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Database: PDB
Entry: 4QYL
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Original site: 4QYL 
HEADER    PROTEIN BINDING                         24-JUL-14   4QYL              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN BRPF1 BROMODOMAIN IN COMPLEX WITH A    
TITLE    2 HISTONE H2AK5AC PEPTIDE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEREGRIN;                                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: BROMODOMAIN (UNP RESIDUES 629-742);                        
COMPND   5 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1, PROTEIN    
COMPND   6 BR140;                                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HISTONE H2A TYPE 1;                                        
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 FRAGMENT: HISTONE H2AK5AC PEPTIDE (UNP RESIDUES 2-13);               
COMPND  12 SYNONYM: H2A.1, HISTONE H2A/P;                                       
COMPND  13 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: BR140, BRPF1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2DE3PLYSS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST15;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    BROMODOMAIN-PHD FINGER PROTEIN 1 (BRPF1), HISTONE ACETYLTRANSFERASE   
KEYWDS   2 (HAT), MONOCYTIC LEUKEMIA ZINC-FINGER (MOZ), EPIGENETICS, CHROMATIN  
KEYWDS   3 READER, BROMODOMAIN, HISTONE POST-TRANSCRIPTIONAL MODIFICATION (PTM) 
KEYWDS   4 READER DOMAIN, ACETYLLYSINE, NUCLEUS, PROTEIN BINDING                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.Y.LUBULA,K.C.GLASS                                                  
REVDAT   3   17-DEC-14 4QYL    1       JRNL                                     
REVDAT   2   22-OCT-14 4QYL    1       JRNL                                     
REVDAT   1   24-SEP-14 4QYL    0                                                
JRNL        AUTH   M.Y.LUBULA,B.E.ECKENROTH,S.CARLSON,A.POPLAWSKI,M.CHRUSZCZ,   
JRNL        AUTH 2 K.C.GLASS                                                    
JRNL        TITL   STRUCTURAL INSIGHTS INTO RECOGNITION OF ACETYLATED HISTONE   
JRNL        TITL 2 LIGANDS BY THE BRPF1 BROMODOMAIN.                            
JRNL        REF    FEBS LETT.                    V. 588  3844 2014              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   25281266                                                     
JRNL        DOI    10.1016/J.FEBSLET.2014.09.028                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 48421                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2587                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3536                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 197                          
REMARK   3   BIN FREE R VALUE                    : 0.3260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4087                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 722                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : 0.66000                                              
REMARK   3    B33 (A**2) : -1.00000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.09000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.156         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.149         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.095         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
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):  4354 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4147 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5881 ; 1.775 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9554 ; 1.351 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   539 ; 5.890 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   233 ;33.971 ;24.764       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   778 ;12.263 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ; 8.287 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   617 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5060 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1033 ; 0.007 ; 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   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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A     1   117       B     1    117     7510  0.07  0.05    
REMARK   3    2      A     1   117       C     1    117     7370  0.08  0.05    
REMARK   3    3      A     1   117       D     1    117     7384  0.07  0.05    
REMARK   3    4      B     1   117       C     1    117     7214  0.07  0.05    
REMARK   3    5      B     1   117       D     1    117     7228  0.07  0.05    
REMARK   3    6      C     1   117       D     1    117     7159  0.09  0.05    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4QYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086676.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48421                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3RCW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4SO4, 0.1 M MES MONOHYDRATE,     
REMARK 280  PH 6.5, 30% W/V POLYETHYLENE GLYCOL MONOMETHYL ETHER (PEG) 5000,    
REMARK 280  1% PROPYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       27.79050            
REMARK 290   SMTRY3   2  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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7630 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7730 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7550 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7630 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
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     ARG E    11                                                      
REMARK 465     ALA E    12                                                      
REMARK 465     ARG F    11                                                      
REMARK 465     ALA F    12                                                      
REMARK 465     ARG G    11                                                      
