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Database: PDB
Entry: 2X4X
LinkDB: 2X4X
Original site: 2X4X 
HEADER    TRANSCRIPTION                           02-FEB-10   2X4X              
TITLE     MOLECULAR BASIS OF HISTONE H3K36ME3 RECOGNITION BY THE PWWP DOMAIN OF 
TITLE    2 BRPF1.                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEREGRIN;                                                  
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: BRPF1 PWWP DOMAIN, RESIDUES 1076-1205;                     
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 H3.2;                                              
COMPND  10 CHAIN: B, D, F, H;                                                   
COMPND  11 FRAGMENT: RESIDUES 23-43;                                            
COMPND  12 SYNONYM: HUMAN H3 HISTONE, H3/M, H3/O;                               
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: TRIMETHYLATION AT POSITION 36                         
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 BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PRSETA;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSCRIPTION, METAL-BINDING, ZINC-FINGER, CHROMATIN REGULATOR,       
KEYWDS   2 TRANSCRIPTION REGULATION, NUCLEOSOME                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.VEZZOLI,N.BONADIES,M.D.ALLEN,S.M.V.FREUND,C.M.SANTIVERI,B.KVINLAUG, 
AUTHOR   2 B.J.P.HUNTLY,B.GOTTGENS,M.BYCROFT                                    
REVDAT   4   24-JAN-18 2X4X    1       SOURCE                                   
REVDAT   3   15-JUN-11 2X4X    1       JRNL   REMARK DBREF  SEQADV              
REVDAT   2   28-APR-10 2X4X    1       JRNL                                     
REVDAT   1   21-APR-10 2X4X    0                                                
JRNL        AUTH   A.VEZZOLI,N.BONADIES,M.D.ALLEN,S.M.V.FREUND,C.M.SANTIVERI,   
JRNL        AUTH 2 B.KVINLAUG,B.J.P.HUNTLY,B.GOTTGENS,M.BYCROFT                 
JRNL        TITL   MOLECULAR BASIS OF HISTONE H3K36ME3 RECOGNITION BY THE PWWP  
JRNL        TITL 2 DOMAIN OF BRPF1.                                             
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   617 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20400950                                                     
JRNL        DOI    10.1038/NSMB.1797                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.310                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 57745                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5393                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.0039 -  5.7402    0.95     3411   187  0.1873 0.1924        
REMARK   3     2  5.7402 -  4.5594    0.98     3545   175  0.1714 0.1856        
REMARK   3     3  4.5594 -  3.9840    0.97     3472   233  0.1590 0.1884        
REMARK   3     4  3.9840 -  3.6201    0.97     3528   184  0.1703 0.2224        
REMARK   3     5  3.6201 -  3.3609    0.97     3495   179  0.1735 0.2316        
REMARK   3     6  3.3609 -  3.1628    0.97     3483   181  0.1867 0.2175        
REMARK   3     7  3.1628 -  3.0045    0.97     3527   185  0.2057 0.2510        
REMARK   3     8  3.0045 -  2.8738    0.96     3475   173  0.2043 0.2441        
REMARK   3     9  2.8738 -  2.7632    0.95     3397   192  0.1951 0.2403        
REMARK   3    10  2.7632 -  2.6679    0.95     3515   170  0.1988 0.2844        
REMARK   3    11  2.6679 -  2.5845    0.96     3396   176  0.2117 0.2829        
REMARK   3    12  2.5845 -  2.5107    0.95     3443   209  0.2166 0.2610        
REMARK   3    13  2.5107 -  2.4446    0.95     3412   180  0.2101 0.2726        
REMARK   3    14  2.4446 -  2.3850    0.95     3381   159  0.2110 0.2813        
REMARK   3    15  2.3850 -  2.3307    0.94     3483   173  0.1994 0.2319        
REMARK   3    16  2.3307 -  2.2812    0.94     3363   172  0.1836 0.2567        
REMARK   3    17  2.2812 -  2.2355    0.94     3399   189  0.1925 0.2382        
REMARK   3    18  2.2355 -  2.1934    0.94     3476   160  0.1970 0.3060        
REMARK   3    19  2.1934 -  2.1542    0.94     3382   170  0.2019 0.2562        
