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Database: PDB
Entry: 3P57
LinkDB: 3P57
Original site: 3P57 
HEADER    TRANSFERASE/TRANSCRIPTION ACTIVATOR/DNA 08-OCT-10   3P57              
TITLE     CRYSTAL STRUCTURE OF THE P300 TAZ2 DOMAIN BOUND TO MEF2 ON DNA        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOCYTE-SPECIFIC ENHANCER FACTOR 2A;                       
COMPND   3 CHAIN: A, B, C, D, I, J;                                             
COMPND   4 FRAGMENT: N TERMINAL DOMAIN (UNP RESIDUES 2-91);                     
COMPND   5 SYNONYM: SERUM RESPONSE FACTOR-LIKE PROTEIN 1;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(*A*AP*AP*CP*TP*AP*TP*TP*TP*AP*TP*AP*AP*GP*A)-3');
COMPND   9 CHAIN: E, G, K;                                                      
COMPND  10 FRAGMENT: CH3 DOMAIN (UNP RESIDUES 1721-1837);                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES;                                                       
COMPND  13 OTHER_DETAILS: MEF2 BINDING SITE;                                    
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: DNA (5'-D(*TP*TP*CP*TP*TP*AP*TP*AP*AP*AP*TP*AP*GP*TP*T)-   
COMPND  16 3');                                                                 
COMPND  17 CHAIN: F, H, L;                                                      
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: MEF2 BINDING SITE;                                    
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: HISTONE ACETYLTRANSFERASE P300;                            
COMPND  22 CHAIN: P;                                                            
COMPND  23 SYNONYM: P300 HAT, E1A-ASSOCIATED PROTEIN P300;                      
COMPND  24 EC: 2.3.1.48;                                                        
COMPND  25 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: MEF2, MEF2A;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630;                                               
SOURCE  15 OTHER_DETAILS: CHEMICAL SYNTHESIS;                                   
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  19 ORGANISM_TAXID: 32630;                                               
SOURCE  20 OTHER_DETAILS: CHEMICAL SYNTHESIS;                                   
SOURCE  21 MOL_ID: 4;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: EP300, P300;                                                   
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PROTEIN-DNA COMPLEX, TRANSCRIPTION FACTOR, TRANSCRIPTIONAL            
KEYWDS   2 ACTIVATION, P300, ZINC FINGER, TRANSFERASE-TRANSCRIPTION ACTIVATOR-  
KEYWDS   3 DNA COMPLEX                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HE,J.YE,C.RIQUELME,J.O.LIU                                          
REVDAT   3   17-JUL-19 3P57    1       SOURCE REMARK                            
REVDAT   2   08-NOV-17 3P57    1       REMARK                                   
REVDAT   1   10-AUG-11 3P57    0                                                
JRNL        AUTH   J.HE,J.YE,Y.CAI,C.RIQUELME,J.O.LIU,X.LIU,A.HAN,L.CHEN        
JRNL        TITL   STRUCTURE OF P300 BOUND TO MEF2 ON DNA REVEALS A MECHANISM   
JRNL        TITL 2 OF ENHANCEOSOME ASSEMBLY.                                    
