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 11609

Title: Solution structure of the isolated histone H2A-H2B heterodimer   PubMed: 27181506

Authors: Moriwaki, Yoshihito; Yamane, Tsutomu; Ohtomo, Hideaki; Ikeguchi, Mitsunori; Kurita, Jun-ichi; Sato, Masahiko; Nagadoi, Aritaka; Shimojo, Hideaki; Nishimura, Yoshifumi

Citation: Moriwaki, Yoshihito; Yamane, Tsutomu; Ohtomo, Hideaki; Ikeguchi, Mitsunori; Kurita, Jun-ichi; Sato, Masahiko; Nagadoi, Aritaka; Shimojo, Hideaki; Nishimura, Yoshifumi. "Solution structure of the isolated histone H2A-H2B heterodimer"  Sci. Rep. 6, 24999-24999 (2016).

Assembly members:
entity_1, polymer, 133 residues, 14376.907 Da.
entity_2, polymer, 129 residues, 14146.588 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: GPGMSGRGKQGGKARAKAKT RSSRAGLQFPVGRVHRLLRK GNYSERVGAGAPVYLAAVLE YLTAEILELAGNAARDNKKT RIIPRHLQLAIRNDEELNKL LGRVTIAQGGVLPNIQAVLL PKKTESHHKAKGK
entity_2: GPGMPEPAKSAPAPKKGSKK AVTKAQKKDGKKRKRSRKES YSIYVYKVLKQVHPDTGISS KAMGIMNSFVNDIFERIAGE ASRLAHYNKRSTITSREIQT AVRLLLPGELAKHAVSEGTK AVTKYTSAK

Data sets:
Data typeCount
13C chemical shifts736
15N chemical shifts242
1H chemical shifts243

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_1 133 residues - 14376.907 Da.

1   GLYPROGLYMETSERGLYARGGLYLYSGLN
2   GLYGLYLYSALAARGALALYSALALYSTHR
3   ARGSERSERARGALAGLYLEUGLNPHEPRO
4   VALGLYARGVALHISARGLEULEUARGLYS
5   GLYASNTYRSERGLUARGVALGLYALAGLY
6   ALAPROVALTYRLEUALAALAVALLEUGLU
7   TYRLEUTHRALAGLUILELEUGLULEUALA
8   GLYASNALAALAARGASPASNLYSLYSTHR
9   ARGILEILEPROARGHISLEUGLNLEUALA
10   ILEARGASNASPGLUGLULEUASNLYSLEU
11   LEUGLYARGVALTHRILEALAGLNGLYGLY
12   VALLEUPROASNILEGLNALAVALLEULEU
13   PROLYSLYSTHRGLUSERHISHISLYSALA
14   LYSGLYLYS

Entity 2, entity_2 129 residues - 14146.588 Da.

1   GLYPROGLYMETPROGLUPROALALYSSER
2   ALAPROALAPROLYSLYSGLYSERLYSLYS
3   ALAVALTHRLYSALAGLNLYSLYSASPGLY
4   LYSLYSARGLYSARGSERARGLYSGLUSER
5   TYRSERILETYRVALTYRLYSVALLEULYS
6   GLNVALHISPROASPTHRGLYILESERSER
7   LYSALAMETGLYILEMETASNSERPHEVAL
8   ASNASPILEPHEGLUARGILEALAGLYGLU
9   ALASERARGLEUALAHISTYRASNLYSARG
10   SERTHRILETHRSERARGGLUILEGLNTHR
11   ALAVALARGLEULEULEUPROGLYGLULEU
12   ALALYSHISALAVALSERGLUGLYTHRLYS
13   ALAVALTHRLYSTYRTHRSERALALYS

Samples:

sample_1: entity_1, [U-13C; U-15N; U-2H], 0.1 – 0.3 mM; entity_2, [U-13C; U-15N; U-2H], 0.1 – 0.3 mM; MES 25 mM; KCl 400 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 400 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
TROSY-HNCACBsample_1isotropicsample_conditions_1
TROSY-HN(CA)COsample_1isotropicsample_conditions_1
TROSY-HNCOsample_1isotropicsample_conditions_1
HCCCONHsample_1isotropicsample_conditions_1
TROSY-1H-15N HSQCsample_1isotropicsample_conditions_1
TROSY-1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links: