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Database: PDB
Entry: 4BUP
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HEADER    TRANSFERASE                             21-JUN-13   4BUP              
TITLE     A NOVEL ROUTE TO PRODUCT SPECIFICITY IN THE SUV4-20 FAMILY            
TITLE    2 OF HISTONE H4K20 METHYLTRANSFERASES                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SUV420H1;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN, RESIDUES 70-336;                               
COMPND   5 SYNONYM: SUPPRESSOR OF VARIEGATION 4-20 HOMOLOG 1, SU(VAR)4-20       
COMPND   6  HOMOLOG 1, SUV4-20H1;                                               
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: RIL;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    TRANSFERASE, EPIGENETICS, HISTONE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.SOUTHALL,N.B.CRONIN,J.R.WILSON                                    
REVDAT   2   15-JAN-14 4BUP    1       JRNL                                     
REVDAT   1   02-OCT-13 4BUP    0                                                
JRNL        AUTH   S.M.SOUTHALL,N.B.CRONIN,J.R.WILSON                           
JRNL        TITL   A NOVEL ROUTE TO PRODUCT SPECIFICITY IN THE SUV4-20 FAMILY   
JRNL        TITL 2 OF HISTONE H4K20 METHYLTRANSFERASES.                         
JRNL        REF    NUCLEIC ACIDS RES.            V.  42   661 2014              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   24049080                                                     
JRNL        DOI    10.1093/NAR/GKT776                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.166                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.640                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.91                          
REMARK   3   NUMBER OF REFLECTIONS             : 28969                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2012                          
REMARK   3   R VALUE            (WORKING SET) : 0.1980                          
REMARK   3   FREE R VALUE                     : 0.2594                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1460                            
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 46.6509 -  4.6651    0.90     2781   173  0.1970 0.2318        
REMARK   3     2  4.6651 -  3.7033    0.96     2970   149  0.1694 0.2313        
REMARK   3     3  3.7033 -  3.2353    0.85     2552   139  0.1939 0.2588        
REMARK   3     4  3.2353 -  2.9396    0.95     2832   171  0.2138 0.2597        
REMARK   3     5  2.9396 -  2.7289    0.96     2916   138  0.2127 0.2835        
REMARK   3     6  2.7289 -  2.5680    0.97     2958   134  0.2189 0.3179        
REMARK   3     7  2.5680 -  2.4394    0.84     2510   120  0.2078 0.2939        
REMARK   3     8  2.4394 -  2.3332    0.85     2572   136  0.2081 0.2693        
REMARK   3     9  2.3332 -  2.2434    0.90     2714   156  0.2099 0.3020        
REMARK   3    10  2.2434 -  2.1660    0.90     2704   144  0.2103 0.2876        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.28             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.62            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.2                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.007           3869                                  
REMARK   3   ANGLE     :  1.113           5194                                  
REMARK   3   CHIRALITY :  0.081            545                                  
REMARK   3   PLANARITY :  0.004            672                                  
REMARK   3   DIHEDRAL  : 16.880           1448                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4BUP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57392.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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 (PILATUS 2M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28977                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.60                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY                : 6.2                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.10                               
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: PDB ENTRY 4AU7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 10 % PEG 10K                 
