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Database: PDB
Entry: 3MU6
LinkDB: 3MU6
Original site: 3MU6 
HEADER    DNA BINDING PROTEIN/DNA                 01-MAY-10   3MU6              
TITLE     INHIBITING THE BINDING OF CLASS IIA HISTONE DEACETYLASES TO MYOCYTE   
TITLE    2 ENHANCER FACTOR-2 BY SMALL MOLECULES                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOCYTE-SPECIFIC ENHANCER FACTOR 2A;                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: SERUM RESPONSE FACTOR-LIKE PROTEIN 1;                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(*AP*AP*AP*GP*CP*TP*AP*TP*TP*AP*TP*TP*AP*GP*CP*TP*T)-3');           
COMPND  10 CHAIN: E, G;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA (5'-                                                   
COMPND  14 D(*TP*AP*AP*GP*CP*TP*AP*AP*TP*AP*AP*TP*AP*GP*CP*TP*T)-3');           
COMPND  15 CHAIN: F, H;                                                         
COMPND  16 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: MEF2A, MEF2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 MOL_ID: 3;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    MADS-BOX/MEF2 DOMAIN, TRANSCRIPTION CO-FACTORS, PROTEIN-DNA COMPLEX,  
KEYWDS   2 PROTEIN-PROTEIN DOCKING, DNA BINDING PROTEIN-DNA COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.JAYATHILAKA,A.HAN,K.GAFFNEY,R.DEY,J.HE,J.YE,T.GAO,N.A.PETASIS,      
AUTHOR   2 L.CHEN                                                               
REVDAT   5   08-NOV-17 3MU6    1       REMARK                                   
REVDAT   4   25-JUL-12 3MU6    1       JRNL                                     
REVDAT   3   21-MAR-12 3MU6    1       JRNL                                     
REVDAT   2   22-FEB-12 3MU6    1       JRNL                                     
REVDAT   1   02-NOV-11 3MU6    0                                                
JRNL        AUTH   N.JAYATHILAKA,A.HAN,K.J.GAFFNEY,R.DEY,J.A.JARUSIEWICZ,       
JRNL        AUTH 2 K.NORIDOMI,M.A.PHILIPS,X.LEI,J.HE,J.YE,T.GAO,N.A.PETASIS,    
JRNL        AUTH 3 L.CHEN                                                       
JRNL        TITL   INHIBITION OF THE FUNCTION OF CLASS IIA HDACS BY BLOCKING    
JRNL        TITL 2 THEIR INTERACTION WITH MEF2.                                 
JRNL        REF    NUCLEIC ACIDS RES.            V.  40  5378 2012              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   22396528                                                     
JRNL        DOI    10.1093/NAR/GKS189                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.1_357                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.44                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 19819                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1026                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.4470 -  4.6530    0.98     2733   158  0.1850 0.2020        
REMARK   3     2  4.6530 -  3.6950    0.96     2695   176  0.1850 0.2000        
REMARK   3     3  3.6950 -  3.2280    0.96     2707   127  0.1960 0.2340        
REMARK   3     4  3.2280 -  2.9330    0.95     2707   141  0.2420 0.2660        
REMARK   3     5  2.9330 -  2.7230    0.95     2703   142  0.2690 0.3180        
REMARK   3     6  2.7230 -  2.5620    0.95     2664   142  0.2590 0.2920        
REMARK   3     7  2.5620 -  2.4340    0.89     2584   140  0.2820 0.3210        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 21.40                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.58000                                             
REMARK   3    B22 (A**2) : 7.44700                                              
REMARK   3    B33 (A**2) : -1.86700                                             
REMARK   3    B12 (A**2) : -0.45900                                             
REMARK   3    B13 (A**2) : 0.83700                                              
REMARK   3    B23 (A**2) : -11.44600                                            
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3946                                  
REMARK   3   ANGLE     :  1.330           5574                                  
REMARK   3   CHIRALITY :  0.068            628                                  
REMARK   3   PLANARITY :  0.004            456                                  
REMARK   3   DIHEDRAL  : 23.841           1605                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 8                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A RESID 2:60                          
REMARK   3     SELECTION          : CHAIN B RESID 2:60                          
REMARK   3     ATOM PAIRS NUMBER  : 485                                         
REMARK   3     RMSD               : 0.019                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C RESID 2:60                          
REMARK   3     SELECTION          : CHAIN D RESID 2:60                          
REMARK   3     ATOM PAIRS NUMBER  : 485                                         
REMARK   3     RMSD               : 0.012                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C RESID 2:60                          
REMARK   3     SELECTION          : CHAIN B RESID 2:60                          
