BMRB Entry 11308

Title:
Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus"  .

Assembly members:

Assembly members:
C2H2 zinc finger domain, polymer, 121 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: P040126-40

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts112
1H chemical shifts809

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C2H2 zinc finger domain1
2ZINC ION2

Entities:

Entity 1, C2H2 zinc finger domain 121 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUPROALA
2   HISGLYARGGLNHISTHRPROCYSLEUPHE
3   CYSASPARGLEUPHEALASERALAGLUGLU
4   THRPHESERHISCYSLYSLEUGLUHISGLN
5   PHEASNILEASPSERMETVALHISLYSHIS
6   GLYLEUGLUPHETYRGLYTYRILELYSLEU
7   ILEASNPHEILEARGLEULYSASNPROTHR
8   VALGLUTYRMETASNSERILETYRASNPRO
9   VALPROTRPGLULYSASPGLUTYRLEULYS
10   PROVALLEUGLUASPASPLEULEULEUGLN
11   PHEASPVALGLUASPLEUTYRGLUPROVAL
12   SERTHRPROPHESERSERGLYPROSERSER
13   GLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: C2H2 zinc finger domain, [U-13C; U-15N], 1.14 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.1 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

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

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAC25300 BAC27531 BAC39708 BAG60456
GB AAH50775 AAN84530 EAW68334 EDL22978 ERE78768
REF NP_001138639 NP_598501 XP_003254364 XP_004711656 XP_005578451
SP Q922H1
AlphaFold Q922H1

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