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Database: PDB
Entry: 3U5K
LinkDB: 3U5K
Original site: 3U5K 
HEADER    SIGNALING PROTEIN/INHIBITOR             11-OCT-11   3U5K              
TITLE     CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX   
TITLE    2 WITH MIDAZOLAM                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PROTEIN HUNK1;                                              
COMPND   5 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: BRD4, HUNK1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    BROMODOMAIN-CONTAINING PROTEIN 4 ISOFORM LONG, BRD4, BROMODOMAIN      
KEYWDS   2 CONTAINING PROTEIN 4, CAP, HUNK1, MCAP, MITOTIC CHROMOSOME           
KEYWDS   3 ASSOCIATED PROTEIN, STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNALING   
KEYWDS   4 PROTEIN-INHIBITOR COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FILIPPAKOPOULOS,S.PICAUD,I.FELLETAR,O.FEDOROV,F.VON DELFT,          
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,STRUCTURAL    
AUTHOR   3 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   4   13-SEP-23 3U5K    1       REMARK SEQADV                            
REVDAT   3   21-MAR-12 3U5K    1       JRNL                                     
REVDAT   2   07-MAR-12 3U5K    1       JRNL                                     
REVDAT   1   23-NOV-11 3U5K    0                                                
JRNL        AUTH   P.FILIPPAKOPOULOS,S.PICAUD,O.FEDOROV,M.KELLER,M.WROBEL,      
JRNL        AUTH 2 O.MORGENSTERN,F.BRACHER,S.KNAPP                              
JRNL        TITL   BENZODIAZEPINES AND BENZOTRIAZEPINES AS PROTEIN INTERACTION  
JRNL        TITL 2 INHIBITORS TARGETING BROMODOMAINS OF THE BET FAMILY.         
JRNL        REF    BIOORG.MED.CHEM.              V.  20  1878 2012              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   22137933                                                     
JRNL        DOI    10.1016/J.BMC.2011.10.080                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 51217                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1921                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3088                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.4340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4035                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 231                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.38000                                              
REMARK   3    B22 (A**2) : 0.38000                                              
REMARK   3    B33 (A**2) : -0.76000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.030         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.103         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.613         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4278 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2876 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5848 ; 1.640 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7023 ; 1.011 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   491 ; 6.135 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   189 ;34.941 ;25.344       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   713 ;15.961 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;18.955 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   624 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4624 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   772 ; 0.001 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.505                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.495                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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    42        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  79.4670   8.8604  11.4359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1009 T22:   0.1021                                     
REMARK   3      T33:   0.1445 T12:   0.0048                                     
REMARK   3      T13:   0.0125 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1470 L22:   0.5590                                     
REMARK   3      L33:   0.1032 L12:   0.2349                                     
REMARK   3      L13:  -0.0830 L23:  -0.0570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0031 S12:   0.0415 S13:   0.0050                       
REMARK   3      S21:   0.0448 S22:   0.0320 S23:   0.0076                       
REMARK   3      S31:   0.0042 S32:  -0.0004 S33:  -0.0289                       
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 :   B    43        B   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.9520  39.2403  -1.8961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1017 T22:   0.1192                                     
REMARK   3      T33:   0.1251 T12:   0.0141                                     
REMARK   3      T13:   0.0089 T23:   0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4530 L22:   0.3778                                     
REMARK   3      L33:   0.0280 L12:  -0.0621                                     
REMARK   3      L13:   0.0581 L23:   0.0329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0157 S12:   0.0260 S13:   0.0081                       
REMARK   3      S21:   0.0299 S22:   0.0536 S23:   0.0198                       
REMARK   3      S31:  -0.0146 S32:  -0.0055 S33:  -0.0379                       
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 :   C    43        C   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.1478  25.3132  32.9712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0919 T22:   0.1061                                     
REMARK   3      T33:   0.1332 T12:  -0.0169                                     
REMARK   3      T13:   0.0171 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3760 L22:   0.4689                                     
REMARK   3      L33:   0.2669 L12:  -0.2074                                     
REMARK   3      L13:  -0.0171 L23:  -0.2923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:  -0.0501 S13:   0.0131                       
REMARK   3      S21:  -0.0772 S22:   0.0526 S23:   0.0216                       
REMARK   3      S31:   0.0538 S32:  -0.0362 S33:  -0.0538                       
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 :   D    42        D   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.4514  46.8087  11.4293              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1208 T22:   0.0906                                     
REMARK   3      T33:   0.1529 T12:  -0.0181                                     
REMARK   3      T13:   0.0159 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3897 L22:   0.4822                                     
