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Database: PDB
Entry: 5D3S
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Original site: 5D3S 
HEADER    TRANSCRIPTION                           06-AUG-15   5D3S              
TITLE     FIRST BROMODOMAIN OF BRD4 BOUND TO INHIBITOR XD44                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FIRST BROMODOMAIN, UNP RESIDUES 44-168;                    
COMPND   5 SYNONYM: PROTEIN HUNK1;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRD4, HUNK1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GENE REGULATION, BROMODOMAIN, INHIBITOR, TRANSCRIPTION                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WOHLWEND,M.HUEGLE                                                   
REVDAT   3   06-SEP-17 5D3S    1       REMARK                                   
REVDAT   2   09-MAR-16 5D3S    1       JRNL                                     
REVDAT   1   20-JAN-16 5D3S    0                                                
JRNL        AUTH   M.HUGLE,X.LUCAS,G.WEITZEL,D.OSTROVSKYI,B.BREIT,S.GERHARDT,   
JRNL        AUTH 2 O.EINSLE,S.GUNTHER,D.WOHLWEND                                
JRNL        TITL   4-ACYL PYRROLE DERIVATIVES YIELD NOVEL VECTORS FOR DESIGNING 
JRNL        TITL 2 INHIBITORS OF THE ACETYL-LYSINE RECOGNITION SITE OF BRD4(1). 
JRNL        REF    J.MED.CHEM.                   V.  59  1518 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26731611                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01267                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 10693                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1151                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 782                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1046                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : 0.55000                                              
REMARK   3    B33 (A**2) : -0.51000                                             
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): 0.147         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.054         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1146 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1093 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1566 ; 1.356 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2523 ; 0.773 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   131 ; 4.748 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    54 ;40.487 ;25.926       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   199 ;13.684 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;19.207 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   164 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1289 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   256 ; 0.004 ; 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):   518 ; 0.386 ; 0.765       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   517 ; 0.387 ; 0.763       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   651 ; 0.677 ; 1.142       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   652 ; 0.677 ; 1.145       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   628 ; 0.685 ; 0.918       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   629 ; 0.684 ; 0.921       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):   916 ; 1.002 ; 1.346       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4843 ; 3.333 ; 7.917       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4740 ; 3.063 ; 7.555       
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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A    52                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2544  -9.9158 -23.5208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0359 T22:   0.1504                                     
REMARK   3      T33:   0.0683 T12:   0.0007                                     
REMARK   3      T13:   0.0418 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0033 L22:   6.1722                                     
REMARK   3      L33:   6.0204 L12:  -0.5501                                     
REMARK   3      L13:   4.7179 L23:  -1.1438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0930 S12:   0.9318 S13:   0.0194                       
REMARK   3      S21:  -0.1266 S22:  -0.1571 S23:   0.0159                       
REMARK   3      S31:   0.0116 S32:   0.8832 S33:   0.0641                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    53        A    57                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5908  -6.2480 -37.1042              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2049 T22:   0.2295                                     
REMARK   3      T33:   0.1968 T12:  -0.0149                                     
REMARK   3      T13:   0.0275 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8136 L22:   0.8487                                     
REMARK   3      L33:   0.3408 L12:  -1.8591                                     
REMARK   3      L13:   1.5898 L23:  -0.4588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0138 S12:   0.1210 S13:  -0.1878                       
REMARK   3      S21:  -0.0482 S22:   0.0067 S23:  -0.1553                       
REMARK   3      S31:   0.0151 S32:   0.0320 S33:   0.0071                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    58        A   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4625  -6.0006 -16.6368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0280 T22:   0.0113                                     
REMARK   3      T33:   0.0209 T12:  -0.0091                                     
REMARK   3      T13:  -0.0079 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0270 L22:   1.5781                                     
REMARK   3      L33:   2.1870 L12:  -0.0598                                     
REMARK   3      L13:   1.0199 L23:   0.1405                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1356 S12:  -0.0460 S13:   0.1520                       
REMARK   3      S21:   0.0645 S22:   0.0128 S23:  -0.0570                       