JRNL        REF    NUCLEIC ACIDS RES.            V.  39  4464 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   21278418                                                     
JRNL        DOI    10.1093/NAR/GKR030                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 49213                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.090                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4968                            
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 29.6685 -  6.7850    0.99     1670   175  0.1582 0.1637        
REMARK   3     2  6.7850 -  5.3960    1.00     1592   183  0.1940 0.2678        
REMARK   3     3  5.3960 -  4.7170    1.00     1595   166  0.1751 0.2031        
REMARK   3     4  4.7170 -  4.2871    1.00     1553   177  0.1643 0.2103        
REMARK   3     5  4.2871 -  3.9806    1.00     1561   168  0.1800 0.2188        
REMARK   3     6  3.9806 -  3.7464    0.99     1554   176  0.1952 0.2386        
REMARK   3     7  3.7464 -  3.5591    0.99     1511   181  0.1895 0.2723        
REMARK   3     8  3.5591 -  3.4044    1.00     1529   182  0.2073 0.2496        
REMARK   3     9  3.4044 -  3.2735    0.99     1517   185  0.2227 0.2546        
REMARK   3    10  3.2735 -  3.1607    0.99     1536   174  0.2377 0.3080        
REMARK   3    11  3.1607 -  3.0620    0.99     1509   183  0.2596 0.3099        
REMARK   3    12  3.0620 -  2.9745    0.98     1502   177  0.2555 0.3150        
REMARK   3    13  2.9745 -  2.8963    0.98     1484   189  0.2523 0.3202        
REMARK   3    14  2.8963 -  2.8257    0.98     1531   157  0.2661 0.2970        
REMARK   3    15  2.8257 -  2.7615    0.98     1481   170  0.2566 0.2949        
REMARK   3    16  2.7615 -  2.7028    0.99     1503   175  0.2378 0.3459        
REMARK   3    17  2.7028 -  2.6487    0.97     1512   151  0.2325 0.2845        
REMARK   3    18  2.6487 -  2.5988    0.97     1485   147  0.2257 0.2908        
REMARK   3    19  2.5988 -  2.5524    0.97     1472   159  0.2349 0.3321        
REMARK   3    20  2.5524 -  2.5091    0.98     1505   153  0.2280 0.2645        
REMARK   3    21  2.5091 -  2.4687    0.96     1465   168  0.2166 0.2729        
REMARK   3    22  2.4687 -  2.4307    0.96     1470   157  0.2207 0.2872        
REMARK   3    23  2.4307 -  2.3950    0.95     1461   147  0.2209 0.3108        
REMARK   3    24  2.3950 -  2.3613    0.95     1455   165  0.2179 0.3050        
REMARK   3    25  2.3613 -  2.3294    0.94     1435   158  0.2179 0.3174        
REMARK   3    26  2.3294 -  2.2991    0.94     1413   179  0.2231 0.2840        
REMARK   3    27  2.2991 -  2.2704    0.89     1334   150  0.2390 0.2902        
REMARK   3    28  2.2704 -  2.2431    0.83     1294   143  0.3087 0.3822        
REMARK   3    29  2.2431 -  2.2170    0.78     1155   146  0.2881 0.3554        
REMARK   3    30  2.2170 -  2.1921    0.76     1161   127  0.2507 0.3577        
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              : 0.34                                          
REMARK   3   B_SOL              : 28.37                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.24430                                             
REMARK   3    B22 (A**2) : -0.07680                                             
REMARK   3    B33 (A**2) : 1.48760                                              
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           7362                                  
REMARK   3   ANGLE     :  1.324          10236                                  
REMARK   3   CHIRALITY :  0.080           1147                                  
REMARK   3   PLANARITY :  0.004            998                                  
REMARK   3   DIHEDRAL  : 21.607           2990                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3P57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000061970.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59524                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.66000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1EGW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 1000, PH 6.8, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 288K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       37.42300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.40100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.46300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.40100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.42300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.46300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIDECAMERIC                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, I, J, E, F, G, H,         
REMARK 350                    AND CHAINS: K, L, P                               
