1ccm
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ccn|1CCN]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ccm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccm OCA], [http://www.ebi.ac.uk/pdbsum/1ccm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ccm RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: plant seed protein]] | [[Category: plant seed protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:02 2008'' |
Revision as of 16:19, 30 March 2008
| |||||||
| Related: | 1CCN
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING ANNEALING PROTOCOL
Overview
The structure in solution of crambin, a small protein of 46 residues, has been determined from 2D NMR data using an iterative relaxation matrix approach (IRMA) together with distance geometry, distance bound driven dynamics, molecular dynamics, and energy minimization. A new protocol based on an "ensemble" approach is proposed and compared to the more standard initial rate analysis approach and a "single structure" relaxation matrix approach. The effects of fast local motions are included and R-factor calculations are performed on NOE build-ups to describe the quality of agreement between theory and experiment. A new method for stereospecific assignment of prochiral groups, based on a comparison of theoretical and experimental NOE intensities, has been applied. The solution structure of crambin could be determined with a precision (rmsd from the average structure) of 0.7 A on backbone atoms and 1.1 A on all heavy atoms and is largely similar to the crystal structure with a small difference observed in the position of the side chain of Tyr-29 which is determined in solution by both J-coupling and NOE data. Regions of higher structural variability (suggesting higher mobility) are found in the solution structure, in particular for the loop between the two helices (Gly-20 to Pro-22).
About this Structure
1CCM is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA.
Reference
"Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin., Bonvin AM, Rullmann JA, Lamerichs RM, Boelens R, Kaptein R, Proteins. 1993 Apr;15(4):385-400. PMID:8460109
Page seeded by OCA on Sun Mar 30 19:19:02 2008
