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 16463

Title: Backbone and side-chain 1H, 13C and 15N resonance assignments of LEN, a human immunoglobulin kIV light-chain variable domain   PubMed: 19768664

Deposition date: 2009-08-20 Original release date: 2009-11-19

Authors: Mukherjee, Sujoy; Pondaven, Simon; Hofer, Nicole; Jaroniec, Christopher

Citation: Mukherjee, Sujoy; Pondaven, Simon; Hofer, Nicole; Jaroniec, Christopher. "Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain."  Biomol NMR Assign 3, 255-259 (2009).

Assembly members:
LEN, polymer, 114 residues, Formula weight is not available

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: pASK40

Entity Sequences (FASTA):
LEN: DIVMTQSPDSLAVSLGERAT INCKSSQSVLYSSNSKNYLA WYQQKPGQPPKLLIYWASTR ESGVPDRFSGSGSGTDFTLT ISSLQAEDVAVYYCQQYYST PYSFGQGTKLEIKR

Data sets:
Data typeCount
13C chemical shifts429
15N chemical shifts110
1H chemical shifts675

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1light chain variable domain1

Entities:

Entity 1, light chain variable domain 114 residues - Formula weight is not available

1   ASPILEVALMETTHRGLNSERPROASPSER
2   LEUALAVALSERLEUGLYGLUARGALATHR
3   ILEASNCYSLYSSERSERGLNSERVALLEU
4   TYRSERSERASNSERLYSASNTYRLEUALA
5   TRPTYRGLNGLNLYSPROGLYGLNPROPRO
6   LYSLEULEUILETYRTRPALASERTHRARG
7   GLUSERGLYVALPROASPARGPHESERGLY
8   SERGLYSERGLYTHRASPPHETHRLEUTHR
9   ILESERSERLEUGLNALAGLUASPVALALA
10   VALTYRTYRCYSGLNGLNTYRTYRSERTHR
11   PROTYRSERPHEGLYGLNGLYTHRLYSLEU
12   GLUILELYSARG

Samples:

13C_15N-sample: LEN, [U-13C; U-15N], 1.5 mM; H2O 93%; D2O 7%; NaCl 100 mM; Sodium Phosphate 20 mM

15N-sample: LEN, [U-15N], 1.7 mM; H2O 93%; D2O 7%; NaCl 100 mM; Sodium Phosphate 20 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-sampleisotropicsample_conditions_1
3D HNCA13C_15N-sampleisotropicsample_conditions_1
3D HNCACB13C_15N-sampleisotropicsample_conditions_1
3D HNCO13C_15N-sampleisotropicsample_conditions_1
3D HN(CO)CA13C_15N-sampleisotropicsample_conditions_1
3D HCCH-TOCSY13C_15N-sampleisotropicsample_conditions_1
3D 1H-15N TOCSY15N-sampleisotropicsample_conditions_1
3D 1H-15N NOESY15N-sampleisotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAC01688 BAC01708
EMBL CAA26317 CAA81384 CAA83046 CAA86592 CAC10807
GB AAA72130 AAB22366 AAB26921 AAB31509 AAD01817
PIR A49138 S37529
PRF 2001180A 751423A
SP P01625 P06312
AlphaFold P01625 P06312

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