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Database: PDB
Entry: 3KOV
LinkDB: 3KOV
Original site: 3KOV 
HEADER    TRANSCRIPTION/DNA                       14-NOV-09   3KOV              
TITLE     STRUCTURE OF MEF2A BOUND TO DNA REVEALS A COMPLETELY FOLDED MADS-     
TITLE    2 BOX/MEF2 DOMAIN THAT RECOGNIZES DNA AND RECRUITS TRANSCRIPTION CO-   
TITLE    3 FACTORS                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOCYTE-SPECIFIC ENHANCER FACTOR 2A;                       
COMPND   3 CHAIN: A, B, I, J;                                                   
COMPND   4 SYNONYM: SERUM RESPONSE FACTOR-LIKE PROTEIN 1;                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (5'-D(*AP*AP*CP*TP*AP*TP*TP*TP*AP*TP*AP*AP*G)-3');     
COMPND   8 CHAIN: C, K;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: DNA (5'-D(*TP*CP*TP*TP*AP*TP*AP*AP*AP*TP*AP*GP*T)-3');     
COMPND  12 CHAIN: D, L;                                                         
COMPND  13 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, ACETYLATION, ACTIVATOR, ALTERNATIVE         
KEYWDS   3 SPLICING, APOPTOSIS, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, DISEASE 
KEYWDS   4 MUTATION, DNA-BINDING, ISOPEPTIDE BOND, NEUROGENESIS, NUCLEUS,       
KEYWDS   5 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, UBL         
KEYWDS   6 CONJUGATION, TRANSCRIPTION-DNA COMPLEX                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.WU,R.DEY,A.HAN,N.JAYATHILAKA,M.PHILIPS,J.YE,L.CHEN                  
REVDAT   4   04-APR-18 3KOV    1       REMARK                                   
REVDAT   3   01-NOV-17 3KOV    1       REMARK                                   
REVDAT   2   23-MAR-10 3KOV    1       JRNL                                     
REVDAT   1   16-FEB-10 3KOV    0                                                
JRNL        AUTH   Y.WU,R.DEY,A.HAN,N.JAYATHILAKA,M.PHILIPS,J.YE,L.CHEN         
JRNL        TITL   STRUCTURE OF THE MADS-BOX/MEF2 DOMAIN OF MEF2A BOUND TO DNA  
JRNL        TITL 2 AND ITS IMPLICATION FOR MYOCARDIN RECRUITMENT.               
JRNL        REF    J.MOL.BIOL.                   V. 397   520 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20132824                                                     
JRNL        DOI    10.1016/J.JMB.2010.01.067                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 14094                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 704                             
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 44.0593 -  4.9572    0.91     2726   129  0.2111 0.2445        
REMARK   3     2  4.9572 -  3.9355    0.94     2670   127  0.1910 0.2676        
REMARK   3     3  3.9355 -  3.4382    0.96     2686   151  0.2223 0.2965        
REMARK   3     4  3.4382 -  3.1239    0.96     2656   148  0.2476 0.3029        
REMARK   3     5  3.1239 -  2.9000    0.96     2652   149  0.3017 0.3735        
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              : 0.31                                          
REMARK   3   B_SOL              : 69.48                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.28600                                              
REMARK   3    B22 (A**2) : 8.62000                                              
REMARK   3    B33 (A**2) : 16.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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           4778                                  
REMARK   3   ANGLE     :  1.227           6741                                  
REMARK   3   CHIRALITY :  0.061            758                                  
REMARK   3   PLANARITY :  0.003            586                                  
REMARK   3   DIHEDRAL  : 24.530           1932                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3433  32.0434  80.5156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7517 T22:   0.6428                                     
REMARK   3      T33:   0.5708 T12:   0.0612                                     
REMARK   3      T13:  -0.2334 T23:   0.0588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1714 L22:   1.5541                                     
REMARK   3      L33:   1.1831 L12:   0.0448                                     
REMARK   3      L13:  -0.4187 L23:   1.2344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0895 S12:  -0.0611 S13:  -0.0492                       
REMARK   3      S21:   0.5618 S22:  -0.0846 S23:  -0.0046                       
REMARK   3      S31:   0.2893 S32:   0.3341 S33:   0.0870                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 3                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN I                                     
REMARK   3     SELECTION          : CHAIN J                                     
REMARK   3     ATOM PAIRS NUMBER  : 743                                         
REMARK   3     RMSD               : 0.048                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN I                                     
REMARK   3     SELECTION          : CHAIN A                                     
REMARK   3     ATOM PAIRS NUMBER  : 743                                         
REMARK   3     RMSD               : 0.043                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN I                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 743                                         
REMARK   3     RMSD               : 0.041                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056261.                                   
