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Database: PDB
Entry: 4MR3
LinkDB: 4MR3
Original site: 4MR3 
HEADER    TRANSCRIPTION/TRANSCRIPTION INHIBITOR   17-SEP-13   4MR3              
TITLE     CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX   
TITLE    2 WITH A QUINAZOLINONE LIGAND (RVX-OH)                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 44-168;                                       
COMPND   5 SYNONYM: PROTEIN HUNK1;                                              
COMPND   6 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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    BRD4, CAP, HUNK1, MCAP, MITOTIC CHROMOSOME ASSOCIATED PROTEIN, BRD,   
KEYWDS   2 SMALL MOLECULE INHIBITOR, RVX-OH, STRUCTURAL GENOMICS CONSORTIUM,    
KEYWDS   3 SGC, TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FILIPPAKOPOULOS,S.PICAUD,I.FELLETAR,S.MARTIN,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   3   20-SEP-23 4MR3    1       REMARK SEQADV                            
REVDAT   2   22-JAN-14 4MR3    1       JRNL                                     
REVDAT   1   27-NOV-13 4MR3    0                                                
JRNL        AUTH   S.PICAUD,C.WELLS,I.FELLETAR,D.BROTHERTON,S.MARTIN,           
JRNL        AUTH 2 P.SAVITSKY,B.DIEZ-DACAL,M.PHILPOTT,C.BOUNTRA,H.LINGARD,      
JRNL        AUTH 3 O.FEDOROV,S.MULLER,P.E.BRENNAN,S.KNAPP,P.FILIPPAKOPOULOS     
JRNL        TITL   RVX-208, AN INHIBITOR OF BET TRANSCRIPTIONAL REGULATORS WITH 
JRNL        TITL 2 SELECTIVITY FOR THE SECOND BROMODOMAIN.                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 19754 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24248379                                                     
JRNL        DOI    10.1073/PNAS.1310658110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.68 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) : 1.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 14232                          
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) : 0.142                           
REMARK   3   R VALUE            (WORKING SET) : 0.140                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 728                             
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) : 1.68                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 902                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 44                           
REMARK   3   BIN FREE R VALUE                    : 0.1860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1050                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 195                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14000                                              
REMARK   3    B22 (A**2) : -0.21000                                             
REMARK   3    B33 (A**2) : 0.07000                                              
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): 0.095         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.099         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.055         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.980         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1122 ; 0.013 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1063 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1531 ; 1.571 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2449 ; 0.847 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   130 ; 5.332 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;36.632 ;25.472       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   194 ;13.035 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;16.141 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   160 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1359 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   255 ; 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):   511 ; 2.963 ; 1.078       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   512 ; 2.960 ; 1.078       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   638 ; 3.844 ; 1.957       
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  : 1                                          
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   168                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1119  35.0357  12.9267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0479 T22:   0.0455                                     
REMARK   3      T33:   0.0489 T12:  -0.0010                                     
REMARK   3      T13:   0.0028 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2303 L22:   0.1587                                     
REMARK   3      L33:   0.2508 L12:  -0.0527                                     
REMARK   3      L13:   0.0043 L23:   0.1413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0044 S12:  -0.0259 S13:  -0.0085                       
REMARK   3      S21:  -0.0066 S22:   0.0056 S23:  -0.0032                       
REMARK   3      S31:  -0.0064 S32:   0.0073 S33:  -0.0101                       
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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES: WITH TLS ADDED                                            
REMARK   4                                                                      
REMARK   4 4MR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082260.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14268                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.03200                            
REMARK 200  R SYM                      (I) : 0.03200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 13.90                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.2                                          
REMARK 200 STARTING MODEL: PDB ENTRY 2OSS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NABR, 0.1M BTPROP, 20.0% PEG3350,   
REMARK 280  10% ETGLY, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  277K                                                                
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       20.87000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.76950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.98600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       28.76950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.87000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.98600            
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 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 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     LYS A  76    NZ                                                  
REMARK 470     LYS A 155    CE   NZ                                             
REMARK 470     GLU A 167    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 168    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 A   369     O    HOH A   422              1.77            
REMARK 500   O    HOH A   452     O    HOH A   482              2.09            
REMARK 500   NH2  ARG A    68     O    HOH A   459              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1K0 A  202                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1K0 A 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MR4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MR5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MR6   RELATED DB: PDB                                   
DBREF  4MR3 A   44   168  UNP    O60885   BRD4_HUMAN      44    168             
SEQADV 4MR3 SER A   42  UNP  O60885              EXPRESSION TAG                 
SEQADV 4MR3 MET A   43  UNP  O60885              EXPRESSION TAG                 
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                      
HET    EDO  A 201       4                                                       
HET    1K0  A 202      24                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     1K0 2-[4-(2-HYDROXYETHOXY)-3,5-DIMETHYLPHENYL]-5,7-                  
HETNAM   2 1K0  DIMETHOXYQUINAZOLIN-4(3H)-ONE                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    C2 H6 O2                                                     
FORMUL   3  1K0    C20 H22 N2 O5                                                
FORMUL   4  HOH   *195(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   88  ASN A   93  1                                   6    
HELIX    5   5 ASP A   96  ILE A  101  1                                   6    
HELIX    6   6 ASP A  106  ASN A  116  1                                  11    
HELIX    7   7 ASN A  121  ASN A  140  1                                  20    
HELIX    8   8 ASP A  144  GLU A  163  1                                  20    
SITE     1 AC1  6 ILE A 100  LYS A 102  THR A 103  ASN A 135                    
SITE     2 AC1  6 ILE A 138  HOH A 443                                          
SITE     1 AC2 14 PRO A  82  PHE A  83  GLN A  85  VAL A  87                    
SITE     2 AC2 14 LEU A  92  TYR A 139  ASN A 140  ILE A 146                    
SITE     3 AC2 14 HOH A 304  HOH A 310  HOH A 336  HOH A 364                    
SITE     4 AC2 14 HOH A 474  HOH A 486                                          
CRYST1   41.740   51.972   57.539  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      0.023958  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019241  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017380        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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