BMRB Entry 50229

Name: 1H, 13C and 15N resonance assignments for the microtubule-binding region of the kinetoplastid kinetochore protein KKT4 115-343
Published: 2020-07-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50229

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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 microtubule-binding region of the kinetoplastid kinetochore protein KKT4 115-343

Deposition date:

2020-04-09

Original release date:

2020-07-24

Authors:

Ludzia, Patryk; Akiyoshi, Bungo; Redfield, Christina

Citation:

Citation: Ludzia, Patryk; Akiyoshi, Bungo; Redfield, Christina. "1 H, 13 C and 15 N resonance assignments for the microtubule-binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei" Biomol. NMR Assignments 14, 309-315 (2020).
PubMed: 32696260

Assembly members:

Assembly members:
entity_1, polymer, 231 residues, 25701.57 Da.

Natural source:

Natural source: Common Name: Trypanosoma brucei 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: pRSF_Duet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMKYGVVSVERYERLMARYK ELEKQSHRRQGKRSEPVVDT QRVLDLEEEVARLKRTIGHL QGVVEEKESALEKHATQHNL EVHEMKKNYELKIKSLTQTH EAAVRKLVSAQELVTAARNY QTAVCANNVGGGNSVSTTSG QPLSNTVNHTRGLTTTSSGS GPNQPYTLPHPDGNAWMSAT TSDDRSAPVTTKNSHSVKRE REGTVSTTPTRPLKKRNPRT PSYTVADRISE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	134
1H chemical shifts	523

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KKT4 115-343	1

Entities:

Entity 1, KKT4 115-343 231 residues - 25701.57 Da.

Residues 1-2 (113S, 114M) represent part of a linker that remained after TEV protease cleavage.

1

SER

MET

LYS

TYR

GLY

VAL

SER

VAL

GLU

2

ARG

TYR

GLU

ARG

LEU

MET

ALA

ARG

TYR

LYS

3

GLU

LEU

GLU

LYS

GLN

SER

HIS

ARG

GLN

4

GLY

LYS

ARG

SER

GLU

PRO

VAL

ASP

THR

5

GLN

ARG

VAL

LEU

ASP

LEU

GLU

VAL

6

ALA

ARG

LEU

LYS

ARG

THR

ILE

GLY

HIS

LEU

7

GLN

GLY

VAL

GLU

LYS

GLU

SER

ALA

8

LEU

GLU

LYS

HIS

ALA

THR

GLN

HIS

ASN

LEU

9

GLU

VAL

HIS

GLU

MET

LYS

ASN

TYR

GLU

10

LEU

LYS

ILE

LYS

SER

LEU

THR

GLN

THR

HIS

11

GLU

ALA

VAL

ARG

LYS

LEU

VAL

SER

ALA

12

GLN

GLU

LEU

VAL

THR

ALA

ARG

ASN

TYR

13

GLN

THR

ALA

VAL

CYS

ALA

ASN

VAL

GLY

14

GLY

ASN

SER

VAL

SER

THR

SER

GLY

15

GLN

PRO

LEU

SER

ASN

THR

VAL

ASN

HIS

THR

16

ARG

GLY

LEU

THR

SER

GLY

SER

17

GLY

PRO

ASN

GLN

PRO

TYR

THR

LEU

PRO

HIS

18

PRO

ASP

GLY

ASN

ALA

TRP

MET

SER

ALA

THR

19

THR

SER

ASP

ARG

SER

ALA

PRO

VAL

THR

20

THR

LYS

ASN

SER

HIS

SER

VAL

LYS

ARG

GLU

21

ARG

GLU

GLY

THR

VAL

SER

THR

PRO

THR

22

ARG

PRO

LEU

LYS

ARG

ASN

PRO

ARG

THR

23

PRO

SER

TYR

THR

VAL

ALA

ASP

ARG

ILE

SER

24

GLU

Samples:

sample_1: KKT4_115_343, [U-13C; U-15N], 0.35 ± 0.02 mM; sodium chloride 150 ± 0 mM; HEPES 25 ± 0 mM; TCEP 0.5 ± 0 mM

sample_2: KKT4_115_343, [U-15N], 0.35 ± 0.02 mM; sodium chloride 150 ± 0 mM; HEPES 25 ± 0 mM; TCEP 0.5 ± 0 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 293.15 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_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)N(CA)NNH	sample_1	isotropic	sample_conditions_1
3D (H)N(COCA)NNH	sample_1	isotropic	sample_conditions_1
2D BEST TROSY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D BEST TROSY	sample_1	isotropic	sample_conditions_1
HCA(CO)N	sample_1	isotropic	sample_conditions_1
HCAN	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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

UniProt	A0A3L6L4L8
AlphaFold	A0A3L6L4L8