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
13624 1v9w 10080 cing 1-original MR format comment


*HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   03-FEB-04   1V9W              
*TITLE     SOLUTION STRUCTURE OF MOUSE PUTATIVE 42-9-9 PROTEIN                   
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: PUTATIVE 42-9-9 PROTEIN;                                   
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 ENGINEERED: YES                                                      
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
*SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
*SOURCE   4 ORGANISM_TAXID: 10090;                                               
*SOURCE   5 GENE: RIKEN CDNA 1110050H17;                                         
*SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
*SOURCE   7 EXPRESSION_SYSTEM_PLASMID: P020128-01;                               
*SOURCE   8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS                           
*KEYWDS    THIOREDOXIN-LIKE FOLD, STRUCTURAL GENOMICS, RIKEN                     
*KEYWDS   2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN             
*KEYWDS   3 FUNCTION                                                             
*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 1V9W    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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