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       25.00500            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    95                                                      
REMARK 465     ALA A    96                                                      
REMARK 465     PHE A    97                                                      
REMARK 465     PRO A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     ARG A   100                                                      
REMARK 465     SER A   101                                                      
REMARK 465     SER A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     HIS A   104                                                      
REMARK 465     ILE A   105                                                      
REMARK 465     SER A   106                                                      
REMARK 465     LYS A   107                                                      
REMARK 465     ALA A   108                                                      
REMARK 465     ASP A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     PHE A   111                                                      
REMARK 465     SER A   112                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     ASN A   114                                                      
REMARK 465     ASN A   115                                                      
REMARK 465     PRO A   116                                                      
REMARK 465     VAL A   117                                                      
REMARK 465     ARG A   118                                                      
REMARK 465     PHE A   119                                                      
REMARK 465     ARG A   120                                                      
REMARK 465     PRO A   121                                                      
REMARK 465     ILE A   122                                                      
REMARK 465     LYS A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     GLU A   153                                                      
REMARK 465     TRP A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     HIS A   157                                                      
REMARK 465     TYR A   158                                                      
REMARK 465     PHE A   159                                                      
REMARK 465     ARG A   327                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     SER B    58                                                      
REMARK 465     HIS B    59                                                      
REMARK 465     MET B    60                                                      
REMARK 465     THR B    94                                                      
REMARK 465     SER B    95                                                      
REMARK 465     ALA B    96                                                      
REMARK 465     PHE B    97                                                      
REMARK 465     PRO B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     ARG B   100                                                      
REMARK 465     SER B   101                                                      
REMARK 465     SER B   102                                                      
REMARK 465     ARG B   103                                                      
REMARK 465     HIS B   104                                                      
REMARK 465     ILE B   105                                                      
REMARK 465     SER B   106                                                      
REMARK 465     LYS B   107                                                      
REMARK 465     ALA B   108                                                      
REMARK 465     ASP B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     PHE B   111                                                      
REMARK 465     SER B   112                                                      
REMARK 465     HIS B   113                                                      
REMARK 465     ASN B   114                                                      
REMARK 465     ASN B   115                                                      
REMARK 465     PRO B   116                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     ARG B   118                                                      
REMARK 465     PHE B   119                                                      