REMARK   3    20  2.1542 -  2.1177    0.93     3338   181  0.2084 0.2477        
REMARK   3    21  2.1177 -  2.0835    0.94     3464   197  0.2253 0.2800        
REMARK   3    22  2.0835 -  2.0515    0.93     3311   164  0.2340 0.2683        
REMARK   3    23  2.0515 -  2.0213    0.93     3330   157  0.2302 0.2571        
REMARK   3    24  2.0213 -  1.9928    0.93     3464   161  0.2446 0.3099        
REMARK   3    25  1.9928 -  1.9659    0.93     3329   194  0.2469 0.2960        
REMARK   3    26  1.9659 -  1.9404    0.93     3298   196  0.2447 0.3046        
REMARK   3    27  1.9404 -  1.9161    0.92     3281   189  0.2509 0.2982        
REMARK   3    28  1.9161 -  1.8930    0.92     3355   192  0.2587 0.2848        
REMARK   3    29  1.8930 -  1.8710    0.92     3322   168  0.2619 0.3221        
REMARK   3    30  1.8710 -  1.8500    0.91     3326   147  0.2737 0.2823        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 49.73                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.38730                                              
REMARK   3    B22 (A**2) : -3.83230                                             
REMARK   3    B33 (A**2) : -0.55500                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 6.85870                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           4573                                  
REMARK   3   ANGLE     :  1.259           6197                                  
REMARK   3   CHIRALITY :  0.094            653                                  
REMARK   3   PLANARITY :  0.006            792                                  
REMARK   3   DIHEDRAL  : 16.575           1783                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED REGIONS WERE MODELED           
REMARK   3  STEREOCHEMICALLY                                                    
REMARK   4                                                                      
REMARK   4 2X4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290042622.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9334                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57772                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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   (%): 49.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M LITHIUM SULPHATE,      
REMARK 280  0.1M TRIS (PH 8.5) 0.01M NACL                                       
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       51.47050            
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: 1290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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: 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: 1350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8330 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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: 1350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8250 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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 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: 1580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8650 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1074                                                      
REMARK 465     GLY A  1075                                                      
REMARK 465     SER A  1076                                                      
REMARK 465     GLU A  1077                                                      
REMARK 465     ASP A  1078                                                      
REMARK 465     GLU A  1079                                                      
REMARK 465     THR B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     ARG B    26                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     ARG B    42                                                      
REMARK 465     GLY C  1074                                                      
REMARK 465     GLY C  1075                                                      
REMARK 465     SER C  1076                                                      
