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 18280

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for CD81LEL   PubMed: 22740401

Deposition date: 2012-02-20 Original release date: 2013-02-18

Authors: Berditchevski, Fedor; Sridhar, Pooja; Cocquerel, Laurence; Tews, Birke

Citation: Rajesh, Sundaresan; Sridhar, Pooja; Tews, Birke Andrea; Feneant, Lucie; Cocquerel, Laurence; Ward, Douglas; Berditchevski, Fedor; Overduin, Michael. "Structural basis of ligand interactions of the large extracellular domain of tetraspanin CD81."  J. Virol. 86, 9606-9616 (2012).

Assembly members:
CD81_large_extracellular_loop, polymer, 102 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

Entity Sequences (FASTA):
CD81_large_extracellular_loop: GPLGSGFVNKDQIAKDVKQF YDQALQQAVVDDDANNAKAV VKTFHETLDCCGSSTLTALT TSVLKNNLCPSGSNIISNLF KEDCHQKIDDLFSGKLHHHH HH

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts85
1H chemical shifts85

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CD81 LEL1

Entities:

Entity 1, CD81 LEL 102 residues - Formula weight is not available

Residues 107-111 represent vector sequence after GST cleavage and residues 203-208 are the affinity His-tag sequence

1   GLYPROLEUGLYSERGLYPHEVALASNLYS
2   ASPGLNILEALALYSASPVALLYSGLNPHE
3   TYRASPGLNALALEUGLNGLNALAVALVAL
4   ASPASPASPALAASNASNALALYSALAVAL
5   VALLYSTHRPHEHISGLUTHRLEUASPCYS
6   CYSGLYSERSERTHRLEUTHRALALEUTHR
7   THRSERVALLEULYSASNASNLEUCYSPRO
8   SERGLYSERASNILEILESERASNLEUPHE
9   LYSGLUASPCYSHISGLNLYSILEASPASP
10   LEUPHESERGLYLYSLEUHISHISHISHIS
11   HISHIS

Samples:

sample_1: CD81 large extracellular loop, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM; AEBSF protease inhibitor 50 uM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

Analysis_CCPN v2.1, Boucher, CCPN, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, data analysis, data analysis

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
GB AAA36663 AAD11440 AAH02978 AAH93047 AAV38313
REF NP_001009023 NP_001284578 NP_004347 XP_003282135 XP_004050511
SP P60033 P60034

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