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Database: PDB
Entry: 4Z1Q
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Original site: 4Z1Q 
HEADER    TRANSCRIPTION                           27-MAR-15   4Z1Q              
TITLE     CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 BOUND TO     
TITLE    2 BENZOTRIAZOLO-DIAZEPINE SCAFFOLD                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN HUNK1;                                              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRD4, HUNK1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BROMODOMAIN, TRANSCRIPTION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.W.SETSER,F.POY,Y.TANG,S.F.BELLON                                    
REVDAT   3   06-MAR-24 4Z1Q    1       REMARK                                   
REVDAT   2   30-MAR-16 4Z1Q    1       JRNL                                     
REVDAT   1   08-APR-15 4Z1Q    0                                                
JRNL        AUTH   A.M.TAYLOR,R.G.VASWANI,V.S.GEHLING,M.C.HEWITT,Y.LEBLANC,     
JRNL        AUTH 2 J.E.AUDIA,S.BELLON,R.T.CUMMINGS,A.COTE,J.C.HARMANGE,         
JRNL        AUTH 3 H.JAYARAM,S.JOSHI,J.M.LORA,J.A.MERTZ,A.NEISS,E.PARDO,        
JRNL        AUTH 4 C.G.NASVESCHUK,F.POY,P.SANDY,J.W.SETSER,R.J.SIMS,Y.TANG,     
JRNL        AUTH 5 B.K.ALBRECHT                                                 
JRNL        TITL   DISCOVERY OF BENZOTRIAZOLO[4,3-D][1,4]DIAZEPINES AS ORALLY   
JRNL        TITL 2 ACTIVE INHIBITORS OF BET BROMODOMAINS.                       
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   145 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26985289                                                     
JRNL        DOI    10.1021/ML500411H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0069                                      
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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 40551                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2084                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1880                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2091                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.67000                                             
REMARK   3    B33 (A**2) : 0.54000                                              
REMARK   3    B12 (A**2) : -0.18000                                             
REMARK   3    B13 (A**2) : 0.05000                                              
REMARK   3    B23 (A**2) : -0.22000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.065         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.152         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2318 ; 0.022 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2194 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3182 ; 2.064 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5074 ; 0.987 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   271 ; 5.325 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;37.981 ;25.926       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   404 ;15.914 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;20.550 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   333 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2652 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   532 ; 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):  1057 ; 1.054 ; 0.944       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1056 ; 1.054 ; 0.941       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1337 ; 1.653 ; 1.404       
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  : 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    43        A   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.5735 -52.3493 148.0565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0052 T22:   0.0689                                     
REMARK   3      T33:   0.0098 T12:   0.0104                                     
REMARK   3      T13:   0.0046 T23:   0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0528 L22:   0.1982                                     
REMARK   3      L33:   0.6187 L12:  -0.1776                                     
REMARK   3      L13:  -0.2715 L23:  -0.0662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:  -0.0318 S13:  -0.0326                       
REMARK   3      S21:   0.0051 S22:  -0.0216 S23:   0.0175                       
REMARK   3      S31:  -0.0264 S32:   0.0348 S33:  -0.0157                       
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    41        B   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5975 -32.7761 173.2828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0078 T22:   0.0745                                     
REMARK   3      T33:   0.0142 T12:   0.0169                                     
REMARK   3      T13:   0.0091 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2011 L22:   0.3223                                     
REMARK   3      L33:   0.8043 L12:   0.1697                                     
REMARK   3      L13:  -0.4331 L23:  -0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0659 S12:   0.0290 S13:   0.0714                       
REMARK   3      S21:   0.0183 S22:  -0.0207 S23:  -0.0078                       