REMARK 465     GLU C  1077                                                      
REMARK 465     ASP C  1078                                                      
REMARK 465     GLU C  1079                                                      
REMARK 465     GLU C  1205                                                      
REMARK 465     THR D    22                                                      
REMARK 465     LYS D    23                                                      
REMARK 465     ALA D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     ARG D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     ARG D    40                                                      
REMARK 465     TYR D    41                                                      
REMARK 465     ARG D    42                                                      
REMARK 465     GLY E  1074                                                      
REMARK 465     GLY E  1075                                                      
REMARK 465     SER E  1076                                                      
REMARK 465     GLU E  1077                                                      
REMARK 465     ASP E  1078                                                      
REMARK 465     GLU E  1079                                                      
REMARK 465     THR F    22                                                      
REMARK 465     LYS F    23                                                      
REMARK 465     ALA F    24                                                      
REMARK 465     ALA F    25                                                      
REMARK 465     ARG F    26                                                      
REMARK 465     LYS F    27                                                      
REMARK 465     HIS F    39                                                      
REMARK 465     ARG F    40                                                      
REMARK 465     TYR F    41                                                      
REMARK 465     ARG F    42                                                      
REMARK 465     GLY G  1074                                                      
REMARK 465     GLY G  1075                                                      
REMARK 465     SER G  1076                                                      
REMARK 465     GLU G  1077                                                      
REMARK 465     ASP G  1078                                                      
REMARK 465     GLU G  1079                                                      
REMARK 465     ASP G  1080                                                      
REMARK 465     SER G  1081                                                      
REMARK 465     GLY G  1204                                                      
REMARK 465     GLU G  1205                                                      
REMARK 465     THR H    22                                                      
REMARK 465     LYS H    23                                                      
REMARK 465     ALA H    24                                                      
REMARK 465     ALA H    25                                                      
REMARK 465     ARG H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     ARG H    40                                                      
REMARK 465     TYR H    41                                                      
REMARK 465     ARG H    42                                                      
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   O3   SO4 A  2206     O    HOH A  2147              2.18            
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    PHE A1148       30.85    -87.89                                   
REMARK 500    ARG A1152       71.09     56.27                                   
REMARK 500    ARG C1152       71.14     55.49                                   
REMARK 500    PHE E1148       34.26    -85.98                                   
REMARK 500    ARG E1152       66.50     61.30                                   