REMARK 465     ALA G    12                                                      
REMARK 465     ARG H    11                                                      
REMARK 465     ALA H    12                                                      
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  45    CG   CD   CE   NZ                                   
REMARK 470     LYS C  45    CG   CD   CE   NZ                                   
REMARK 470     ARG C 105    NE   CZ   NH1  NH2                                  
REMARK 470     ILE C 116    CB   CG1  CG2  CD1                                  
REMARK 470     LYS D  45    CG   CD   CE   NZ                                   
REMARK 470     LYS D  85    CG   CD   CE   NZ                                   
REMARK 470     ILE D 116    CG1  CG2  CD1                                       
REMARK 470     ARG E   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G   3    CG   CD   NE   CZ   NH1  NH2                        
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 C    99     O    HOH C   501              2.05            
REMARK 500   OE1  GLN D    99     O    HOH D   398              2.11            
REMARK 500   O    HOH C   379     O    HOH C   409              2.12            
REMARK 500   OD1  ASN B    26     O    HOH B   436              2.14            
REMARK 500   O    HOH B   441     O    HOH B   488              2.17            
REMARK 500   NE2  GLN D    99     O    HOH D   424              2.19            
REMARK 500   O    HOH B   486     O    HOH C   415              2.19            
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 B   401     O    HOH C   444     2748     2.08            
REMARK 500   OE1  GLN D    99     O    HOH A   420     1565     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  66   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP C 117   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 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    ILE C 116       65.60     67.43                                   
REMARK 500    ILE D 116       50.27   -141.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE C  116     ASP C  117                   42.53                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 449        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B 435        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH B 456        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B 462        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B 464        DISTANCE =  7.66 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QYD   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH THE HISTONE H4K12AC PEPTIDE              
DBREF  4QYL A    4   117  UNP    P55201   BRPF1_HUMAN    629    742             
DBREF  4QYL B    4   117  UNP    P55201   BRPF1_HUMAN    629    742             
DBREF  4QYL C    4   117  UNP    P55201   BRPF1_HUMAN    629    742             
DBREF  4QYL D    4   117  UNP    P55201   BRPF1_HUMAN    629    742             
DBREF  4QYL E    1    12  UNP    P0C0S8   H2A1_HUMAN       2     13             
DBREF  4QYL F    1    12  UNP    P0C0S8   H2A1_HUMAN       2     13             
DBREF  4QYL G    1    12  UNP    P0C0S8   H2A1_HUMAN       2     13             
DBREF  4QYL H    1    12  UNP    P0C0S8   H2A1_HUMAN       2     13             
SEQADV 4QYL GLY A    1  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL PRO A    2  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL LEU A    3  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL GLY B    1  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL PRO B    2  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL LEU B    3  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL GLY C    1  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL PRO C    2  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL LEU C    3  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL GLY D    1  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL PRO D    2  UNP  P55201              EXPRESSION TAG                 
SEQADV 4QYL LEU D    3  UNP  P55201              EXPRESSION TAG                 
SEQRES   1 A  117  GLY PRO LEU GLN LEU THR PRO PHE LEU ILE LEU LEU ARG          
SEQRES   2 A  117  LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY ASN          
SEQRES   3 A  117  ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO ASP          
SEQRES   4 A  117  TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE THR          
SEQRES   5 A  117  MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN PHE          
SEQRES   6 A  117  ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER ASN          
SEQRES   7 A  117  CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR ARG          
SEQRES   8 A  117  ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL LEU          
SEQRES   9 A  117  ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY ILE ASP          
SEQRES   1 B  117  GLY PRO LEU GLN LEU THR PRO PHE LEU ILE LEU LEU ARG          
SEQRES   2 B  117  LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY ASN          
SEQRES   3 B  117  ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO ASP          
SEQRES   4 B  117  TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE THR          
SEQRES   5 B  117  MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN PHE          
SEQRES   6 B  117  ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER ASN          
SEQRES   7 B  117  CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR ARG          
SEQRES   8 B  117  ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL LEU          
SEQRES   9 B  117  ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY ILE ASP          
SEQRES   1 C  117  GLY PRO LEU GLN LEU THR PRO PHE LEU ILE LEU LEU ARG          
SEQRES   2 C  117  LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY ASN          
SEQRES   3 C  117  ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO ASP          
SEQRES   4 C  117  TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE THR          