REMARK   3      S31:  -0.0480 S32:  -0.0513 S33:  -0.0452                       
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 4Z1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208451.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HS                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42635                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.399                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 54.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: INTERNAL MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M BIS-TRIS    
REMARK 280  PH 6.5, AND 25% POLYETHYLENE GLYCOL (PEG) 3350, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     GLU A   167                                                      
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    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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  52      112.29   -163.26                                   
REMARK 500    LEU A  94       75.62   -110.42                                   
REMARK 500    ASN B  52      100.65   -175.65                                   
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 558 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 558 B 201                 
DBREF  4Z1Q A   42   167  UNP    O60885   BRD4_HUMAN      42    167             
DBREF  4Z1Q B   42   167  UNP    O60885   BRD4_HUMAN      42    167             
SEQADV 4Z1Q GLY A   41  UNP  O60885              EXPRESSION TAG                 
SEQADV 4Z1Q GLY B   41  UNP  O60885              EXPRESSION TAG                 
SEQRES   1 A  127  GLY SER THR ASN PRO PRO PRO PRO GLU THR SER ASN PRO          
SEQRES   2 A  127  ASN LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU          
SEQRES   3 A  127  LEU ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE          
SEQRES   4 A  127  ALA TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU          
SEQRES   5 A  127  ASN LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET          
SEQRES   6 A  127  ASP MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR          
SEQRES   7 A  127  TYR TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR          
SEQRES   8 A  127  MET PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP          
SEQRES   9 A  127  ASP ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE          
SEQRES  10 A  127  LEU GLN LYS ILE ASN GLU LEU PRO THR GLU                      
SEQRES   1 B  127  GLY SER THR ASN PRO PRO PRO PRO GLU THR SER ASN PRO          
SEQRES   2 B  127  ASN LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU          
SEQRES   3 B  127  LEU ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE          
SEQRES   4 B  127  ALA TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU          
SEQRES   5 B  127  ASN LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET          
SEQRES   6 B  127  ASP MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR          
SEQRES   7 B  127  TYR TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR          
SEQRES   8 B  127  MET PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP          
SEQRES   9 B  127  ASP ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE          
SEQRES  10 B  127  LEU GLN LYS ILE ASN GLU LEU PRO THR GLU                      
HET    558  A 201      30                                                       
HET    558  B 201      30                                                       
HETNAM     558 5-[(4R)-6-(4-CHLOROPHENYL)-1,4-DIMETHYL-5,6-DIHYDRO-4H-          
HETNAM   2 558  [1,2,4]TRIAZOLO[4,3-A][1,5]BENZODIAZEPIN-8-YL]PYRIDIN-          
HETNAM   3 558  2-AMINE                                                         
FORMUL   3  558    2(C23 H21 CL N6)                                             
FORMUL   5  HOH   *209(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    
HELIX    8 AA8 THR B   60  VAL B   69  1                                  10    
HELIX    9 AA9 VAL B   69  LYS B   76  1                                   8    
HELIX   10 AB1 ALA B   80  GLN B   84  5                                   5    
HELIX   11 AB2 ASP B   96  ILE B  101  1                                   6    
HELIX   12 AB3 ASP B  106  ASN B  116  1                                  11    
HELIX   13 AB4 ASN B  121  ASN B  140  1                                  20    
HELIX   14 AB5 ASP B  144  ASN B  162  1                                  19    
SITE     1 AC1  7 TRP A  81  PRO A  82  LEU A  92  TYR A 139                    
SITE     2 AC1  7 ASN A 140  ILE A 146  HOH A 318                               
SITE     1 AC2 10 HIS A  77  PHE A  79  ASP A 145  PRO B  82                    
SITE     2 AC2 10 PHE B  83  LEU B  92  TYR B 139  ASN B 140                    
SITE     3 AC2 10 ILE B 146  HOH B 318                                          
CRYST1   30.293   39.501   57.230  83.07  75.35  89.85 P 1           2          
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      0.033011 -0.000088 -0.008687        0.00000                         
SCALE2      0.000000  0.025316 -0.003163        0.00000                         
SCALE3      0.000000  0.000000  0.018201        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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