REMARK 500    LEU G1086        5.44     80.79                                   
REMARK 500    PHE G1148       31.74    -91.64                                   
REMARK 500    ARG G1152       71.11     58.53                                   
REMARK 500    PRO H  38      150.87    -49.61                                   
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 A2007        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH E2004        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH E2005        DISTANCE =  5.81 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 2206                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2D9E   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE BROMODOMAIN OF PEREGRIN                    
REMARK 900 RELATED ID: 2X35   RELATED DB: PDB                                   
REMARK 900 MOLECULAR BASIS OF HISTONE H3K36ME3 RECOGNITION BY THE PWWP DOMAIN   
REMARK 900 OF BRPF1.                                                            
REMARK 900 RELATED ID: 2X4Y   RELATED DB: PDB                                   
REMARK 900 MOLECULAR BASIS OF HISTONE H3K36ME3 RECOGNITION BY THE PWWP DOMAIN   
REMARK 900 OF BRPF1.                                                            
REMARK 900 RELATED ID: 2X4W   RELATED DB: PDB                                   
REMARK 900 MOLECULAR BASIS OF HISTONE H3K36ME3 RECOGNITION BY THE PWWP DOMAIN   
REMARK 900 OF BRPF1.                                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 LYSINE 36 IS TRIMETHYLATED                                           
DBREF  2X4X A 1076  1205  UNP    P55201   BRPF1_HUMAN   1076   1205             
DBREF  2X4X B   22    42  UNP    Q71DI3   H32_HUMAN       23     43             
DBREF  2X4X C 1076  1205  UNP    P55201   BRPF1_HUMAN   1076   1205             
DBREF  2X4X D   22    42  UNP    Q71DI3   H32_HUMAN       23     43             
DBREF  2X4X E 1076  1205  UNP    P55201   BRPF1_HUMAN   1076   1205             
DBREF  2X4X F   22    42  UNP    Q71DI3   H32_HUMAN       23     43             
DBREF  2X4X G 1076  1205  UNP    P55201   BRPF1_HUMAN   1076   1205             
DBREF  2X4X H   22    42  UNP    Q71DI3   H32_HUMAN       23     43             
SEQADV 2X4X GLY A 1074  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY A 1075  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY C 1074  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY C 1075  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY E 1074  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY E 1075  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY G 1074  UNP  P55201              EXPRESSION TAG                 
SEQADV 2X4X GLY G 1075  UNP  P55201              EXPRESSION TAG                 
SEQRES   1 A  132  GLY GLY SER GLU ASP GLU ASP SER PRO LEU ASP ALA LEU          
SEQRES   2 A  132  ASP LEU VAL TRP ALA LYS CYS ARG GLY TYR PRO SER TYR          
SEQRES   3 A  132  PRO ALA LEU ILE ILE ASP PRO LYS MET PRO ARG GLU GLY          
SEQRES   4 A  132  MET PHE HIS HIS GLY VAL PRO ILE PRO VAL PRO PRO LEU          
SEQRES   5 A  132  GLU VAL LEU LYS LEU GLY GLU GLN MET THR GLN GLU ALA          
SEQRES   6 A  132  ARG GLU HIS LEU TYR LEU VAL LEU PHE PHE ASP ASN LYS          
SEQRES   7 A  132  ARG THR TRP GLN TRP LEU PRO ARG THR LYS LEU VAL PRO          
SEQRES   8 A  132  LEU GLY VAL ASN GLN ASP LEU ASP LYS GLU LYS MET LEU          
SEQRES   9 A  132  GLU GLY ARG LYS SER ASN ILE ARG LYS SER VAL GLN ILE          
SEQRES  10 A  132  ALA TYR HIS ARG ALA LEU GLN HIS ARG SER LYS VAL GLN          
SEQRES  11 A  132  GLY GLU                                                      
SEQRES   1 B   21  THR LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY          
SEQRES   2 B   21  VAL M3L LYS PRO HIS ARG TYR ARG                              
SEQRES   1 C  132  GLY GLY SER GLU ASP GLU ASP SER PRO LEU ASP ALA LEU          
SEQRES   2 C  132  ASP LEU VAL TRP ALA LYS CYS ARG GLY TYR PRO SER TYR          
SEQRES   3 C  132  PRO ALA LEU ILE ILE ASP PRO LYS MET PRO ARG GLU GLY          
SEQRES   4 C  132  MET PHE HIS HIS GLY VAL PRO ILE PRO VAL PRO PRO LEU          
