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Database: PDB
Entry: 5G4R
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HEADER    TRANSCRIPTION                           16-MAY-16   5G4R              
TITLE     BROMODOMAIN OF HUMAN BRPF1 WITH  N-1,3-DIMETHYL-6-2R-2-               
TITLE    2 METHYLPIPERAZIN-1-YL-2-OXO-2,3-DIHYDRO-1H-1,3-BENZODIAZOL-           
TITLE    3 5-YL-2-METHOXYBENZAMIDE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEREGRIN;                                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: BROMODOMAIN OF BRPF1, UNP RESIDUES 622-738;                
COMPND   5 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1, PROTEIN    
COMPND   6  BR140,;                                                             
COMPND   7 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    TRANSCRIPTION                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHUNG                                                               
REVDAT   1   06-JUL-16 5G4R    0                                                
JRNL        AUTH   P.BAMBOROUGH,H.A.BARNETT,I.BECHER,M.J.BIRD,C.CHUNG,          
JRNL        AUTH 2 P.D.CRAGGS,E.H.DEMONT,H.DIALLO,D.J.FALLON,L.J.GORDON,        
JRNL        AUTH 3 P.GRANDI,C.I.HOBBS,E.HOOPER-GREENHILL,E.J.JONES,R.P.LAW,     
JRNL        AUTH 4 A.LE GALL,D.LUGO,A.MICHON,D.J.MITCHELL,R.K.PRINJHA,          
JRNL        AUTH 5 R.J.SHEPPARD,A.J.B.WATSON,R.J.WATSON                         
JRNL        TITL   GSK6853, A CHEMICAL PROBE FOR INHIBITION OF THE BRPF1        
JRNL        TITL 2 BROMODOMAIN.                                                 
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   552 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   27326325                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.6B00092                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.96 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) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.93                          
REMARK   3   NUMBER OF REFLECTIONS             : 31410                          
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) : 0.20237                         
REMARK   3   R VALUE            (WORKING SET) : 0.20028                         
REMARK   3   FREE R VALUE                     : 0.24031                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1667                            
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) : 1.963                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.014                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2334                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.322                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.378                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3677                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 120                                     
REMARK   3   SOLVENT ATOMS            : 400                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.842                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.15                                                
REMARK   3    B22 (A**2) : 0.61                                                 
REMARK   3    B33 (A**2) : -2.87                                                
REMARK   3    B12 (A**2) : 2.50                                                 
REMARK   3    B13 (A**2) : -0.15                                                
REMARK   3    B23 (A**2) : 0.85                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.179         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.139         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.756         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3882 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2702 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5249 ; 1.353 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6538 ; 0.889 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   440 ; 5.037 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   207 ;36.291 ;24.203       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   688 ;15.899 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;18.412 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   551 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4252 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   824 ; 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  : 4                                          
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   630        A   738                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9044   8.5308 -46.0648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0446 T22:   0.1188                                     
REMARK   3      T33:   0.0951 T12:  -0.0354                                     
REMARK   3      T13:   0.0148 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1108 L22:   1.5381                                     
REMARK   3      L33:   3.5443 L12:  -0.0235                                     
REMARK   3      L13:   0.1819 L23:   1.0998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0314 S12:  -0.0531 S13:   0.0612                       