SEQRES   5 C  117  MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN PHE          
SEQRES   6 C  117  ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER ASN          
SEQRES   7 C  117  CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR ARG          
SEQRES   8 C  117  ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL LEU          
SEQRES   9 C  117  ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY ILE ASP          
SEQRES   1 D  117  GLY PRO LEU GLN LEU THR PRO PHE LEU ILE LEU LEU ARG          
SEQRES   2 D  117  LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY ASN          
SEQRES   3 D  117  ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO ASP          
SEQRES   4 D  117  TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE THR          
SEQRES   5 D  117  MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN PHE          
SEQRES   6 D  117  ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER ASN          
SEQRES   7 D  117  CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR ARG          
SEQRES   8 D  117  ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL LEU          
SEQRES   9 D  117  ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY ILE ASP          
SEQRES   1 E   12  SER GLY ARG GLY ALY GLN GLY GLY LYS ALA ARG ALA              
SEQRES   1 F   12  SER GLY ARG GLY ALY GLN GLY GLY LYS ALA ARG ALA              
SEQRES   1 G   12  SER GLY ARG GLY ALY GLN GLY GLY LYS ALA ARG ALA              
SEQRES   1 H   12  SER GLY ARG GLY ALY GLN GLY GLY LYS ALA ARG ALA              
MODRES 4QYL ALY E    5  LYS  N(6)-ACETYLLYSINE                                  
MODRES 4QYL ALY F    5  LYS  N(6)-ACETYLLYSINE                                  
MODRES 4QYL ALY G    5  LYS  N(6)-ACETYLLYSINE                                  
MODRES 4QYL ALY H    5  LYS  N(6)-ACETYLLYSINE                                  
HET    ALY  E   5      12                                                       
HET    ALY  F   5      12                                                       
HET    ALY  G   5      12                                                       
HET    ALY  H   5      12                                                       
HET    SO4  A 201       5                                                       
HET    SO4  B 201       5                                                       
HET    SO4  C 201       5                                                       
HET    SO4  D 201       5                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  ALY    4(C8 H16 N2 O3)                                              
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  13  HOH   *722(H2 O)                                                    
HELIX    1   1 THR A    6  ASP A   23  1                                  18    
HELIX    2   2 ASP A   39  ILE A   44  1                                   6    
HELIX    3   3 ASP A   49  ALA A   59  1                                  11    
HELIX    4   4 ASN A   64  ASN A   83  1                                  20    
HELIX    5   5 THR A   87  MET A  114  1                                  28    
HELIX    6   6 THR B    6  ASP B   23  1                                  18    
HELIX    7   7 ASP B   39  ILE B   44  1                                   6    
HELIX    8   8 ASP B   49  ALA B   59  1                                  11    
HELIX    9   9 ASN B   64  ASN B   83  1                                  20    
HELIX   10  10 THR B   87  MET B  114  1                                  28    
HELIX   11  11 THR C    6  ASP C   23  1                                  18    
HELIX   12  12 ASP C   39  ILE C   44  1                                   6    
HELIX   13  13 ASP C   49  ALA C   59  1                                  11    
HELIX   14  14 ASN C   64  ASN C   83  1                                  20    
HELIX   15  15 THR C   87  MET C  114  1                                  28    
HELIX   16  16 THR D    6  LYS D   22  1                                  17    
HELIX   17  17 ASP D   39  ILE D   44  1                                   6    
HELIX   18  18 ASP D   49  ALA D   59  1                                  11    
HELIX   19  19 ASN D   64  ASN D   83  1                                  20    
HELIX   20  20 THR D   87  MET D  114  1                                  28    
LINK         C   GLY E   4                 N   ALY E   5     1555   1555  1.33  
LINK         C   ALY E   5                 N   GLN E   6     1555   1555  1.33  
LINK         C   GLY F   4                 N   ALY F   5     1555   1555  1.32  
LINK         C   ALY F   5                 N   GLN F   6     1555   1555  1.30  
LINK         C   GLY G   4                 N   ALY G   5     1555   1555  1.33  
LINK         C   ALY G   5                 N  AGLN G   6     1555   1555  1.31  
LINK         C   ALY G   5                 N  BGLN G   6     1555   1555  1.34  
LINK         C   GLY H   4                 N   ALY H   5     1555   1555  1.33  
LINK         C   ALY H   5                 N   GLN H   6     1555   1555  1.31  
SITE     1 AC1  7 ARG A  91  ARG A  95  HOH A 314  HOH A 316                    
SITE     2 AC1  7 ARG D 109  GLN D 110  LYS D 113                               
SITE     1 AC2  9 ARG B  91  ARG B  95  HOH B 339  HOH B 427                    
SITE     2 AC2  9 HOH B 484  ARG C 109  GLN C 110  LYS C 113                    
SITE     3 AC2  9 HOH C 321                                                     
SITE     1 AC3  8 ARG B 109  GLN B 110  LYS B 113  HOH B 304                    
SITE     2 AC3  8 ARG C  91  ARG C  95  HOH C 334  HOH C 463                    
SITE     1 AC4  8 ARG A 109  GLN A 110  LYS A 113  HOH A 309                    
SITE     2 AC4  8 ARG D  91  ARG D  95  HOH D 360  HOH D 422                    
CRYST1   60.908   55.581   82.135  90.00  93.58  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016418  0.000000  0.001027        0.00000                         
SCALE2      0.000000  0.017992  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012199        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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