BMRB Entry 51773

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51773

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Title:
CTADC-H2AH2B complex
Deposition date:
2023-01-09
Original release date:
2023-06-30
Authors:
Ohtomo, Hideaki; Kurita, Junichi; Nishimura, Yoshifumi
Citation:

Citation: Ohtomo, Hideaki; Yamane, Tsutomu; Oda, Takashi; Kodera, Noriyuki; Kurita, Junichi; Tsunaka, Yasuo; Amyot, Romain; Ikeguchi, Mutsunori; Nishimura, Yoshifumi. "Dynamic solution structures of whole human NAP1 dimer bound to one and two histone H2A-H2B heterodimers obtained by integrative methods"  J. Mol. Biol. 435, 168189-168189 (2023).
PubMed: 37380014

Assembly members:

Assembly members:
entity_1, polymer, 25 residues, Formula weight is not available
entity_2, polymer, 134 residues, Formula weight is not available
entity_3, polymer, 130 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LGSEEEGDEENDPDYDPKKD QNPAE
entity_2: AGPGMSGRGKQGGKARAKAK TRSSRAGLQFPVGRVHRLLR KGNYSERVGAGAPVYLAAVL EYLTAEILELAGNAARDNKK TRIIPRHLQLAIRNDEELNK LLGRVTIAQGGVLPNIQAVL LPKKTESHHKAKGK
entity_3: AGPGMPEPAKSAPAPKKGSK KAVTKAQKKDGKKRKRSRKE SYSIYVYKVLKQVHPDTGIS SKAMGIMNSFVNDIFERIAG EASRLAHYNKRSTITSREIQ TAVRLLLPGELAKHAVSEGT KAVTKYTSAK

Data typeCount
15N chemical shifts243
1H chemical shifts243

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTADC1
2H2A2
3H2B3

Entities:

Entity 1, CTADC 25 residues - Formula weight is not available

1   LEUGLYSERGLUGLUGLUGLYASPGLUGLU
2   ASNASPPROASPTYRASPPROLYSLYSASP
3   GLNASNPROALAGLU

Entity 2, H2A 134 residues - Formula weight is not available

1   ALAGLYPROGLYMETSERGLYARGGLYLYS
2   GLNGLYGLYLYSALAARGALALYSALALYS
3   THRARGSERSERARGALAGLYLEUGLNPHE
4   PROVALGLYARGVALHISARGLEULEUARG
5   LYSGLYASNTYRSERGLUARGVALGLYALA
6   GLYALAPROVALTYRLEUALAALAVALLEU
7   GLUTYRLEUTHRALAGLUILELEUGLULEU
8   ALAGLYASNALAALAARGASPASNLYSLYS
9   THRARGILEILEPROARGHISLEUGLNLEU
10   ALAILEARGASNASPGLUGLULEUASNLYS
11   LEULEUGLYARGVALTHRILEALAGLNGLY
12   GLYVALLEUPROASNILEGLNALAVALLEU
13   LEUPROLYSLYSTHRGLUSERHISHISLYS
14   ALALYSGLYLYS

Entity 3, H2B 130 residues - Formula weight is not available

1   ALAGLYPROGLYMETPROGLUPROALALYS
2   SERALAPROALAPROLYSLYSGLYSERLYS
3   LYSALAVALTHRLYSALAGLNLYSLYSASP
4   GLYLYSLYSARGLYSARGSERARGLYSGLU
5   SERTYRSERILETYRVALTYRLYSVALLEU
6   LYSGLNVALHISPROASPTHRGLYILESER
7   SERLYSALAMETGLYILEMETASNSERPHE
8   VALASNASPILEPHEGLUARGILEALAGLY
9   GLUALASERARGLEUALAHISTYRASNLYS
10   ARGSERTHRILETHRSERARGGLUILEGLN
11   THRALAVALARGLEULEULEUPROGLYGLU
12   LEUALALYSHISALAVALSERGLUGLYTHR
13   LYSALAVALTHRLYSTYRTHRSERALALYS

Samples:

sample_1: CTADC of NAP1, [U-98% 15N], 475 uM; H2A 475 uM; H2B 475 uM

sample_2: CTADC of NAP1 475 uM; H2A, [U-98% 15N], 475 uM; H2B, [U-98% 15N], 475 uM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1

Software:

Olivia - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 950 MHz

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