REMARK   3      S21:  -0.0419 S22:  -0.1171 S23:   0.0742                       
REMARK   3      S31:   0.2369 S32:  -0.1409 S33:   0.0857                       
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   627        B   738                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7447   4.9577 -23.2791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0857 T22:   0.0569                                     
REMARK   3      T33:   0.1380 T12:  -0.0569                                     
REMARK   3      T13:   0.0052 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8263 L22:   0.6145                                     
REMARK   3      L33:   1.3516 L12:  -0.4485                                     
REMARK   3      L13:   0.8899 L23:  -0.1207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1554 S12:  -0.0272 S13:  -0.0691                       
REMARK   3      S21:  -0.1158 S22:  -0.0059 S23:  -0.0175                       
REMARK   3      S31:   0.0817 S32:  -0.0118 S33:  -0.1495                       
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 :   C   627        C   738                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3066 -13.4801 -24.7137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0421 T22:   0.0569                                     
REMARK   3      T33:   0.1598 T12:  -0.0252                                     
REMARK   3      T13:   0.0017 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2942 L22:   1.0063                                     
REMARK   3      L33:   2.0041 L12:  -0.3782                                     
REMARK   3      L13:  -0.4591 L23:   1.0751                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0448 S12:  -0.0152 S13:  -0.0093                       
REMARK   3      S21:  -0.1118 S22:  -0.0445 S23:  -0.0730                       
REMARK   3      S31:  -0.1543 S32:  -0.1263 S33:  -0.0003                       
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 :   D   630        D   738                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2482  18.6139 -55.5374              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0383 T22:   0.1298                                     
REMARK   3      T33:   0.1357 T12:  -0.0604                                     
REMARK   3      T13:  -0.0010 T23:   0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6153 L22:   1.3940                                     
REMARK   3      L33:   1.8531 L12:  -0.3243                                     
REMARK   3      L13:   0.5105 L23:  -0.1906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0167 S12:   0.0548 S13:   0.0752                       
REMARK   3      S21:  -0.0190 S22:   0.1725 S23:   0.0439                       
REMARK   3      S31:   0.0290 S32:   0.0582 S33:  -0.1558                       
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 5G4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAY-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-66865.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979163                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS (PILATUS 6M)               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33077                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.96                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.57                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 1.8                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.20                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.18                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% P550MME_P20K, 0.1M BUFFER 3,         
REMARK 280   PH8.5,  10% ETHYLENE GLYCOLS                                       
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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   621                                                      
REMARK 465     GLN A   622                                                      
REMARK 465     GLN A   623                                                      
REMARK 465     ILE A   624                                                      
REMARK 465     ALA A   625                                                      
REMARK 465     MET A   626                                                      
REMARK 465     GLU A   627                                                      
REMARK 465     MET A   628                                                      
REMARK 465     GLN A   629                                                      
REMARK 465     GLY B   621                                                      
REMARK 465     GLN B   622                                                      
REMARK 465     GLN B   623                                                      
REMARK 465     ILE B   624                                                      
REMARK 465     ALA B   625                                                      
REMARK 465     MET B   626                                                      
REMARK 465     GLY C   621                                                      
REMARK 465     GLN C   622                                                      
REMARK 465     GLN C   623                                                      
REMARK 465     ILE C   624                                                      
REMARK 465     ALA C   625                                                      
REMARK 465     MET C   626                                                      
REMARK 465     GLY D   621                                                      
REMARK 465     GLN D   622                                                      
REMARK 465     GLN D   623                                                      
REMARK 465     ILE D   624                                                      
REMARK 465     ALA D   625                                                      
REMARK 465     MET D   626                                                      
REMARK 465     GLU D   627                                                      
REMARK 465     MET D   628                                                      
REMARK 465     GLN D   629                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 738    CG   CD   CE   NZ                                   
REMARK 470     LYS B 738    CG   CD   CE   NZ                                   
REMARK 470     LYS C 738    CG   CD   CE   NZ                                   
REMARK 470     GLU D 737    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 738    CG   CD   CE   NZ                                   
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   OD1  ASN A   651     O    HOH A  2021              2.05            
REMARK 500   NE2  GLN B   680     O    HOH B  2058              2.09            
REMARK 500   O    HOH C  2052     O    HOH C  2096              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2059     O    HOH C  2062     2565     2.07            
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    ASP A 711       30.67    -86.50                                   
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 LF1 A1739                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LF1 B1739                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LF1 C1739                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LF1 D1739                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5G4S   RELATED DB: PDB                                   
REMARK 900  BROMODOMAIN OF HUMAN BRPF1 WITH N-1,3-DIMETHYL-6-                   
REMARK 900  2R-2-METHYLPIPERAZIN-1-YL-2-OXO-2,3-DIHYDRO-1H-1                    
REMARK 900  ,3-BENZODIAZOL-5-YL-N-ETHYL-2-METHOXYBENZAMIDE                      
DBREF  5G4R A  622   738  UNP    P55201   BRPF1_HUMAN    622    738             
DBREF  5G4R B  622   738  UNP    P55201   BRPF1_HUMAN    622    738             
DBREF  5G4R C  622   738  UNP    P55201   BRPF1_HUMAN    622    738             
DBREF  5G4R D  622   738  UNP    P55201   BRPF1_HUMAN    622    738             
SEQADV 5G4R GLY A  621  UNP  P55201              EXPRESSION TAG                 
SEQADV 5G4R GLY B  621  UNP  P55201              EXPRESSION TAG                 
SEQADV 5G4R GLY C  621  UNP  P55201              EXPRESSION TAG                 
SEQADV 5G4R GLY D  621  UNP  P55201              EXPRESSION TAG                 
SEQRES   1 A  118  GLY GLN GLN ILE ALA MET GLU MET GLN LEU THR PRO PHE          
SEQRES   2 A  118  LEU ILE LEU LEU ARG LYS THR LEU GLU GLN LEU GLN GLU          
SEQRES   3 A  118  LYS ASP THR GLY ASN ILE PHE SER GLU PRO VAL PRO LEU          
SEQRES   4 A  118  SER GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS LYS PRO          
SEQRES   5 A  118  MET ASP PHE PHE THR MET LYS GLN ASN LEU GLU ALA TYR          
SEQRES   6 A  118  ARG TYR LEU ASN PHE ASP ASP PHE GLU GLU ASP PHE ASN          
SEQRES   7 A  118  LEU ILE VAL SER ASN CYS LEU LYS TYR ASN ALA LYS ASP          
SEQRES   8 A  118  THR ILE PHE TYR ARG ALA ALA VAL ARG LEU ARG GLU GLN          
SEQRES   9 A  118  GLY GLY ALA VAL LEU ARG GLN ALA ARG ARG GLN ALA GLU          
SEQRES  10 A  118  LYS                                                          
SEQRES   1 B  118  GLY GLN GLN ILE ALA MET GLU MET GLN LEU THR PRO PHE          
SEQRES   2 B  118  LEU ILE LEU LEU ARG LYS THR LEU GLU GLN LEU GLN GLU          
SEQRES   3 B  118  LYS ASP THR GLY ASN ILE PHE SER GLU PRO VAL PRO LEU          
SEQRES   4 B  118  SER GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS LYS PRO          
SEQRES   5 B  118  MET ASP PHE PHE THR MET LYS GLN ASN LEU GLU ALA TYR          
SEQRES   6 B  118  ARG TYR LEU ASN PHE ASP ASP PHE GLU GLU ASP PHE ASN          
SEQRES   7 B  118  LEU ILE VAL SER ASN CYS LEU LYS TYR ASN ALA LYS ASP          
SEQRES   8 B  118  THR ILE PHE TYR ARG ALA ALA VAL ARG LEU ARG GLU GLN          
SEQRES   9 B  118  GLY GLY ALA VAL LEU ARG GLN ALA ARG ARG GLN ALA GLU          
SEQRES  10 B  118  LYS                                                          
SEQRES   1 C  118  GLY GLN GLN ILE ALA MET GLU MET GLN LEU THR PRO PHE          
SEQRES   2 C  118  LEU ILE LEU LEU ARG LYS THR LEU GLU GLN LEU GLN GLU          
SEQRES   3 C  118  LYS ASP THR GLY ASN ILE PHE SER GLU PRO VAL PRO LEU          
SEQRES   4 C  118  SER GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS LYS PRO          
SEQRES   5 C  118  MET ASP PHE PHE THR MET LYS GLN ASN LEU GLU ALA TYR          
SEQRES   6 C  118  ARG TYR LEU ASN PHE ASP ASP PHE GLU GLU ASP PHE ASN          
