BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 51512

Title: Backbone 1H, 13C, and 15N chemical shift assignments for the chromoshadow domain (residue 112-176) of human heterochromatin protein 1a (HP1a).   PubMed: 36537242

Deposition date: 2022-07-08 Original release date: 2023-06-30

Authors: Her, Cheenou; Debelouchina, Galia

Citation: Her, Cheenou; Phan, Tien; Jovic, Nina; Kapoor, Utkarsh; Ackermann, Bryce; Rizuan, Azamat; Kim, Young; Mittal, Jeetain; Debelouchina, Galia. "Molecular interactions underlying the phase separation of HP1a: role of phosphorylation, ligand and nucleic acid binding"  Nucleic Acids Res. 50, 12702-12722 (2022).

Assembly members:
entity_1, polymer, 66 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: pET (2B-T)

Entity Sequences (FASTA):
entity_1: SDIARGFERGLEPEKIIGAT DSCGDLMFLMKWKDTDEADL VLAKEANVKCPQIVIAFYEE RLTWHA

Data sets:
Data typeCount
13C chemical shifts126
15N chemical shifts62
1H chemical shifts62

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HP1a-CSD1

Entities:

Entity 1, HP1a-CSD 66 residues - Formula weight is not available

1   SERASPILEALAARGGLYPHEGLUARGGLY
2   LEUGLUPROGLULYSILEILEGLYALATHR
3   ASPSERCYSGLYASPLEUMETPHELEUMET
4   LYSTRPLYSASPTHRASPGLUALAASPLEU
5   VALLEUALALYSGLUALAASNVALLYSCYS
6   PROGLNILEVALILEALAPHETYRGLUGLU
7   ARGLEUTHRTRPHISALA

Samples:

sample_1: potassium chloride 75 mM; TCEP 1 mM; HEPES 20 mM; sodium azide 0.05%; Chromoshadow domain of human heterochromatin protein 1a (HP1a), [U-99% 13C; U-99% 15N], 400 uM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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