REMARK 465     ARG B   120                                                      
REMARK 465     PRO B   121                                                      
REMARK 465     SER B   326                                                      
REMARK 465     ARG B   327                                                      
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     ARG A 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 128    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 122    CG1  CG2  CD1                                       
REMARK 470     LYS B 123    CG   CD   CE   NZ                                   
REMARK 470     ARG B 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 268    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 325    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   239     O    HOH A  2068              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLY B    63     NH2  ARG B   318     1455     2.15            
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    SER A  58       89.85   -171.61                                   
REMARK 500    SER A  61      173.52    179.76                                   
REMARK 500    THR A  89     -177.26    -62.93                                   
REMARK 500    ASN A  93     -125.28   -129.07                                   
REMARK 500    GLN A 126      -75.41    -71.93                                   
REMARK 500    GLU A 128      -90.95     65.51                                   
REMARK 500    ASN A 213       -2.54     79.89                                   
REMARK 500    PHE A 304       61.16   -104.06                                   
REMARK 500    SER B  62      -21.39     71.76                                   
REMARK 500    LYS B 123      -53.36   -142.82                                   
REMARK 500    ARG B 125       82.12     50.40                                   
REMARK 500    ASN B 213       -5.71     73.24                                   
REMARK 500    PHE B 304       59.28    -99.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 267   SG                                                     
REMARK 620 2 CYS A 311   SG  108.9                                              
REMARK 620 3 CYS A 313   SG  114.3 104.7                                        
REMARK 620 4 CYS A 316   SG  101.7 115.6 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 311   SG                                                     
REMARK 620 2 CYS B 313   SG  102.4                                              
REMARK 620 3 CYS B 267   SG  110.0 116.5                                        
REMARK 620 4 CYS B 316   SG  110.8 115.3 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1327                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4AU7   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF THE SUV4-20H2 TERNARY COMPLEX WITH                 
REMARK 900  HISTONE H4                                                          
DBREF  4BUP A   61   327  UNP    Q3U8K7   SV421_MOUSE     70    336             
DBREF  4BUP B   61   327  UNP    Q3U8K7   SV421_MOUSE     70    336             
SEQADV 4BUP GLY A   57  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP SER A   58  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP HIS A   59  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP MET A   60  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP GLY B   57  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP SER B   58  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP HIS B   59  UNP  Q3U8K7              EXPRESSION TAG                 
SEQADV 4BUP MET B   60  UNP  Q3U8K7              EXPRESSION TAG                 
SEQRES   1 A  271  GLY SER HIS MET SER SER GLY MET SER ALA LYS GLU LEU          
SEQRES   2 A  271  CYS GLU ASN ASP ASP LEU ALA THR SER LEU VAL LEU ASP          
SEQRES   3 A  271  PRO TYR LEU GLY PHE GLN THR HIS LYS MET ASN THR SER          
SEQRES   4 A  271  ALA PHE PRO SER ARG SER SER ARG HIS ILE SER LYS ALA          
SEQRES   5 A  271  ASP SER PHE SER HIS ASN ASN PRO VAL ARG PHE ARG PRO          
SEQRES   6 A  271  ILE LYS GLY ARG GLN GLU GLU LEU LYS GLU VAL ILE GLU          
SEQRES   7 A  271  ARG PHE LYS LYS ASP GLU HIS LEU GLU LYS ALA PHE LYS          
SEQRES   8 A  271  CYS LEU THR SER GLY GLU TRP ALA ARG HIS TYR PHE LEU          
SEQRES   9 A  271  ASN LYS ASN LYS MET GLN GLU LYS LEU PHE LYS GLU HIS          
SEQRES  10 A  271  VAL PHE ILE TYR LEU ARG MET PHE ALA THR ASP SER GLY          
SEQRES  11 A  271  PHE GLU ILE LEU PRO CYS ASN ARG TYR SER SER GLU GLN          
SEQRES  12 A  271  ASN GLY ALA LYS ILE VAL ALA THR LYS GLU TRP LYS ARG          
SEQRES  13 A  271  ASN ASP LYS ILE GLU LEU LEU VAL GLY CYS ILE ALA GLU          
SEQRES  14 A  271  LEU SER GLU ILE GLU GLU ASN MET LEU LEU ARG HIS GLY          
SEQRES  15 A  271  GLU ASN ASP PHE SER VAL MET TYR SER THR ARG LYS ASN          
SEQRES  16 A  271  CYS ALA GLN LEU TRP LEU GLY PRO ALA ALA PHE ILE ASN          
SEQRES  17 A  271  HIS ASP CYS ARG PRO ASN CYS LYS PHE VAL SER THR GLY          
SEQRES  18 A  271  ARG ASP THR ALA CYS VAL LYS ALA LEU ARG ASP ILE GLU          
SEQRES  19 A  271  PRO GLY GLU GLU ILE SER CYS TYR TYR GLY ASP GLY PHE          
SEQRES  20 A  271  PHE GLY GLU ASN ASN GLU PHE CYS GLU CYS TYR THR CYS          
SEQRES  21 A  271  GLU ARG ARG GLY THR GLY ALA PHE LYS SER ARG                  
SEQRES   1 B  271  GLY SER HIS MET SER SER GLY MET SER ALA LYS GLU LEU          
SEQRES   2 B  271  CYS GLU ASN ASP ASP LEU ALA THR SER LEU VAL LEU ASP          
SEQRES   3 B  271  PRO TYR LEU GLY PHE GLN THR HIS LYS MET ASN THR SER          
SEQRES   4 B  271  ALA PHE PRO SER ARG SER SER ARG HIS ILE SER LYS ALA          
SEQRES   5 B  271  ASP SER PHE SER HIS ASN ASN PRO VAL ARG PHE ARG PRO          
SEQRES   6 B  271  ILE LYS GLY ARG GLN GLU GLU LEU LYS GLU VAL ILE GLU          
SEQRES   7 B  271  ARG PHE LYS LYS ASP GLU HIS LEU GLU LYS ALA PHE LYS          
SEQRES   8 B  271  CYS LEU THR SER GLY GLU TRP ALA ARG HIS TYR PHE LEU          
SEQRES   9 B  271  ASN LYS ASN LYS MET GLN GLU LYS LEU PHE LYS GLU HIS          
SEQRES  10 B  271  VAL PHE ILE TYR LEU ARG MET PHE ALA THR ASP SER GLY          
SEQRES  11 B  271  PHE GLU ILE LEU PRO CYS ASN ARG TYR SER SER GLU GLN          
SEQRES  12 B  271  ASN GLY ALA LYS ILE VAL ALA THR LYS GLU TRP LYS ARG          
SEQRES  13 B  271  ASN ASP LYS ILE GLU LEU LEU VAL GLY CYS ILE ALA GLU          
SEQRES  14 B  271  LEU SER GLU ILE GLU GLU ASN MET LEU LEU ARG HIS GLY          
SEQRES  15 B  271  GLU ASN ASP PHE SER VAL MET TYR SER THR ARG LYS ASN          
SEQRES  16 B  271  CYS ALA GLN LEU TRP LEU GLY PRO ALA ALA PHE ILE ASN          
SEQRES  17 B  271  HIS ASP CYS ARG PRO ASN CYS LYS PHE VAL SER THR GLY          
SEQRES  18 B  271  ARG ASP THR ALA CYS VAL LYS ALA LEU ARG ASP ILE GLU          
SEQRES  19 B  271  PRO GLY GLU GLU ILE SER CYS TYR TYR GLY ASP GLY PHE          
SEQRES  20 B  271  PHE GLY GLU ASN ASN GLU PHE CYS GLU CYS TYR THR CYS          
SEQRES  21 B  271  GLU ARG ARG GLY THR GLY ALA PHE LYS SER ARG                  
HET     ZN  A 400       1                                                       
HET    SAM  A 500      27                                                       
HET     ZN  B 400       1                                                       
HET    SAM  B 500      27                                                       
HET    GOL  A1327       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  HOH   *198(H2 O)                                                    
HELIX    1   1 SER A   65  LEU A   81  1                                  17    
HELIX    2   2 LEU A   81  GLY A   86  1                                   6    
HELIX    3   3 GLU A  128  GLU A  140  1                                  13    
HELIX    4   4 HIS A  141  THR A  150  1                                  10    
HELIX    5   5 ASN A  163  ARG A  179  1                                  17    
HELIX    6   6 MET A  180  ALA A  182  5                                   3    
HELIX    7   7 SER A  227  LEU A  235  1                                   9    
HELIX    8   8 GLY A  258  ILE A  263  5                                   6    
HELIX    9   9 GLY A  305  GLU A  309  5                                   5    
HELIX   10  10 CYS A  313  GLY A  320  1                                   8    
HELIX   11  11 THR A  321  LYS A  325  5                                   5    
HELIX   12  12 SER B   65  LEU B   81  1                                  17    
HELIX   13  13 LEU B   81  GLY B   86  1                                   6    
HELIX   14  14 ARG B  125  GLU B  140  1                                  16    
HELIX   15  15 HIS B  141  THR B  150  1                                  10    
HELIX   16  16 GLY B  152  PHE B  159  1                                   8    
