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Structural genomics, unknown function PDB-id
1vdy
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Protein chain
140 a.a. *

* Residue conservation analysis
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PDB id: 1vdy
Name: Structural genomics, unknown function
Title: Nmr structure of the hypothetical enth-vhs domain at3g16270 from arabidopsis thaliana

Structure:
Hypothetical protein (rafl09-17-b18). Chain: a. Fragment: enth-vhs hypothetical domain. Engineered: yes

Source:
Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: riken cdna rafl09-17-b18. Other_details: e.Coli cell-free protein synthesis

UniProt:
Q9C5H4 (Y3627_ARATH) Pfam   ArchSchema ?
Seq:
Struc:
Seq:
Struc:
Seq: 690 a.a.
Struc: 140 a.a.*
Key:    PfamA domain  PfamB domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 11 residue positions (black crosses)

Resolution:
not givenÅ

NMR structure:
20 models

Authors:
B.Lopez-Mendez,D.Pantoja-Uceda,T.Tomizawa,S.Koshiba, T.Kigawa,M.Shirouzu,T.Terada,M.Inoue,T.Yabuki,M.Aoki,E.Seki T.Matsuda,H.Hirota,M.Yoshida,A.Tanaka,T.Osanai,M.Seki, K.Shinozaki,S.Yokoyama,P.Guntert,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:
B.López-Méndez et al. (2004). NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana.. J Biomol NMR, 29, 205-206. [PubMed id: 15014234] [DOI: 10.1023/B:JNMR.0000019239.44783.66]

Date:
25-Mar-04

Release date:
03-May-05

Related entries:
5928 related db: bmrb
chemical shift data
atr001000337 related db: targetdb
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    Key reference    
 
 
DOI no: 10.1023/B:JNMR.0000019239.44783.66 J Biomol NMR 29:205-206 (2004)
PubMed id: 15014234  
 
 
NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana.
B.López-Méndez, D.Pantoja-Uceda, T.Tomizawa, S.Koshiba, T.Kigawa, M.Shirouzu, T.Terada, M.Inoue, T.Yabuki, M.Aoki, E.Seki, T.Matsuda, H.Hirota, M.Yoshida, A.Tanaka, T.Osanai, M.Seki, K.Shinozaki, S.Yokoyama, P.Güntert.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18807026 P.Güntert (2009).
Automated structure determination from NMR spectra.
  Eur Biophys J, 38, 129-143.  
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