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Database: PDB
Entry: 2YEM
LinkDB: 2YEM
Original site: 2YEM 
HEADER    SIGNALING PROTEIN                       25-MAR-11   2YEM              
TITLE     CRYSTAL STRUCTURE OF THE SECOND BROMODOMAIN OF HUMAN BRD4 WITH THE    
TITLE    2 INHIBITOR GW841819X                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TERMINAL BROMODOMAIN, RESIDUES 333-460;                  
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SIGNALING PROTEIN, HISTONE, EPIGENETIC READER                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.W.CHUNG                                                             
REVDAT   4   20-DEC-23 2YEM    1       REMARK                                   
REVDAT   3   21-AUG-19 2YEM    1       REMARK                                   
REVDAT   2   08-MAY-13 2YEM    1       COMPND                                   
REVDAT   1   15-JUN-11 2YEM    0                                                
JRNL        AUTH   C.W.CHUNG,H.COSTE,J.H.WHITE,O.MIRGUET,J.WILDE,R.L.GOSMINI,   
JRNL        AUTH 2 C.DELVES,S.M.MAGNY,R.WOODWARD,S.A.HUGHES,E.V.BOURSIER,       
JRNL        AUTH 3 H.FLYNN,A.M.BOUILLOT,P.BAMBOROUGH,J.M.BRUSQ,F.J.GELLIBERT,   
JRNL        AUTH 4 E.J.JONES,A.M.RIOU,P.HOMES,S.L.MARTIN,I.J.UINGS,J.TOUM,      
JRNL        AUTH 5 C.A.CLEMENT,A.B.BOULLAY,R.L.GRIMLEY,F.M.BLANDEL,R.K.PRINJHA, 
JRNL        AUTH 6 K.LEE,J.KIRILOVSKY,E.NICODEME                                
JRNL        TITL   DISCOVERY AND CHARACTERIZATION OF SMALL MOLECULE INHIBITORS  
JRNL        TITL 2 OF THE BET FAMILY BROMODOMAINS.                              
JRNL        REF    J.MED.CHEM.                   V.  54  3827 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21568322                                                     
JRNL        DOI    10.1021/JM200108T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14004                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 745                             
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 998                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 60                           
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1802                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.96                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.13000                                              
REMARK   3    B22 (A**2) : -0.90000                                             
REMARK   3    B33 (A**2) : -2.23000                                             
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): 0.250         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.062        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1966 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1386 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2652 ; 1.081 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3363 ; 0.820 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   231 ; 4.524 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;31.148 ;23.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   354 ;15.899 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;18.170 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   261 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2269 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   452 ; 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):  1136 ; 0.721 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   443 ; 0.090 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1833 ; 1.435 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   830 ; 1.792 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   816 ; 2.756 ; 6.000       
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  : 2                                          
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   349        A   458                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7633   6.4512 -24.0448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0138 T22:   0.0439                                     
REMARK   3      T33:   0.0833 T12:  -0.0109                                     
REMARK   3      T13:   0.0005 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7726 L22:   3.5029                                     
REMARK   3      L33:   3.1457 L12:  -0.1314                                     
REMARK   3      L13:   0.2766 L23:   0.0924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0615 S12:  -0.0586 S13:   0.0249                       
REMARK   3      S21:   0.0114 S22:   0.0895 S23:  -0.0672                       
REMARK   3      S31:  -0.1683 S32:   0.1675 S33:  -0.0280                       
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   349        B   459                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9962   3.6294 -45.0215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0320 T22:   0.1269                                     
REMARK   3      T33:   0.0375 T12:  -0.0376                                     
REMARK   3      T13:   0.0259 T23:  -0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6045 L22:   2.8329                                     
REMARK   3      L33:   4.9280 L12:  -1.2955                                     
REMARK   3      L13:   2.4160 L23:  -1.5470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1143 S12:   0.2679 S13:   0.0460                       
REMARK   3      S21:  -0.1892 S22:   0.0090 S23:  -0.2127                       
REMARK   3      S31:  -0.0754 S32:   0.6317 S33:   0.1053                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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.                                                          
REMARK   4                                                                      
REMARK   4 2YEM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290047844.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-09                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14749                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OUO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M (NH4)2SO4, 0.1 M TRIS PH 8.5.      
