BMRB Entry 26823

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26823

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments, HNHA scalar coupling, and 15N backbone relaxation data for TDP-43 C-terminal domain wild type PubMed: 27545621

Deposition date: 2016-06-20 Original release date: 2016-08-19

Authors: Conicella, Alexander; Fawzi, Nicolas

Citation: Conicella, Alexander; Zerze, Gul; Mittal, Jeetain; Fawzi, Nicolas. "ALS Mutations Disrupt Phase Separation Mediated by alpha-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain" Structure (Cambridge, MA, U.S.) 24, 1537-1549 (2016).

Assembly members:
WT_TDP-43_267-414, polymer, 151 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

Entity Sequences (FASTA):
WT_TDP-43_267-414: GHMNRQLERSGRFGGNPGGF GNQGGFGNSRGGGAGLGNNQ GSNMGGGMNFGAFSINPAMM AAAQAALQSSWGMMGMLASQ QNQSGPSGNNQNQGNMQREP NQAFGSGNNSYSGSNSGAAI GWGSASNAGSGSGFNGGFGS SMDSKSSGWGM

Data sets:

assigned_chemical_shifts
- WT_TDP-43_267-414_298_K
- WT_TDP-43_267-414_283_K
coupling_constants
- WT_TDP-43_267-414_3JHNHA
heteronucl_NOEs
- WT_TDP-43_267-414_850_MHz_HetNOE
- WT_TDP-43_267-414_500_MHz_HetNOE
heteronucl_T1_relaxation
- WT_TDP-43_267-414_850_MHz_R1
- WT_TDP-43_267-414_500_MHz_R1
heteronucl_T2_relaxation
- WT_TDP-43_267-414_850_MHz_R2
- WT_TDP-43_267-414_500_MHz_R2

Data type	Count
13C chemical shifts	660
15N chemical shifts	286
1H chemical shifts	292
T1 relaxation values	222
T2 relaxation values	259
coupling constants	101
heteronuclear NOE values	196

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WT TDP-43_267-414 Monomer	1

Entities:

Entity 1, WT TDP-43_267-414 Monomer 151 residues - Formula weight is not available

Residues 1-3 comprise the cloning artifact left after removal of the N-terminal affinity tag by cleavage with TEV protease.

1

GLY

HIS

MET

ASN

ARG

GLN

LEU

GLU

ARG

SER

2

GLY

ARG

PHE

GLY

ASN

PRO

GLY

PHE

3

GLY

ASN

GLN

GLY

PHE

GLY

ASN

SER

ARG

4

GLY

ALA

GLY

LEU

GLY

ASN

GLN

5

GLY

SER

ASN

MET

GLY

MET

ASN

PHE

6

GLY

ALA

PHE

SER

ILE

ASN

PRO

ALA

MET

7

ALA

GLN

ALA

LEU

GLN

SER

8

TRP

GLY

MET

GLY

MET

LEU

ALA

SER

GLN

9

GLN

ASN

GLN

SER

GLY

PRO

SER

GLY

ASN

10

GLN

ASN

GLN

GLY

ASN

MET

GLN

ARG

GLU

PRO

11

ASN

GLN

ALA

PHE

GLY

SER

GLY

ASN

SER

12

TYR

SER

GLY

SER

ASN

SER

GLY

ALA

ILE

13

GLY

TRP

GLY

SER

ALA

SER

ASN

ALA

GLY

SER

14

GLY

SER

GLY

PHE

ASN

GLY

PHE

GLY

SER

15

SER

MET

ASP

SER

LYS

SER

GLY

TRP

GLY

16

MET

Samples:

sample-1: WT TDP-43_267-414, [U-99% 13C; U-99% 15N], 20 uM; MES 20 mM

sample-2: WT TDP-43_267-414, [U-99% 15N], 20 uM; MES 20 mM

283_K: pH: 6.1; pressure: 1 atm; temperature: 283 K

298_K: pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample-1	isotropic	298_K
3D HNCACB	sample-1	isotropic	298_K
3D CBCA(CO)NH	sample-1	isotropic	298_K
3D HNCO	sample-1	isotropic	298_K
3D HN(CA)CO	sample-1	isotropic	298_K
2D 1H-15N HSQC	sample-1	isotropic	283_K
3D HNCACB	sample-1	isotropic	283_K
3D CBCA(CO)NH	sample-1	isotropic	283_K
hnhagp3d	sample-2	isotropic	283_K
hsqct1etf3gpsitc3d.nlf	sample-2	isotropic	283_K
hsqct2etf3gpsitc3d.ac	sample-2	isotropic	283_K
hsqcnoef3gpsi	sample-2	isotropic	283_K
hsqct1etf3gpsitc3d.nlf	sample-2	isotropic	283_K
hsqct2etf3gpsitc3d.ac	sample-2	isotropic	283_K
hsqcnoef3gpsi	sample-2	isotropic	283_K

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 850 MHz
Bruker Avance 500 MHz

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