BMRB Entry 51542

Name: 1H, 13C and 15N resonance assignments for the BRCT domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei
Published: 2024-03-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51542

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 13C and 15N resonance assignments for the BRCT domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei

Deposition date:

2022-08-02

Original release date:

2024-03-20

Authors:

Ludzia, Patryk; Robinson, Timothy; Akiyoshi, Bungo; Redfield, Christina

Citation:

Citation: Ludzia, Patryk; Hayashi, Hanako; Robinson, Timothy; Akiyoshi, Bungo; Redfield, Christina. "NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4" Biomol. NMR Assignments 18, 15-25 (2024).
PubMed: 38453826

Assembly members:

Assembly members:
entity_1, polymer, 185 residues, 19889.60 Da.

Natural source:

Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMSGASSAVGGSTRSPSPVD PKRGAVQPRYFITTSLTEKE RNSVMEAIQKLGQRAVLVDN KVDEILPLNTTHIVLRGPPR SVKALCGVVSSKWLVQPSYV FDSLGAGFWLDEEVEGGLRY FPPPLRCQRFLLTMPEGVVK TMLQRVVEFGGGEVVGTKRN GSSNDQDVVVVSSGDELLRF AISRD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	642
15N chemical shifts	180
1H chemical shifts	988

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KKT4	1

Entities:

Entity 1, KKT4 185 residues - 19889.60 Da.

Residues 1-2 (461S, 462M) represent part of a remained linker after TEV protease cleavage.

1

SER

MET

SER

GLY

ALA

SER

ALA

VAL

GLY

2

GLY

SER

THR

ARG

SER

PRO

SER

PRO

VAL

ASP

3

PRO

LYS

ARG

GLY

ALA

VAL

GLN

PRO

ARG

TYR

4

PHE

ILE

THR

SER

LEU

THR

GLU

LYS

GLU

5

ARG

ASN

SER

VAL

MET

GLU

ALA

ILE

GLN

LYS

6

LEU

GLY

GLN

ARG

ALA

VAL

LEU

VAL

ASP

ASN

7

LYS

VAL

ASP

GLU

ILE

LEU

PRO

LEU

ASN

THR

8

THR

HIS

ILE

VAL

LEU

ARG

GLY

PRO

ARG

9

SER

VAL

LYS

ALA

LEU

CYS

GLY

VAL

SER

10

SER

LYS

TRP

LEU

VAL

GLN

PRO

SER

TYR

VAL

11

PHE

ASP

SER

LEU

GLY

ALA

GLY

PHE

TRP

LEU

12

ASP

GLU

VAL

GLU

GLY

LEU

ARG

TYR

13

PHE

PRO

LEU

ARG

CYS

GLN

ARG

PHE

14

LEU

THR

MET

PRO

GLU

GLY

VAL

LYS

15

THR

MET

LEU

GLN

ARG

VAL

GLU

PHE

GLY

16

GLY

GLU

VAL

GLY

THR

LYS

ARG

ASN

17

GLY

SER

ASN

ASP

GLN

ASP

VAL

18

VAL

SER

GLY

ASP

GLU

LEU

ARG

PHE

19

ALA

ILE

SER

ARG

ASP

Samples:

sample_1: KKT4 463-645, [U-100% 15N], 0.475 mM; sodium phosphate 50 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_2: KKT4 463-645, [U-100% 13C; U-100% 15N], 0.475 mM; sodium phosphate 50 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 293.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N BEST TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N BEST TROSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D BT-HNCA	sample_2	isotropic	sample_conditions_1
3D BT-HNCO	sample_2	isotropic	sample_conditions_1
3D BT-HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D BT-HNCACB	sample_2	isotropic	sample_conditions_1
3D BT-HN(CO)CACB	sample_2	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D (H)CCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5.1 - chemical shift assignment

NMRPipe v9.7 - processing

TOPSPIN v3.2 - collection

hmsIST v211_64b - processing

NMR spectrometers:

Bruker AVANCE III 750 MHz
Bruker AVANCE III 950 MHz