HELIX   17  17 LEU B  160  LYS B  162  5                                   3    
HELIX   18  18 ASN B  163  ARG B  179  1                                  17    
HELIX   19  19 MET B  180  ALA B  182  5                                   3    
HELIX   20  20 SER B  227  LEU B  235  1                                   9    
HELIX   21  21 GLY B  258  ILE B  263  5                                   6    
HELIX   22  22 GLY B  305  GLU B  309  5                                   5    
HELIX   23  23 CYS B  313  GLY B  320  1                                   8    
HELIX   24  24 THR B  321  LYS B  325  5                                   5    
SHEET    1  AA 2 PHE A 187  CYS A 192  0                                        
SHEET    2  AA 2 GLY A 201  ALA A 206 -1  O  GLY A 201   N  CYS A 192           
SHEET    1  AB 5 VAL A 244  SER A 247  0                                        
SHEET    2  AB 5 CYS A 252  LEU A 257 -1  O  CYS A 252   N  SER A 247           
SHEET    3  AB 5 LYS A 215  LEU A 226 -1  O  CYS A 222   N  LEU A 257           
SHEET    4  AB 5 THR A 280  ALA A 285 -1  O  ALA A 281   N  GLY A 221           
SHEET    5  AB 5 CYS A 271  SER A 275 -1  O  LYS A 272   N  LYS A 284           
SHEET    1  AC 2 ASN A 264  HIS A 265  0                                        
SHEET    2  AC 2 SER A 296  CYS A 297  1  N  CYS A 297   O  ASN A 264           
SHEET    1  BA 2 PHE B 187  CYS B 192  0                                        
SHEET    2  BA 2 GLY B 201  ALA B 206 -1  O  GLY B 201   N  CYS B 192           
SHEET    1  BB 5 VAL B 244  SER B 247  0                                        
SHEET    2  BB 5 CYS B 252  LEU B 257 -1  O  CYS B 252   N  SER B 247           
SHEET    3  BB 5 LYS B 215  LEU B 226 -1  O  CYS B 222   N  LEU B 257           
SHEET    4  BB 5 THR B 280  ALA B 285 -1  O  ALA B 281   N  GLY B 221           
SHEET    5  BB 5 CYS B 271  SER B 275 -1  O  LYS B 272   N  LYS B 284           
SHEET    1  BC 2 ASN B 264  HIS B 265  0                                        
SHEET    2  BC 2 SER B 296  CYS B 297  1  N  CYS B 297   O  ASN B 264           
LINK        ZN    ZN A 400                 SG  CYS A 267     1555   1555  2.36  
LINK        ZN    ZN A 400                 SG  CYS A 311     1555   1555  2.35  
LINK        ZN    ZN A 400                 SG  CYS A 313     1555   1555  2.27  
LINK        ZN    ZN A 400                 SG  CYS A 316     1555   1555  2.37  
LINK        ZN    ZN B 400                 SG  CYS B 313     1555   1555  2.15  
LINK        ZN    ZN B 400                 SG  CYS B 267     1555   1555  2.35  
LINK        ZN    ZN B 400                 SG  CYS B 316     1555   1555  2.56  
LINK        ZN    ZN B 400                 SG  CYS B 311     1555   1555  2.42  
CISPEP   1 SER A   61    SER A   62          0        -1.67                     
CISPEP   2 GLU A  127    GLU A  128          0        -1.10                     
SITE     1 AC1  4 CYS A 267  CYS A 311  CYS A 313  CYS A 316                    
SITE     1 AC2 18 HIS A  90  TYR A 195  SER A 197  GLU A 198                    
SITE     2 AC2 18 GLY A 201  ALA A 202  PHE A 242  ALA A 261                    
SITE     3 AC2 18 ILE A 263  ASN A 264  HIS A 265  TYR A 299                    
SITE     4 AC2 18 PHE A 304  CYS A 311  GLU A 312  GOL A1327                    
SITE     5 AC2 18 HOH A2019  HOH A2050                                          
SITE     1 AC3  4 CYS B 267  CYS B 311  CYS B 313  CYS B 316                    
SITE     1 AC4 17 HIS B  90  TYR B 195  SER B 197  GLU B 198                    
SITE     2 AC4 17 GLY B 201  ALA B 202  PHE B 242  ALA B 261                    
SITE     3 AC4 17 ILE B 263  ASN B 264  HIS B 265  TYR B 299                    
SITE     4 AC4 17 PHE B 304  CYS B 311  GLU B 312  CYS B 313                    
SITE     5 AC4 17 HOH B2014                                                     
SITE     1 AC5  9 SER A 243  MET A 245  TRP A 256  ALA A 260                    
SITE     2 AC5  9 ALA A 261  ILE A 263  PHE A 273  SAM A 500                    
SITE     3 AC5  9 HOH A2095                                                     
CRYST1   46.310   50.010  129.400  90.00  92.82  90.00 P 1 21 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      0.021594  0.000000  0.001064        0.00000                         
SCALE2      0.000000  0.019996  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007737        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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