BMRB Entry 52244

Name: H2A and H2B chemical shifts in the Xenopus H2A/H2B heterodimer
Published: 2024-03-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52244

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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:

H2A and H2B chemical shifts in the Xenopus H2A/H2B heterodimer

Deposition date:

2023-12-14

Original release date:

2024-03-18

Authors:

Lorton, Benjamin; Warren, Christopher; Ilyas, Humaira; Cahill, Sean; Cowburn, David; Shechter, David

Citation:

Citation: Lorton, Benjamin; Warren, Christopher; Ilyas, Humaira; Nandigrami, Prithviraj; Hegde, Subray; Cahill, Sean; Lehman, Stephanie; Shabanowitz, Jeffrey; Hunt, Donald; Fiser, Andras; Cowburn, David; Shechter, David. "Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA mimicry and histone chaperone efficiency" iScience ., .-. (2024).
PubMed: 37790377

Assembly members:

Assembly members:
entity_1, polymer, 129 residues, 13950 Da.
entity_2, polymer, 125 residues, 13817 Da.

Natural source:

Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-histone expression plasmid

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGRGKQGGKTRAKAKTRSSR AGLQFPVGRVHRLLRKGNYA ERVGAGAPVYLAAVLEYLTA EILELAGNAARDNKKTRIIP RHLQLAVRNDEELNKLLGRV TIAQGGVLPNIQSVLLPKKT ESSKSAKSK
entity_2: PEPAKSAPAPKKGSKKAVTK TQKKDGKKRRKTRKESYAIY VYKVLKQVHPDTGISSKAMS IMNSFVNDVFERIAGEASRL AHYNKRSTITSREIQTAVRL LLPGELAKHAVSEGTKAVTK YTSAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	580
15N chemical shifts	186
1H chemical shifts	186

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H2A	1
2	H2B	2

Entities:

Entity 1, H2A 129 residues - 13950 Da.

Uniprot accesion number for H2A used in this study: P06897

1

SER

GLY

ARG

GLY

LYS

GLN

GLY

LYS

THR

2

ARG

ALA

LYS

ALA

LYS

THR

ARG

SER

ARG

3

ALA

GLY

LEU

GLN

PHE

PRO

VAL

GLY

ARG

VAL

4

HIS

ARG

LEU

ARG

LYS

GLY

ASN

TYR

ALA

5

GLU

ARG

VAL

GLY

ALA

GLY

ALA

PRO

VAL

TYR

6

LEU

ALA

VAL

LEU

GLU

TYR

LEU

THR

ALA

7

GLU

ILE

LEU

GLU

LEU

ALA

GLY

ASN

ALA

8

ARG

ASP

ASN

LYS

THR

ARG

ILE

PRO

9

ARG

HIS

LEU

GLN

LEU

ALA

VAL

ARG

ASN

ASP

10

GLU

LEU

ASN

LYS

LEU

GLY

ARG

VAL

11

THR

ILE

ALA

GLN

GLY

VAL

LEU

PRO

ASN

12

ILE

GLN

SER

VAL

LEU

PRO

LYS

THR

13

GLU

SER

LYS

SER

ALA

LYS

SER

LYS

Entity 2, H2B 125 residues - 13817 Da.

Uniprot accesion number for H2B used in this study: P02281

1

PRO

GLU

PRO

ALA

LYS

SER

ALA

PRO

ALA

PRO

2

LYS

GLY

SER

LYS

ALA

VAL

THR

LYS

3

THR

GLN

LYS

ASP

GLY

LYS

ARG

4

LYS

THR

ARG

LYS

GLU

SER

TYR

ALA

ILE

TYR

5

VAL

TYR

LYS

VAL

LEU

LYS

GLN

VAL

HIS

PRO

6

ASP

THR

GLY

ILE

SER

LYS

ALA

MET

SER

7

ILE

MET

ASN

SER

PHE

VAL

ASN

ASP

VAL

PHE

8

GLU

ARG

ILE

ALA

GLY

GLU

ALA

SER

ARG

LEU

9

ALA

HIS

TYR

ASN

LYS

ARG

SER

THR

ILE

THR

10

SER

ARG

GLU

ILE

GLN

THR

ALA

VAL

ARG

LEU

11

LEU

PRO

GLY

GLU

LEU

ALA

LYS

HIS

ALA

12

VAL

SER

GLU

GLY

THR

LYS

ALA

VAL

THR

LYS

13

TYR

THR

SER

ALA

LYS

Samples:

sample_1: H2A of the Xenopus H2A/H2B heterodimer, [U-100% 13C; U-100% 15N; U-80% 2H], 0.6 mM; H2B of the Xenopus H2A/H2B heterodimer 0.6 mM; Na2PO4 25 mM; NaCl 150 mM; EDTA 1 mM; TSP 0.05 mM

sample_2: H2A of the Xenopus H2A/H2B heterodimer 0.6 mM; H2B of the Xenopus H2A/H2B heterodimer, [U-100% 13C; U-100% 15N; U-80% 2H], 0.6 mM; Na2PO4 25 mM; NaCl 150 mM; EDTA 1 mM; TSP 0.05 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN vv 3.6 - collection

NMRPipe - processing

CcpNMR v2.4 - chemical shift assignment

NMRbox - data analysis

PINE - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 700 MHz
Bruker AVANCE III HD 800 MHz