BMRB Entry 50204

Name: Musashi-1 C-terminal domain, residues 194-362
Published: 2020-06-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50204

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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:

Musashi-1 C-terminal domain, residues 194-362

Deposition date:

2020-02-24

Original release date:

2020-06-09

Authors:

Chen, Tsai-chen; Huang, Jie-rong

Citation:

Citation: Chen, Tsai-chen; Huang, Jie-rong. "Musashi-1: An Example of How Polyalanine Tracts Contribute to Self-Association in the Intrinsically Disordered Regions of RNA-Binding Proteins" Int. J. Mol. Sci. 21, 2289-2289 (2020).
PubMed: 32225071

Assembly members:

Assembly members:
Musashi-1, polymer, 169 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: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Musashi-1: GSARGRSRVMPYGMDAFMLG IGMLGYPGFQATTYASRSYT GLAPGYTYQFPEFRVERSPL PSAPVLPELTAIPLTAYGPM AAAAAAAAVVRGTGSHPWTM APPPGSTPSRTGGFLGTTSP GPMAELYGAANQDSGVSSYI SAASPAPSTGFGHSLGGPLI ATAFTNGYH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	462
15N chemical shifts	145
1H chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Musashi-1	1

Entities:

Entity 1, Musashi-1 169 residues - Formula weight is not available

1

GLY

SER

ALA

ARG

GLY

ARG

SER

ARG

VAL

MET

2

PRO

TYR

GLY

MET

ASP

ALA

PHE

MET

LEU

GLY

3

ILE

GLY

MET

LEU

GLY

TYR

PRO

GLY

PHE

GLN

4

ALA

THR

TYR

ALA

SER

ARG

SER

TYR

THR

5

GLY

LEU

ALA

PRO

GLY

TYR

THR

TYR

GLN

PHE

6

PRO

GLU

PHE

ARG

VAL

GLU

ARG

THR

PRO

LEU

7

PRO

SER

ALA

PRO

VAL

LEU

PRO

GLU

LEU

THR

8

ALA

ILE

PRO

LEU

THR

ALA

TYR

GLY

PRO

MET

9

ALA

VAL

10

ARG

GLY

THR

GLY

SER

HIS

PRO

TRP

THR

MET

11

ALA

PRO

GLY

SER

THR

PRO

SER

ARG

12

THR

GLY

PHE

LEU

GLY

THR

SER

PRO

13

GLY

PRO

MET

ALA

GLU

LEU

TYR

GLY

ALA

14

ASN

GLN

ASP

SER

GLY

VAL

SER

TYR

ILE

15

SER

ALA

SER

PRO

ALA

PRO

SER

THR

GLY

16

PHE

GLY

HIS

SER

LEU

GLY

PRO

LEU

ILE

17

ALA

THR

ALA

PHE

THR

ASN

GLY

TYR

HIS

Samples:

sample_1: Musashi-1, [U-99% 15N], 20-100 uM

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 283 K

Experiments:

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

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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