BMRB Entry 27602

Title:
13C-15N solid-state chemical shifts of three polymorphs of 6aJL2-R24G amyloid fibrils
Deposition date:
2018-09-11
Original release date:
2019-02-06
Authors:
Lecoq, Lauriane; Wiegand, Thomas; Cadalbert, Riccardo; del Pozo-Yauner, Luis; Meier, Beat; Bockmann, Anja
Citation:

Citation: Lecoq, Lauriane; Wiegand, Thomas; Rodriguez-Alvarez, Francisco; Cadalbert, Riccardo; Herrera, Guillermo; Del Pozo-Yauner, Luis; Meier, Beat; Bockmann, Anja. "A Substantial Structural Conversion of the Native Monomer Leads to In-Register Parallel Amyloid Fibril Formation in Light Chain Amyloidosis"  Chembiochem 20, 1027-1031 (2019).
PubMed: 30565364

Assembly members:

Assembly members:
6aJL2, polymer, 111 residues, 11853.8 Da.

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: pET27b

Data sets:
Data typeCount
13C chemical shifts557
15N chemical shifts158

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
16aJL21

Entities:

Entity 1, 6aJL2 111 residues - 11853.8 Da.

R24G mutation (increased fibrillogenicity)

1   ASNPHEMETLEUTHRGLNPROHISSERVAL
2   SERGLUSERPROGLYLYSTHRVALTHRILE
3   SERCYSTHRGLYSERSERGLYSERILEALA
4   SERASNTYRVALGLNTRPTYRGLNGLNARG
5   PROGLYSERSERPROTHRTHRVALILETYR
6   GLUASPASNGLNARGPROSERGLYVALPRO
7   ASPARGPHESERGLYSERILEASPSERSER
8   SERASNSERALASERLEUTHRILESERGLY
9   LEULYSTHRGLUASPGLUALAASPTYRTYR
10   CYSGLNSERTYRASPSERSERASNHISVAL
11   VALPHEGLYGLYGLYTHRLYSLEUTHRVAL
12   LEU

Samples:

sample_1: 6aJL2, [U-100% 13C; U-100% 15N], 0.25 mg/mL; DSS 0.3 mM

sample_2: 6aJL2, [U-100% 13C; U-100% 15N], 0.25 mg/mL; DSS 0.3 mM

mixed_labeled_sample_3: 6aJL2, [U-100% 15N], 0.25 mg/mL; 6aJL2, [U-100% 13C], 0.25 mg/mL; DSS 0.3 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D DARR C-C 20 mssample_1isotropicsample_conditions_1
3D NCACXsample_1isotropicsample_conditions_1
3D NCACBsample_1isotropicsample_conditions_1
3D NCOCXsample_1isotropicsample_conditions_1
2D NCAsample_1isotropicsample_conditions_1
2D NCOsample_1isotropicsample_conditions_1
3D CANCOsample_1isotropicsample_conditions_1
2D INEPT H-Csample_1isotropicsample_conditions_1
2D DARR C-C 20 mssample_2isotropicsample_conditions_1
3D CCCsample_2isotropicsample_conditions_1
3D NCACBsample_2isotropicsample_conditions_1
3D NCACXsample_2isotropicsample_conditions_1
3D NCOCXsample_2isotropicsample_conditions_1
2D NCAsample_2isotropicsample_conditions_1
2D NCOsample_2isotropicsample_conditions_1
3D CANCOsample_2isotropicsample_conditions_1
2D INEPT H-Csample_2isotropicsample_conditions_1
2D INEPT TOBSY C-Csample_2isotropicsample_conditions_1
2D DARR C-C 20 msmixed_labeled_sample_3isotropicsample_conditions_1
2D PAIN N-Cmixed_labeled_sample_3isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

CcpNmr v2.4.2, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

UNP P01721 Q5NV88
PDB
AlphaFold Q5NV88 P06319