BMRB Entry 27538

Name: Chemical Shift Assignments for the triphosphorylated C-terminal domain of histone H1.0
Published: 2018-11-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27538

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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:

Chemical Shift Assignments for the triphosphorylated C-terminal domain of histone H1.0

Deposition date:

2018-07-06

Original release date:

2018-11-16

Authors:

Jimenez, M. Angeles; Pantoja-Uceda, David; Chaves-Arquero, Belen

Citation:

Citation: Chaves-Arquero, Belen; Pantoja-Uceda, David; Roque, Alicia; Ponte, Inmaculada; Suau, Pedro; Jimenez, M. Angeles. "A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study" J. Biomol. NMR 72, 139-148 (2018).
PubMed: 30414042

Assembly members:

Assembly members:
pT-C-H1.0, polymer, 105 residues, Formula weight is not available

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: pCTH1.0

Entity Sequences (FASTA):

Entity Sequences (FASTA):
pT-C-H1.0: MDEPKRSVAFKKTKKEVKKV AXPKKAAKPKKAASKAPSKK PKAXPVKKAKKKPAAXPKKA KKPKVVKVKPVKASKPKKAK TVKPKAKSSAKRASKKKRSH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1

Data type	Count
13C chemical shifts	288
15N chemical shifts	98
1H chemical shifts	56
heteronuclear NOE values	56

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pT-C-H1.0	1

Entities:

Entity 1, pT-C-H1.0 105 residues - Formula weight is not available

Residues 2-97 correspond to residues 98-193 of histone H1.0 from mouse. Residues 98-105 are the cloning-tag. Thr residues at positions 22, 44 and 56 are phosphorylated.

1

MET

ASP

GLU

PRO

LYS

ARG

SER

VAL

ALA

PHE

2

LYS

THR

LYS

GLU

VAL

LYS

VAL

3

ALA

TPO

PRO

LYS

ALA

LYS

PRO

LYS

4

LYS

ALA

SER

LYS

ALA

PRO

SER

LYS

5

PRO

LYS

ALA

TPO

PRO

VAL

LYS

ALA

LYS

6

LYS

PRO

ALA

TPO

PRO

LYS

ALA

7

LYS

PRO

LYS

VAL

LYS

VAL

LYS

PRO

8

VAL

LYS

ALA

SER

LYS

PRO

LYS

ALA

LYS

9

THR

VAL

LYS

PRO

LYS

ALA

LYS

SER

ALA

10

LYS

ARG

ALA

SER

LYS

ARG

SER

HIS

11

HIS

Samples:

sample_1: pT-C-H1.0, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: pT-C-H1.0, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 10 mM; sodium chloride 10 mM

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1
3D hacacoNcaNCO	sample_1	isotropic	sample_conditions_1
3D hacaCOncaNCO	sample_1	isotropic	sample_conditions_1
3D CBCANCO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N-HETNOE	sample_2	isotropic	sample_conditions_1
3D HncacoNH	sample_2	isotropic	sample_conditions_1
3D hNcacoNH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

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