NMR Restraints Grid

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

image	mrblock_id	pdb_id	cing	stage	program	type
	28155	2yrn	cing	1-original	MR format	comment

*HEADER    HYDROLASE                               02-APR-07   2YRN              
*TITLE     SOLUTION STRUCTURE OF THE CH DOMAIN FROM HUMAN NEURON                 
*TITLE    2 NAVIGATOR 2                                                          
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: NEURON NAVIGATOR 2 ISOFORM 4;                              
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 FRAGMENT: CH DOMAIN;                                                 
*COMPND   5 SYNONYM: HELICASE APC DOWN-REGULATED 1, RETINOIC ACID                
*COMPND   6 INDUCIBLE IN NEUROBLASTOMA 1, STEERIN-2, PORE MEMBRANE               
*COMPND   7 AND/OR FILAMENT-INTERACTING-LIKE PROTEIN 2, UNC-53 HOMOLOG           
*COMPND   8 2, UNC53H2;                                                          
*COMPND   9 EC: 3.6.1.-;                                                         
*COMPND  10 ENGINEERED: YES;                                                     
*COMPND  11 MUTATION: YES                                                        
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
*SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
*SOURCE   4 ORGANISM_TAXID: 9606;                                                
*SOURCE   5 GENE: NAV2;                                                          
*SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
*SOURCE   7 EXPRESSION_SYSTEM_PLASMID: P041004-11;                               
*SOURCE   8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS                           
*KEYWDS    CALPONIN HOMOLGY DOMAIN, HELICASE, ALL ALPHA, STRUCTURAL              
*KEYWDS   2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL             
*KEYWDS   3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL                            
*KEYWDS   4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE                      
*EXPDTA    SOLUTION NMR                                                          
*NUMMDL    20                                                                    
*AUTHOR    T.TOMIZAWA, N.TOCHIO, S.KOSHIBA, M.INOUE, Y.NAKAMURA,                 
*AUTHOR   2 Y.FURUKAWA, T.KIGAWA, S.YOKOYAMA, RIKEN STRUCTURAL                   
*AUTHOR   3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)                                
*REVDAT   1   12-MAY-09 2YRN    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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