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 10090

Title: Solution structure of hypothetical protein F20O9.120 from Arabidopsis thaliana

Deposition date: 2007-01-24 Original release date: 2008-08-14

Authors: Sato, M.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Sato, M.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of hypothetical protein F20O9.120 from Arabidopsis thaliana"  . ., .-..

Assembly members:
residues 14-145, polymer, 145 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
residues 14-145: GSSGSSGSTVKRKPVFVKVE QLKPGTTGHTLTVKVIEANI VVPVTRKTRPASSLSRPSQP SRIVECLIGDETGCILFTAR NDQVDLMKPGATVILRNSRI DMFKGTMRLGVDKWGRIEAT GAASFTVKEDNNLSLVEYES GPSSG

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts130
1H chemical shifts952

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein F20O9.1201

Entities:

Entity 1, hypothetical protein F20O9.120 145 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERTHRVAL
2   LYSARGLYSPROVALPHEVALLYSVALGLU
3   GLNLEULYSPROGLYTHRTHRGLYHISTHR
4   LEUTHRVALLYSVALILEGLUALAASNILE
5   VALVALPROVALTHRARGLYSTHRARGPRO
6   ALASERSERLEUSERARGPROSERGLNPRO
7   SERARGILEVALGLUCYSLEUILEGLYASP
8   GLUTHRGLYCYSILELEUPHETHRALAARG
9   ASNASPGLNVALASPLEUMETLYSPROGLY
10   ALATHRVALILELEUARGASNSERARGILE
11   ASPMETPHELYSGLYTHRMETARGLEUGLY
12   VALASPLYSTRPGLYARGILEGLUALATHR
13   GLYALAALASERPHETHRVALLYSGLUASP
14   ASNASNLEUSERLEUVALGLUTYRGLUSER
15   GLYPROSERSERGLY

Samples:

sample_1: residues 14-145, [U-13C; U-15N], 0.8 mM; d-Tris HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_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 v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
EMBL CAA16883 CAB79646
GB AAK93582 AAL08288 AAM14346 AAM65628 AEE85487
REF NP_194573 XP_002869502
SP O49453

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