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Database: PDB
Entry: 6E4A
LinkDB: 6E4A
Original site: 6E4A 
HEADER    PROTEIN BINDING                         17-JUL-18   6E4A              
TITLE     CRYSTAL STRUCTURE OF HUMAN BRD4(1) IN COMPLEX WITH CN750              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A, B;                                                         
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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS401                              
KEYWDS    BRD4(BD1), PROTEIN BINDING                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.FONTANO,A.WHITE,D.LAKSHMINARASIMHAN,R.K.SUTO                        
REVDAT   5   13-MAR-24 6E4A    1       REMARK                                   
REVDAT   4   24-OCT-18 6E4A    1       COMPND JRNL                              
REVDAT   3   10-OCT-18 6E4A    1       COMPND JRNL                              
REVDAT   2   03-OCT-18 6E4A    1       REMARK                                   
REVDAT   1   12-SEP-18 6E4A    0                                                
JRNL        AUTH   S.M.YANG,D.J.URBAN,M.YOSHIOKA,J.W.STROVEL,S.FLETCHER,        
JRNL        AUTH 2 A.Q.WANG,X.XU,P.SHAH,X.HU,M.D.HALL,A.JADHAV,D.J.MALONEY      
JRNL        TITL   DISCOVERY AND LEAD IDENTIFICATION OF QUINAZOLINE-BASED BRD4  
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    BIOORG. MED. CHEM. LETT.      V.  28  3483 2018              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   30268702                                                     
JRNL        DOI    10.1016/J.BMCL.2018.08.039                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 58739                          
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) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2857                            
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) : 1.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4138                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 178                          
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2095                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 450                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : 0.56000                                              
REMARK   3    B33 (A**2) : -0.46000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.050         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.053         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.721         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2400 ; 0.021 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  2305 ; 0.003 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3283 ; 2.297 ; 1.722       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5343 ; 1.189 ; 1.692       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   279 ; 6.023 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;40.416 ;25.780       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   422 ;13.521 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;12.003 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   302 ; 0.141 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2747 ; 0.015 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   551 ; 0.003 ; 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  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6E4A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000235690.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9774                             
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61603                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRISHCL PH 8.5, 25% PEG 3350,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.73400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     THR A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     GLU B   167                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     THR B   169                                                      
REMARK 465     GLU B   170                                                      
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   OE2  GLU A   151     O    HOH A   303              2.17            
REMARK 500   O    SER A    42     O    HOH A   304              2.18            
REMARK 500   O    HOH A   351     O    HOH A   391              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A 124   CD    GLU A 124   OE2    -0.091                       
REMARK 500    GLY A 143   N     GLY A 143   CA      0.115                       
REMARK 500    GLU B 124   CD    GLU B 124   OE2    -0.082                       
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    GLN A  59   CB  -  CA  -  C   ANGL. DEV. =  13.6 DEGREES          
REMARK 500    ARG B  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
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 HRY 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 HRY B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 203                 
DBREF  6E4A A   44   170  UNP    O60885   BRD4_HUMAN      44    170             
DBREF  6E4A B   44   170  UNP    O60885   BRD4_HUMAN      44    170             
SEQADV 6E4A SER A   42  UNP  O60885              EXPRESSION TAG                 
SEQADV 6E4A MET A   43  UNP  O60885              EXPRESSION TAG                 
SEQADV 6E4A SER B   42  UNP  O60885              EXPRESSION TAG                 
SEQADV 6E4A MET B   43  UNP  O60885              EXPRESSION TAG                 
SEQRES   1 A  129  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 A  129  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 A  129  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 A  129  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 A  129  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 A  129  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 A  129  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 A  129  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 A  129  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 A  129  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU THR GLU              
SEQRES   1 B  129  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 B  129  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 B  129  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA          
SEQRES   4 B  129  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 B  129  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 B  129  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 B  129  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 B  129  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 B  129  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 B  129  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU THR GLU              
HET    HRY  A 201      38                                                       
HET    GOL  A 202       6                                                       
HET    HRY  B 201      38                                                       
HET    GOL  B 202       6                                                       
HET    GOL  B 203       6                                                       
HETNAM     HRY 5-(4-{[(3-CHLOROPHENYL)METHYL]AMINO}-2-{4-[2-                    
HETNAM   2 HRY  (DIMETHYLAMINO)ETHYL]PIPERAZIN-1-YL}QUINAZOLIN-6-YL)-           
HETNAM   3 HRY  1-METHYLPYRIDIN-2(1H)-ONE                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  HRY    2(C29 H34 CL N7 O)                                           
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *450(H2 O)                                                    
HELIX    1 AA1 THR A   60  VAL A   69  1                                  10    
HELIX    2 AA2 VAL A   69  HIS A   77  1                                   9    
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  116  1                                  11    
HELIX    6 AA6 ASN A  121  ASN A  140  1                                  20    
HELIX    7 AA7 ASP A  144  GLU A  163  1                                  20    
HELIX    8 AA8 THR B   60  VAL B   69  1                                  10    
HELIX    9 AA9 VAL B   69  LYS B   76  1                                   8    
HELIX   10 AB1 ALA B   80  GLN B   84  5                                   5    
HELIX   11 AB2 ASP B   96  ILE B  101  1                                   6    
HELIX   12 AB3 ASP B  106  ASN B  116  1                                  11    
HELIX   13 AB4 ASN B  121  ASN B  140  1                                  20    
HELIX   14 AB5 ASP B  144  ASN B  162  1                                  19    
SITE     1 AC1  9 TRP A  81  PRO A  82  LEU A  92  ASN A 140                    
SITE     2 AC1  9 ILE A 146  MET A 149  HOH A 311  HOH A 376                    
SITE     3 AC1  9 HOH A 414                                                     
SITE     1 AC2  8 ILE A 100  ILE A 101  LYS A 102  THR A 103                    
SITE     2 AC2  8 ASN A 135  HOH A 346  HOH A 364  HOH A 441                    
SITE     1 AC3 15 LEU A 148  GLU A 151  LYS A 155  HOH A 310                    
SITE     2 AC3 15 TRP B  81  PRO B  82  PHE B  83  VAL B  87                    
SITE     3 AC3 15 LEU B  92  ASN B 140  MET B 149  HOH B 317                    
SITE     4 AC3 15 HOH B 431  HOH B 446  HOH B 447                               
SITE     1 AC4  7 ILE B 100  ILE B 101  LYS B 102  THR B 103                    
SITE     2 AC4  7 THR B 134  ASN B 135  HOH B 412                               
SITE     1 AC5  4 ARG B  68  LYS B  72  HOH B 306  HOH B 451                    
CRYST1   41.477   51.468   55.297  90.00  90.22  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024110  0.000000  0.000091        0.00000                         
SCALE2      0.000000  0.019430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018084        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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