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
	18176	2diy R C	11108	cing	1-original	MR format	comment
*HEADER    PROTEIN BINDING                         30-MAR-06   2DIY              
*TITLE     THE SOLUTION STRUCTURE OF THE THIOREDOXIN DOMAIN OF HUMAN             
*TITLE    2 THIOREDOXIN-LIKE PROTEIN 2                                           
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: THIOREDOXIN-LIKE PROTEIN 2;                                
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 FRAGMENT: THIOREDOXIN DOMAIN, RESIDUES 8-124;                        
*COMPND   5 SYNONYM: PKC-INTERACTING COUSIN OF THIOREDOXIN, PKC-THETA-           
*COMPND   6 INTERACTING PROTEIN, PKCQ-INTERACTING PROTEIN;                       
*COMPND   7 ENGINEERED: YES                                                      
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
*SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
*SOURCE   4 ORGANISM_TAXID: 9606;                                                
*SOURCE   5 GENE: TXNL2;                                                         
*SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
*SOURCE   7 EXPRESSION_SYSTEM_PLASMID: P050302-06;                               
*SOURCE   8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS                           
*KEYWDS    PKC-INTERACTING COUSIN OF THIOREDOXIN, PKC-THETA-                     
*KEYWDS   2 INTERACTING PROTEIN, PICOT, STRUCTURAL GENOMICS, NPPSFA,             
*KEYWDS   3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL                
*KEYWDS   4 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,           
*KEYWDS   5 RSGI, PROTEIN BINDING                                                
*EXPDTA    SOLUTION NMR                                                          
*NUMMDL    20                                                                    
*AUTHOR    N.TOCHIO, S.KOSHIBA, M.INOUE, T.KIGAWA, S.YOKOYAMA, RIKEN             
*AUTHOR   2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)                     
*REVDAT   1   12-MAY-09 2DIY    0                                                

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During the CYANA calculations automatic implicit swapping of restraints 
involving diastereotopic substitutents was applied for prochrial groups 
without stereospecific assignment. Diastereotopic substitents were 
swapped individually in each conformer to calculate the minimal target 
function and restraint violations.
The optimal swapping for a given prochiral group may differ among 
the 20 conformers that represent the solution structure. The swapping 
is therefore performed implicitly in the program and is not reflected 
in the distance restraint file deposited in the PDB.
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