BMRB Entry 53014

Name: Backbone chemical shifts for TTR A25T
Published: 2025-05-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53014

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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:

Backbone chemical shifts for TTR A25T

Deposition date:

2025-04-07

Original release date:

2025-05-08

Authors:

Sun, Xun; Dyson, Jane; Wright, Peter

Citation:

Citation: Sun, Xun; Ferguson, James; Leach, Benjamin; Stanfield, Robyn; Dyson, H Jane; Wright, Peter. "Probing the Dissociation Pathway of a Kinetically Labile Transthyretin Mutant." J. Am. Chem. Soc. 146, 532-542 (2024).
PubMed: 38134439

Assembly members:

Assembly members:
entity_1, polymer, 128 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: pET29

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGPTGTGESKCPLMVKVLDA VRGSPTINVAVHVFRKAADD TWEPFASGKTSESGELHGLT TEEEFVEGIYKVEIDTKSYW KALGISPFHEHAEVVFTAND SGPRRYTIAALLSPYSYSTT AVVTNPKE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	82
15N chemical shifts	74
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TTR A25T	1

Entities:

Entity 1, TTR A25T 128 residues - Formula weight is not available

1

GLY

PRO

THR

GLY

THR

GLY

GLU

SER

LYS

2

CYS

PRO

LEU

MET

VAL

LYS

VAL

LEU

ASP

ALA

3

VAL

ARG

GLY

SER

PRO

THR

ILE

ASN

VAL

ALA

4

VAL

HIS

VAL

PHE

ARG

LYS

ALA

ASP

5

THR

TRP

GLU

PRO

PHE

ALA

SER

GLY

LYS

THR

6

SER

GLU

SER

GLY

GLU

LEU

HIS

GLY

LEU

THR

7

THR

GLU

PHE

VAL

GLU

GLY

ILE

TYR

8

LYS

VAL

GLU

ILE

ASP

THR

LYS

SER

TYR

TRP

9

LYS

ALA

LEU

GLY

ILE

SER

PRO

PHE

HIS

GLU

10

HIS

ALA

GLU

VAL

PHE

THR

ALA

ASN

ASP

11

SER

GLY

PRO

ARG

TYR

THR

ILE

ALA

12

LEU

SER

PRO

TYR

SER

TYR

SER

THR

13

ALA

VAL

THR

ASN

PRO

LYS

GLU

Samples:

sample_1: TTR A25T, [U-100% 13C; U-100% 15N; U-80% 2H], 390 uM; D2O, [U-2H], 10%; KPi 10 mM; KCl 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRView - 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