NMR Restraints Grid

Result table
 (Save to zip file containing files for each block)
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                                      
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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

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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)

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				      Bounds
Residue	Atom	Residue	Atom	Lower(A)  Upper(A)
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Please acknowledge these references in publications where the data from this site have been utilized.

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