NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
2799 | 1clh | 4037 | cing | 1-original | MR format | comment |
*HEADER ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 20-DEC-93 1CLH *COMPND CYCLOPHILIN (NMR, 12 STRUCTURES) *SOURCE (ESCHERICHIA COLI) *AUTHOR R.T.CLUBB,G.WAGNER *REVDAT 1 31-MAY-94 1CLH 0 ############################################################################## SUPPLEMENTARY MATERIAL Experimental NMR restraints used to determine the three-dimensional solution structure of periplasmic Cyclophilin from E. coli. The structures are based on 1458 interproton distance restraints derived from NOE measurements; 108 hydrogen-bonding distance restraints for 54 hydrogen-bonds identified on the basis of the NOE and amide proton exchange data, as well as initial structure calculations; and 101 phi and 53 chi1 torsion angle restraints derived from coupling constants and NOE data. All the coordinates are included as a separate file: ecyp_brookhaven.pdb References 1. Clubb, R. T., Ferguson, S. B., Walsh, C. T., and Wagner, G. (1994) Biochemistry, in press ############################################################################## NOE RESTRAINTS 1458 Total 483 (|i-j|) = 1 149 (|i-j|) =< 4 574 (|i-j|) > 4 252 Intraresidual ("-1.0" indicates a lower bound equal to the sum of the van der Waals radii) ############################################################################## Bounds Residue Atom Residue Atom Lower(A) Upper(A) ##############################################################################
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