REMARK   3      L33:   0.0968 L12:  -0.4151                                     
REMARK   3      L13:  -0.1865 L23:   0.2034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0649 S12:  -0.0339 S13:   0.0118                       
REMARK   3      S21:  -0.0472 S22:  -0.0235 S23:  -0.0220                       
REMARK   3      S31:  -0.0321 S32:   0.0082 S33:  -0.0414                       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS; U VALUES: WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 3U5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068333.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.52                               
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51230                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.52200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: 2OSS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.5, 0.1M MGCL, 15% PEG      
REMARK 280  6000, 10% ETGLY, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.47033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       42.94067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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   168                                                      
REMARK 465     SER B    42                                                      
REMARK 465     GLU B   167                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     SER C    42                                                      
REMARK 465     THR C   166                                                      
REMARK 465     GLU C   167                                                      
REMARK 465     GLU C   168                                                      
REMARK 465     ASN D    54                                                      
REMARK 465     LYS D    55                                                      
REMARK 465     PRO D    56                                                      
REMARK 465     GLU D   168                                                      
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     GLU A 163    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 167    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  76    CD   CE   NZ                                        
REMARK 470     GLU C  49    CG   CD   OE1  OE2                                  
REMARK 470     ASN C  52    CG   OD1  ND2                                       
REMARK 470     ASN C  54    CG   OD1  ND2                                       
REMARK 470     LYS C  55    CG   CD   CE   NZ                                   
REMARK 470     LYS C  57    CG   CD   CE   NZ                                   
REMARK 470     GLN C  59    CG   CD   OE1  NE2                                  
REMARK 470     ASN C  61    CG   OD1  ND2                                       
REMARK 470     GLN C  62    CD   OE1  NE2                                       
REMARK 470     LYS C  76    CG   CD   CE   NZ                                   
REMARK 470     LYS C 112    CG   CD   CE   NZ                                   
REMARK 470     GLU C 124    CD   OE1  OE2                                       
REMARK 470     GLU C 151    CD   OE1  OE2                                       
REMARK 470     ASN C 162    CG   OD1  ND2                                       
REMARK 470     GLU C 163    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 164    CG   CD1  CD2                                       
REMARK 470     SER D  42    OG                                                  
REMARK 470     GLU D  49    CG   CD   OE1  OE2                                  
REMARK 470     SER D  51    OG                                                  
REMARK 470     ASN D  52    CG   OD1  ND2                                       
REMARK 470     LYS D  57    CG   CD   CE   NZ                                   
REMARK 470     GLN D  59    CG   CD   OE1  NE2                                  
REMARK 470     ASN D  61    CG   OD1  ND2                                       
REMARK 470     GLN D  62    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  76    NZ                                                  
REMARK 470     LYS D  91    CE   NZ                                             
REMARK 470     LYS D 155    CD   CE   NZ                                        
REMARK 470     GLN D 159    CD   OE1  NE2                                       
REMARK 470     LYS D 160    CE   NZ                                             
REMARK 470     ASN D 162    CG   OD1  ND2                                       
REMARK 470     GLU D 163    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 164    CG   CD1  CD2                                       
REMARK 470     GLU D 167    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   193     O    HOH B   214              2.02            
REMARK 500   NE2  GLN A   159     O    HOH A   178              2.12            
REMARK 500   OD1  ASP C   144     O    HOH C   213              2.15            
REMARK 500   OE1  GLN D    85     O    HOH D   179              2.16            
REMARK 500   OG1  THR C   109     O    HOH C   197              2.19            
REMARK 500   O    HOH B   179     O    HOH B   210              2.19            
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    VAL A  69      -62.99   -127.02                                   
REMARK 500    ASN B  52      105.80   -166.15                                   
REMARK 500    VAL B  69      -50.71   -122.64                                   
REMARK 500    LEU B  94       76.84   -113.75                                   
REMARK 500    ASP B 145      -55.24    -24.88                                   
REMARK 500    ASN B 162      -38.89    -31.73                                   
REMARK 500    ASN D  52      107.58   -160.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J C 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 08J D 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U5J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U5L   RELATED DB: PDB                                   
DBREF  3U5K A   42   168  UNP    O60885   BRD4_HUMAN      42    168             
DBREF  3U5K B   42   168  UNP    O60885   BRD4_HUMAN      42    168             
DBREF  3U5K C   42   168  UNP    O60885   BRD4_HUMAN      42    168             
DBREF  3U5K D   42   168  UNP    O60885   BRD4_HUMAN      42    168             
SEQADV 3U5K MET A   43  UNP  O60885    THR    43 CLONING ARTIFACT               
SEQADV 3U5K MET B   43  UNP  O60885    THR    43 CLONING ARTIFACT               
SEQADV 3U5K MET C   43  UNP  O60885    THR    43 CLONING ARTIFACT               
