BMRB Entry 18385

Name: Characterization of the chromoshadow domain-mediated binding of heterochromatin protein 1 alpha (HP1 alpha) to histone H3: Backbone 1H, 15N chemical shift assignments for histone H3 (1-59)
Published: 2012-05-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18385

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Characterization of the chromoshadow domain-mediated binding of heterochromatin protein 1 alpha (HP1 alpha) to histone H3: Backbone 1H, 15N chemical shift assignments for histone H3 (1-59)

Deposition date:

2012-04-10

Original release date:

2012-05-21

Authors:

Richart, Alexandria; Clair, Brunner; Katherine, Stott; Natalia, Murzina; Jean, Thomas

Citation:

Citation: Richart, Alexandria; Brunner, Clair; Stott, Katherine; Murzina, Natalia; Thomas, Jean. "Characterization of Chromoshadow Domain-mediated Binding of Heterochromatin Protein 1 (HP1) to Histone H3." J. Biol. Chem. 287, 18730-18737 (2012).
PubMed: 22493481

Assembly members:

Assembly members:
H3(1-59), polymer, 59 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX2TL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H3(1-59): ARTKQTARKSTGGKAPRKQL ATKAARKSAPATGGVKKPHR YRPGTVALREIRRYQKSTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	55
1H chemical shifts	55

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H3(1-59)	1

Entities:

Entity 1, H3(1-59) 59 residues - Formula weight is not available

1

ALA

ARG

THR

LYS

GLN

THR

ALA

ARG

LYS

SER

2

THR

GLY

LYS

ALA

PRO

ARG

LYS

GLN

LEU

3

ALA

THR

LYS

ALA

ARG

LYS

SER

ALA

PRO

4

ALA

THR

GLY

VAL

LYS

PRO

HIS

ARG

5

TYR

ARG

PRO

GLY

THR

VAL

ALA

LEU

ARG

GLU

6

ILE

ARG

TYR

GLN

LYS

SER

THR

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Related Database Links:

PDB	1AOI 1EQZ 1F66 1HQ3 1KX3 1KX4 1KX5 1S32 1TZY 1U35 1ZBB 1ZLA 2ARO 2CV5 2F8N 2FJ7 2HIO 2IO5 2NQB 2NZD 2PYO 3A6N 3AFA 3AV1 3AV2 3AYW 3AZE 3AZF 3AZG 3AZH 3AZI 3AZJ 3AZK 3AZL 3AZM 3AZN 3B6F 3B6G 3C1B 3C1C 3C9K 3KUY 3KXB 3LEL 3LJA 3LZ0 3LZ1 3MGP 3MGQ 3MGR 3MGS 3MNN 3MVD 3O62 3REH 3REI 3REJ 3REK 3REL 3TU4 3UT9 3UTA 3UTB 3W96 3W97 3W98 3W99 3WA9 3WAA 3WKJ 3WTP 3X1S 3X1T 3X1U 3X1V 4H9N 4H9O 4H9P 4H9Q 4H9R 4H9S 4HGA 4J8U 4J8V 4J8W 4J8X 4KGC 4LD9 4QLC 4R8P 4UUZ 4WU8 4WU9 5BS7 5BSA 5C3I
DBJ	BAA20144 BAA93621 BAA93622 BAA93623 BAA93624
EMBL	CAA24375 CAA24647 CAA24952 CAA25242 CAA25262
GB	AAA19824 AAA29441 AAA29965 AAA30003 AAA30026
PIR	A56580 A56618 A56654 I48113 I49397
PRF	0710252A 0806228A 1202289A 1920342A 2021267A
REF	NP_001005101 NP_001005464 NP_001013074 NP_001014411 NP_001016636
SP	P02299 P06352 P08898 P08903 P22843
TPG	DAA16173 DAA16175 DAA16178 DAA16187 DAA16190
AlphaFold	P02299 P06352 P08898 P08903 P22843

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

BMRB Entry 18385

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: