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Database: PDB
Entry: 5A5S
LinkDB: 5A5S
Original site: 5A5S 
HEADER    HYDROLASE                               20-JUN-15   5A5S              
TITLE     NN-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH 5-5-                       
TITLE    2 METHOXYPYRIDIN-3-YL-3-METHYL-8-PIPERIDIN-4-YLAMINO-1,2-              
TITLE    3 DIHYDRO-1,7-NAPHTHYRIDIN-2-ONE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL BROMODOMAIN, UNP RESIDUES 44-168;               
COMPND   5 SYNONYM: PROTEIN HUNK1, HUMAN BRD4;                                  
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    HYDROLASE, INHIBITOR, HISTONE, EPIGENETIC READER, BROMODOMAIN, BRD4,  
KEYWDS   2 BROMODOMAIN CONTAINING PROTEIN 4, ANTAGONIST                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHUNG,P.BAMBOROUGH,E.DEMONT                                         
REVDAT   2   05-AUG-15 5A5S    1       JRNL                                     
REVDAT   1   22-JUL-15 5A5S    0                                                
JRNL        AUTH   E.H.DEMONT,C.CHUNG,R.C.FURZE,P.GRANDI,A.MICHON,C.WELLAWAY,   
JRNL        AUTH 2 N.BARRETT,A.M.BRIDGES,P.D.CRAGGS,H.DIALLO,D.P.DIXON,         
JRNL        AUTH 3 C.DOUAULT,A.J.EMMONS,E.J.JONES,B.V.KARAMSHI,K.LOCKE,         
JRNL        AUTH 4 D.J.MITCHELL,B.H.MOUZON,R.K.PRINJHA,A.D.ROBERTS,             
JRNL        AUTH 5 R.J.SHEPPARD,R.J.WATSON,P.BAMBOROUGH                         
JRNL        TITL   FRAGMENT-BASED DISCOVERY OF LOW-MICROMOLAR ATAD2             
JRNL        TITL 2 BROMODOMAIN INHIBITORS.                                      
JRNL        REF    J.MED.CHEM.                   V.  58  5649 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26155854                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B00772                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.56                          
REMARK   3   NUMBER OF REFLECTIONS             : 23440                          
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) : 0.20921                         
REMARK   3   R VALUE            (WORKING SET) : 0.20874                         
REMARK   3   FREE R VALUE                     : 0.21779                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1261                            
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) : 1.363                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.398                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1606                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.210                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.233                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1083                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 136                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.079                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.10                                                 
REMARK   3    B22 (A**2) : 0.22                                                 
REMARK   3    B33 (A**2) : -0.32                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.076         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.041         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.844         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1150 ; 0.005 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):   799 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1568 ; 0.970 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1970 ; 0.785 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   134 ; 4.740 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    55 ;35.293 ;26.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   206 ;11.815 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;16.835 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   163 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1240 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   211 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    44        A   168                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8607  -8.3685  17.9035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0017 T22:   0.0063                                     
REMARK   3      T33:   0.0102 T12:  -0.0006                                     
REMARK   3      T13:  -0.0016 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4337 L22:   0.2214                                     
REMARK   3      L33:   0.5644 L12:   0.2348                                     
REMARK   3      L13:   0.2387 L23:   0.2177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:   0.0441 S13:  -0.0042                       
REMARK   3      S21:   0.0010 S22:   0.0351 S23:  -0.0036                       
REMARK   3      S31:   0.0022 S32:   0.0227 S33:  -0.0219                       
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   : 1.20                                          
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 5A5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-64118.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-13                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24744                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.36                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.39                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.0                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.10                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.60                               