REMARK   3     ATOM PAIRS NUMBER  : 485                                         
REMARK   3     RMSD               : 0.016                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C RESID 2:60                          
REMARK   3     SELECTION          : CHAIN D RESID 2:60                          
REMARK   3     ATOM PAIRS NUMBER  : 485                                         
REMARK   3     RMSD               : 0.012                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A RESID 68:72                         
REMARK   3     SELECTION          : CHAIN B RESID 68:72                         
REMARK   3     ATOM PAIRS NUMBER  : 45                                          
REMARK   3     RMSD               : 0.015                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C RESID 68:72                         
REMARK   3     SELECTION          : CHAIN D RESID 68:72                         
REMARK   3     ATOM PAIRS NUMBER  : 45                                          
REMARK   3     RMSD               : 0.008                                       
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C RESID 68:72                         
REMARK   3     SELECTION          : CHAIN B RESID 68:72                         
REMARK   3     ATOM PAIRS NUMBER  : 45                                          
REMARK   3     RMSD               : 0.012                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C RESID 68:72                         
REMARK   3     SELECTION          : CHAIN D RESID 68:72                         
REMARK   3     ATOM PAIRS NUMBER  : 45                                          
REMARK   3     RMSD               : 0.008                                       
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN E                                     
REMARK   3     SELECTION          : CHAIN G                                     
REMARK   3     ATOM PAIRS NUMBER  : 345                                         
REMARK   3     RMSD               : 0.013                                       
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN F                                     
REMARK   3     SELECTION          : CHAIN H                                     
REMARK   3     ATOM PAIRS NUMBER  : 346                                         
REMARK   3     RMSD               : 0.013                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3MU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OTHER                              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19854                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1EGW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM ACETIC ACID, 142MM NACL, 5MM       
REMARK 280  MGCL2, 10MM CACL2, 3.3% GLYCEROL, 22.5% 3K PEG, PH 4.7, HANGING     
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DA E   1   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DA E   2   C3' -  C2' -  C1' ANGL. DEV. =  -5.8 DEGREES          
REMARK 500     DA E   2   O4' -  C1' -  N9  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DC E   5   O4' -  C1' -  N1  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DT E   6   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DT E   8   C1' -  O4' -  C4' ANGL. DEV. =  -7.0 DEGREES          
REMARK 500     DT E   8   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DA F   2   C3' -  C2' -  C1' ANGL. DEV. =  -5.9 DEGREES          
REMARK 500     DA F   2   O4' -  C1' -  N9  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DC F   5   O4' -  C1' -  N1  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DA F  11   O4' -  C1' -  N9  ANGL. DEV. =  -7.6 DEGREES          
REMARK 500     DA G   2   C3' -  C2' -  C1' ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DA G   2   O4' -  C1' -  N9  ANGL. DEV. =   4.2 DEGREES          
REMARK 500     DC G   5   O4' -  C1' -  N1  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DT G   6   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT G   8   C1' -  O4' -  C4' ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     DT G   8   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT G  11   O4' -  C1' -  N1  ANGL. DEV. =  -4.2 DEGREES          
REMARK 500     DT G  11   N3  -  C2  -  O2  ANGL. DEV. =  -4.0 DEGREES          
REMARK 500     DA H   2   C3' -  C2' -  C1' ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DA H   2   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC H   5   O4' -  C1' -  N1  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT H   6   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DA H  10   O4' -  C1' -  N9  ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DA H  11   O4' -  C1' -  N9  ANGL. DEV. =  -7.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  40       70.35     54.41                                   
REMARK 500    ASP B  40       70.37     54.49                                   
REMARK 500    ASN B  49     -178.82    -69.99                                   
REMARK 500    ASP C  40       71.01     53.71                                   
REMARK 500    ASP D  40       70.64     54.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXL A 100                 
DBREF  3MU6 A    2    72  UNP    Q02078   MEF2A_HUMAN      2     72             
