BMRB Entry 27576

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for A97S TTR in 5% DMSO
Published: 2018-09-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27576

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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 1H, 13C, and 15N Chemical Shift Assignments for A97S TTR in 5% DMSO

Deposition date:

2018-08-13

Original release date:

2018-09-12

Authors:

Yu, Tsyr-Yan; Yen, Yueh-Jung; Chang, Yu; Huang, Shing-Jong

Citation:

Citation: Liu, Yo-Tsen; Yen, Yueh-Jung; Ricardo, Frans; Chang, Yu; Wu, Pei-Hao; Huang, Shing-Jong; Lin, Kon-Ping; Yu, Tsyr-Yan. "Biophysical characterization and modulation of Transthyretin Ala97Ser" Ann. Clin. Transl. Neurol. 6, 1961-1970 (2019).
PubMed: 31502419

Assembly members:

Assembly members:
A97S_TTR, polymer, 127 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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A97S_TTR: GPTGTGESKCPLMVKVLDAV RGSPAINVAVHVFRKAADDT WEPFASGKTSESGELHGLTT EEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTSNDS GPRRYTIAALLSPYSYSTTA VVTNPKE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	126
15N chemical shifts	117
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	A97S TTR	1

Entities:

Entity 1, A97S TTR 127 residues - Formula weight is not available

A97S mutation

1

GLY

PRO

THR

GLY

THR

GLY

GLU

SER

LYS

CYS

2

PRO

LEU

MET

VAL

LYS

VAL

LEU

ASP

ALA

VAL

3

ARG

GLY

SER

PRO

ALA

ILE

ASN

VAL

ALA

VAL

4

HIS

VAL

PHE

ARG

LYS

ALA

ASP

THR

5

TRP

GLU

PRO

PHE

ALA

SER

GLY

LYS

THR

SER

6

GLU

SER

GLY

GLU

LEU

HIS

GLY

LEU

THR

7

GLU

PHE

VAL

GLU

GLY

ILE

TYR

LYS

8

VAL

GLU

ILE

ASP

THR

LYS

SER

TYR

TRP

LYS

9

ALA

LEU

GLY

ILE

SER

PRO

PHE

HIS

GLU

HIS

10

ALA

GLU

VAL

PHE

THR

SER

ASN

ASP

SER

11

GLY

PRO

ARG

TYR

THR

ILE

ALA

LEU

12

LEU

SER

PRO

TYR

SER

TYR

SER

THR

ALA

13

VAL

THR

ASN

PRO

LYS

GLU

Samples:

sample_1: A97S TTR, [U-13C; U-15N; U-2H], 0.75 mM; D2O, [U-99% 2H], 6%; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 0.5 mM; DMSO 5%; TCEP 1 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 37 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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA, Rochus Keller - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 850 MHz

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