BMRB Entry 27641

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for MPS1
Published: 2019-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27641

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for MPS1 PubMed: 30784592

Deposition date: 2018-10-09 Original release date: 2019-02-12

Authors: Hiruma, Yoshitaka; Perrakis, Anastassis

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).

Assembly members:
TTK, polymer, 239 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
TTK: MESEDLSGRELTIDSIMNKV RDIKNKFKNEDLTDELSLNK ISADTTDNSGTVNQIMMMAN NPEDWLSLLLKLEKNSVPLS DALLNKLIGRYSQAIEALPP DKYGQNESFARIQVRFAELK AIQEPDDARDYFQMARANCK KFAFVHISFAQFELSQGNVK KSKQLLQKAVERGAVPLEML EIALRNLNLQKKQLLSEEEK KNLSASTVLTAQESFSGSLG HLQNRNNSCDSRGQTTKAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	617
15N chemical shifts	210
1H chemical shifts	210

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

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

1

MET

GLU

SER

GLU

ASP

LEU

SER

GLY

ARG

GLU

2

LEU

THR

ILE

ASP

SER

ILE

MET

ASN

LYS

VAL

3

ARG

ASP

ILE

LYS

ASN

LYS

PHE

LYS

ASN

GLU

4

ASP

LEU

THR

ASP

GLU

LEU

SER

LEU

ASN

LYS

5

ILE

SER

ALA

ASP

THR

ASP

ASN

SER

GLY

6

THR

VAL

ASN

GLN

ILE

MET

ALA

ASN

7

ASN

PRO

GLU

ASP

TRP

LEU

SER

LEU

8

LYS

LEU

GLU

LYS

ASN

SER

VAL

PRO

LEU

SER

9

ASP

ALA

LEU

ASN

LYS

LEU

ILE

GLY

ARG

10

TYR

SER

GLN

ALA

ILE

GLU

ALA

LEU

PRO

11

ASP

LYS

TYR

GLY

GLN

ASN

GLU

SER

PHE

ALA

12

ARG

ILE

GLN

VAL

ARG

PHE

ALA

GLU

LEU

LYS

13

ALA

ILE

GLN

GLU

PRO

ASP

ALA

ARG

ASP

14

TYR

PHE

GLN

MET

ALA

ARG

ALA

ASN

CYS

LYS

15

LYS

PHE

ALA

PHE

VAL

HIS

ILE

SER

PHE

ALA

16

GLN

PHE

GLU

LEU

SER

GLN

GLY

ASN

VAL

LYS

17

LYS

SER

LYS

GLN

LEU

GLN

LYS

ALA

VAL

18

GLU

ARG

GLY

ALA

VAL

PRO

LEU

GLU

MET

LEU

19

GLU

ILE

ALA

LEU

ARG

ASN

LEU

ASN

LEU

GLN

20

LYS

GLN

LEU

SER

GLU

LYS

21

LYS

ASN

LEU

SER

ALA

SER

THR

VAL

LEU

THR

22

ALA

GLN

GLU

SER

PHE

SER

GLY

SER

LEU

GLY

23

HIS

LEU

GLN

ASN

ARG

ASN

SER

CYS

ASP

24

SER

ARG

GLY

GLN

THR

LYS

ALA

ARG

Samples:

sample_1: TTK, [U-13C; U-15N], 500 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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts