BMRB Entry 51171

Name: Characterization of amyloidogenic conformations of monomeric transthyretin from ground-state and excited state NMR Chemical shifts
Published: 2024-02-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51171

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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:

Characterization of amyloidogenic conformations of monomeric transthyretin from ground-state and excited state NMR Chemical shifts

Deposition date:

2021-11-08

Original release date:

2024-02-16

Authors:

Leach, Benjamin; Morgan, Gareth; Ferguson, James; Oyen, David; Kelly, Jeffrey; Dyson, H. Jane; Wright, Peter

Citation:

Citation: Leach, Benjamin; Morgan, Gareth; Ferguson, James; Oyen, David; Kelly, Jeffrey; Dyson, H. Jane; Wright, Peter. "Characterization of amyloidogenic intermediates of Transthyretin from ground-state and excited-state NMR Chemical shifts" .

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 29a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGPTGTGESKCPLMVKVLDA VRGSPAINVAVHVFRKAADD TWEPFASGKTSESGELHGLT TEEEFVEGIYKVEIDTKSYW KALGISPEHEHAEVVFTAND SGPRRYTIAALLSPYSYSTT AVVTNPKE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	224
15N chemical shifts	104
1H chemical shifts	104

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TTR F87E	1

Entities:

Entity 1, TTR F87E 128 residues - Formula weight is not available

1

MET

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

ALA

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

GLU

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 F87E, [U-13C; U-15N], 400 uM; Bis Tris 50 uM; MES 50 uM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.1 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 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 HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2 - collection

NMRPipe v9.4 - processing

CoMD/NMR - processing

NMRFAM-SPARKY v1.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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