SEQRES   5 C  132  GLU VAL LEU LYS LEU GLY GLU GLN MET THR GLN GLU ALA          
SEQRES   6 C  132  ARG GLU HIS LEU TYR LEU VAL LEU PHE PHE ASP ASN LYS          
SEQRES   7 C  132  ARG THR TRP GLN TRP LEU PRO ARG THR LYS LEU VAL PRO          
SEQRES   8 C  132  LEU GLY VAL ASN GLN ASP LEU ASP LYS GLU LYS MET LEU          
SEQRES   9 C  132  GLU GLY ARG LYS SER ASN ILE ARG LYS SER VAL GLN ILE          
SEQRES  10 C  132  ALA TYR HIS ARG ALA LEU GLN HIS ARG SER LYS VAL GLN          
SEQRES  11 C  132  GLY GLU                                                      
SEQRES   1 D   21  THR LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY          
SEQRES   2 D   21  VAL M3L LYS PRO HIS ARG TYR ARG                              
SEQRES   1 E  132  GLY GLY SER GLU ASP GLU ASP SER PRO LEU ASP ALA LEU          
SEQRES   2 E  132  ASP LEU VAL TRP ALA LYS CYS ARG GLY TYR PRO SER TYR          
SEQRES   3 E  132  PRO ALA LEU ILE ILE ASP PRO LYS MET PRO ARG GLU GLY          
SEQRES   4 E  132  MET PHE HIS HIS GLY VAL PRO ILE PRO VAL PRO PRO LEU          
SEQRES   5 E  132  GLU VAL LEU LYS LEU GLY GLU GLN MET THR GLN GLU ALA          
SEQRES   6 E  132  ARG GLU HIS LEU TYR LEU VAL LEU PHE PHE ASP ASN LYS          
SEQRES   7 E  132  ARG THR TRP GLN TRP LEU PRO ARG THR LYS LEU VAL PRO          
SEQRES   8 E  132  LEU GLY VAL ASN GLN ASP LEU ASP LYS GLU LYS MET LEU          
SEQRES   9 E  132  GLU GLY ARG LYS SER ASN ILE ARG LYS SER VAL GLN ILE          
SEQRES  10 E  132  ALA TYR HIS ARG ALA LEU GLN HIS ARG SER LYS VAL GLN          
SEQRES  11 E  132  GLY GLU                                                      
SEQRES   1 F   21  THR LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY          
SEQRES   2 F   21  VAL M3L LYS PRO HIS ARG TYR ARG                              
SEQRES   1 G  132  GLY GLY SER GLU ASP GLU ASP SER PRO LEU ASP ALA LEU          
SEQRES   2 G  132  ASP LEU VAL TRP ALA LYS CYS ARG GLY TYR PRO SER TYR          
SEQRES   3 G  132  PRO ALA LEU ILE ILE ASP PRO LYS MET PRO ARG GLU GLY          
SEQRES   4 G  132  MET PHE HIS HIS GLY VAL PRO ILE PRO VAL PRO PRO LEU          
SEQRES   5 G  132  GLU VAL LEU LYS LEU GLY GLU GLN MET THR GLN GLU ALA          
SEQRES   6 G  132  ARG GLU HIS LEU TYR LEU VAL LEU PHE PHE ASP ASN LYS          
SEQRES   7 G  132  ARG THR TRP GLN TRP LEU PRO ARG THR LYS LEU VAL PRO          
SEQRES   8 G  132  LEU GLY VAL ASN GLN ASP LEU ASP LYS GLU LYS MET LEU          
SEQRES   9 G  132  GLU GLY ARG LYS SER ASN ILE ARG LYS SER VAL GLN ILE          
SEQRES  10 G  132  ALA TYR HIS ARG ALA LEU GLN HIS ARG SER LYS VAL GLN          
SEQRES  11 G  132  GLY GLU                                                      
SEQRES   1 H   21  THR LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY          
SEQRES   2 H   21  VAL M3L LYS PRO HIS ARG TYR ARG                              
MODRES 2X4X M3L B   36  LYS  N-TRIMETHYLLYSINE                                  
MODRES 2X4X M3L D   36  LYS  N-TRIMETHYLLYSINE                                  
MODRES 2X4X M3L F   36  LYS  N-TRIMETHYLLYSINE                                  
MODRES 2X4X M3L H   36  LYS  N-TRIMETHYLLYSINE                                  
HET    M3L  B  36      12                                                       
HET    M3L  D  36      12                                                       
HET    M3L  F  36      12                                                       
HET    M3L  H  36      12                                                       
HET    SO4  A2206       5                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  M3L    4(C9 H21 N2 O2 1+)                                           
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  10  HOH   *574(H2 O)                                                    
HELIX    1   1 PRO A 1124  ARG A 1139  1                                  16    
HELIX    2   2 ASN A 1168  LEU A 1177  1                                  10    
HELIX    3   3 LYS A 1181  GLN A 1203  1                                  23    
HELIX    4   4 PRO C 1124  ARG C 1139  1                                  16    
