BMRB Entry 17960

Name: Complete 1H, 13C and 15N assignments of the kinetochore localisation domain of BUBR1 bound to a Blinkin motif
Published: 2011-11-21

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17960

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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:

Complete 1H, 13C and 15N assignments of the kinetochore localisation domain of BUBR1 bound to a Blinkin motif

Deposition date:

2011-09-26

Original release date:

2011-11-21

Authors:

Simpson, Peter; Blundell, Tom; Cota-Segura, Ernesto; Bolanos-Garcia, Victor

Citation:

Citation: Bolanos-Garcia, Victor; Lischetti, Tiziana; Matak-Vinkovic, Dijana; Cota, Ernesto; Simpson, Pete; Chirgadze, Dimitri; Spring, David; Robinson, Carol; Nilsson, Jakob; Blundell, Tom. "Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding Site." Structure 19, 1691-1700 (2011).
PubMed: 22000412

Assembly members:

Assembly members:
Bubr1N, polymer, 167 residues, 19844.2 Da.
Blinkin_peptide, polymer, 15 residues, 1826.2 Da.

Natural source:

Natural source: Common Name: humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bubr1N: GPLQQKRAFEYEIRFYTGND PLDVWDRYISWTEQNYPQGG KESNMSTLLERAVEALQGEK RYYSDPRFLNLWLKLGRLCN EPLDMYSYLHNQGIGVSLAQ FYISWAEEYEARENFRKADA IFQEGIQQKAEPLERLQSQH RQFQARVSRQTLLALEKEEE EEVFESS
Blinkin_peptide: KIDFNDFIKRLKTGK

Data sets:

assigned_chemical_shifts
- assignments_bubr1_nv

Data type	Count
13C chemical shifts	715
1H chemical shifts	1043
15N chemical shifts	162

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Bubr1 N domain	1
2	Blinkin residues 212-226	2

Entities:

Entity 1, Bubr1 N domain 167 residues - 19844.2 Da.

The first 3 residues are vector encoded. Q4 corresponds to Q57 of the native sequence

1

GLY

PRO

LEU

GLN

LYS

ARG

ALA

PHE

GLU

2

TYR

GLU

ILE

ARG

PHE

TYR

THR

GLY

ASN

ASP

3

PRO

LEU

ASP

VAL

TRP

ASP

ARG

TYR

ILE

SER

4

TRP

THR

GLU

GLN

ASN

TYR

PRO

GLN

GLY

5

LYS

GLU

SER

ASN

MET

SER

THR

LEU

GLU

6

ARG

ALA

VAL

GLU

ALA

LEU

GLN

GLY

GLU

LYS

7

ARG

TYR

SER

ASP

PRO

ARG

PHE

LEU

ASN

8

LEU

TRP

LEU

LYS

LEU

GLY

ARG

LEU

CYS

ASN

9

GLU

PRO

LEU

ASP

MET

TYR

SER

TYR

LEU

HIS

10

ASN

GLN

GLY

ILE

GLY

VAL

SER

LEU

ALA

GLN

11

PHE

TYR

ILE

SER

TRP

ALA

GLU

TYR

GLU

12

ALA

ARG

GLU

ASN

PHE

ARG

LYS

ALA

ASP

ALA

13

ILE

PHE

GLN

GLU

GLY

ILE

GLN

LYS

ALA

14

GLU

PRO

LEU

GLU

ARG

LEU

GLN

SER

GLN

HIS

15

ARG

GLN

PHE

GLN

ALA

ARG

VAL

SER

ARG

GLN

16

THR

LEU

ALA

LEU

GLU

LYS

GLU

17

GLU

VAL

PHE

GLU

SER

Entity 2, Blinkin residues 212-226 15 residues - 1826.2 Da.

The peptide corresponds to Blinkin residues 212-226

1

LYS

ILE

ASP

PHE

ASN

ASP

PHE

ILE

LYS

ARG

2

LEU

LYS

THR

GLY

LYS

Samples:

sample_1: Bubr1N, [U-100% 13C; U-100% 15N], 0.25 ± 0.05 mM; Blinkin peptide 0.4 ± 0.05 mM; sodium chloride 200 ± 20 mM; sodium phosphate 50 ± 5 mM; sodium azide 1 ± 0.5 mM; TSP 0.1 ± 0.01 mM; TCEP 1 ± 0.1 mM; H2O 90%; D2O 10%

sample_d2o: Bubr1N, [U-100% 13C; U-100% 15N], 0.25 ± 0.05 mM; Blinkin peptide 0.4 ± 0.05 mM; sodium chloride 200 ± 20 mM; sodium phosphate 50 ± 5 mM; sodium azide 1 ± 0.5 mM; TSP 0.1 ± 0.01 mM; TCEP 1 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.5 M; pH: 7; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 0.5 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_2
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(C)CH-TOCSY	sample_d2o	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_d2o	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_d2o	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_d2o	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_d2o	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

NMRView v5.2.2_01, Johnson, One Moon Scientific - data analysis

NMRPipe v2010 release, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

UNP	O60566 Q8NG31
PDB	2WVI 2WVI 3SI5 3SI5
DBJ	BAD92019 BAG10575 BAG35587 BAC05691
GB	AAC06260 AAC12730 AAC19118 AAC23736 AAC33435 AAF97513 AAH29373 AAI72422 AAL67803 AAM45143
REF	NP_001202 XP_002753645 XP_002804771 XP_002825334 XP_003266770 NP_653091 NP_733468 XP_004056050 XP_008950270 XP_009247989
SP	O60566 Q8NG31
AlphaFold	Q96KM4 Q9NR92 O60566 Q8NG31