BMRB Entry 27513

Name: NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations
Published: 2019-01-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27513

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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:

NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations

Deposition date:

2018-06-08

Original release date:

2019-01-07

Authors:

Wright, Peter; Leach, Benjamin; Zhang, Xin; Kelly, Jeffery; Dyson, Jane

Citation:

Citation: Leach, Benjamin; Zhang, Xin; Kelly, Jeffery; Dyson, Jane; Wright, Peter. "NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations" Biochemistry 57, 4421-4430 (2018).
PubMed: 29972637

Assembly members:

Assembly members:
L55P, polymer, 147 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 29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L55P: MASHRLLLLCLAGLVFVSEA GPTGTGESKCPLMVKVLDAV RGSPAINVAVHVFRKAADDT WEPFASGKTSESGEPHGLTT EEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDS GPRRYTIAALLSPYSYSTTA VVTNPKE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	121
15N chemical shifts	114
1H chemical shifts	114

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Transthyretin	1

Entities:

Entity 1, Transthyretin 147 residues - Formula weight is not available

1

MET

ALA

SER

HIS

ARG

LEU

CYS

2

LEU

ALA

GLY

LEU

VAL

PHE

VAL

SER

GLU

ALA

3

GLY

PRO

THR

GLY

THR

GLY

GLU

SER

LYS

CYS

4

PRO

LEU

MET

VAL

LYS

VAL

LEU

ASP

ALA

VAL

5

ARG

GLY

SER

PRO

ALA

ILE

ASN

VAL

ALA

VAL

6

HIS

VAL

PHE

ARG

LYS

ALA

ASP

THR

7

TRP

GLU

PRO

PHE

ALA

SER

GLY

LYS

THR

SER

8

GLU

SER

GLY

GLU

PRO

HIS

GLY

LEU

THR

9

GLU

PHE

VAL

GLU

GLY

ILE

TYR

LYS

10

VAL

GLU

ILE

ASP

THR

LYS

SER

TYR

TRP

LYS

11

ALA

LEU

GLY

ILE

SER

PRO

PHE

HIS

GLU

HIS

12

ALA

GLU

VAL

PHE

THR

ALA

ASN

ASP

SER

13

GLY

PRO

ARG

TYR

THR

ILE

ALA

LEU

14

LEU

SER

PRO

TYR

SER

TYR

SER

THR

ALA

15

VAL

THR

ASN

PRO

LYS

GLU

Samples:

sample_1: sodium phosphate 10 mM; potassium chloride 100 mM; 2H Transthyretin L55P, [U-13C; U-15N; U-2H;], 800 uM

sample_conditions_1: ionic strength: 100 mM; pH: 7; 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

Software:

xwinnmr, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, collection, processing

NMR spectrometers:

Bruker AMX 750 MHz

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