMRKESYSIYVYKV LKQVHPDTGISSKAMGIMNS FVNDIFERIAGEASRLAHYN KRSTITSREIQTAVRLLLPG ELAKHAVSEGTKAVTKYTSS ASAKTRSSRAGLQFPVGRVH RLLRKGNYSERVGAGAPVYL AAVLEYLTAEILELAGNAAR DNKKTRIIPRHLQLAIRNDE ELNKLLGRVTIAQG
entity_2: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
entity_3: GHMDPVLREMEQKLQQEEED RQLALQLQRMFDNERRTVSR RKGSVDQYLLRSSNMAGAK

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts1268
15N chemical shifts319
1H chemical shifts2144

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_33

Entities:

Entity 1, entity_1 194 residues - 21658.943 Da.

1   METHISHISHISHISHISHISMETARGLYS
2   GLUSERTYRSERILETYRVALTYRLYSVAL
3   LEULYSGLNVALHISPROASPTHRGLYILE
4   SERSERLYSALAMETGLYILEMETASNSER
5   PHEVALASNASPILEPHEGLUARGILEALA
6   GLYGLUALASERARGLEUALAHISTYRASN
7   LYSARGSERTHRILETHRSERARGGLUILE
8   GLNTHRALAVALARGLEULEULEUPROGLY
9   GLULEUALALYSHISALAVALSERGLUGLY
10   THRLYSALAVALTHRLYSTYRTHRSERSER
11   ALASERALALYSTHRARGSERSERARGALA
12   GLYLEUGLNPHEPROVALGLYARGVALHIS
13   ARGLEULEUARGLYSGLYASNTYRSERGLU
14   ARGVALGLYALAGLYALAPROVALTYRLEU
15   ALAALAVALLEUGLUTYRLEUTHRALAGLU
16   ILELEUGLULEUALAGLYASNALAALAARG
17   ASPASNLYSLYSTHRARGILEILEPROARG
18   HISLEUGLNLEUALAILEARGASNASPGLU
19   GLULEUASNLYSLEULEUGLYARGVALTHR
20   ILEALAGLNGLY

Entity 2, entity_2 76 residues - 8576.831 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Entity 3, entity_3 59 residues - 7016.938 Da.

1   GLYHISMETASPPROVALLEUARGGLUMET
2   GLUGLNLYSLEUGLNGLNGLUGLUGLUASP
3   ARGGLNLEUALALEUGLNLEUGLNARGMET
4   PHEASPASNGLUARGARGTHRVALSERARG
5   ARGLYSGLYSERVALASPGLNTYRLEULEU
6   ARGSERSERASNMETALAGLYALALYS

Samples:

sample_1: EDTA 4 mM; KCl 50 mM; MES-Bis-TRIS 25 mM; RNF169 3 mM; Ubiquitylated H2A-H2B 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
ALL_Experimentssample_1isotropicsample_conditions_1

Software:

NMRDRAW - structure solution

NMRPIPE - structure solution

NMRVIEW - structure solution

SPARKY - structure solution

TALOS - structure solution

TOPSPIN - structure solution

X-PLOR NIH, SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links: