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Database: PDB
Entry: 5D25
LinkDB: 5D25
Original site: 5D25 
HEADER    TRANSCRIPTION                           05-AUG-15   5D25              
TITLE     FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD27                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 43-168;                                       
COMPND   5 SYNONYM: PROTEIN HUNK1;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRD4, HUNK1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    GENE REGULATION, INHIBITOR, BROMODOMAIN, TRANSCRIPTION                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WOHLWEND,M.HUEGLE,S.GERHARDT                                        
REVDAT   3   06-SEP-17 5D25    1       REMARK                                   
REVDAT   2   09-MAR-16 5D25    1       JRNL                                     
REVDAT   1   20-JAN-16 5D25    0                                                
JRNL        AUTH   M.HUGLE,X.LUCAS,G.WEITZEL,D.OSTROVSKYI,B.BREIT,S.GERHARDT,   
JRNL        AUTH 2 O.EINSLE,S.GUNTHER,D.WOHLWEND                                
JRNL        TITL   4-ACYL PYRROLE DERIVATIVES YIELD NOVEL VECTORS FOR DESIGNING 
JRNL        TITL 2 INHIBITORS OF THE ACETYL-LYSINE RECOGNITION SITE OF BRD4(1). 
JRNL        REF    J.MED.CHEM.                   V.  59  1518 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26731611                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01267                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0071                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 11677                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1272                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 846                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1037                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.09000                                             
REMARK   3    B22 (A**2) : 2.19000                                              
REMARK   3    B33 (A**2) : -1.10000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.492         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1141 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1559 ; 1.229 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   131 ; 4.283 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;37.144 ;25.849       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   200 ;13.236 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ; 7.976 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   164 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   880 ; 0.006 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   515 ; 0.257 ; 0.887       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   649 ; 0.416 ; 1.328       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   626 ; 0.469 ; 1.014       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4921 ; 3.315 ; 9.131       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6609  61.0255   7.9354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0719 T22:   0.0772                                     
REMARK   3      T33:   0.0536 T12:  -0.0056                                     
REMARK   3      T13:  -0.0469 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7148 L22:   7.7865                                     
REMARK   3      L33:   9.8229 L12:  -2.1884                                     
REMARK   3      L13:  -6.6200 L23:   0.6071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2528 S12:   0.0840 S13:   0.0737                       
REMARK   3      S21:  -0.0123 S22:   0.0026 S23:   0.1717                       
REMARK   3      S31:  -0.0014 S32:  -0.3309 S33:  -0.2555                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    50        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4580  52.7420   0.1980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0718 T22:   0.0268                                     
REMARK   3      T33:   0.0533 T12:  -0.0163                                     
REMARK   3      T13:  -0.0026 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4413 L22:   0.8248                                     
REMARK   3      L33:   6.1039 L12:  -0.1070                                     
REMARK   3      L13:   0.8595 L23:  -0.2240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0442 S12:   0.2961 S13:   0.0267                       
REMARK   3      S21:  -0.1314 S22:  -0.0058 S23:  -0.0012                       
REMARK   3      S31:   0.1385 S32:   0.1646 S33:   0.0500                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    71        A   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4699  58.3632  17.4768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0158 T22:   0.0486                                     
REMARK   3      T33:   0.0046 T12:  -0.0206                                     
REMARK   3      T13:  -0.0047 T23:   0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4661 L22:   3.0432                                     
REMARK   3      L33:   1.9834 L12:  -1.2482                                     
REMARK   3      L13:  -0.0183 L23:  -0.3781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:  -0.1903 S13:  -0.0684                       
REMARK   3      S21:   0.0974 S22:   0.0013 S23:   0.0540                       
REMARK   3      S31:   0.0156 S32:  -0.1397 S33:  -0.0038                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   107        A   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9616  56.2713   3.3676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0134 T22:   0.0211                                     
REMARK   3      T33:   0.0271 T12:  -0.0111                                     
REMARK   3      T13:  -0.0153 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1191 L22:   0.8920                                     
REMARK   3      L33:   4.6545 L12:  -0.4543                                     
REMARK   3      L13:  -2.7604 L23:   0.9563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0051 S12:   0.1490 S13:  -0.0888                       
