NMR Restraints Grid

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

image	mrblock_id	pdb_id	bmrb_id	cing	in_recoord	stage	program	type
	4224	1ezp	4986	cing	recoord	1-original	MR format	comment

*HEADER    SUGAR BINDING PROTEIN                   11-MAY-00   1EZP              
*TITLE     GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH            
*TITLE    2 BETA-CYCLODEXTRIN USING PEPTIDE ORIENTATIONS FROM DIPOLAR            
*TITLE    3 COUPLINGS                                                            
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: MALTODEXTRIN BINDING PERIPLASMIC PROTEIN;                  
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 SYNONYM: MALTODEXTRIN BINDING PROTEIN;                               
*COMPND   5 ENGINEERED: YES;                                                     
*COMPND   6 MUTATION: YES                                                        
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
*SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
*SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
*SOURCE   5 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
*SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
*SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
*SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PBR322                                    
*KEYWDS    RESIDUAL DIPLAR COUPLINGS, DEUTERATION, METHYL LABELING               
*EXPDTA    NMR, 10 STRUCTURES                                                    
*AUTHOR    G.A.MUELLER, W.Y.CHOY, D.YANG, J.D.FORMAN-KAY, R.A.VENTERS,           
*AUTHOR   2 L.E.KAY                                                              
*REVDAT   1   08-MAY-01 1EZP    0                                                
! A reexamination of a few residues for which there seem to folded assignments
!

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