BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19870

Title: Solution Structure of 6aJL2 Amyloidogenic Light Chain Protein

Deposition date: 2014-03-20 Original release date: 2014-06-23

Authors: Amero, Carlos; Maya, Robero; Gil, Paloma

Citation: Maya, Robero; Gil, Paloma; Amero, Carlos. "Solution Structure of 6aJL2 and 6aJL2-R24G Amyloidogenic Light Chain Proteins"  .

Assembly members:
6aJL2, polymer, 111 residues, 11962.002 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET27

Entity Sequences (FASTA):
6aJL2: NFMLTQPHSVSESPGKTVTI SCTRSSGSIASNYVQWYQQR PGSSPTTVIYEDNQRPSGVP DRFSGSIDSSSNSASLTISG LKTEDEADYYCQSYDSSNHV VFGGGTKLTVL

Data sets:
Data typeCount
1H chemical shifts638
15N chemical shifts98
13C chemical shifts384

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
16aJL2 Amyloidogenic Light Chain Protein1

Entities:

Entity 1, 6aJL2 Amyloidogenic Light Chain Protein 111 residues - 11962.002 Da.

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

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 75 mM; D2O 5%; 6aJL2, [U-100% 15N], 1 mM; H2O 95%

sample_2: sodium phosphate 50 mM; sodium chloride 75 mM; D2O 5%; 6aJL2, [U-100% 13C; U-100% 15N], 1 mM; H2O 95%

sample_conditions: temperature: 298 K; pH: 7.4; pressure: 1 atm; ionic strength: 75 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions
3D HNCACBsample_2isotropicsample_conditions
3D HNCAsample_2isotropicsample_conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions
3D CBCA(CO)NHsample_2isotropicsample_conditions
3D HNCOsample_2isotropicsample_conditions
3D HCCH-TOCSYsample_2isotropicsample_conditions
3D HCACOsample_2isotropicsample_conditions

Software:

NMRView v5.2.2_01, Johnson, One Moon Scientific - peak picking

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution, refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA, Rochus L.J. Keller - chemical shift assignment

NMR spectrometers:

  • Varian Uniform NMR System 700 MHz

Related Database Links:

BMRB 15276 19798
PDB
DBJ BAA19991 BAC01822 BAC01823 BAC01857 BAC01860
EMBL CAA85625 CAD43014 CAJ75494 CAJ75495 CAP74492
GB AAB33217 AAG24684 AAG24687 AAG24688 AAG24689

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