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465      DA E     1                                                      
REMARK 465      DT H     1                                                      
REMARK 465     LYS P    50                                                      
REMARK 465     ARG P    51                                                      
REMARK 465     LYS P    52                                                      
REMARK 465     THR P    53                                                      
REMARK 465     ASN P    54                                                      
REMARK 465     GLY P    55                                                      
REMARK 465     GLY P    56                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470      DA E   2    P    OP1  OP2                                       
REMARK 470      DT H   2    P    OP1  OP2                                       
REMARK 470      DT H   5    O2                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DT E   5   O3'    DT E   5   C3'    -0.063                       
REMARK 500     DT L   7   O3'    DT L   7   C3'    -0.043                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   2   O4' -  C4' -  C3' ANGL. DEV. =  -4.1 DEGREES          
REMARK 500     DC E   4   O4' -  C1' -  N1  ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     DT E   5   O5' -  C5' -  C4' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DT E   7   C5  -  C4  -  O4  ANGL. DEV. =  -4.4 DEGREES          
REMARK 500     DA E  10   O4' -  C1' -  N9  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DT E  11   O4' -  C1' -  C2' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DA F   6   O4' -  C1' -  N9  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DA F   9   O4' -  C1' -  N9  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DT F  14   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DT F  15   C4' -  C3' -  C2' ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     DA G   1   O4' -  C1' -  N9  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DT G   5   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DA G   6   O4' -  C1' -  N9  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DA G  10   O4' -  C1' -  N9  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DG G  14   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DA H  10   O4' -  C1' -  N9  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DT H  11   C3' -  C2' -  C1' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DT K  11   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT L   1   O4' -  C1' -  N1  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DT L   1   N3  -  C4  -  O4  ANGL. DEV. =   5.0 DEGREES          
REMARK 500     DT L  14   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500    CYS P  74   CA  -  CB  -  SG  ANGL. DEV. =   6.7 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 B  61      117.06    -32.32                                   
REMARK 500    ASN B  73       54.27   -153.24                                   
REMARK 500    LYS C  90       31.79    -94.34                                   
REMARK 500    THR D  60     -168.59   -111.55                                   
REMARK 500    THR I  60     -159.50   -143.73                                   
REMARK 500    ASN I  73       56.10   -118.58                                   
REMARK 500    THR J  60      -61.04   -130.83                                   
REMARK 500    ASN P  30       42.45   -105.48                                   
REMARK 500    GLN P  44       11.32    -67.06                                   
REMARK 500    THR P  46       12.11    -68.11                                   
REMARK 500    PRO P  58      108.84    -44.10                                   
REMARK 500    HIS P  73       -8.99   -146.95                                   
REMARK 500    PHE P  83      -12.23     75.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P 120  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  22   NE2                                                    
REMARK 620 2 CYS P  36   SG  117.7                                              
REMARK 620 3 CYS P  31   SG  104.1 114.9                                        
REMARK 620 4 CYS P  26   SG  102.4 106.1 110.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P 121  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS P  60   SG                                                     
REMARK 620 2 HIS P  45   ND1  96.3                                              
REMARK 620 3 CYS P  49   SG  106.2  81.7                                        
REMARK 620 4 CYS P  57   SG  179.2  83.0  73.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P 122  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  70   NE2                                                    
