BMRB Entry 27642

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Mps1 TPR domain
Published: 2019-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27642

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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Mps1 TPR domain

Deposition date:

2018-10-09

Original release date:

2019-02-12

Authors:

Hiruma, Yoshitaka; Perrakis, Anastassis

Citation:

Citation: Pachis, Spyridon; Hiruma, Yoshitaka; Tromer, Eelco; Perrakis, Anastassis; Kops, Geert. "Interactions between N-terminal Modules in MPS1 Enable Spindle Checkpoint Silencing." Cell Rep. 26, 2101-2112 (2019).
PubMed: 30784592

Assembly members:

Assembly members:
TTK, polymer, 178 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TTK: PEDWLSLLLKLEKNSVPLSD ALLNKLIGRYSQAIEALPPD KYGQNESFARIQVRFAELKA IQEPDDARDYFQMARANCKK FAFVHISFAQFELSQGNVKK SKQLLQKAVERGAVPLEMLE IALRNLNLQKKQLLSEEEKK NLSASTVLTAQESFSGSLGH LQNRNNSCDSRGQTTKAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	487
15N chemical shifts	159
1H chemical shifts	159

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mps1 62-239	1

Entities:

Entity 1, Mps1 62-239 178 residues - Formula weight is not available

1

PRO

GLU

ASP

TRP

LEU

SER

LEU

LYS

2

LEU

GLU

LYS

ASN

SER

VAL

PRO

LEU

SER

ASP

3

ALA

LEU

ASN

LYS

LEU

ILE

GLY

ARG

TYR

4

SER

GLN

ALA

ILE

GLU

ALA

LEU

PRO

ASP

5

LYS

TYR

GLY

GLN

ASN

GLU

SER

PHE

ALA

ARG

6

ILE

GLN

VAL

ARG

PHE

ALA

GLU

LEU

LYS

ALA

7

ILE

GLN

GLU

PRO

ASP

ALA

ARG

ASP

TYR

8

PHE

GLN

MET

ALA

ARG

ALA

ASN

CYS

LYS

9

PHE

ALA

PHE

VAL

HIS

ILE

SER

PHE

ALA

GLN

10

PHE

GLU

LEU

SER

GLN

GLY

ASN

VAL

LYS

11

SER

LYS

GLN

LEU

GLN

LYS

ALA

VAL

GLU

12

ARG

GLY

ALA

VAL

PRO

LEU

GLU

MET

LEU

GLU

13

ILE

ALA

LEU

ARG

ASN

LEU

ASN

LEU

GLN

LYS

14

LYS

GLN

LEU

SER

GLU

LYS

15

ASN

LEU

SER

ALA

SER

THR

VAL

LEU

THR

ALA

16

GLN

GLU

SER

PHE

SER

GLY

SER

LEU

GLY

HIS

17

LEU

GLN

ASN

ARG

ASN

SER

CYS

ASP

SER

18

ARG

GLY

GLN

THR

LYS

ALA

ARG

Samples:

sample_1: TTK, [U-13C; U-15N], 600 uM; HEPES/NaOH 20 mM; KCl 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CCPN, CCPN - chemical shift assignment

UNP	P33981
AlphaFold	Q9NTM0