could you please suggest any auto assignment web servers online to assign N-15 & C13- EDIT NOESY experiments data?
Thanking you
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[Question from NMRWiki Q&A forum] what is best pulse sequence for c13 edit noesy on vnmrj ?
what is best pulse sequence for c13 edit noesy on vnmrj ?
Hi
What is best pulse sequence in bio pack on vnmrj for C-13 edit NOESY ? I am working with 12 kd size protein which can exist as homo dimers ( i.e total size of homo-dimer is 24 kd ). Most frequent problems we are encountering as follows !line broadening , baseline , phase correction problems ( huge signal at 2.8 ppm )in first increments and f2f3 planes huge strips errors !
Thanking you in advance !
nmrlearner
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01-10-2012 03:38 PM
[Question from NMRWiki Q&A forum] Problem while genrating the constraints form N-15 edit AND C-13 EDIT NOESY files
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I am encountering the problem while generating the constraints form N-15 edit AND C-13 EDIT NOESY files that very few constraints 200 out of 2400 peaks .Calibration is OK .chemical shift file is good agreement with secondary structure of know crystal structure .Completeness of assignment:Completeness of all atom assignment is 80.74 %.Completeness of proton atom assignment is 82.50 %.Completeness of heavy atom assignment is 74.56 %.Completeness of all atom assignment is 74.58 %.Completeness of proton atom...
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12-24-2011 12:27 AM
[Question from NMRWiki Q&A forum] Auto peak picking of N15Edit NOESY and C13 Edit NOESY spectrum
Auto peak picking of N15Edit NOESY and C13 Edit NOESY spectrum
Dear friends,
I am in process of doing structure calculation of a dimeric protein. The problem I faced is regarding the assignment of N15Edit NOESY and C13 Edit NOESY spectrum.I have already processed the fid data and converted to sparky ucsf format. Is there options available in sparky for auto peak picking, integration and assignment of my NOESY spectrum? And second query is regarding the generation of input files for structure calculation. In our Lab we are using ARIA 2.1 software for structure calculation? Is there any...
nmrlearner
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12-14-2011 07:14 PM
[Question from NMRWiki Q&A forum] c13 edit noesy phasing problem
c13 edit noesy phasing problem
Dear NMR Wiki'ers
I Have acquired c13-edit noesy experiment on 700vnmr for my target protein (20kd) with mixing time of 120ms , I tried my best to correct the phasing, still it seems to be negative contours ,Peak broadening and noise is more after processing .How to overcome this problem ?
Fig-1 1D projections fig-2 f1f3 projection in process in t1fig-3 f1f3 projection in process in t1 after transformation (1026-512-256)
<img width=50% src="http://qa.nmrwiki.org/upfiles/13204074491921939.png" /img>
nmrlearner
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11-04-2011 04:53 PM
[Question from NMRWiki Q&A forum] Randomly duterated protein is useful to get noesy experments ?
Randomly duterated protein is useful to get noesy experments ?
Dear NMR WIKIers
I got doubt that can I use Randomly duterated protein (40 to 60 percent ) to get 3D (C13 EDIT and N15 EDIT) noesy experiments ? because if i duteriated the protein randomly the peak intensity drop would be there. but from standard formula NOE = 1/R6.
I am afraid of error from intensity drop .
could you please suggest any reference related to this ?
Thnaking you
nmrlearner
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10-03-2011 08:39 AM
[Question from NMRWiki Q&A forum] optimization of mixing time 3D NOESY experments
optimization of mixing time 3D NOESY experments
Could you please explain that how to optimize mixing time for 3D NOESY experiments for protein like C13 edit NOESY and N15 EDIT NOESY and i want keep spin diffusion as much as less ?
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nmrlearner
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09-21-2011 05:25 AM
[Question from NMRWiki Q&A forum] Aminoacid residue identification or assignment of protein from 3D NMR Experments
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05-15-2011 08:19 PM
PASD: auto NOE assignment & structure calculation
Completely Automated, Highly Error-Tolerant Macromolecular Structure Determination from Multidimensional Nuclear Overhauser Enhancement Spectra and Chemical Shift Assignments
Kuszewski, J.; Schwieters, C. D.; Garrett, D. S.; Byrd, R. A.; Tjandra, N.; Clore, G. M.;
J. Am. Chem. Soc. 2004; 126(20); 6258-6273
http://pubs.acs.org/isubscribe/journals/jacsat/126/i20/figures/ja049786hn00001.gif
Abstract:
The major rate-limiting step in high-throughput NMR protein structure determination involves the calculation of a reliable initial fold, the elimination of incorrect nuclear Overhauser...