BMRB Entry 36431

Name: The solution structure of the second RRM domain of Matrin-3
Published: 2022-02-24

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PDB ID: 7fbv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36431
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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: The solution structure of the second RRM domain of Matrin-3

Deposition date: 2021-07-13 Original release date: 2022-02-24

Authors: Muto, Y.; Kobayashi, N.; Yokoyama, S.; RIKEN Structural Genomics/Proteomics Initiative (RSGI), RSGI

Citation: He, F.; Kuwasako, K.; Takizawa, M.; Takahashi, M.; Tsuda, K.; Nagata, T.; Watanabe, S.; Tanaka, A.; Kobayashi, N.; Kigawa, T.; Guntert, P.; Shirouzu, M.; Yokoyama, S.; Muto, Y.. "1H, 13C and 15N resonance assignments of the two RRM domains of Matrin-3" .

Assembly members:
Matrin-3, polymer, 112 residues, 12499.458 Da.

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

Experimental source: Production method: recombinant technology Host organism: Cell-free gateway cloning vector N-term 8xHis eGFP pCellFree_G03

Entity Sequences (FASTA):
Matrin-3: GSSGSSGKKPEGKPDQKFDQ KQELGRVIHLSNLPHSGYSD SAVLKLAEPYGKIKNYILMR MKSQAFIEMETREDAMAMVD HCLKKALWFQGRCVKVDLSE KYKKLVSGPSSG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	459
15N chemical shifts	96
1H chemical shifts	723

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 112 residues - 12499.458 Da.

1

GLY

SER

GLY

SER

GLY

LYS

PRO

2

GLU

GLY

LYS

PRO

ASP

GLN

LYS

PHE

ASP

GLN

3

LYS

GLN

GLU

LEU

GLY

ARG

VAL

ILE

HIS

LEU

4

SER

ASN

LEU

PRO

HIS

SER

GLY

TYR

SER

ASP

5

SER

ALA

VAL

LEU

LYS

LEU

ALA

GLU

PRO

TYR

6

GLY

LYS

ILE

LYS

ASN

TYR

ILE

LEU

MET

ARG

7

MET

LYS

SER

GLN

ALA

PHE

ILE

GLU

MET

GLU

8

THR

ARG

GLU

ASP

ALA

MET

ALA

MET

VAL

ASP

9

HIS

CYS

LEU

LYS

ALA

LEU

TRP

PHE

GLN

10

GLY

ARG

CYS

VAL

LYS

VAL

ASP

LEU

SER

GLU

11

LYS

TYR

LYS

LEU

VAL

SER

GLY

PRO

SER

12

SER

GLY

Samples:

sample_1: RNA binding protein, [U-99% 13C; U-99% 15N], 1 mM; Tris-Hcl, [U-100% 2H], 20 mM; NaCl 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_13C,15N-SEPARATED_NOESY SPECTRA	sample_1	isotropic	sample_conditions_1

Software:

Amber v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure calculation

KUJIRA v0.863, N. Kobayashi, T. Kigawa, S. Yokoyama - chemical shift assignment

NMRPipe v2007, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - peak picking

TALOS v2007, Cornilescu, Delaglio and Bax - geometry optimization

TopSpin v2.1, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE 800 MHz

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