BMRB Entry 51887

Name: Abf2
Published: 2023-09-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51887

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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

Deposition date:

2023-03-27

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, 157 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 KKEFDEKLPPKKPAGPFIKY ANEVRSQVFAQHPDKSQLDL MKIIGDKWQSLDQSIKDKYI QEYKKAIQEYNARYPLN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	136
1H chemical shifts	338

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 157 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

LYS

LEU

PRO

10

LYS

PRO

ALA

GLY

PRO

PHE

ILE

LYS

TYR

11

ALA

ASN

GLU

VAL

ARG

SER

GLN

VAL

PHE

ALA

12

GLN

HIS

PRO

ASP

LYS

SER

GLN

LEU

ASP

LEU

13

MET

LYS

ILE

GLY

ASP

LYS

TRP

GLN

SER

14

LEU

ASP

GLN

SER

ILE

LYS

ASP

LYS

TYR

ILE

15

GLN

GLU

TYR

LYS

ALA

ILE

GLN

GLU

TYR

16

ASN

ALA

ARG

TYR

PRO

LEU

ASN

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
3D 1H-13C NOESY aliphatic	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