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 10130

Title: Solution structure of a novel beta-grasp fold like domain of Hypothetical protein (Arabidopsis thaliana)

Authors: Qin, X.; Hayashi, F.; Yokoyama, S.

Citation: Qin, X.; Hayashi, F.; Yokoyama, S.. "Solution structure of a novel beta-grasp fold like domain of Hypothetical protein (Arabidopsis thaliana)"  Not known ., .-..

Assembly members:
Hypothetical domain, polymer, 107 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):
Hypothetical domain: GSSGSSGTMLRVRSRDGLER VSVDGPHITVSQLKTLIQDQ LQIPIHNQTLSTNRNLLLAK SPSDFLAFTDMADPNLRISS LNLAHGSMVYLAYEGERTIR GSGPSSG

Data sets:
Data typeCount
13C chemical shifts457
15N chemical shifts111
1H chemical shifts737

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NPL4 family protein1

Entities:

Entity 1, NPL4 family protein 107 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRMETLEU
2   ARGVALARGSERARGASPGLYLEUGLUARG
3   VALSERVALASPGLYPROHISILETHRVAL
4   SERGLNLEULYSTHRLEUILEGLNASPGLN
5   LEUGLNILEPROILEHISASNGLNTHRLEU
6   SERTHRASNARGASNLEULEULEUALALYS
7   SERPROSERASPPHELEUALAPHETHRASP
8   METALAASPPROASNLEUARGILESERSER
9   LEUASNLEUALAHISGLYSERMETVALTYR
10   LEUALATYRGLUGLYGLUARGTHRILEARG
11   GLYSERGLYPROSERSERGLY

Samples:

sample_1: Hypothetical domain, [U-13C; U-15], 1.07 mM; PiNa 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.854, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
EMBL CAB87745
GB AAK59569 AAL07248 ABG89129 AEE80422
REF NP_191859
SP Q9LYC2