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 50438

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50438

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Title: H2A and H2B tails in nucleosome   PubMed: 34153285

Deposition date: 2020-08-17 Original release date: 2021-06-30

Authors: Ohtomo, Hideaki; Kurita, Jun-ichi; Nishimura, Yoshifumi

Citation: Ohtomo, Hideaki; Kurita, Jun-Ichi; Sakuraba, Shun; Li, Zhenhai; Arimura, Yasuhiro; Wakamori, Masatoshi; Tsunaka, Yasuo; Umehara, Takashi; Kurumizaka, Hitoshi; Kono, Hidetoshi; Nishimura, Yoshifumi. "The N-terminal tails of histones H2A and H2B adopt two distinct conformations in the nucleosome with contact and reduced contact to DNA."  J. Mol. Biol. 433, 167110-167110 (2021).

Assembly members:
entity_1, polymer, 133 residues, Formula weight is not available
entity_2, polymer, 129 residues, Formula weight is not available

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   Vector: pET23b

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 shifts144
15N chemical shifts894
1H chemical shifts894
H exchange rates196
T1 relaxation values420
T2 relaxation values422
heteronuclear NOE values419

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H2A1
2H2B2

Entities:

Entity 1, H2A 133 residues - Formula weight is not available

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, H2B 129 residues - Formula weight is not available

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: H2A, [U-100% 13C; U-100% 15N; U-80% 2H], 0.16 mM; H2B, [U-100% 13C; U-100% 15N; U-80% 2H], 0.16 mM; H3 0.16 mM; H4 0.16 mM; 145 bp DNA 0.08 mM

sample_2: H2A, [U-100% 13C; U-100% 15N; U-80% 2H], 0.2 mM; H2B, [U-100% 13C; U-100% 15N; U-80% 2H], 0.2 mM; H3 0.2 mM; H4 0.2 mM; 193 bp DNA 0.1 mM

sample_conditions_1: ionic strength: 0.4 M; pH: 6; pressure: 1 atm; temperature: 293 K

sample_conditions_2: ionic strength: 0.2 M; pH: 6; pressure: 1 atm; temperature: 293 K

sample_conditions_3: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 293 K

sample_conditions_4: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 293 K

sample_conditions_5: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 278 K

sample_conditions_6: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 283 K

sample_conditions_7: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 288 K

sample_conditions_8: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 298 K

sample_conditions_9: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 303 K

sample_conditions_10: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 308 K

sample_conditions_11: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 313 K

sample_conditions_12: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 318 K

sample_conditions_13: ionic strength: 0.025 M; pH: 6; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_2
2D 1H-15N TROSYsample_1isotropicsample_conditions_3
2D 1H-15N TROSYsample_1isotropicsample_conditions_4
2D 1H-15N TROSYsample_2isotropicsample_conditions_4
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_5
2D 1H-15Nsample_2isotropicsample_conditions_6
2D 1H-15Nsample_2isotropicsample_conditions_7
2D 1H-15Nsample_2isotropicsample_conditions_4
2D 1H-15Nsample_2isotropicsample_conditions_8
2D 1H-15Nsample_2isotropicsample_conditions_9
2D 1H-15Nsample_2isotropicsample_conditions_10
2D 1H-15Nsample_2isotropicsample_conditions_11
2D 1H-15Nsample_2isotropicsample_conditions_12
2D 1H-15Nsample_2isotropicsample_conditions_13
T1/R1 relaxationsample_2isotropicsample_conditions_4
T1/R1 relaxationsample_2isotropicsample_conditions_4
T1/R1 relaxationsample_2isotropicsample_conditions_1
T1/R1 relaxationsample_2isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_4
T1/R1 relaxationsample_1isotropicsample_conditions_4
T1/R1 relaxationsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_2isotropicsample_conditions_4
T2/R2 relaxationsample_2isotropicsample_conditions_4
T2/R2 relaxationsample_2isotropicsample_conditions_1
T2/R2 relaxationsample_2isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_4
T2/R2 relaxationsample_1isotropicsample_conditions_4
T2/R2 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_4
1H-15N heteronoesample_2isotropicsample_conditions_4
1H-15N heteronoesample_2isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_4
1H-15N heteronoesample_1isotropicsample_conditions_4
1H-15N heteronoesample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
HETex-BEST-TROSYsample_2isotropicsample_conditions_4
HETex-BEST-TROSYsample_2isotropicsample_conditions_1
HETex-BEST-TROSYsample_1isotropicsample_conditions_4
HETex-BEST-TROSYsample_1isotropicsample_conditions_1

Software:

Olivia - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 950 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 700 MHz

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