GenomeNet

Database: PDB
Entry: 3MO8
LinkDB: 3MO8
Original site: 3MO8 
HEADER    TRANSCRIPTION                           22-APR-10   3MO8              
TITLE     PWWP DOMAIN OF HUMAN BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1  
TITLE    2 IN COMPLEX WITH TRIMETHYLATED H3K36 PEPTIDE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEREGRIN;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1079-1207;                                    
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 TRIMETHYLATED H3K36 PEPTIDE;                  
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUE 31-42;                                         
COMPND  12 SYNONYM: HISTONE H3/M, HISTONE H3/O;                                 
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: BL21-(DE3)-V2R-PRARE2;                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;                                
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    PEREGRIN, PROTEIN BR140, HISTONE H3 ACETYLATION, TRANSCRIPTION,       
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.LAM,H.ZENG,S.NI,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,     
AUTHOR   2 A.BOCHKAREV,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)          
REVDAT   3   08-NOV-17 3MO8    1       REMARK                                   
REVDAT   2   20-JUL-11 3MO8    1       JRNL                                     
REVDAT   1   02-JUN-10 3MO8    0                                                
JRNL        AUTH   H.WU,H.ZENG,R.LAM,W.TEMPEL,M.F.AMAYA,C.XU,L.DOMBROVSKI,      
JRNL        AUTH 2 W.QIU,Y.WANG,J.MIN                                           
JRNL        TITL   STRUCTURAL AND HISTONE BINDING ABILITY CHARACTERIZATIONS OF  
JRNL        TITL 2 HUMAN PWWP DOMAINS.                                          
JRNL        REF    PLOS ONE                      V.   6 18919 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21720545                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0018919                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.5.0109                               
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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 18540                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1005                            
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) : 1.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1201                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1124                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 107                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24000                                             
REMARK   3    B22 (A**2) : 2.40000                                              
REMARK   3    B33 (A**2) : -2.16000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.100         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.093         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.050         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1170 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1587 ; 1.214 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   141 ; 4.969 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    52 ;27.124 ;22.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   205 ;13.057 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;12.200 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   167 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   886 ; 0.006 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):   703 ; 0.770 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1138 ; 1.444 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   467 ; 2.111 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   447 ; 3.504 ; 4.500       
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   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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  1078        A  1204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9190  19.4870  18.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0624 T22:   0.0121                                     
REMARK   3      T33:   0.0926 T12:  -0.0054                                     
REMARK   3      T13:   0.0106 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8213 L22:   0.6005                                     
REMARK   3      L33:   1.7663 L12:   0.1870                                     
REMARK   3      L13:  -0.5033 L23:   0.0764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0323 S12:  -0.0180 S13:   0.0472                       
REMARK   3      S21:  -0.0229 S22:   0.0287 S23:  -0.0384                       
REMARK   3      S31:   0.0086 S32:   0.0080 S33:  -0.0610                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    12                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4490  29.7360  13.3060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1240 T22:   0.0177                                     
REMARK   3      T33:   0.0984 T12:   0.0110                                     
REMARK   3      T13:   0.0030 T23:   0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5390 L22:   8.2628                                     
REMARK   3      L33:   1.9003 L12:   0.4753                                     
REMARK   3      L13:  -0.2621 L23:   1.2125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0626 S12:   0.0864 S13:   0.1270                       
REMARK   3      S21:  -0.1429 S22:  -0.0095 S23:   0.2037                       
REMARK   3      S31:  -0.2913 S32:  -0.0888 S33:   0.0721                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3MO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058792.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-10                          
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               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97935                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK HIGH-RESOLUTION     
REMARK 200                                   DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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 3L42                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM FORMATE, 0.1M TRIS-HCL       
REMARK 280  PH8.5, H3K36ME3 PEPTIDE, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       21.54300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.30250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.76950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       21.54300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.30250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.76950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       21.54300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.30250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       56.76950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       21.54300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       35.30250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       56.76950            
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 300 REMARK: AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS A MONOMER      
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: 1340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8520 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     GLU A  1205                                                      
REMARK 465     GLN A  1206                                                      
REMARK 465     SER A  1207                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A1079    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1126    CG   CD   OE1  OE2                                  
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       36.48    -85.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L42   RELATED DB: PDB                                   
DBREF  3MO8 A 1079  1207  UNP    P55201   BRPF1_HUMAN   1079   1207             
DBREF  3MO8 B    1    12  UNP    Q71DI3   H32_HUMAN       31     42             
SEQADV 3MO8 GLY A 1078  UNP  P55201              EXPRESSION TAG                 
SEQRES   1 A  130  GLY GLU ASP SER PRO LEU ASP ALA LEU ASP LEU VAL TRP          
SEQRES   2 A  130  ALA LYS CYS ARG GLY TYR PRO SER TYR PRO ALA LEU ILE          
SEQRES   3 A  130  ILE ASP PRO LYS MET PRO ARG GLU GLY MET PHE HIS HIS          
SEQRES   4 A  130  GLY VAL PRO ILE PRO VAL PRO PRO LEU GLU VAL LEU LYS          
SEQRES   5 A  130  LEU GLY GLU GLN MET THR GLN GLU ALA ARG GLU HIS LEU          
SEQRES   6 A  130  TYR LEU VAL LEU PHE PHE ASP ASN LYS ARG THR TRP GLN          
SEQRES   7 A  130  TRP LEU PRO ARG THR LYS LEU VAL PRO LEU GLY VAL ASN          
SEQRES   8 A  130  GLN ASP LEU ASP LYS GLU LYS MET LEU GLU GLY ARG LYS          
SEQRES   9 A  130  SER ASN ILE ARG LYS SER VAL GLN ILE ALA TYR HIS ARG          
SEQRES  10 A  130  ALA LEU GLN HIS ARG SER LYS VAL GLN GLY GLU GLN SER          
SEQRES   1 B   12  PRO ALA THR GLY GLY VAL M3L LYS PRO HIS ARG TYR              
MODRES 3MO8 M3L B    7  LYS  N-TRIMETHYLLYSINE                                  
HET    M3L  B   7      12                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
FORMUL   2  M3L    C9 H21 N2 O2 1+                                              
FORMUL   3  HOH   *107(H2 O)                                                    
HELIX    1   1 PRO A 1124  ALA A 1138  1                                  15    
HELIX    2   2 PRO A 1158  THR A 1160  5                                   3    
HELIX    3   3 ASN A 1168  LEU A 1177  1                                  10    
HELIX    4   4 LYS A 1181  GLY A 1204  1                                  24    
SHEET    1   A 5 TRP A1154  LEU A1157  0                                        
SHEET    2   A 5 TYR A1143  PHE A1147 -1  N  TYR A1143   O  LEU A1157           
SHEET    3   A 5 TYR A1099  ILE A1104 -1  N  ILE A1104   O  LEU A1144           
SHEET    4   A 5 LEU A1088  ALA A1091 -1  N  VAL A1089   O  ALA A1101           
SHEET    5   A 5 LEU A1162  PRO A1164 -1  O  VAL A1163   N  TRP A1090           
SHEET    1   B 2 MET A1113  HIS A1115  0                                        
SHEET    2   B 2 VAL A1118  ILE A1120 -1  O  VAL A1118   N  HIS A1115           
LINK         C   VAL B   6                 N   M3L B   7     1555   1555  1.34  
LINK         C   M3L B   7                 N   LYS B   8     1555   1555  1.33  
CRYST1   43.086   70.605  113.539  90.00  90.00  90.00 I 2 2 2       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      0.023209  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014163  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008808        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system