REMARK 620 2 CYS P  79   SG  111.7                                              
REMARK 620 3 CYS P  74   SG   86.1  51.5                                        
REMARK 620 4 CYS P  84   SG  103.1  88.8  50.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 120                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 121                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 122                  
DBREF  3P57 A    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3P57 B    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3P57 C    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3P57 D    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3P57 I    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3P57 J    2    91  UNP    Q02078   MEF2A_HUMAN      2     91             
DBREF  3P57 P    4   113  UNP    Q09472   EP300_HUMAN   1726   1835             
DBREF  3P57 E    1    15  PDB    3P57     3P57             1     15             
DBREF  3P57 G    1    15  PDB    3P57     3P57             1     15             
DBREF  3P57 K    1    15  PDB    3P57     3P57             1     15             
DBREF  3P57 F    1    15  PDB    3P57     3P57             1     15             
DBREF  3P57 H    1    15  PDB    3P57     3P57             1     15             
DBREF  3P57 L    1    15  PDB    3P57     3P57             1     15             
SEQADV 3P57 HIS P    2  UNP  Q09472              EXPRESSION TAG                 
SEQADV 3P57 MET P    3  UNP  Q09472              EXPRESSION TAG                 
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 C   90  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 C   90  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 C   90  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 C   90  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 C   90  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 C   90  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 C   90  THR ASN SER ASP ILE VAL GLU ALA LEU ASN LYS LYS              
SEQRES   1 D   90  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 D   90  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 D   90  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU CYS ASP          
SEQRES   4 D   90  CYS GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 D   90  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 D   90  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 D   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 E   15   DA  DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA          
SEQRES   2 E   15   DG  DA                                                      
SEQRES   1 F   15   DT  DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG          
SEQRES   2 F   15   DT  DT                                                      
SEQRES   1 G   15   DA  DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA          
SEQRES   2 G   15   DG  DA                                                      
SEQRES   1 H   15   DT  DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG          
SEQRES   2 H   15   DT  DT                                                      
SEQRES   1 K   15   DA  DA  DA  DC  DT  DA  DT  DT  DT  DA  DT  DA  DA          
SEQRES   2 K   15   DG  DA                                                      
SEQRES   1 L   15   DT  DT  DC  DT  DT  DA  DT  DA  DA  DA  DT  DA  DG          
SEQRES   2 L   15   DT  DT                                                      
SEQRES   1 P  112  HIS MET SER PRO GLY ASP SER ARG ARG LEU SER ILE GLN          
SEQRES   2 P  112  ARG CYS ILE GLN SER LEU VAL HIS ALA CYS GLN CYS ARG          
SEQRES   3 P  112  ASN ALA ASN CYS SER LEU PRO SER CYS GLN LYS MET LYS          
SEQRES   4 P  112  ARG VAL VAL GLN HIS THR LYS GLY CYS LYS ARG LYS THR          
SEQRES   5 P  112  ASN GLY GLY CYS PRO ILE CYS LYS GLN LEU ILE ALA LEU          
SEQRES   6 P  112  CYS CYS TYR HIS ALA LYS HIS CYS GLN GLU ASN LYS CYS          
SEQRES   7 P  112  PRO VAL PRO PHE CYS LEU ASN ILE LYS GLN LYS LEU ARG          
SEQRES   8 P  112  GLN GLN GLN LEU GLN HIS ARG LEU GLN GLN ALA GLN MET          
SEQRES   9 P  112  LEU ARG ARG ARG MET ALA SER MET                              
HET     ZN  P 120       1                                                       
HET     ZN  P 121       1                                                       
HET     ZN  P 122       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  14   ZN    3(ZN 2+)                                                     
FORMUL  17  HOH   *262(H2 O)                                                    
HELIX    1   1 ASP A   13  ASP A   40  1                                  28    
HELIX    2   2 ASP A   61  TYR A   72  1                                  12    
