BMRB Entry 27613

Name: 1H, 15N and 13C backbone assignment of apoTDP-43 RNA Recognition Motifs
Published: 2018-09-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27613

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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:

1H, 15N and 13C backbone assignment of apoTDP-43 RNA Recognition Motifs

Deposition date:

2018-09-14

Original release date:

2018-09-25

Authors:

Scott, David; Kumirov, Vlad; Francois-Moutal, Liberty; Khanna, May

Citation:

Citation: Scott, David; Francois-Moutal, Liberty; Kumirov, Vlad; Khanna, May. "1H, 15N and 13C backbone assignment of apo TDP-43 RNA recognition motifs" Biomol. NMR Assignments 13, 163-167 (2019).
PubMed: 30694439

Assembly members:

Assembly members:
TDP43, polymer, 202 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TDP43: MGSSHHHHHHSSGLVPRGSH MASMTGGQQMGRGSKTSDLI VLGLPWKTTEQDLKEYFSTF GEVLMVQVKKDLKTGHSKGF GFVRFTEYETQVKVMSQRHM IDGRWCDCKLPNSKQSQDEP LRSRKVFVGRCTEDMTEDEL REFFSQYGDVMDVFIPKPFR AFAFVTFADDQIAQSLCGED LIIKGISVHISNAEPKHNSN RQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	435
15N chemical shifts	142
1H chemical shifts	142

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM, chain 1	1
2	RRM, chain 2	1

Entities:

Entity 1, RRM, chain 1 202 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

SER

MET

THR

GLY

GLN

MET

4

GLY

ARG

GLY

SER

LYS

THR

SER

ASP

LEU

ILE

5

VAL

LEU

GLY

LEU

PRO

TRP

LYS

THR

GLU

6

GLN

ASP

LEU

LYS

GLU

TYR

PHE

SER

THR

PHE

7

GLY

GLU

VAL

LEU

MET

VAL

GLN

VAL

LYS

8

ASP

LEU

LYS

THR

GLY

HIS

SER

LYS

GLY

PHE

9

GLY

PHE

VAL

ARG

PHE

THR

GLU

TYR

GLU

THR

10

GLN

VAL

LYS

VAL

MET

SER

GLN

ARG

HIS

MET

11

ILE

ASP

GLY

ARG

TRP

CYS

ASP

CYS

LYS

LEU

12

PRO

ASN

SER

LYS

GLN

SER

GLN

ASP

GLU

PRO

13

LEU

ARG

SER

ARG

LYS

VAL

PHE

VAL

GLY

ARG

14

CYS

THR

GLU

ASP

MET

THR

GLU

ASP

GLU

LEU

15

ARG

GLU

PHE

SER

GLN

TYR

GLY

ASP

VAL

16

MET

ASP

VAL

PHE

ILE

PRO

LYS

PRO

PHE

ARG

17

ALA

PHE

ALA

PHE

VAL

THR

PHE

ALA

ASP

18

GLN

ILE

ALA

GLN

SER

LEU

CYS

GLY

GLU

ASP

19

LEU

ILE

LYS

GLY

ILE

SER

VAL

HIS

ILE

20

SER

ASN

ALA

GLU

PRO

LYS

HIS

ASN

SER

ASN

21

ARG

GLN

Samples:

sample_1: TDP43, [U-100% 13C; U-100% 15N], 450 uM; DTT 4 mM; sodium azide 0.5%; HEPES 40 mM; sodium chloride 500 mM; D2O 10%

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 298 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 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.134, Goddard - chemical shift assignment, data analysis, peak picking

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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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