BMRB Entry 51891

Name: Abf2-HMG1
Published: 2023-09-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51891

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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:

Abf2-HMG1

Deposition date:

2023-03-30

Original release date:

2023-09-01

Authors:

Lidmann, Jens; Sallova, Ylber; Matecko-Burmann, Irena; Burmann, Bjorn

Citation:

Citation: Lidmann, Jens; Sallova, Ylber; Matecko-Burmann, Irena; Burmann, Bjorn. "Structure and dynamics of the mitochondrial DNA-compaction factor Abf2 from S. cerevisiae" J. Struct. Biol. 215, 108008-108008 (2023).
PubMed: 37543301

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28_SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KASKRTQLRNELIKQGPKRP TSAYFLYLQDHRSQFVKENP TLRPAEISKIAGEKWQNLEA DIKEKYISERKKLYSEYQKA KKEFDE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	294
15N chemical shifts	88
1H chemical shifts	262

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Abf2	1

Entities:

Entity 1, Abf2 86 residues - Formula weight is not available

1

LYS

ALA

SER

LYS

ARG

THR

GLN

LEU

ARG

ASN

2

GLU

LEU

ILE

LYS

GLN

GLY

PRO

LYS

ARG

PRO

3

THR

SER

ALA

TYR

PHE

LEU

TYR

LEU

GLN

ASP

4

HIS

ARG

SER

GLN

PHE

VAL

LYS

GLU

ASN

PRO

5

THR

LEU

ARG

PRO

ALA

GLU

ILE

SER

LYS

ILE

6

ALA

GLY

GLU

LYS

TRP

GLN

ASN

LEU

GLU

ALA

7

ASP

ILE

LYS

GLU

LYS

TYR

ILE

SER

GLU

ARG

8

LYS

LEU

TYR

SER

GLU

TYR

GLN

LYS

ALA

9

LYS

GLU

PHE

ASP

GLU

Samples:

sample_1: Abf2, [U-100% 13C; U-100% 15N], 500 uM; DTT 1 mM; NaCl 800 mM; D2O 10%; NaPi 20 mM

sample_conditions_1: ionic strength: 800 mM; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D CBCANH	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:

CARA - chemical shift assignment

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 800 MHz

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