HELIX    5   5 ASN C 1168  LEU C 1177  1                                  10    
HELIX    6   6 LYS C 1181  GLY C 1204  1                                  24    
HELIX    7   7 PRO E 1124  ARG E 1139  1                                  16    
HELIX    8   8 PRO E 1158  THR E 1160  5                                   3    
HELIX    9   9 ASN E 1168  LEU E 1177  1                                  10    
HELIX   10  10 LYS E 1181  GLY E 1204  1                                  24    
HELIX   11  11 PRO G 1124  ARG G 1139  1                                  16    
HELIX   12  12 ASN G 1168  LEU G 1177  1                                  10    
HELIX   13  13 LYS G 1181  GLN G 1203  1                                  23    
SHEET    1  AA 5 TRP A1154  PRO A1158  0                                        
SHEET    2  AA 5 LEU A1142  PHE A1147 -1  O  TYR A1143   N  LEU A1157           
SHEET    3  AA 5 TYR A1099  ILE A1104 -1  O  LEU A1102   N  LEU A1146           
SHEET    4  AA 5 LEU A1088  ALA A1091 -1  O  VAL A1089   N  ALA A1101           
SHEET    5  AA 5 LEU A1162  PRO A1164 -1  O  VAL A1163   N  TRP A1090           
SHEET    1  AB 2 MET A1113  HIS A1115  0                                        
SHEET    2  AB 2 VAL A1118  ILE A1120 -1  O  VAL A1118   N  HIS A1115           
SHEET    1  CA 5 TRP C1154  PRO C1158  0                                        
SHEET    2  CA 5 LEU C1142  PHE C1147 -1  O  TYR C1143   N  LEU C1157           
SHEET    3  CA 5 TYR C1099  ILE C1104 -1  O  LEU C1102   N  LEU C1146           
SHEET    4  CA 5 LEU C1088  ALA C1091 -1  O  VAL C1089   N  ALA C1101           
SHEET    5  CA 5 LEU C1162  PRO C1164 -1  O  VAL C1163   N  TRP C1090           
SHEET    1  CB 2 MET C1113  HIS C1115  0                                        
SHEET    2  CB 2 VAL C1118  ILE C1120 -1  O  VAL C1118   N  HIS C1115           
SHEET    1  EA 5 TRP E1154  LEU E1157  0                                        
SHEET    2  EA 5 TYR E1143  PHE E1147 -1  O  TYR E1143   N  LEU E1157           
SHEET    3  EA 5 TYR E1099  ILE E1104 -1  O  LEU E1102   N  LEU E1146           
SHEET    4  EA 5 LEU E1088  ALA E1091 -1  O  VAL E1089   N  ALA E1101           
SHEET    5  EA 5 LEU E1162  PRO E1164 -1  O  VAL E1163   N  TRP E1090           
SHEET    1  EB 2 MET E1113  HIS E1115  0                                        
SHEET    2  EB 2 VAL E1118  ILE E1120 -1  O  VAL E1118   N  HIS E1115           
SHEET    1  GA 5 TRP G1154  PRO G1158  0                                        
SHEET    2  GA 5 LEU G1142  PHE G1147 -1  O  TYR G1143   N  LEU G1157           
SHEET    3  GA 5 TYR G1099  ILE G1104 -1  O  LEU G1102   N  LEU G1146           
SHEET    4  GA 5 LEU G1088  ALA G1091 -1  O  VAL G1089   N  ALA G1101           
SHEET    5  GA 5 LEU G1162  PRO G1164 -1  O  VAL G1163   N  TRP G1090           
SHEET    1  GB 2 PHE G1114  HIS G1115  0                                        
SHEET    2  GB 2 VAL G1118  PRO G1119 -1  O  VAL G1118   N  HIS G1115           
LINK         C   VAL B  35                 N   M3L B  36     1555   1555  1.33  
LINK         C   M3L B  36                 N   LYS B  37     1555   1555  1.33  
LINK         C   VAL D  35                 N   M3L D  36     1555   1555  1.33  
LINK         C   M3L D  36                 N   LYS D  37     1555   1555  1.33  
LINK         C   VAL F  35                 N   M3L F  36     1555   1555  1.33  
LINK         C   M3L F  36                 N   LYS F  37     1555   1555  1.33  
LINK         C   VAL H  35                 N   M3L H  36     1555   1555  1.33  
LINK         C   M3L H  36                 N   LYS H  37     1555   1555  1.33  
SITE     1 AC1  6 ARG A1110  LEU A1125  HOH A2147  HOH A2148                    
SITE     2 AC1  6 HOH A2149  HOH A2150                                          
CRYST1   38.437  102.941   88.654  90.00 100.33  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      0.026017  0.000000  0.004742        0.00000                         
SCALE2      0.000000  0.009714  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011466        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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