HELIX    3   3 THR A   80  LYS A   91  1                                  12    
HELIX    4   4 ASP B   13  CYS B   39  1                                  27    
HELIX    5   5 ASP B   61  GLU B   71  1                                  11    
HELIX    6   6 THR B   80  LYS B   91  1                                  12    
HELIX    7   7 ASP C   13  ASP C   40  1                                  28    
HELIX    8   8 ASP C   61  TYR C   72  1                                  12    
HELIX    9   9 THR C   80  LYS C   90  1                                  11    
HELIX   10  10 ASP D   13  ASP D   40  1                                  28    
HELIX   11  11 ASP D   61  TYR D   72  1                                  12    
HELIX   12  12 THR D   80  LYS D   91  1                                  12    
HELIX   13  13 ASP I   13  ASP I   40  1                                  28    
HELIX   14  14 ASP I   61  GLU I   71  1                                  11    
HELIX   15  15 THR I   80  LYS I   90  1                                  11    
HELIX   16  16 ASP J   13  ASP J   40  1                                  28    
HELIX   17  17 ASP J   61  TYR J   72  1                                  12    
HELIX   18  18 THR J   80  LYS J   91  1                                  12    
HELIX   19  19 SER P    4  CYS P   26  1                                  23    
HELIX   20  20 SER P   35  GLN P   44  1                                  10    
HELIX   21  21 ILE P   59  LYS P   72  1                                  14    
HELIX   22  22 PHE P   83  MET P  113  1                                  31    
SHEET    1   A 6 SER A  78  ARG A  79  0                                        
SHEET    2   A 6 LEU B  54  ALA B  58  1  O  GLN B  56   N  ARG A  79           
SHEET    3   A 6 GLU B  42  PHE B  48 -1  N  LEU B  45   O  TYR B  57           
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  TYR A  57   N  LEU A  45           
SHEET    6   A 6 GLU B  77  ARG B  79  1  O  ARG B  79   N  GLN A  56           
SHEET    1   B 6 GLU C  77  ARG C  79  0                                        
SHEET    2   B 6 LEU D  54  ALA D  58  1  O  GLN D  56   N  ARG C  79           
SHEET    3   B 6 GLU D  42  PHE D  48 -1  N  LEU D  45   O  TYR D  57           
SHEET    4   B 6 GLU C  42  PHE C  48 -1  N  ALA C  44   O  ILE D  46           
SHEET    5   B 6 LEU C  54  ALA C  58 -1  O  PHE C  55   N  ILE C  47           
SHEET    6   B 6 GLU D  77  ARG D  79  1  O  ARG D  79   N  GLN C  56           
SHEET    1   C 6 SER I  78  ARG I  79  0                                        
SHEET    2   C 6 LEU J  54  ALA J  58  1  O  GLN J  56   N  ARG I  79           
SHEET    3   C 6 GLU J  42  PHE J  48 -1  N  LEU J  45   O  TYR J  57           
SHEET    4   C 6 GLU I  42  PHE I  48 -1  N  ALA I  44   O  ILE J  46           
SHEET    5   C 6 LEU I  54  ALA I  58 -1  O  TYR I  57   N  LEU I  45           
SHEET    6   C 6 GLU J  77  ARG J  79  1  O  GLU J  77   N  GLN I  56           
SSBOND   1 CYS P   74    CYS P   79                          1555   1555  2.05  
SSBOND   2 CYS P   74    CYS P   84                          1555   1555  2.08  
LINK         NE2 HIS P  22                ZN    ZN P 120     1555   1555  2.13  
LINK         SG  CYS P  60                ZN    ZN P 121     1555   1555  2.18  
LINK         SG  CYS P  36                ZN    ZN P 120     1555   1555  2.20  
LINK         NE2 HIS P  70                ZN    ZN P 122     1555   1555  2.32  
LINK         SG  CYS P  79                ZN    ZN P 122     1555   1555  2.35  
LINK         SG  CYS P  74                ZN    ZN P 122     1555   1555  2.36  
LINK         SG  CYS P  31                ZN    ZN P 120     1555   1555  2.40  
LINK         SG  CYS P  84                ZN    ZN P 122     1555   1555  2.48  
LINK         SG  CYS P  26                ZN    ZN P 120     1555   1555  2.53  
LINK         ND1 HIS P  45                ZN    ZN P 121     1555   1555  2.70  
LINK         SG  CYS P  49                ZN    ZN P 121     1555   1555  2.86  
LINK         SG  CYS P  57                ZN    ZN P 121     1555   1555  2.88  
SITE     1 AC1  4 HIS P  22  CYS P  26  CYS P  31  CYS P  36                    
SITE     1 AC2  4 HIS P  45  CYS P  49  CYS P  57  CYS P  60                    
SITE     1 AC3  5 HIS P  70  CYS P  74  CYS P  79  VAL P  81                    
SITE     2 AC3  5 CYS P  84                                                     
CRYST1   74.846   90.926  144.802  90.00  90.00  90.00 P 21 21 21   24          
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      0.013361  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010998  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006906        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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