BMRB Entry 10067

Title:
Solution Structure of The FHA Domain of Arabidopsis thaliana Hypothetical Protein
Deposition date:
2006-12-25
Original release date:
2008-08-14
Authors:
Tomizawa, T.; Inoue, M.; Koshiba, S.; Hayashi, F.; Shirouzu, M.; Terada, T.; Yabuki, T.; Aoki, M.; Matsuda, T.; Seki, E.; Hirota, H.; Yoshida, M.; Tanaka, A.; Osanai, T.; Shinozaki, K.; Seki, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tomizawa, T.; Inoue, M.; Koshiba, S.; Hayashi, F.; Shirouzu, M.; Terada, T.; Yabuki, T.; Aoki, M.; Matsuda, T.; Seki, E.; Hirota, H.; Yoshida, M.; Tanaka, A.; Osanai, T.; Shinozaki, K.; Seki, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of The FHA Domain of Arabidopsis thaliana Hypothetical Protein"  .

Assembly members:

Assembly members:
Forkhead Associated Domain, FHA domain, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P021218-71

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts473
15N chemical shifts113
1H chemical shifts761

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1expressed protein1

Entities:

Entity 1, expressed protein 118 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETVALTHR
2   PROSERLEUARGLEUVALPHEVALLYSGLY
3   PROARGGLUGLYASPALALEUASPTYRLYS
4   PROGLYSERTHRILEARGVALGLYARGILE
5   VALARGGLYASNGLUILEALAILELYSASP
6   ALAGLYILESERTHRLYSHISLEUARGILE
7   GLUSERASPSERGLYASNTRPVALILEGLN
8   ASPLEUGLYSERSERASNGLYTHRLEULEU
9   ASNSERASNALALEUASPPROGLUTHRSER
10   VALASNLEUGLYASPGLYASPVALILELYS
11   LEUGLYGLUTYRTHRSERILELEUVALASN
12   PHEVALSERGLYPROSERSERGLY

Samples:

sample_1: FHA domain, [U-13C; U-15N], 1.09 mM; Tris-HCl 20 mM; NaCl 100 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.820, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
EMBL CAB10228 CAB78491
GB AAM20599 AAM91265 AEE83450
REF NP_193185
SP O23305
AlphaFold O23305

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