BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19798

Title: Solution Structure of 6aJL2-R24G Amyloidogenic Light Chain Protein

Deposition date: 2014-02-13 Original release date: 2014-06-16

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

Citation: Maya, Roberto; Gil, Paloma; Amero, Carlos. "Solution Structure of 6aJL2 and 6aJL2-R24G Amyloidogenic Light Chain Proteins"  Not known ., .-..

Assembly members:
entity, polymer, 111 residues, 11861.857 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

Entity Sequences (FASTA):
entity: NFMLTQPHSVSESPGKTVTI SCTGSSGSIASNYVQWYQQR PGSSPTTVIYEDNQRPSGVP DRFSGSIDSSSNSASLTISG LKTEDEADYYCQSYDSSNHV VFGGGTKLTVL

Data sets:
Data typeCount
1H chemical shifts677
15N chemical shifts104
13C chemical shifts392

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
16aJL2-R24G Amyloidogenic Light Chain Protein1

Entities:

Entity 1, 6aJL2-R24G Amyloidogenic Light Chain Protein 111 residues - 11861.857 Da.

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: protein, [U-100% 13C; U-100% 15N], 0.8 – 1.2 mM; sodium phosphate 50 mM; sodium chloride 75 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 75 mM; pH: 7.4; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH v2.33, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

CARA v1.8.4, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Varian Uniform NMR System 700 MHz

Related Database Links:

BMRB 15276 19870
PDB
DBJ BAA19991 BAC01822 BAC01823 BAC01824 BAC01857
EMBL CAD43014 CAJ75494 CAJ75495 CAP74492 CAP74493
GB AAB33217 AAG24687 AAG24691 AAG47681 AAM46210

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