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 26879

Title: Solid-state NMR 13C and 15N chemical shift assignments for AL-09 VL immunoglobulin light chain fibrils   PubMed: 27771830

Deposition date: 2016-08-16 Original release date: 2017-02-16

Authors: Piehl, Dennis; Blancas-Mejia, Luis; Ramirez-Alvarado, Marina; Rienstra, Chad

Citation: Piehl, Dennis; Blancas-Mejia, Luis; Ramirez-Alvarado, Marina; Rienstra, Chad. "Solid-state NMR chemical shift assignments for AL-09 VL immunoglobulin light chain fibrils"  Biomol. NMR Assignments 11, 45-50 (2017).

Assembly members:
AL-09_VL_fibrils, polymer, 110 residues, 12121.3024 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):
AL-09_VL_fibrils: STDIQMTQSPSSLSASVGDR VTITCQASQDINNYLIWYQQ KPGQAPKLLIYDASTLETGV PSRFSGSGSGTEFTFTISSL QPEDLATYHCQQYDNLPYTF GQGTKLEIKR

Data sets:
Data typeCount
13C chemical shifts188
15N chemical shifts54

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1AL-09 VL light chain protein1

Entities:

Entity 1, AL-09 VL light chain protein 110 residues - 12121.3024 Da.

Variable domain sequence of AL-09 light chain protein. Contains two N-terminal residue purification artifacts, S-1 and T0.

1   SERTHRASPILEGLNMETTHRGLNSERPRO
2   SERSERLEUSERALASERVALGLYASPARG
3   VALTHRILETHRCYSGLNALASERGLNASP
4   ILEASNASNTYRLEUILETRPTYRGLNGLN
5   LYSPROGLYGLNALAPROLYSLEULEUILE
6   TYRASPALASERTHRLEUGLUTHRGLYVAL
7   PROSERARGPHESERGLYSERGLYSERGLY
8   THRGLUPHETHRPHETHRILESERSERLEU
9   GLNPROGLUASPLEUALATHRTYRHISCYS
10   GLNGLNTYRASPASNLEUPROTYRTHRPHE
11   GLYGLNGLYTHRLYSLEUGLUILELYSARG

Samples:

sample_1: AL-09 VL fibrils, [U-13C; U-15N], 50 % w/w; H2O 50 % w/w

sample_conditions_1: pH: 7; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
NCACX 25 ms DARRsample_1isotropicsample_conditions_1
NCOCX 25 ms DARRsample_1isotropicsample_conditions_1
CANcoCX 25 ms DARRsample_1isotropicsample_conditions_1
CANCOsample_1isotropicsample_conditions_1
NCA(CB)CO SPC7sample_1isotropicsample_conditions_1
NCOCA SPC7sample_1isotropicsample_conditions_1
NCACX 90 ms DARRsample_1isotropicsample_conditions_1
NCOCX 90 ms DARRsample_1isotropicsample_conditions_1
CC 40 ms DARRsample_1isotropicsample_conditions_1
CCC SPC7 + 50 ms DARRsample_1isotropicsample_conditions_1

Software:

SPARKY v3.116, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian InfinityPlus 600 MHz
  • Varian InfinityPlus 600 MHz
  • Varian VNMRS 750 MHz
  • Varian VNMRS 500 MHz

Related Database Links:

UNP A2NI60 P01594
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