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   : 15478                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.870                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58500                            
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
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 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       38.90050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.98000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.90050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.98000            
REMARK 290   SMTRY3   4  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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
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 C   2   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DA C   2   O4' -  C1' -  N9  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DC C   4   O4' -  C1' -  N1  ANGL. DEV. =   4.2 DEGREES          
REMARK 500     DT C   5   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT C   7   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT C   7   N3  -  C4  -  O4  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DT C  11   C3' -  C2' -  C1' ANGL. DEV. =  -7.4 DEGREES          
REMARK 500     DA C  13   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT D   2   C3' -  C2' -  C1' ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DC D   3   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DC D   3   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT D   5   C4' -  C3' -  C2' ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     DT D  11   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DA K   2   O4' -  C1' -  N9  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DT K   7   C1' -  O4' -  C4' ANGL. DEV. =  -6.7 DEGREES          
REMARK 500     DT K   8   O4' -  C1' -  N1  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DT K  11   C3' -  C2' -  C1' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DA K  13   C3' -  C2' -  C1' ANGL. DEV. =  -6.2 DEGREES          
REMARK 500     DG K  14   O4' -  C1' -  N9  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DT L   2   O4' -  C1' -  N1  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DT L   4   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DT L   7   C3' -  C2' -  C1' ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT L  11   N3  -  C4  -  O4  ANGL. DEV. =   4.7 DEGREES          
REMARK 500     DT L  11   C5  -  C4  -  O4  ANGL. DEV. =  -4.2 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    THR A  60     -107.68   -136.67                                   
REMARK 500    THR B  60     -101.18   -135.86                                   
REMARK 500    THR I  60     -130.51   -140.44                                   
REMARK 500    THR J  60     -105.30   -138.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3KOV I    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3KOV J    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3KOV A    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3KOV B    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3KOV K    2    14  PDB    3KOV     3KOV             2     14             
DBREF  3KOV C    2    14  PDB    3KOV     3KOV             2     14             
DBREF  3KOV L    2    14  PDB    3KOV     3KOV             2     14             
DBREF  3KOV D    2    14  PDB    3KOV     3KOV             2     14             
SEQRES   1 A   90  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 A   90  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 A   90  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 A   90  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 A   90  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 A   90  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 A   90  THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS              
SEQRES   1 B   90  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 B   90  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 B   90  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 B   90  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 B   90  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 B   90  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 B   90  THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS              
SEQRES   1 I   90  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 I   90  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 I   90  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 I   90  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 I   90  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 I   90  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 I   90  THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS              
SEQRES   1 J   90  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 J   90  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 J   90  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 J   90  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 J   90  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 J   90  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 J   90  THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS              
SEQRES   1 C   13   DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA  DG          
SEQRES   1 D   13   DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG  DT          
SEQRES   1 K   13   DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA  DG          
SEQRES   1 L   13   DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG  DT          
HELIX    1   1 ASP A   13  CYS A   39  1                                  27    
HELIX    2   2 ASP A   61  TYR A   72  1                                  12    
HELIX    3   3 ASN A   81  LYS A   90  1                                  10    
HELIX    4   4 ASP B   13  CYS B   39  1                                  27    
HELIX    5   5 ASP B   61  TYR B   72  1                                  12    
HELIX    6   6 ASN B   81  LYS B   90  1                                  10    
HELIX    7   7 ASP I   13  CYS I   39  1                                  27    
HELIX    8   8 ASP I   61  TYR I   72  1                                  12    
HELIX    9   9 ASN I   81  LYS I   90  1                                  10    
HELIX   10  10 ASP J   13  CYS J   39  1                                  27    
HELIX   11  11 ASP J   61  TYR J   72  1                                  12    
HELIX   12  12 ASN J   81  LYS J   90  1                                  10    
SHEET    1   A 6 GLU A  77  THR A  80  0                                        
SHEET    2   A 6 LEU B  54  ALA B  58  1  O  GLN B  56   N  GLU A  77           
SHEET    3   A 6 GLU B  42  PHE B  48 -1  N  ILE B  47   O  PHE B  55           
SHEET    4   A 6 GLU A  42  PHE A  48 -1  N  ILE A  46   O  ALA B  44           
SHEET    5   A 6 LEU A  54  ALA A  58 -1  O  PHE A  55   N  ILE A  47           
SHEET    6   A 6 GLU B  77  THR B  80  1  O  ARG B  79   N  GLN A  56           
SHEET    1   B 6 GLU I  77  THR I  80  0                                        
SHEET    2   B 6 LEU J  54  ALA J  58  1  O  GLN J  56   N  ARG I  79           
SHEET    3   B 6 GLU J  42  PHE J  48 -1  N  LEU J  45   O  TYR J  57           
SHEET    4   B 6 GLU I  42  PHE I  48 -1  N  ILE I  46   O  ALA J  44           
SHEET    5   B 6 LEU I  54  ALA I  58 -1  O  PHE I  55   N  ILE I  47           
SHEET    6   B 6 GLU J  77  THR J  80  1  O  ARG J  79   N  GLN I  56           
CRYST1   77.801   77.960  106.794  90.00  90.00  90.00 P 21 21 2    16          
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      0.012853  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012827  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009364        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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