DBREF  3MU6 B    2    72  UNP    Q02078   MEF2A_HUMAN      2     72             
DBREF  3MU6 C    2    72  UNP    Q02078   MEF2A_HUMAN      2     72             
DBREF  3MU6 D    2    72  UNP    Q02078   MEF2A_HUMAN      2     72             
DBREF  3MU6 E    1    17  PDB    3MU6     3MU6             1     17             
DBREF  3MU6 G    1    17  PDB    3MU6     3MU6             1     17             
DBREF  3MU6 F    1    17  PDB    3MU6     3MU6             1     17             
DBREF  3MU6 H    1    17  PDB    3MU6     3MU6             1     17             
SEQADV 3MU6 ALA A   71  UNP  Q02078    GLU    71 ENGINEERED MUTATION            
SEQADV 3MU6 ALA B   71  UNP  Q02078    GLU    71 ENGINEERED MUTATION            
SEQADV 3MU6 ALA C   71  UNP  Q02078    GLU    71 ENGINEERED MUTATION            
SEQADV 3MU6 ALA D   71  UNP  Q02078    GLU    71 ENGINEERED MUTATION            
SEQRES   1 A   71  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 A   71  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 A   71  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 A   71  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 A   71  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 A   71  LEU LYS TYR THR ALA TYR                                      
SEQRES   1 B   71  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 B   71  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 B   71  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 B   71  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 B   71  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 B   71  LEU LYS TYR THR ALA TYR                                      
SEQRES   1 E   17   DA  DA  DA  DG  DC  DT  DA  DT  DT  DA  DT  DT  DA          
SEQRES   2 E   17   DG  DC  DT  DT                                              
SEQRES   1 F   17   DT  DA  DA  DG  DC  DT  DA  DA  DT  DA  DA  DT  DA          
SEQRES   2 F   17   DG  DC  DT  DT                                              
SEQRES   1 C   71  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 C   71  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 C   71  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 C   71  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 C   71  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 C   71  LEU LYS TYR THR ALA TYR                                      
SEQRES   1 D   71  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 D   71  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 D   71  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 D   71  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 D   71  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 D   71  LEU LYS TYR THR ALA TYR                                      
SEQRES   1 G   17   DA  DA  DA  DG  DC  DT  DA  DT  DT  DA  DT  DT  DA          
SEQRES   2 G   17   DG  DC  DT  DT                                              
SEQRES   1 H   17   DT  DA  DA  DG  DC  DT  DA  DA  DT  DA  DA  DT  DA          
SEQRES   2 H   17   DG  DC  DT  DT                                              
HET    BXL  A 100      25                                                       
HETNAM     BXL (3E)-N~8~-(2-AMINOPHENYL)-N~1~-PHENYLOCT-3-ENEDIAMIDE            
FORMUL   9  BXL    C20 H23 N3 O2                                                
HELIX    1   1 ASP A   13  ASP A   40  1                                  28    
HELIX    2   2 ASP A   61  ALA A   71  1                                  11    
HELIX    3   3 ASP B   13  ASP B   40  1                                  28    
HELIX    4   4 ASP B   61  TYR B   72  1                                  12    
HELIX    5   5 ASP C   13  ASP C   40  1                                  28    
HELIX    6   6 ASP C   61  TYR C   72  1                                  12    
HELIX    7   7 ASP D   13  ASP D   40  1                                  28    
HELIX    8   8 ASP D   61  TYR D   72  1                                  12    
SHEET    1   A 4 LEU A  54  ALA A  58  0                                        
SHEET    2   A 4 GLU A  42  PHE A  48 -1  N  ILE A  47   O  PHE A  55           
SHEET    3   A 4 GLU B  42  PHE B  48 -1  O  ALA B  44   N  ILE A  46           
SHEET    4   A 4 LEU B  54  ALA B  58 -1  O  PHE B  55   N  ILE B  47           
SHEET    1   B 4 LEU C  54  ALA C  58  0                                        
SHEET    2   B 4 GLU C  42  PHE C  48 -1  N  ILE C  47   O  PHE C  55           
SHEET    3   B 4 GLU D  42  PHE D  48 -1  O  ALA D  44   N  ILE C  46           
SHEET    4   B 4 LEU D  54  ALA D  58 -1  O  PHE D  55   N  ILE D  47           
SITE     1 AC1 11 ASP A  61  MET A  62  ASP A  63  LEU A  66                    
SITE     2 AC1 11 LEU A  67  THR A  70  LEU B  66  LEU B  67                    
SITE     3 AC1 11 TYR B  69  THR B  70   DT G  17                               
CRYST1   41.567   61.622   61.478 114.12  89.99  89.95 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024058 -0.000021 -0.000013        0.00000                         
SCALE2      0.000000  0.016228  0.007267        0.00000                         
SCALE3      0.000000  0.000000  0.017822        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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