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 10275

Title: Solution structures of the PAAD_DAPIN domain of mus musculus interferon-activatable protein 205

Deposition date: 2008-12-15 Original release date: 2009-12-14

Authors: Sato, M.; Tochio, N.; Koshiba, S.; Watanabe, M.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Sato, M.; Tochio, N.; Koshiba, S.; Watanabe, M.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structures of the PAAD_DAPIN domain of mus musculus interferon-activatable protein 205"  .

Assembly members:
Interferon-activable protein 205, polymer, 94 residues, Formula weight is not available

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis   Vector: P051212-10

Entity Sequences (FASTA):
Interferon-activable protein 205: GSSGSSGIVLLRGLECINKH YFSLFKSLLARDLNLERDNQ EQYTTIQIANMMEEKFPADS GLGKLIEFCEEVPALRKRAE ILKKERSESGPSSG

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts90
1H chemical shifts645

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Interferon-activable protein 2051

Entities:

Entity 1, Interferon-activable protein 205 94 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYILEVALLEU
2   LEUARGGLYLEUGLUCYSILEASNLYSHIS
3   TYRPHESERLEUPHELYSSERLEULEUALA
4   ARGASPLEUASNLEUGLUARGASPASNGLN
5   GLUGLNTYRTHRTHRILEGLNILEALAASN
6   METMETGLUGLULYSPHEPROALAASPSER
7   GLYLEUGLYLYSLEUILEGLUPHECYSGLU
8   GLUVALPROALALEUARGLYSARGALAGLU
9   ILELEULYSLYSGLUARGSERGLUSERGLY
10   PROSERSERGLY

Samples:

sample_1: Interferon-activable protein 205, [U-13C; U-15N], 0.5 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

PDB
DBJ BAC37930 BAE29634 BAE31415 BAE31495 BAE38635
EMBL CAJ18559
GB AAA39313 AAB26880 AAH10546 AAI32315 AAI32317
PIR I56329
REF NP_001028622 NP_001288674 NP_032355 XP_006496738
SP P15092 Q08619
AlphaFold P15092 Q08619

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