BMRB Entry 50211

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50211

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Title:
Solution-state NMR assignments of the patient FOR005 l-III immunoglobulin light chain variable domain
Deposition date:
2020-03-17
Original release date:
2020-09-18
Authors:
Pradhan, Tejaswini; Annamalai, Karthikeyan; Sarkar, Riddhiman; Hegenbart, Ute; Schonland, Stefan; Fandrich, Marcus; Reif, Bernd
Citation:

Citation: Pradhan, Tejaswini; Annamalai, Karthikeyan; Sarkar, Riddhiman; Hegenbart, Ute; Schonland, Stefan; Fandrich, Marcus; Reif, Bernd. "Solid state NMR assignments of a human l-III immunoglobulin light chain amyloid fibrils"  Biomol. NMR Assign. 15, 9-16 (2021).
PubMed: 32946005

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 ITCQGDSLRSYSASWYQQKP GQAPVLVIFRKSNRPSGIPD RFSGSSSGNTASLTITGAQA EDEADYYCNSRDSSANHQVF GGGTKLTVLG

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts95
1H chemical shifts95

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Immunoglobulin light chain1

Entities:

Entity 1, Immunoglobulin light chain 110 residues - Formula weight is not available

1   GLYSERSERGLULEUTHRGLNASPPROALA
2   VALSERVALALALEUGLYGLNTHRVALARG
3   ILETHRCYSGLNGLYASPSERLEUARGSER
4   TYRSERALASERTRPTYRGLNGLNLYSPRO
5   GLYGLNALAPROVALLEUVALILEPHEARG
6   LYSSERASNARGPROSERGLYILEPROASP
7   ARGPHESERGLYSERSERSERGLYASNTHR
8   ALASERLEUTHRILETHRGLYALAGLNALA
9   GLUASPGLUALAASPTYRTYRCYSASNSER
10   ARGASPSERSERALAASNHISGLNVALPHE
11   GLYGLYGLYTHRLYSLEUTHRVALLEUGLY

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 1 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

CcpNMR vV2, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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