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PDBsum entry 2jwt

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protein links
Transcription PDB id
2jwt
Jmol
Contents
Protein chain
61 a.a. *
* Residue conservation analysis
PDB id:
2jwt
Name: Transcription
Title: Solution structure of engrailed homeodomain wt
Structure: Segmentation polarity homeobox protein engrailed. Chain: a. Fragment: homeobox domain. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: en. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 25 models
Authors: T.L.Religa
Key ref: T.L.Religa (2008). Comparison of multiple crystal structures with NMR data for engrailed homeodomain. J Biomol NMR, 40, 189-202. PubMed id: 18274703
Date:
24-Oct-07     Release date:   01-Apr-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02836  (HMEN_DROME) -  Segmentation polarity homeobox protein engrailed
Seq:
Struc:
 
Seq:
Struc:
552 a.a.
61 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     regulation of transcription, DNA-dependent   1 term 
  Biochemical function     DNA binding     2 terms  

 

 
J Biomol NMR 40:189-202 (2008)
PubMed id: 18274703  
 
 
Comparison of multiple crystal structures with NMR data for engrailed homeodomain.
T.L.Religa.
 
  ABSTRACT  
 
Two methods are currently available to solve high resolution protein structures-X-ray crystallography and nuclear magnetic resonance (NMR). Both methods usually produce highly similar structures, but small differences between both solutions are always observed. Here the raw NMR data as well as the solved NMR structure were compared to the multiple crystal structures solved for the WT 60 residue three helix bundle engrailed homeodomain (EnHD) and single point mutants. There was excellent agreement between TALOS-predicted and crystal structure-observed dihedral angles and a good agreement for the (3) J(H ( N ) H ( alpha )) couplings for the multiple crystal structures. Around 1% of NOEs were violated for any crystal structure, but no NOE was inconsistent with all of the crystal structures. Violations usually occurred for surface residues or for residues for which multiple discreet conformations were observed between the crystal structures. Comparison of the disorder shown in the multiple crystal structures shows little correlation with dynamics under native conditions for this protein.