Dear All We are using cns_solve_1.1 to generate structures for a DNA duplex. Everything is fine until the end of the 'accept' procedure when a '.dat' file is
[NMR paper] An empirical backbone-backbone hydrogen-bonding potential in proteins and its applica
An empirical backbone-backbone hydrogen-bonding potential in proteins and its applications to NMR structure refinement and validation.
Related Articles An empirical backbone-backbone hydrogen-bonding potential in proteins and its applications to NMR structure refinement and validation.
J Am Chem Soc. 2004 Jun 16;126(23):7281-92
Authors: Grishaev A, Bax A
A new multidimensional potential is described that encodes for the relative spatial arrangement of the peptidyl backbone units as observed within a large database of high-resolution X-ray...
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11-24-2010 09:51 PM
[NMR paper] Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated pro
Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23fyp from Schizosaccharomyces pombe.
Related Articles Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23fyp from Schizosaccharomyces pombe.
J Biomol NMR. 2000 Jan;16(1):83-4
Authors: Baxter NJ, Thaw P, Higgins LD, Sedelnikova SE, Bramley AL, Price C, Waltho JP, Craven CJ
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11-18-2010 09:15 PM
[NMR paper] Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Related Articles Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Biochemistry. 1995 Apr 18;34(15):5212-23
Authors: Zheng Z, Czaplicki J, Jardetzky O
Backbone dynamics of trp repressor, a 25 kDa DNA binding protein, have been studied using 15N relaxation data measured by proton-detected two-dimensional 1H-15N NMR spectroscopy. 15N spin-lattice relaxation time (T1), spin-spin relaxation time (T2), and heteronuclear NOEs were determined for all visible backbone...
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08-22-2010 03:41 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p
1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus.
Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus.
J Biomol NMR. 1994 Mar;4(2):257-78
Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ
1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...
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08-22-2010 03:33 AM
[NMR paper] Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166)
Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy.
Related Articles Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy.
J Biomol NMR. 1992 Nov;2(6):639-46
Authors: Campbell-Burk SL, Domaille PJ, Starovasnik MA, Boucher W, Laue ED
The c-H-ras p21 protein is the product of the human ras proto-oncogene, a member of a ubiquitous eukaryotic gene family which is highly conserved in evolution. These proteins play...
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08-21-2010 11:45 PM
[NMR paper] Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Related Articles Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Biochemistry. 1990 Jul 10;29(27):6341-62
Authors: McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW
The proton and nitrogen (15NH-H alpha-H beta) resonances of bacteriophage T4 lysozyme were assigned by 15N-aided 1H NMR. The assignments were directed from the backbone amide 1H-15N nuclei, with the heteronuclear single-multiple-quantum coherence (HSMQC)...
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08-21-2010 11:04 PM
automated backbone assignment
Can anyone suggest me a most commonly used and worthful software for automated backbone assignment of triple labeled proteins.
Thanks.
sarun
NMR Questions and Answers
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03-30-2007 03:21 PM
Mars - automatic backbone assignment of proteins
Link to the program
Mars - robust automatic backbone assignment of proteins.
Jung YS, Zweckstetter M. J Biomol NMR. 2004 Sep;30(1):11-23.
Abstract:
MARS is a program for robust automatic backbone assignment of 13C/15N labeled proteins. It can be applied independent of the assignment complexity, it does not require tight thresholds for establishing sequential connectivity or detailed adjustment of these thresholds, it can work with a wide variety of NMR experiments and it is robust against missing chemical shift information. In case of a known 3D structure, residual dipolar...
backbone rmsd from accept.inp
Linear Mode
