BMRB Entry 52461

Name: 1H, 13C and 15N resonance assignments for the acetyltransferase domain of the kinetoplastid kinetochore protein KKT23 in the presence of acetyl coenzyme A
Published: 2024-08-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52461

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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:

1H, 13C and 15N resonance assignments for the acetyltransferase domain of the kinetoplastid kinetochore protein KKT23 in the presence of acetyl coenzyme A

Deposition date:

2024-05-13

Original release date:

2024-08-28

Authors:

Ludzia, Patryk; Nugent, Charlotte; Akiyoshi, Bungo; Redfield, Christina

Citation:

Citation: Ludzia, Patryk; Ishii, Midori; Deak, Gauri; Spanos, Christos; Wilson, Marcus; Redfield, Christina; Akiyoshi, Bungo. "The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail" Structure ., .-. (2024).

Assembly members:

Assembly members:
entity_1, polymer, 226 residues, 26086.91 Da.
entity_ACO, non-polymer, 809.571 Da.

Natural source:

Natural source: Common Name: Trypanosoma brucei brucei Taxonomy ID: 5702 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRSF_Duet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSQQLTYSQLVLRTAIQDQY SKLSGDGPFPMAFGLVLSEE ERREVIDLYSLQFQYPDQPE LQRLVILPQTHSTRTRRRAK GSYTWYLRSLNTNEMVCAVT IMAHHYETHHFVEVPLFATG VGYKKHGFGRLMNAALLQWC VETGFEFVMISADVKAIPFW SHLGYKTMEKSELTRIVFYY EHNCYKFKGAEVMIRYCRTW PTDGVKEALARVQKVIVSGH VGLMDA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	677
15N chemical shifts	196
1H chemical shifts	843

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KKT4 125-348	1
2	Acetyl coenzyme A	2

Entities:

Entity 1, KKT4 125-348 226 residues - 26086.91 Da.

Residues 1-2 (123G, 124S) represent part of a linker that remained after TEV protease cleavage.

1

GLY

SER

GLN

LEU

THR

TYR

SER

GLN

LEU

2

VAL

LEU

ARG

THR

ALA

ILE

GLN

ASP

GLN

TYR

3

SER

LYS

LEU

SER

GLY

ASP

GLY

PRO

PHE

PRO

4

MET

ALA

PHE

GLY

LEU

VAL

LEU

SER

GLU

5

GLU

ARG

GLU

VAL

ILE

ASP

LEU

TYR

SER

6

LEU

GLN

PHE

GLN

TYR

PRO

ASP

GLN

PRO

GLU

7

LEU

GLN

ARG

LEU

VAL

ILE

LEU

PRO

GLN

THR

8

HIS

SER

THR

ARG

THR

ARG

ALA

LYS

9

GLY

SER

TYR

THR

TRP

TYR

LEU

ARG

SER

LEU

10

ASN

THR

ASN

GLU

MET

VAL

CYS

ALA

VAL

THR

11

ILE

MET

ALA

HIS

TYR

GLU

THR

HIS

12

PHE

VAL

GLU

VAL

PRO

LEU

PHE

ALA

THR

GLY

13

VAL

GLY

TYR

LYS

HIS

GLY

PHE

GLY

ARG

14

LEU

MET

ASN

ALA

LEU

GLN

TRP

CYS

15

VAL

GLU

THR

GLY

PHE

GLU

PHE

VAL

MET

ILE

16

SER

ALA

ASP

VAL

LYS

ALA

ILE

PRO

PHE

TRP

17

SER

HIS

LEU

GLY

TYR

LYS

THR

MET

GLU

LYS

18

SER

GLU

LEU

THR

ARG

ILE

VAL

PHE

TYR

19

GLU

HIS

ASN

CYS

TYR

LYS

PHE

LYS

GLY

ALA

20

GLU

VAL

MET

ILE

ARG

TYR

CYS

ARG

THR

TRP

21

PRO

THR

ASP

GLY

VAL

LYS

GLU

ALA

LEU

ALA

22

ARG

VAL

GLN

LYS

VAL

ILE

VAL

SER

GLY

HIS

23

VAL

GLY

LEU

MET

ASP

ALA

Entity 2, Acetyl coenzyme A - C23 H38 N7 O17 P3 S - 809.571 Da.

1

ACO

Samples:

sample_1: KKT23_125_348, [U-13C; U-15N], 0.435 ± 0 mM; sodium chloride 150 ± 0 mM; sodium phosphate 50 ± 0 mM; TCEP 0.5 ± 0 mM; Acetyl Coenzyme A (AcCoA) 0.5 ± 0 mM

sample_2: KKT23_125_348, [U-100% 15N], 0.350 ± 0 mM; sodium chloride 150 ± 0 mM; HEPES 25 ± 0 mM; TCEP 0.5 ± 0 mM; Acetyl Coenzyme A (AcCoA) 0.7 ± 0 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

sample_conditions_2: ionic strength: 150 mM; pH: 7.15; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D BT HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
3D (H)CC(CO)NH	sample_1	isotropic	sample_conditions_1
2D BEST TROSY	sample_1	isotropic	sample_conditions_1
2D BEST TROSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
H(CCCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-COSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_2
3D BT HNCOCACB	sample_1	isotropic	sample_conditions_1
3D BT HNCO	sample_1	isotropic	sample_conditions_1
3D BT HNCACO	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.4.2 - chemical shift assignment

NMRPipe v9.7 - processing

hmsIST vv211_64b - processing

TOPSPIN v3.2 - collection

NMR spectrometers:

Bruker Avance III HD 750 MHz
Bruker Avance III HD 950 MHz