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 5843

Title: Solution Structure of At3g17210

Authors: Volkman, B.

Citation: Lytle, Betsy; Peterson, Francis; Kjer, Kelly; Frederick, Ronnie; Zhao, Qin; Thao, Sandy; Bingman, Craig; Johnson, Kenneth; Phillips, Georage; Volkman, Brian. "Letter to the Editor: Structure of the hypothetical protein At3g17210 from Arabidopsis thaliana"  J. Biomol. NMR 28, 397-400 (2004).

Assembly members:
expressed protein At3g17210.1, polymer, 112 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: recombinant technology

Entity Sequences (FASTA):
expressed protein At3g17210.1: GSHMEEAKGPVKHVLLASFK DGVSPEKIEELIKGYANLVN LIEPMKAFHWGKDVSIENLH QGYTHIFESTFESKEAVAEY IAHPAHVEFATIFLGSLDKV LVIDYKPTSVSL

Data sets:
Data typeCount
1H chemical shifts776
13C chemical shifts493
15N chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein At3g17210, chain 11
2hypothetical protein At3g17210, chain 21

Entities:

Entity 1, hypothetical protein At3g17210, chain 1 112 residues - Formula weight is not available

1   GLYSERHISMETGLUGLUALALYSGLYPRO
2   VALLYSHISVALLEULEUALASERPHELYS
3   ASPGLYVALSERPROGLULYSILEGLUGLU
4   LEUILELYSGLYTYRALAASNLEUVALASN
5   LEUILEGLUPROMETLYSALAPHEHISTRP
6   GLYLYSASPVALSERILEGLUASNLEUHIS
7   GLNGLYTYRTHRHISILEPHEGLUSERTHR
8   PHEGLUSERLYSGLUALAVALALAGLUTYR
9   ILEALAHISPROALAHISVALGLUPHEALA
10   THRILEPHELEUGLYSERLEUASPLYSVAL
11   LEUVALILEASPTYRLYSPROTHRSERVAL
12   SERLEU

Samples:

sample_1: expressed protein At3g17210.1, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 70 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1not availablesample_cond_1
3D 13C-separated NOESYsample_1not availablesample_cond_1
3D HNCOsample_1not availablesample_cond_1
3D HNCACOsample_1not availablesample_cond_1
3D HNCAsample_1not availablesample_cond_1
3D HNCOCAsample_1not availablesample_cond_1
3D HNCACBsample_1not availablesample_cond_1
3D CCONHsample_1not availablesample_cond_1
3D 15N-edited TOCSY-HSQCsample_1not availablesample_cond_1
HCCH-TOCSYsample_1not availablesample_cond_1
15N-1H HSQCsample_1not availablesample_cond_1
3D 13C-separated NOESY (arom)sample_1not availablesample_cond_1

Software:

XWINNMR v3.0 - collection

NMRPIPE v97.027.12.56 - processing

XEASY v1.4 - data analysis

CYANA v1.0.6 - structure solution, refinement

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAB02723 BAF02259
GB AAK43839 AAL47379 AAM63750 AEE75921
REF NP_566569
SP Q9LUV2