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Database: PDB
Entry: 5FFY
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Original site: 5FFY 
HEADER    TRANSCRIPTION                           19-DEC-15   5FFY              
TITLE     CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BRPF1 IN COMPLEX WITH A 
TITLE    2 BENZIMIDAZOLE LIGAND                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEREGRIN;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 626-740;                                      
COMPND   5 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1,PROTEIN     
COMPND   6 BR140;                                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRPF1, BR140;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    PEREGRIN, MOZ-MORF COMPLEX, TRANSCRIPTION                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.TALLANT,P.SAVITSKY,G.NUNEZ-ALONSO,J.KOPEC,O.FEDOROV,                
AUTHOR   2 P.FILIPPAKOPOULOS,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,  
AUTHOR   3 S.KNAPP                                                              
REVDAT   1   30-DEC-15 5FFY    0                                                
JRNL        AUTH   C.TALLANT,P.SAVITSKY,G.NUNEZ-ALONSO,J.KOPEC,O.FEDOROV,       
JRNL        AUTH 2 P.FILIPPAKOPOULOS,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,    
JRNL        AUTH 3 C.BOUNTRA,S.KNAPP                                            
JRNL        TITL   CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BRPF1 IN       
JRNL        TITL 2 COMPLEX WITH A BENZIMIDAZOLE LIGAND                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19595                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1058                            
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1424                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.35                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 926                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.15000                                              
REMARK   3    B22 (A**2) : -0.82000                                             
REMARK   3    B33 (A**2) : -0.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.73000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.078         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.080         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.051         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.514         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   994 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):   969 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1346 ; 1.633 ; 2.015       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2223 ; 0.794 ; 3.007       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   116 ; 4.851 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;34.603 ;23.962       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   186 ;13.227 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;20.913 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   142 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1114 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   241 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   449 ; 3.983 ; 3.224       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   448 ; 3.935 ; 3.207       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   561 ; 4.940 ; 5.953       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   562 ; 4.935 ; 5.975       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   545 ; 9.511 ; 4.528       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   546 ; 9.502 ; 4.528       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):   783 ;12.700 ; 7.795       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1304 ;12.122 ;20.476       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1305 ;12.120 ;20.477       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   630        A   739                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6840 -18.2590  10.2441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0306 T22:   0.0372                                     
REMARK   3      T33:   0.0386 T12:  -0.0108                                     
REMARK   3      T13:   0.0052 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8112 L22:   2.5016                                     
REMARK   3      L33:   0.3056 L12:  -1.2858                                     
REMARK   3      L13:  -0.4103 L23:   0.4480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0032 S12:  -0.0285 S13:   0.1695                       
REMARK   3      S21:  -0.0821 S22:   0.0860 S23:  -0.2660                       
REMARK   3      S31:   0.0470 S32:  -0.0194 S33:  -0.0828                       
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 5FFY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216532.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.03700                            
REMARK 200  R SYM                      (I) : 0.02200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4LC2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ROD                                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS TRIS PROPANE PH 9, 10%         
REMARK 280  ETHYLENE GLYCOL, 0.15 M SODIUM NITRATE, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 277.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       4555   -X+1/2,Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       19.63477            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.93450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       25.19471            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       19.63477            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.93450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       25.19471            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 7050 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 958  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 985  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1003  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1024  LIES ON A SPECIAL POSITION.                          
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     SER A   625                                                      
REMARK 465     MET A   626                                                      
REMARK 465     GLU A   627                                                      
REMARK 465     MET A   628                                                      
REMARK 465     GLY A   740                                                      
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 A1023        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH A1024        DISTANCE =  7.13 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5XD A 801                 
DBREF  5FFY A  626   740  UNP    P55201   BRPF1_HUMAN    626    740             
SEQADV 5FFY SER A  625  UNP  P55201              EXPRESSION TAG                 
SEQRES   1 A  116  SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU          
SEQRES   2 A  116  ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY          
SEQRES   3 A  116  ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO          
SEQRES   4 A  116  ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE          
SEQRES   5 A  116  THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN          
SEQRES   6 A  116  PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER          
SEQRES   7 A  116  ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR          
SEQRES   8 A  116  ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL          
SEQRES   9 A  116  LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY              
HET    5XD  A 801      26                                                       
HETNAM     5XD 4-ETHYL-~{N}-(6-METHOXY-1,3-DIMETHYL-2-OXIDANYLIDENE-            
HETNAM   2 5XD  BENZIMIDAZOL-5-YL)BENZENESULFONAMIDE                            
FORMUL   2  5XD    C18 H21 N3 O4 S                                              
FORMUL   3  HOH   *124(H2 O)                                                    
HELIX    1 AA1 THR A  631  ASP A  648  1                                  18    
HELIX    2 AA2 ASP A  664  ILE A  669  1                                   6    
HELIX    3 AA3 ASP A  674  ALA A  684  1                                  11    
HELIX    4 AA4 ASN A  689  ASN A  708  1                                  20    
HELIX    5 AA5 THR A  712  LYS A  738  1                                  27    
SITE     1 AC1 13 LYS A 639  GLU A 642  ILE A 652  PHE A 653                    
SITE     2 AC1 13 VAL A 657  PRO A 658  GLU A 661  VAL A 662                    
SITE     3 AC1 13 ASN A 708  PHE A 714  HOH A 907  HOH A 939                    
SITE     4 AC1 13 HOH A 959                                                     
CRYST1   48.545   59.869   51.236  90.00 100.43  90.00 I 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020599  0.000000  0.003794        0.00000                         
SCALE2      0.000000  0.016703  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019846        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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