BMRB Entry 11161

Title:
Solution structure of the Zinc finger, C3HC4 type (RING finger) domain Tripartite motif protein 30
Deposition date:
2010-04-15
Original release date:
2011-05-05
Authors:
Abe, H.; Miyamoto, K.; Tochio, N.; Yoneyama, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Abe, H.; Miyamoto, K.; Tochio, N.; Yoneyama, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the Zinc finger, C3HC4 type (RING finger) domain Tripartite motif protein 30"  .

Assembly members:

Assembly members:
RING-type, residues 6-85, polymer, 85 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P060417-23

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts347
15N chemical shifts81
1H chemical shifts553

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RING-type, residues 6-851
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, RING-type, residues 6-85 85 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETALASER
2   SERVALLEUGLUMETILELYSGLUGLUVAL
3   THRCYSPROILECYSLEUGLULEULEULYS
4   GLUPROVALSERALAASPCYSASNHISSER
5   PHECYSARGALACYSILETHRLEUASNTYR
6   GLUSERASNARGASNTHRASPGLYLYSGLY
7   ASNCYSPROVALCYSARGVALPROTYRPRO
8   PHEGLYASNLEULYSPROASNLEUHISVAL
9   ALAASNILEVALGLU

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: RING-type, residues 6-85, [U-13C; U-15N], 1.13 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 50 uM; IDA 1 mM; H2O 90%; D2O 10%

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

Experiments:

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

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9747, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAE22032 BAE23387 BAE23595
GB AAA40073 AAG53468 AAG53469 AAH05447 EDL16723
REF NP_033125 XP_006507534
SP P15533
AlphaFold P15533

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