Percent of identity/similarity is a number that might be often misleading when 
used as a judgement rule for molecular replacement. Very high or very low 
numbers are almost always indicative of corresponding outcome. The numbers in 
twilight zone of 20 to 35%, however, are not. When aligning sequences of target 
protein with potential MR models pay attention to residues like Cys, Trp, Phe, 
Tyr. Last three could be used in place of each other. Aligned Cys, for example, 
are very good indication of fold similarity. Ding between aligned Cys is 
indicative of difference in loop lengths, etc. When possible use more sequences 
to align, not just two. Also, there might be some info about your protein’s 
either binding partner or an active site, if it is an enzyme. In that case 
check out alignment of residues associated with the function.

Regards,

Vaheh Oganesyan
www.medimmune.com

From: CCP4 bulletin board [mailto:[email protected]] On Behalf Of Nishant 
Varshney
Sent: Tuesday, August 29, 2017 6:51 AM
To: [email protected]
Subject: [ccp4bb] NMR or Homology Model as a MR model

Dear Crystallographers,

I am working to solve an human protein structure which has a domain sequence 
identity of 24% with domain of another protein.  As Phaser as well as Molrep 
failed to give any definite solution (TFZ=3.7 from MR), I want to ask, if 
solution structure of another protein having domain sequence similarity of 25% 
or a homology model can be used as a template for MR?
Many thanks and Regards
Nishant

--
Dr. Nishant Kumar Varshney,
Research Associate,
C/O Dr. Sameena Khan,
Drug Discovery Research Center,
Translational Health Science and Technology Institute (THSTI)
NCR Biotech Science Cluster,
3rd Milestone, Faridabad – Gurgaon Expressway,
Faridabad – 121001 (HARYANA), India
Ph: +91- 0129-2876477<tel:+91%20129%20287%206477>
Mob: 8390564690
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