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You can typically assign the histidine orientation based on analysis of the hydrogen bond network. In ambiguous cases you might have to look a few residues deep. WHAT_CHECK does this for you by a global optimization of the hydrogen bond network.

Cheers,
Robbie

Sent with my Windows Phone

Van: Smith Liu
Verzonden: ‎20-‎5-‎2015 14:12
Aan: [log in to unmask]
Onderwerp: [ccp4bb] HIS related crystallography issue

Dear All,
 
Suppose the protein crystal resolution is about 2-3A, then in the map it should be rather difficult to distinguish the C and N in the sidechain of HIS. In this way we may regard the sidechain of HIS is flippable. But suppose in one flipped conformation of the HIS, the free N in the sidechain of HIS can form H-bond with the neighbour H of the OH of the Thr, in the other flipped conformation of the HIS, the free N in the sidechain of HIS cannot form H-bond with the neighbour H of the OH of the Thr (caused by distance issue).
 
Suppose whether the H-bond forms between the free N in the sidechain of HIS and the neighbour H of the OH of the Thr was very important biologically, in this situation how can we distinguish whether the H-bond forms?
 
Smith