BMRB Entry 27186

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for APLF acidic domain
Published: 2018-06-21

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27186

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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: Backbone 1H, 13C, and 15N Chemical Shift Assignments for APLF acidic domain PubMed: 29905837

Deposition date: 2017-07-21 Original release date: 2018-06-21

Authors: van Ingen, Hugo; Corbeski, Ivan; Dolinar, Klemen; Wienk, Hans; Boelens, Rolf

Citation: Corbeski, Ivan; Dolinar, Klemen; Wienk, Hans; Boelens, Rolf; van Ingen, Hugo. "DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface" Nucleic Acids Res. 46, 7138-7152 (2018).

Assembly members:
APLF_acidic_domain, polymer, 65 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
APLF_acidic_domain: GSLDEDNDNVGQPNEYDLND SFLDDEEEDYEPTDEDSDWE PGKEDEEKEDVEELLKEAKR FMKRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	190
15N chemical shifts	60
1H chemical shifts	119

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	APLF acidic domain	1

Entities:

Entity 1, APLF acidic domain 65 residues - Formula weight is not available

1

GLY

SER

LEU

ASP

GLU

ASP

ASN

ASP

ASN

VAL

2

GLY

GLN

PRO

ASN

GLU

TYR

ASP

LEU

ASN

ASP

3

SER

PHE

LEU

ASP

GLU

ASP

TYR

4

GLU

PRO

THR

ASP

GLU

ASP

SER

ASP

TRP

GLU

5

PRO

GLY

LYS

GLU

ASP

GLU

LYS

GLU

ASP

6

VAL

GLU

LEU

LYS

GLU

ALA

LYS

ARG

7

PHE

MET

LYS

ARG

LYS

Samples:

sample_1: APLF acidic domain, [U-100% 13C; U-100% 15N], 200 – 300 uM

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 300 K

Experiments:

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

Software:

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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