SEQRES   7 C  118  LEU ILE VAL SER ASN CYS LEU LYS TYR ASN ALA LYS ASP          
SEQRES   8 C  118  THR ILE PHE TYR ARG ALA ALA VAL ARG LEU ARG GLU GLN          
SEQRES   9 C  118  GLY GLY ALA VAL LEU ARG GLN ALA ARG ARG GLN ALA GLU          
SEQRES  10 C  118  LYS                                                          
SEQRES   1 D  118  GLY GLN GLN ILE ALA MET GLU MET GLN LEU THR PRO PHE          
SEQRES   2 D  118  LEU ILE LEU LEU ARG LYS THR LEU GLU GLN LEU GLN GLU          
SEQRES   3 D  118  LYS ASP THR GLY ASN ILE PHE SER GLU PRO VAL PRO LEU          
SEQRES   4 D  118  SER GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS LYS PRO          
SEQRES   5 D  118  MET ASP PHE PHE THR MET LYS GLN ASN LEU GLU ALA TYR          
SEQRES   6 D  118  ARG TYR LEU ASN PHE ASP ASP PHE GLU GLU ASP PHE ASN          
SEQRES   7 D  118  LEU ILE VAL SER ASN CYS LEU LYS TYR ASN ALA LYS ASP          
SEQRES   8 D  118  THR ILE PHE TYR ARG ALA ALA VAL ARG LEU ARG GLU GLN          
SEQRES   9 D  118  GLY GLY ALA VAL LEU ARG GLN ALA ARG ARG GLN ALA GLU          
SEQRES  10 D  118  LYS                                                          
HET    LF1  A1739      30                                                       
HET    LF1  B1739      30                                                       
HET    LF1  C1739      30                                                       
HET    LF1  D1739      30                                                       
HETNAM     LF1 N-[1,3-DIMETHYL-6-[(2R)-2-METHYLPIPERAZIN-1-                     
HETNAM   2 LF1  YL]-2-OXIDANYLIDENE-BENZIMIDAZOL-5-YL]-2-                       
HETNAM   3 LF1  METHOXY-BENZAMIDE                                               
FORMUL   2  LF1    4(C22 H27 N5 O3)                                             
FORMUL   3  HOH   *400(H2 O)                                                    
HELIX    1   1 LEU A  630  ASP A  648  1                                  19    
HELIX    2   2 ASP A  664  ILE A  669  1                                   6    
HELIX    3   3 ASP A  674  ALA A  684  1                                  11    
HELIX    4   4 ASN A  689  ASN A  708  1                                  20    
HELIX    5   5 THR A  712  LYS A  738  1                                  27    
HELIX    6   6 GLN B  629  ASP B  648  1                                  20    
HELIX    7   7 ASP B  664  ILE B  669  1                                   6    
HELIX    8   8 ASP B  674  ALA B  684  1                                  11    
HELIX    9   9 ASN B  689  ASN B  708  1                                  20    
HELIX   10  10 THR B  712  ALA B  736  1                                  25    
HELIX   11  11 GLN C  629  ASP C  648  1                                  20    
HELIX   12  12 ASP C  664  ILE C  669  1                                   6    
HELIX   13  13 ASP C  674  ALA C  684  1                                  11    
HELIX   14  14 ASN C  689  ASN C  708  1                                  20    
HELIX   15  15 THR C  712  LYS C  738  1                                  27    
HELIX   16  16 LEU D  630  ASP D  648  1                                  19    
HELIX   17  17 ASP D  664  ILE D  669  1                                   6    
HELIX   18  18 ASP D  674  ALA D  684  1                                  11    
HELIX   19  19 ASN D  689  ASN D  708  1                                  20    
HELIX   20  20 THR D  712  GLU D  737  1                                  26    
SITE     1 AC1 18 ASN A 651  ILE A 652  GLU A 655  PRO A 656                    
SITE     2 AC1 18 VAL A 657  PRO A 658  GLU A 661  VAL A 662                    
SITE     3 AC1 18 TYR A 707  ASN A 708  PHE A 714  HOH A2031                    
SITE     4 AC1 18 HOH A2085  HOH A2086  GLU B 683  ALA C 684                    
SITE     5 AC1 18 TYR C 685  HOH C2052                                          
SITE     1 AC2 13 LYS A 639  ASN B 651  ILE B 652  GLU B 655                    
SITE     2 AC2 13 PRO B 656  VAL B 657  PRO B 658  GLU B 661                    
SITE     3 AC2 13 TYR B 707  ASN B 708  PHE B 714  HOH B2032                    
SITE     4 AC2 13 HOH B2046                                                     
SITE     1 AC3 10 ASN C 651  ILE C 652  GLU C 655  PRO C 656                    
SITE     2 AC3 10 VAL C 657  PRO C 658  ASN C 708  PHE C 714                    
SITE     3 AC3 10 HOH C2029  HOH C2036                                          
SITE     1 AC4 18 ALA B 684  TYR B 685  HOH B2063  HOH B2065                    
SITE     2 AC4 18 ARG C 638  ASN D 651  ILE D 652  GLU D 655                    
SITE     3 AC4 18 PRO D 656  VAL D 657  PRO D 658  GLU D 661                    
SITE     4 AC4 18 VAL D 662  TYR D 707  ASN D 708  PHE D 714                    
SITE     5 AC4 18 HOH D2035  HOH D2086                                          
CRYST1   47.444   50.703   61.981  72.61  71.36  66.64 P 1           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      0.021077 -0.009104 -0.005415        0.00000                         
SCALE2      0.000000  0.021484 -0.004337        0.00000                         
SCALE3      0.000000  0.000000  0.017371        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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