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 10108

Title: Solution Structure of DC1 Domain of PDI-like Hypothetical Protein from Arabidopsis thaliana

Deposition date: 2007-02-13 Original release date: 2008-08-29

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

Citation: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of DC1 Domain of PDI-like Hypothetical Protein from Arabidopsis thaliana"  .

Assembly members:
PDI-like Hypothetical Protein At1g60420, polymer, 89 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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

Experimental source:   Production method: cell free synthesis   Vector: P030421-05

Entity Sequences (FASTA):
PDI-like Hypothetical Protein At1g60420: GSSGSSGTEERLKEIEAKYD EIAKDWPKKVKHVLHEEHEL ELTRVQVYTCDKCEEEGTIW SYHCDECDFDLHAKCALNED TKESGPSSG

Data sets:
Data typeCount
13C chemical shifts353
15N chemical shifts80
1H chemical shifts541

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDI-like Hypothetical Protein At1g604201
2zinc ion, 12
3zinc ion, 22

Entities:

Entity 1, PDI-like Hypothetical Protein At1g60420 89 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLUGLU
2   ARGLEULYSGLUILEGLUALALYSTYRASP
3   GLUILEALALYSASPTRPPROLYSLYSVAL
4   LYSHISVALLEUHISGLUGLUHISGLULEU
5   GLULEUTHRARGVALGLNVALTYRTHRCYS
6   ASPLYSCYSGLUGLUGLUGLYTHRILETRP
7   SERTYRHISCYSASPGLUCYSASPPHEASP
8   LEUHISALALYSCYSALALEUASNGLUASP
9   THRLYSGLUSERGLYPROSERSERGLY

Entity 2, zinc ion, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: DC1 Domain, [U-13C; U-15N], 1.05 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: 298 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 v0.863, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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