BMRB Entry 36058

Name: Refined solution structure of musashi1 RBD2
Published: 2017-12-11

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PDB ID: 5x3y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36058
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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:

Refined solution structure of musashi1 RBD2

Deposition date:

2017-02-09

Original release date:

2017-12-11

Authors:

Iwaoka, R.; Nagata, T.; Tsuda, K.; Imai, T.; Okano, H.; Kobayashi, N.; Katahira, M.

Citation:

Citation: Iwaoka, R.; Nagata, T.; Tsuda, K.; Imai, T.; Okano, H.; Kobayashi, N.; Katahira, M.. "Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA" Molecules 22, 1207-1207 (2017).
PubMed: 28753936

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 10945.506 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMKKIFVGGLSVNTTVED VKHYFEQFGKVDDAMLMFDK TTNRHRGFGFVTFESEDIVE KVCEIHFHEINNKMVECKKA QPKEVMSPTGSARGRS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	404
15N chemical shifts	93
1H chemical shifts	598

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 96 residues - 10945.506 Da.

1

GLY

SER

HIS

MET

LYS

ILE

PHE

VAL

GLY

2

GLY

LEU

SER

VAL

ASN

THR

VAL

GLU

ASP

3

VAL

LYS

HIS

TYR

PHE

GLU

GLN

PHE

GLY

LYS

4

VAL

ASP

ALA

MET

LEU

MET

PHE

ASP

LYS

5

THR

ASN

ARG

HIS

ARG

GLY

PHE

GLY

PHE

6

VAL

THR

PHE

GLU

SER

GLU

ASP

ILE

VAL

GLU

7

LYS

VAL

CYS

GLU

ILE

HIS

PHE

HIS

GLU

ILE

8

ASN

LYS

MET

VAL

GLU

CYS

LYS

ALA

9

GLN

PRO

LYS

GLU

VAL

MET

SER

PRO

THR

GLY

10

SER

ALA

ARG

GLY

ARG

SER

Samples:

sample_1: Msi1 RBD2, [U-100% 13C; U-100% 15N], 250 uM; MES 20 mM; sodium chloride 100 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

MagRO, Kobayashi - chemical shift assignment

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz

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