Re: [ccp4bb] Model Building: continuous update of distances as fragment moved

Hi Eric - I remember that the "neighbor atom" distances would dynamically update, and even appear and disappear as your moving atom crosses the 3.2 A distance threshold to another atom. I don't remember if the regular "distance define" distances would do the same; I think not. I'm fairly sure

Re: [ccp4bb] Model Building: continuous update of distances as fragment moved

On Feb 14, 2011, at 4:01 PM, Paul McLaughlin wrote: In doing some model building I want to move a domain of a protein manually, as a rigid body, and see in real time continuous updates of some distances from points on the domain to the rest of the protein (we have cross linking data). I dimly

Re: [ccp4bb] help in CONTACT

On 02/15/2011 04:36 PM, vineet joshi wrote: Dear CCP4ers, Is there any specific way that can help me locate the interactions between ligand (GTP) to any other residue in the protein(GTPase) using CONTACT. And how do I run CONTACT for a number of .pdb files(around 650) in one single step and sepa

[ccp4bb] help in CONTACT

Dear CCP4ers, Is there any specific way that can help me locate the interactions between ligand (GTP) to any other residue in the protein(GTPase) using CONTACT. And how do I run CONTACT for a number of .pdb files(around 650) in one single step and separate them based on their interactions without

Re: [ccp4bb] PDB deposition ADIT without frames?

Thanks a lot for your suggestions! Meanwhile, my colleague entered the desired sequence information into the first website without frames, and after that, the usual frame layout re-appeared! I don't know whether this is a bug or intended ... Best regards, Dirk. Am 15.02.11 17:00, schrieb Dir

[ccp4bb] PDB deposition ADIT without frames?

Dear CCP4ers, a colleague of mine is just going through the PDB deposition process using the usual ADIT website. In contrast to my experience and to the ADIT turorial, she has only one frame in the browser. The left frame with the overview is missing. So, there is no way to jump between the d

[ccp4bb] postdoctoral position on radical-SAM Fe-S protein

Dear All, A postdoctoral position is available in my laboratory (University of Bristol, Medical Sciences Building) to continue our characterisation of the radical SAM enzyme Cfr, an Fe-S-containing rRNA methyltransferase that confers resistance to multiple classes of ribosome-acting antibiotic