BMRB Entry 6384

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6384
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution Structure of TACI_D2
Deposition date:
2004-11-10
Original release date:
2005-01-14
Authors:
Hymowitz, S.; Patel, D.; Wallweber, H.; Runyon, S.; Yan, M.; Yin, J.; Shriver, S.; Gordon, N.; Pan, B.; Skelton, N.; Kelley, R.; Starovasnik, M.
Citation:

Citation: Hymowitz, S.; Patel, D.; Wallweber, H.; Runyon, S.; Yan, M.; Yin, J.; Shriver, S.; Gordon, N.; Pan, B.; Skelton, N.; Kelley, R.; Starovasnik, M.. "Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high-affinity ligand binding"  J. Biol. Chem. 280, 7218-7227 (2005).
PubMed: 15542592

Assembly members:

Assembly members:
TACI_D2, polymer, 46 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: pET32-tacid2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TACI_D2: GSPWSLSCRKEQGKFYDHLL RDCISCASICGQHPKQCAYF CENKLR

Data sets:
Data typeCount
13C chemical shifts150
15N chemical shifts45
1H chemical shifts270

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TACI_D21

Entities:

Entity 1, TACI_D2 46 residues - Formula weight is not available

1   GLYSERPROTRPSERLEUSERCYSARGLYS
2   GLUGLNGLYLYSPHETYRASPHISLEULEU
3   ARGASPCYSILESERCYSALASERILECYS
4   GLYGLNHISPROLYSGLNCYSALATYRPHE
5   CYSGLUASNLYSLEUARG

Samples:

sample_1: TACI_D2, [U-13C; U-15N], 0.8 – 1.0 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 1 mM; D2O 10%

sample_cond_1: ionic strength: 200 mM; pH: 7.2; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-SEPARATED NOESYnot availablenot availablenot available
3D 13C-SEPARATED NOESYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D 13C HSQCnot availablenot availablenot available
3D-HNHBnot availablenot availablenot available

Software:

TALOS v2002 - refinement

CNX v2002 - refinement

FELIX v2000.1 - structure solution

SPARKY v3.11 - structure solution

XWINNMR v3.5 - structure solution

CYANA v1.1 - structure solution

NMR spectrometers:

  • BRUKER DRX 800 MHz

Related Database Links:

PDB
DBJ BAD97173 BAE16555 BAG36107 BAG64372
GenBank AAC51790 AAI09393 AAP57629 ABK41894 EAW55728
REF NP_036584 XP_001161260 XP_001161317 XP_001161361
SWISS-PROT O14836

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