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Dear All:

Thank you very much for your advices and comments.

Following your instructions, I am able to change the CYS to CSX.

Both "Get Monomer" and "Replace Residue" work well.

I have the refined conformation CSX (by "real space refinment" ) attached
(named as M-CSX-1).

The Fo-Fc map is shown with sigma @[log in to unmask]

Is this conformation reasonable? Why there are two bond conformation there?

Thank you for comments.

Uma

On Fri, May 4, 2012 at 12:10 PM, Hugo Correia
<[log in to unmask]>wrote:

> Dear Uma,
>
> You can do this using coot. Go to Extensions > Modelling > Replace
> Residue... and enter the three letter code.
>
> Cheers
>
> Hugo Correia
>
>
> 2012/5/4 Uma Ratu <[log in to unmask]>
>
>> Dear All:
>>
>> My protein has a key cysteine residue involved in catalytic activity.
>>
>> The template structure used for the modeling has the same key cysteine.
>> In the template structure, this key cysteine residue is assigned as CSX
>> based on the observation from its electronic density.
>>
>> I compared the electron density from the template as well as my model. I
>> can't tell if the cysteine in my model is oxidized or not. The ones from
>> the template also looks different from each other, although both assigned
>> as CSX.
>>
>> I have the snapshots of these cysteines attached. The ones from my model
>> named as "M-", and the ones from the template named as "T-".
>>
>> Plus, how to change the residue label from Cys to CSX if the cystein is
>> oxidized? In coot, I could not find such function.
>>
>> Thank you very much for your advice
>>
>> Uma
>>
>
>