BMRB Entry 28060

Name: HP1
Published: 2020-01-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28060

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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:

HP1

Deposition date:

2020-01-03

Original release date:

2020-01-21

Authors:

Leighton, Gage; Williams, David

Citation:

Citation: Krone, Mackenzie; Albanese, Katherine; Leighton, Gage; He, Cyndi Qixin; Lee, Ga Young; Garcia-Borras, Marc; Guseman, Alex; Williams, David; Houk, K.; Brustad, Eric; Waters, Marcey. "Thermodynamic consequences of Tyr to Trp mutations in the cation-pai-mediated binding of trimethyllysine by the HP1 chromodomain" Chem. Sci. 11, 3495-3500 (2020).
PubMed: 34109021

Assembly members:

Assembly members:
HP1, polymer, 69 residues, Formula weight is not available

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HP1: MKKHHHHHHAEEEEEEYAVE KIIDRRVRKGMVEYYLKWKG YPETENTWEPENNLDCQDLI QQYEASRKD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	187
15N chemical shifts	61
1H chemical shifts	61

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HP1	1

Entities:

Entity 1, HP1 69 residues - Formula weight is not available

1

MET

LYS

HIS

ALA

2

GLU

TYR

ALA

VAL

GLU

3

LYS

ILE

ASP

ARG

VAL

ARG

LYS

GLY

4

MET

VAL

GLU

TYR

LEU

LYS

TRP

LYS

GLY

5

TYR

PRO

GLU

THR

GLU

ASN

THR

TRP

GLU

PRO

6

GLU

ASN

LEU

ASP

CYS

GLN

ASP

LEU

ILE

7

GLN

TYR

GLU

ALA

SER

ARG

LYS

ASP

Samples:

sample_1: HP1, [U-100% 13C; U-100% 15N], 250 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 40 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

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

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

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