BMRB Entry 11605

Title:
Solution structure of the chromodomain of HP1alpha with the phosphorylated N-terminal tail
Deposition date:
2015-12-18
Original release date:
2021-07-16
Authors:
Kawaguchi, Ayumi; Nishimura, Yoshifumi
Citation:

Citation: Shimojo, Hideaki; Kawaguchi, Ayumi; Oda, Takashi; Hashiguchi, Nobuto; Omori, Satoshi; Moritsugu, Kei; Kidera, Akinori; Hiragami-Hamada, Kyoko; Nakayama, Jun-Ichi; Sato, Mamoru; Nishimura, Yoshifumi. "Extended string-like binding of the phosphorylated HP1? N-terminal tail to the lysine 9-methylated histone H3 tail"  Sci. Rep. 6, 22527-22527 (2016).
PubMed: 26934956

Assembly members:

Assembly members:
entity, polymer, 83 residues, 10169.125 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts374
15N chemical shifts88
1H chemical shifts570

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 83 residues - 10169.125 Da.

1   GLYSERHISMETGLYLYSLYSTHRLYSARG
2   THRALAASPSEPSEPSEPSEPGLUASPGLU
3   GLUGLUTYRVALVALGLULYSVALLEUASP
4   ARGARGMETVALLYSGLYGLNVALGLUTYR
5   LEULEULYSTRPLYSGLYPHESERGLUGLU
6   HISASNTHRTRPGLUPROGLULYSASNLEU
7   ASPCYSPROGLULEUILESERGLUPHEMET
8   LYSLYSTYRLYSLYSMETLYSGLUGLYGLU
9   ASNASNLYS

Samples:

sample_1: HP1alpha, [U-99% 13C; U-99% 15N], mM; potassium phosphate 20 mM; sodium chloride 10 mM; DTT 5 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: HP1alpha, [U-99% 13C; U-99% 15N], mM; potassium phosphate 20 mM; sodium chloride 10 mM; DTT 5 mM; D2O, [U-2H], 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Olivia, Yokochi, M., Sekiguchi, S. and Inagaki, F. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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