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: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2NAF, 20% PEG3350                      
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       19.69500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.61500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       29.61500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.69500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.69500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 168    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN A    64     NH2  ARG A    68              1.81            
REMARK 500   O    HOH A  2025     O    HOH A  2026              1.56            
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    MET A  43      152.65     73.37                                   
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 EDO A1169                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NP8 A1170                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5A5N   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ATAD2 BROMODOMAIN IN COMPLEX             
REMARK 900   WITH (2S)-2,6-DIACETAMIDO-N-METHYLHEXANAMIDE                       
REMARK 900 RELATED ID: 5A5O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ATAD2 BROMODOMAIN IN COMPLEX             
REMARK 900   WITH 3-METHYL-1,2-DIHYDROQUINOLIN-2-ONE                            
REMARK 900 RELATED ID: 5A5P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ATAD2 BROMODOMAIN IN COMPLEX             
REMARK 900   WITH 8-2-(DIMETHYLAMINO)ETHYLAMINO-3-METHYL-1,2-                   
REMARK 900  DIHYDROQUINOLIN-2-ONE                                               
REMARK 900 RELATED ID: 5A5Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ATAD2 BROMODOMAIN IN COMPLEX             
REMARK 900   WITH 3-METHYL-8-PIPERIDIN-4-YLAMINO-1,2-DIHYDRO-                   
REMARK 900  1,7-NAPHTHYRIDIN-2-ONE HYDROCHLORIDE                                
REMARK 900 RELATED ID: 5A5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ATAD2 BROMODOMAIN IN COMPLEX             
REMARK 900   WITH 5-5-METHOXYPYRIDIN-3-YL-3-METHYL-8-PIPERIDIN                  
REMARK 900  -4-YLAMINO-1,2-DIHYDRO-1,7-NAPHTHYRIDIN-2-ONE                       
DBREF  5A5S A   44   168  UNP    O60885   BRD4_HUMAN      44    168             
SEQADV 5A5S SER A   42  UNP  O60885              EXPRESSION TAG                 
SEQADV 5A5S MET A   43  UNP  O60885              EXPRESSION TAG                 
SEQADV 5A5S LYS A   78  UNP  O60885    GLN    78 CONFLICT                       
SEQRES   1 A  127  SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN          
SEQRES   2 A  127  LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU          
SEQRES   3 A  127  ARG VAL VAL LEU LYS THR LEU TRP LYS HIS LYS PHE ALA          
SEQRES   4 A  127  TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN          
SEQRES   5 A  127  LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP          
SEQRES   6 A  127  MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR          
SEQRES   7 A  127  TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET          
SEQRES   8 A  127  PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP          
SEQRES   9 A  127  ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU          
SEQRES  10 A  127  GLN LYS ILE ASN GLU LEU PRO THR GLU GLU                      
HET    EDO  A1169       4                                                       
HET    NP8  A1170      27                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     NP8 5-(5-METHOXYPYRIDIN-3-YL)-3-METHYL-8-[(PIPERIDIN-4-YL)AMINO]-    
HETNAM   2 NP8  1,2-DIHYDRO-1,7-NAPHTHYRIDIN-2-ONE                              
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    C2 H6 O2                                                     
FORMUL   3  NP8    C20 H23 N5 O2                                                
FORMUL   4  HOH   *136(H2 O)                                                    
HELIX    1   1 THR A   60  VAL A   69  1                                  10    
HELIX    2   2 VAL A   69  LYS A   76  1                                   8    
HELIX    3   3 ALA A   80  GLN A   84  5                                   5    
HELIX    4   4 ASP A   96  ILE A  101  1                                   6    
HELIX    5   5 ASP A  106  ASN A  116  1                                  11    
HELIX    6   6 ASN A  121  ASN A  140  1                                  20    
HELIX    7   7 ASP A  144  ASN A  162  1                                  19    
SITE     1 AC1  5 ILE A 100  ILE A 101  LYS A 102  THR A 103                    
SITE     2 AC1  5 ASN A 135                                                     
SITE     1 AC2 11 TRP A  81  PRO A  82  GLN A  85  VAL A  87                    
SITE     2 AC2 11 LEU A  92  ASN A 140  ASP A 144  LYS A 155                    
SITE     3 AC2 11 HOH A2085  HOH A2135  HOH A2136                               
CRYST1   39.390   49.390   59.230  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      0.025387  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020247  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016883        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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