BMRB Entry 10060

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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/BMR10060
MolProbity Validation Chart

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Title:
Solution structure of hypothetical protein C330018D20Rik from Mus musculus
Deposition date:
2006-11-29
Original release date:
2008-08-13
Authors:
Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of hypothetical protein C330018D20Rik from Mus musculus"  .

Assembly members:

Assembly members:
glutaredoxin domain, polymer, 100 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P031125-30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
glutaredoxin domain: GSSGSSGNLSASNRALPVLT LFTKAPCPLCDEAKEVLQPY KDRFILQEVDITLPENSTWY ERYKFDIPVFHLNGQFLMMH RVNTSKLEKQLRKLSGPSSG

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts94
1H chemical shifts699

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1C330018D20rik protein1

Entities:

Entity 1, C330018D20rik protein 100 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASNLEUSER
2   ALASERASNARGALALEUPROVALLEUTHR
3   LEUPHETHRLYSALAPROCYSPROLEUCYS
4   ASPGLUALALYSGLUVALLEUGLNPROTYR
5   LYSASPARGPHEILELEUGLNGLUVALASP
6   ILETHRLEUPROGLUASNSERTHRTRPTYR
7   GLUARGTYRLYSPHEASPILEPROVALPHE
8   HISLEUASNGLYGLNPHELEUMETMETHIS
9   ARGVALASNTHRSERLYSLEUGLULYSGLN
10   LEUARGLYSLEUSERGLYPROSERSERGLY

Samples:

sample_1: glutaredoxin domain, [U-13C; U-15N], 0.6 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 10 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

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SPARKY: Backbone or all simulated peaks