REMARK   3      S21:  -0.0309 S22:   0.0755 S23:   0.0442                       
REMARK   3      S31:   0.0021 S32:  -0.0803 S33:  -0.0806                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   128        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8966  63.9264  21.1317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0541 T22:   0.0655                                     
REMARK   3      T33:   0.0365 T12:  -0.0183                                     
REMARK   3      T13:  -0.0133 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4611 L22:   2.1283                                     
REMARK   3      L33:   1.8566 L12:  -0.4404                                     
REMARK   3      L13:   0.1014 L23:   0.6035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0155 S12:  -0.1584 S13:   0.0206                       
REMARK   3      S21:   0.2899 S22:   0.0353 S23:  -0.1064                       
REMARK   3      S31:   0.0022 S32:  -0.0359 S33:  -0.0198                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   154        A   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6673  56.1656  14.0054              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0539 T22:   0.1634                                     
REMARK   3      T33:   0.1136 T12:  -0.0363                                     
REMARK   3      T13:  -0.0276 T23:   0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.9286 L22:   4.3850                                     
REMARK   3      L33:   8.7152 L12:  -2.4774                                     
REMARK   3      L13:  -8.6091 L23:   2.0152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0463 S12:   0.1794 S13:   0.0165                       
REMARK   3      S21:  -0.1105 S22:  -0.0423 S23:  -0.4775                       
REMARK   3      S31:  -0.0924 S32:   0.3655 S33:  -0.0040                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5D25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212563.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12993                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, HEPES, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
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       19.68000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.02500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.90500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       29.02500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.68000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.90500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 520 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7450 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     GLU A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 56M A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 A 203                 
DBREF  5D25 A   43   168  UNP    O60885   BRD4_HUMAN      43    168             
SEQADV 5D25 MET A   43  UNP  O60885    THR    43 ENGINEERED MUTATION            
SEQRES   1 A  126  MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN LYS          
SEQRES   2 A  126  PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU ARG          
SEQRES   3 A  126  VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA TRP          
SEQRES   4 A  126  PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN LEU          
SEQRES   5 A  126  PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP MET          
SEQRES   6 A  126  GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR TRP          
SEQRES   7 A  126  ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET PHE          
SEQRES   8 A  126  THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP ILE          
SEQRES   9 A  126  VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU GLN          
SEQRES  10 A  126  LYS ILE ASN GLU LEU PRO THR GLU GLU                          
HET    56M  A 201      28                                                       
HET    GOL  A 202       6                                                       
HET    BU3  A 203       6                                                       
HETNAM     56M 4-ACETYL-N-[5-(DIETHYLSULFAMOYL)-2-HYDROXYPHENYL]-3,5-           
HETNAM   2 56M  DIMETHYL-1H-PYRROLE-2-CARBOXAMIDE                               
HETNAM     GOL GLYCEROL                                                         
HETNAM     BU3 (R,R)-2,3-BUTANEDIOL                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  56M    C19 H25 N3 O5 S                                              
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  BU3    C4 H10 O2                                                    
FORMUL   5  HOH   *103(H2 O)                                                    
HELIX    1 AA1 THR A   60  VAL A   69  1                                  10    
HELIX    2 AA2 VAL A   69  LYS A   76  1                                   8    
HELIX    3 AA3 ALA A   80  GLN A   84  5                                   5    
HELIX    4 AA4 ASP A   96  ILE A  101  1                                   6    
HELIX    5 AA5 ASP A  106  ASN A  117  1                                  12    
HELIX    6 AA6 ASN A  121  ASN A  140  1                                  20    
HELIX    7 AA7 ASP A  144  ASN A  162  1                                  19    
SITE     1 AC1 15 GLN A  59  PRO A  82  GLN A  85  VAL A  87                    
SITE     2 AC1 15 LYS A  91  LEU A  92  ASN A 117  ASN A 140                    
SITE     3 AC1 15 ILE A 146  GOL A 202  BU3 A 203  HOH A 317                    
SITE     4 AC1 15 HOH A 323  HOH A 327  HOH A 379                               
SITE     1 AC2  3 ASP A 145  56M A 201  HOH A 360                               
SITE     1 AC3  7 GLN A  59  GLN A  64  LEU A 114  ASN A 117                    
SITE     2 AC3  7 56M A 201  HOH A 305  HOH A 364                               
CRYST1   39.360   49.810   58.050  90.00  90.00  90.00 P 21 21 21    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      0.025407  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020076  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017227        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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