BMRB Entry 27700

Name: Human linker histone NGH1x in low ionic strength conditions
Published: 2019-01-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27700

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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:

Human linker histone NGH1x in low ionic strength conditions

Deposition date:

2018-11-21

Original release date:

2019-01-02

Authors:

De Wit, Herna; Vallet, Alicia; Brutscher, Bernhard; Koorsen, Gerrit

Citation:

Citation: De Wit, Herna; Vallet, Alicia; Brutscher, Bernhard; Koorsen, Gerrit; De Wit, Herna; Vallet, Alicia; Brutscher, Bernhard; Koorsen, Gerrit. "NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate" Biomol. NMR Assign. 13, 249-254 (2019).
PubMed: 30868366

Assembly members:

Assembly members:
NGH1x_no_salt, polymer, 119 residues, 13101.1949 Da.

Natural source:

Natural source: Common Name: NGH1x Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NGH1x_no_salt: MSVELEEALPVTTAEGMAKK VTKAGGSAALSPSKKRKNSK KKNQPGKYSQLVVETIRRLG ERNGSSLAKIYTEAKKVPWF DQQNGRTYLKYSIKALVQND TLLQVKGTGANGSFKLNRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	307
15N chemical shifts	107
1H chemical shifts	107

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NGH1x no salt	1

Entities:

Entity 1, NGH1x no salt 119 residues - 13101.1949 Da.

1

MET

SER

VAL

GLU

LEU

GLU

ALA

LEU

PRO

2

VAL

THR

ALA

GLU

GLY

MET

ALA

LYS

3

VAL

THR

LYS

ALA

GLY

SER

ALA

LEU

4

SER

PRO

SER

LYS

ARG

LYS

ASN

SER

LYS

5

LYS

ASN

GLN

PRO

GLY

LYS

TYR

SER

GLN

6

LEU

VAL

GLU

THR

ILE

ARG

LEU

GLY

7

GLU

ARG

ASN

GLY

SER

LEU

ALA

LYS

ILE

8

TYR

THR

GLU

ALA

LYS

VAL

PRO

TRP

PHE

9

ASP

GLN

ASN

GLY

ARG

THR

TYR

LEU

LYS

10

TYR

SER

ILE

LYS

ALA

LEU

VAL

GLN

ASN

ASP

11

THR

LEU

GLN

VAL

LYS

GLY

THR

GLY

ALA

12

ASN

GLY

SER

PHE

LYS

LEU

ASN

ARG

LYS

Samples:

NGH1x_low_ionic_strength: NGH1x_no_salt, [U-99% 13C; U-99% 15N], 0.5 mM

CondSet1: ionic strength: 20 mM; pH: 7.000; temperature: 278.000 K

CondSet4: pH: 7.0; temperature: 278 K

CondSet13: pH: 7.0; temperature: 278 K

CondSet14: pH: 7.0; temperature: 278 K

CondSet15: pH: 7.0; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	NGH1x_low_ionic_strength	isotropic	CondSet1
3D HNCO	NGH1x_low_ionic_strength	isotropic	CondSet4
3D HNCACB	NGH1x_low_ionic_strength	isotropic	CondSet13
HNCOCACB (H[N[co[{CA\|ca[C]}]]])	NGH1x_low_ionic_strength	isotropic	CondSet14
HNCACO (H[N[ca[CO]]])	NGH1x_low_ionic_strength	isotropic	CondSet15

Software:

CcpNmr_Analysis v2.4, CCPN - Spectral analysis

NMR spectrometers:

Bruker Avance 950 MHz

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