SEQADV 3U5K MET D   43  UNP  O60885    THR    43 CLONING ARTIFACT               
SEQRES   1 A  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 A  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 A  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 A  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 A  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 A  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 A  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 A  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 A  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 A  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
SEQRES   1 B  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 B  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 B  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 B  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 B  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 B  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 B  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 B  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 B  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 B  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
SEQRES   1 C  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 C  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 C  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 C  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 C  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 C  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 C  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 C  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 C  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 C  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
SEQRES   1 D  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 D  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 D  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 D  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 D  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 D  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 D  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 D  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 D  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 D  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
HET    08J  A   1      23                                                       
HET    08J  B   2      23                                                       
HET    08J  C   3      23                                                       
HET    08J  D   4      23                                                       
HETNAM     08J 8-CHLORO-6-(2-FLUOROPHENYL)-1-METHYL-4H-IMIDAZO[1,5-             
HETNAM   2 08J  A][1,4]BENZODIAZEPINE                                           
HETSYN     08J MIDAZOLAM                                                        
FORMUL   5  08J    4(C18 H13 CL F N3)                                           
FORMUL   9  HOH   *231(H2 O)                                                    
HELIX    1   1 THR A   60  VAL A   69  1                                  10    
HELIX    2   2 VAL A   69  LYS A   76  1                                   8    
HELIX    3   3 ALA A   80  GLN A   84  5                                   5    
HELIX    4   4 ASP A   96  ILE A  101  1                                   6    
HELIX    5   5 ASP A  106  ASN A  116  1                                  11    
HELIX    6   6 ASN A  121  ASN A  140  1                                  20    
HELIX    7   7 ASP A  144  ILE A  161  1                                  18    
HELIX    8   8 ASN A  162  LEU A  164  5                                   3    
HELIX    9   9 THR B   60  VAL B   69  1                                  10    
HELIX   10  10 VAL B   69  LYS B   76  1                                   8    
HELIX   11  11 ALA B   80  GLN B   84  5                                   5    
HELIX   12  12 ASP B   96  ILE B  101  1                                   6    
HELIX   13  13 ASP B  106  ASN B  116  1                                  11    
HELIX   14  14 ASN B  121  ASN B  140  1                                  20    
HELIX   15  15 ASP B  144  ASN B  162  1                                  19    
HELIX   16  16 THR C   60  VAL C   69  1                                  10    
HELIX   17  17 VAL C   69  LYS C   76  1                                   8    
HELIX   18  18 ALA C   80  GLN C   84  5                                   5    
HELIX   19  19 ASP C   96  ILE C  101  1                                   6    
HELIX   20  20 ASP C  106  ASN C  116  1                                  11    
HELIX   21  21 ASN C  121  ASN C  140  1                                  20    
HELIX   22  22 ASP C  144  ILE C  161  1                                  18    
HELIX   23  23 THR D   60  VAL D   69  1                                  10    
HELIX   24  24 VAL D   69  LYS D   76  1                                   8    
HELIX   25  25 ALA D   80  GLN D   84  5                                   5    
HELIX   26  26 ASP D   96  ILE D  101  1                                   6    
HELIX   27  27 ASP D  106  ASN D  116  1                                  11    
HELIX   28  28 ASN D  121  ASN D  140  1                                  20    
HELIX   29  29 ASP D  144  GLU D  163  1                                  20    
SITE     1 AC1 10 HOH A   5  TRP A  81  PRO A  82  VAL A  87                    
SITE     2 AC1 10 LEU A  92  LEU A  94  ASN A 140  ILE A 146                    
SITE     3 AC1 10 HOH A 169  HOH A 187                                          
SITE     1 AC2  9 TRP B  81  PRO B  82  LEU B  92  LEU B  94                    
SITE     2 AC2  9 ASN B 140  ILE B 146  HOH B 169  HOH B 231                    
SITE     3 AC2  9 HOH B 232                                                     
SITE     1 AC3  9 HOH C  28  TRP C  81  PRO C  82  VAL C  87                    
SITE     2 AC3  9 LEU C  92  ASN C 140  ILE C 146  MET C 149                    
SITE     3 AC3  9 HOH C 199                                                     
SITE     1 AC4  8 TRP D  81  PRO D  82  PHE D  83  LEU D  92                    
SITE     2 AC4  8 LEU D  94  ASN D 140  ILE D 146  MET D 149                    
CRYST1   89.550   89.550   64.411  90.00  90.00 120.00 P 31         12          
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      0.011167  0.006447  0.000000        0.00000                         
SCALE2      0.000000  0.012895  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015525        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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