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       29.83700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.18100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.74600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.18100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.83700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.74600            
REMARK 290   SMTRY3   4  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 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 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     SER A   331                                                      
REMARK 465     MET A   332                                                      
REMARK 465     LYS A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     VAL A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     ASP A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     GLN A   339                                                      
REMARK 465     GLN A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     ALA A   343                                                      
REMARK 465     PRO A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     LYS A   346                                                      
REMARK 465     SER A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     ASP A   459                                                      
REMARK 465     GLU A   460                                                      
REMARK 465     SER B   331                                                      
REMARK 465     MET B   332                                                      
REMARK 465     LYS B   333                                                      
REMARK 465     ASP B   334                                                      
REMARK 465     VAL B   335                                                      
REMARK 465     PRO B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     SER B   338                                                      
REMARK 465     GLN B   339                                                      
REMARK 465     GLN B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     PRO B   342                                                      
REMARK 465     ALA B   343                                                      
REMARK 465     PRO B   344                                                      
REMARK 465     GLU B   345                                                      
REMARK 465     LYS B   346                                                      
REMARK 465     SER B   347                                                      
REMARK 465     SER B   348                                                      
REMARK 465     GLU B   460                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WSH A 1459                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WSH B 1460                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YEL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 WITH THE    
REMARK 900 INHIBITOR GW841819X                                                  
REMARK 900 RELATED ID: 2YEK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD2 WITH THE    
REMARK 900 INHIBITOR GSK525762 (IBET)                                           
DBREF  2YEM A  333   460  UNP    O60885   BRD4_HUMAN     333    460             
DBREF  2YEM B  333   460  UNP    O60885   BRD4_HUMAN     333    460             
SEQADV 2YEM SER A  331  UNP  O60885              EXPRESSION TAG                 
SEQADV 2YEM MET A  332  UNP  O60885              EXPRESSION TAG                 
SEQADV 2YEM SER B  331  UNP  O60885              EXPRESSION TAG                 
SEQADV 2YEM MET B  332  UNP  O60885              EXPRESSION TAG                 
SEQRES   1 A  130  SER MET LYS ASP VAL PRO ASP SER GLN GLN HIS PRO ALA          
SEQRES   2 A  130  PRO GLU LYS SER SER LYS VAL SER GLU GLN LEU LYS CYS          
SEQRES   3 A  130  CYS SER GLY ILE LEU LYS GLU MET PHE ALA LYS LYS HIS          
SEQRES   4 A  130  ALA ALA TYR ALA TRP PRO PHE TYR LYS PRO VAL ASP VAL          
SEQRES   5 A  130  GLU ALA LEU GLY LEU HIS ASP TYR CYS ASP ILE ILE LYS          
SEQRES   6 A  130  HIS PRO MET ASP MET SER THR ILE LYS SER LYS LEU GLU          
SEQRES   7 A  130  ALA ARG GLU TYR ARG ASP ALA GLN GLU PHE GLY ALA ASP          
SEQRES   8 A  130  VAL ARG LEU MET PHE SER ASN CYS TYR LYS TYR ASN PRO          
SEQRES   9 A  130  PRO ASP HIS GLU VAL VAL ALA MET ALA ARG LYS LEU GLN          
SEQRES  10 A  130  ASP VAL PHE GLU MET ARG PHE ALA LYS MET PRO ASP GLU          
SEQRES   1 B  130  SER MET LYS ASP VAL PRO ASP SER GLN GLN HIS PRO ALA          
SEQRES   2 B  130  PRO GLU LYS SER SER LYS VAL SER GLU GLN LEU LYS CYS          
SEQRES   3 B  130  CYS SER GLY ILE LEU LYS GLU MET PHE ALA LYS LYS HIS          
SEQRES   4 B  130  ALA ALA TYR ALA TRP PRO PHE TYR LYS PRO VAL ASP VAL          
SEQRES   5 B  130  GLU ALA LEU GLY LEU HIS ASP TYR CYS ASP ILE ILE LYS          
SEQRES   6 B  130  HIS PRO MET ASP MET SER THR ILE LYS SER LYS LEU GLU          
SEQRES   7 B  130  ALA ARG GLU TYR ARG ASP ALA GLN GLU PHE GLY ALA ASP          
SEQRES   8 B  130  VAL ARG LEU MET PHE SER ASN CYS TYR LYS TYR ASN PRO          
SEQRES   9 B  130  PRO ASP HIS GLU VAL VAL ALA MET ALA ARG LYS LEU GLN          
SEQRES  10 B  130  ASP VAL PHE GLU MET ARG PHE ALA LYS MET PRO ASP GLU          
HET    WSH  A1459      32                                                       
HET    WSH  B1460      32                                                       
HETNAM     WSH BENZYL [(4R)-1-METHYL-6-PHENYL-4H-[1,2,4]TRIAZOLO[4,3-           
HETNAM   2 WSH  A][1,4]BENZODIAZEPIN-4-YL]CARBAMATE                             
FORMUL   3  WSH    2(C25 H21 N5 O2)                                             
FORMUL   5  HOH   *133(H2 O)                                                    
HELIX    1   1 LYS A  349  PHE A  365  1                                  17    
HELIX    2   2 ALA A  366  LYS A  368  5                                   3    
HELIX    3   3 HIS A  369  TRP A  374  1                                   6    
HELIX    4   4 PRO A  375  TYR A  377  5                                   3    
HELIX    5   5 ASP A  381  GLY A  386  1                                   6    
HELIX    6   6 ASP A  389  ILE A  394  1                                   6    
HELIX    7   7 ASP A  399  ALA A  409  1                                  11    
HELIX    8   8 ASP A  414  ASN A  433  1                                  20    
HELIX    9   9 HIS A  437  LYS A  456  1                                  20    
HELIX   10  10 LYS B  349  PHE B  365  1                                  17    
HELIX   11  11 ALA B  366  LYS B  368  5                                   3    
HELIX   12  12 HIS B  369  TRP B  374  1                                   6    
HELIX   13  13 PRO B  375  TYR B  377  5                                   3    
HELIX   14  14 ASP B  381  GLY B  386  1                                   6    
HELIX   15  15 ASP B  389  ILE B  394  1                                   6    
HELIX   16  16 ASP B  399  ALA B  409  1                                  11    
HELIX   17  17 ASP B  414  ASN B  433  1                                  20    
HELIX   18  18 HIS B  437  LYS B  456  1                                  20    
SITE     1 AC1  7 PRO A 375  ARG A 413  ASN A 433  VAL A 439                    
SITE     2 AC1  7 HOH A2034  HOH A2067  WSH B1460                               
SITE     1 AC2 10 TRP A 374  WSH A1459  TRP B 374  PRO B 375                    
SITE     2 AC2 10 LEU B 387  ASN B 433  HIS B 437  GLU B 438                    
SITE     3 AC2 10 VAL B 439  HOH B2021                                          
CRYST1   59.674   73.492   74.362  90.00  90.00  90.00 P 21 21 21    8          
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      0.016758  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013607  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013448        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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