NMR Restraints Grid

Result table
 (Save to zip file containing files for each block)
image mrblock_id pdb_id cing stage program type
2882 1cqg cing 1-original MR format comment 

*HEADER   COMPLEX (ELECTRON TRANSPORT/PEPTIDE)    02-APR-96   1CQG    
*TITLE    HIGH RESOLUTION SOLUTION NMR STRUCTURE OF MIXED DISULFIDE   
*TITLE   2 INTERMEDIATE BETWEEN HUMAN THIOREDOXIN (C35A, C62A, C69A,  
*TITLE   3 C73A) MUTANT AND A 13 RESIDUE PEPTIDE COMPRISING ITS TARGET
*TITLE   4 SITE IN HUMAN REF-1 (RESIDUES 59 - 71 OF THE P50 SUBUNIT OF
*TITLE   5 NFKB), NMR, 31 STRUCTURES                                  
*COMPND   MOL_ID: 1;                                                  
*COMPND  2 MOLECULE: THIOREDOXIN;                                     
*COMPND  3 CHAIN: A;                                                  
*COMPND  4 ENGINEERED: YES;                                           
*COMPND  5 MUTATION: CHAIN A, C35A, C62A, C69A, C73A;                 
*COMPND  6 MOL_ID: 2;                                                 
*COMPND  7 MOLECULE: REF-1 PEPTIDE;                                   
*COMPND  8 CHAIN: B;                                                  
*COMPND  9 FRAGMENT: RESIDUES 59 - 71 OF THE P50 SUBUNIT OF NFKB;     
*COMPND 10 EC: 4.2.99.18                                              
*COMPND 11 ENGINEERED: YES;                                           
*SOURCE   MOL_ID: 1;                                                  
*SOURCE  2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                         
*SOURCE  3 ORGANISM_COMMON: HUMAN;                                    
*SOURCE  4 MOL_ID: 2;                                                 
*SOURCE  5 SYNTHETIC: YES                                             
*KEYWDS   COMPLEX, ELECTRON TRANSPORT/PEPTIDE                         
*EXPDTA   NMR, 35 STRUCTURES                                          
*AUTHOR   G.M.CLORE,J.QIN,A.M.GRONENBORN                              
*REVDAT  1   01-AUG-96 1CQG    0                                      

REMARK    The NOE restraints are given in (A), the torsion angle restraints
REMARK    in (B), the coupling constant restraints in (C), the 13C
REMARK    chemical shift restraints in (D), the 1H shift restraints in (E); 
REMARK    and the complete set of 1H, 15N and 13C assignments in (F)

Please acknowledge these references in publications where the data from this site have been utilized.

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