REMARK   3      S31:  -0.1692 S32:   0.0839 S33:   0.1228                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   118        A   152                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1249 -13.0268 -13.5648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0170 T22:   0.0214                                     
REMARK   3      T33:   0.0231 T12:  -0.0066                                     
REMARK   3      T13:   0.0153 T23:  -0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7148 L22:   1.4747                                     
REMARK   3      L33:   3.6216 L12:  -0.4816                                     
REMARK   3      L13:   2.0490 L23:  -1.4038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0220 S12:  -0.0828 S13:  -0.0750                       
REMARK   3      S21:   0.0694 S22:   0.0394 S23:   0.0677                       
REMARK   3      S31:   0.0554 S32:  -0.0955 S33:  -0.0614                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   153        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2379  -6.6416 -14.8567              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0417 T22:   0.0660                                     
REMARK   3      T33:   0.1041 T12:  -0.0118                                     
REMARK   3      T13:   0.0314 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7455 L22:   2.9501                                     
REMARK   3      L33:   7.3982 L12:  -0.3977                                     
REMARK   3      L13:   2.5571 L23:   0.4923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0970 S12:  -0.0139 S13:   0.0253                       
REMARK   3      S21:  -0.1737 S22:   0.0796 S23:   0.1855                       
REMARK   3      S31:  -0.0217 S32:  -0.3109 S33:   0.0174                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5D3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212624.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11878                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, BIS-TRIS, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.74000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.89500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       28.89500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.74000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.75500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 450 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7600 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   168                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     THR A  103   OG1                                                 
REMARK 480     LEU A  158   CD1  CD2                                            
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    THR A 103   CB    THR A 103   OG1    -0.273                       
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    THR A 103   CA  -  CB  -  OG1 ANGL. DEV. =  15.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  54       -9.20     76.70                                   
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 579 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 A 203                 
DBREF  5D3S A   44   168  UNP    O60885   BRD4_HUMAN      44    168             
SEQADV 5D3S MET A   43  UNP  O60885              INITIATING METHIONINE          
SEQRES   1 A  126  MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN LYS          
SEQRES   2 A  126  PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU ARG          
SEQRES   3 A  126  VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA TRP          
SEQRES   4 A  126  PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN LEU          
SEQRES   5 A  126  PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP MET          
SEQRES   6 A  126  GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR TRP          
SEQRES   7 A  126  ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET PHE          
SEQRES   8 A  126  THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP ILE          
SEQRES   9 A  126  VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU GLN          
SEQRES  10 A  126  LYS ILE ASN GLU LEU PRO THR GLU GLU                          
HET    579  A 201      30                                                       
HET    DMS  A 202       4                                                       
HET    BU3  A 203       6                                                       
HETNAM     579 4-ACETYL-3-ETHYL-N-[4-FLUORO-3-(MORPHOLIN-4-                     
HETNAM   2 579  YLSULFONYL)PHENYL]-5-METHYL-1H-PYRROLE-2-CARBOXAMIDE            
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     BU3 (R,R)-2,3-BUTANEDIOL                                             
FORMUL   2  579    C20 H24 F N3 O5 S                                            
FORMUL   3  DMS    C2 H6 O S                                                    
FORMUL   4  BU3    C4 H10 O2                                                    
FORMUL   5  HOH   *119(H2 O)                                                    
HELIX    1 AA1 THR A   60  VAL A   69  1                                  10    
HELIX    2 AA2 VAL A   69  LYS A   76  1                                   8    
HELIX    3 AA3 ALA A   80  GLN A   84  5                                   5    
HELIX    4 AA4 ASP A   96  ILE A  101  1                                   6    
HELIX    5 AA5 ASP A  106  ASN A  116  1                                  11    
HELIX    6 AA6 ASN A  121  ASN A  140  1                                  20    
HELIX    7 AA7 ASP A  144  ASN A  162  1                                  19    
SITE     1 AC1 13 LYS A  57  TRP A  81  PRO A  82  GLN A  85                    
SITE     2 AC1 13 VAL A  87  LEU A  92  ASN A 117  TYR A 139                    
SITE     3 AC1 13 ASN A 140  ILE A 146  BU3 A 203  HOH A 326                    
SITE     4 AC1 13 HOH A 361                                                     
SITE     1 AC2  4 LEU A  92  LEU A 148  GLU A 151  HOH A 313                    
SITE     1 AC3  4 ILE A 146  579 A 201  HOH A 345  HOH A 373                    
CRYST1   39.480   49.510   57.790  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      0.025329  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020198  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017304        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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