BMRB Entry 51708

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51708

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Title:
Solution state chemical shift NMR assignment of human l-III immunoglobulin light chain FOR005_GL
Deposition date:
2022-11-24
Original release date:
2023-05-16
Authors:
Pradhan, Tejaswini; Sarkar, Riddhiman; Zacharias, Martin; Reif, Bernd
Citation:

Citation: Pradhan, Tejaswini; Sarkar, Riddhiman; Meighen-Berger, Kevin; Feige, Matthias; Zacharias, Martin; Reif, Bernd. "Mechanistic insights into the aggregation pathway of the patient-derived immunoglobulin light chain variable domain protein FOR005"  Nat. commun. 14, 3755-3755 (2023).
PubMed: 37353525

Assembly members:

Assembly members:
entity_1, polymer, 110 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: pET 28(b+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSSELTQDPAVSVALGQTVR ITCQGDSLRSYYASWYQQKP GQAPVLVIYGKNNRPSGIPD RFSGSSSGNTASLTITGAQA EDEADYYCNSRDSSGNHQVF GGGTKLTVLG

Data sets:
Data typeCount
13C chemical shifts190
15N chemical shifts101
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VL1

Entities:

Entity 1, VL 110 residues - Formula weight is not available

1   GLYSERSERGLULEUTHRGLNASPPROALA
2   VALSERVALALALEUGLYGLNTHRVALARG
3   ILETHRCYSGLNGLYASPSERLEUARGSER
4   TYRTYRALASERTRPTYRGLNGLNLYSPRO
5   GLYGLNALAPROVALLEUVALILETYRGLY
6   LYSASNASNARGPROSERGLYILEPROASP
7   ARGPHESERGLYSERSERSERGLYASNTHR
8   ALASERLEUTHRILETHRGLYALAGLNALA
9   GLUASPGLUALAASPTYRTYRCYSASNSER
10   ARGASPSERSERGLYASNHISGLNVALPHE
11   GLYGLYGLYTHRLYSLEUTHRVALLEUGLY

Samples:

sample_1: Immunoglobulin light chain variable domain, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.1 - collection, processing

CcpNMR vv2 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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