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Database: PDB
Entry: 3F9W
LinkDB: 3F9W
Original site: 3F9W 
HEADER    TRANSFERASE                             14-NOV-08   3F9W              
TITLE     STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN    
TITLE    2 METHYLTRANSFERASES, SET8-Y334F / H4-LYS20 / ADOHCY                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD8;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: SET DOMAIN: UNP RESIDUES 232-393;                          
COMPND   5 SYNONYM: H4-K20-HMTASE SETD8, SET DOMAIN-CONTAINING PROTEIN 8, PR/SET
COMPND   6 DOMAIN-CONTAINING PROTEIN 07, PR/SET07, PR-SET7, LYSINE N-           
COMPND   7 METHYLTRANSFERASE 5A;                                                
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: HISTONE H4;                                                
COMPND  13 CHAIN: E, F, G, H;                                                   
COMPND  14 FRAGMENT: UNP RESIDUES 16-25;                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: SETD8, KMT5A, PRSET7, SET07, SET8;                             
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PARALLEL;                                  
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHIS2;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: SYNTHETIC PEPTIDE CORRESPONDING TO RESIDUES 16-25 OF  
SOURCE  13 HUMAN HISTONE H4                                                     
KEYWDS    METHYLTRANSFERASE, HISTONE, SET, LYSINE, ALTERNATIVE SPLICING, CELL   
KEYWDS   2 CYCLE, CELL DIVISION, CHROMATIN REGULATOR, CHROMOSOMAL PROTEIN,      
KEYWDS   3 COILED COIL, MITOSIS, NUCLEUS, REPRESSOR, S-ADENOSYL-L-METHIONINE,   
KEYWDS   4 TRANSCRIPTION, TRANSCRIPTION REGULATION, ACETYLATION, DNA-BINDING,   
KEYWDS   5 METHYLATION, NUCLEOSOME CORE, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-F.COUTURE,L.M.A.DIRK,J.S.BRUNZELLE,R.L.HOUTZ,R.C.TRIEVEL           
REVDAT   5   24-JAN-18 3F9W    1       AUTHOR                                   
REVDAT   4   09-JUN-09 3F9W    1       REVDAT                                   
REVDAT   3   24-FEB-09 3F9W    1       VERSN                                    
REVDAT   2   13-JAN-09 3F9W    1       JRNL                                     
REVDAT   1   25-NOV-08 3F9W    0                                                
JRNL        AUTH   J.F.COUTURE,L.M.DIRK,J.S.BRUNZELLE,R.L.HOUTZ,R.C.TRIEVEL     
JRNL        TITL   STRUCTURAL ORIGINS FOR THE PRODUCT SPECIFICITY OF SET DOMAIN 
JRNL        TITL 2 PROTEIN METHYLTRANSFERASES.                                  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 20659 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19088188                                                     
JRNL        DOI    10.1073/PNAS.0806712105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 87774                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4620                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6329                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1510                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 333                          
REMARK   3   BIN FREE R VALUE                    : 0.2220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5423                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 1022                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.01000                                              
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): 0.126         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.146         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5630 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7555 ; 1.254 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   667 ; 5.951 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   275 ;26.842 ;23.309       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1053 ;11.798 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;16.671 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   807 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4216 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2613 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3801 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   867 ; 0.130 ; 0.200       
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):   100 ; 0.158 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    97 ; 0.124 ; 0.200       
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):  3469 ; 1.029 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5357 ; 1.623 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2465 ; 2.532 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2198 ; 3.452 ; 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):  5934 ; 1.832 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  1022 ; 4.229 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5534 ; 2.606 ; 3.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3F9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050329.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91908                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.02700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.14600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.60                              
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 1ZKK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PENTAERYTHRITOL ETHOXYLATE, 50MM     
REMARK 280  AMMONIUM SULFATE, 50MM BIS-TRIS, PH 6.5, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9450 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.7 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9640 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.6 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9650 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9680 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   187                                                      
REMARK 465     ALA A   188                                                      
REMARK 465     MET A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     ARG A   192                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     ALA B   188                                                      
REMARK 465     MET B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     SER B   191                                                      
REMARK 465     ARG B   192                                                      
REMARK 465     GLY C   187                                                      
REMARK 465     ALA C   188                                                      
REMARK 465     MET C   189                                                      
REMARK 465     GLY C   190                                                      
REMARK 465     SER C   191                                                      
REMARK 465     ARG C   192                                                      
REMARK 465     GLY D   187                                                      
REMARK 465     ALA D   188                                                      
REMARK 465     MET D   189                                                      
REMARK 465     GLY D   190                                                      
REMARK 465     SER D   191                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     ALA F    15                                                      
REMARK 465     ASP F    24                                                      
REMARK 465     ALA G    15                                                      
REMARK 465     ALA H    15                                                      
REMARK 465     ASP H    24                                                      
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 D 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  16    CG   CD   CE   NZ                                   
REMARK 470     LYS F  16    CG   CD   CE   NZ                                   
REMARK 470     LYS G  16    CG   CD   CE   NZ                                   
REMARK 470     LYS H  16    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   O    HOH A   542     O    HOH C  1012              2.03            
REMARK 500   OE1  GLN A   276     OG1  THR A   281              2.19            
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    VAL A 242      -62.22   -106.05                                   
REMARK 500    VAL B 242      -60.08   -104.71                                   
REMARK 500    LEU B 278     -126.11     56.55                                   
REMARK 500    VAL C 242      -62.49   -104.53                                   
REMARK 500    ALA D 286       34.38    -98.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZKK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HSET8 IN TERNARY COMPLEX WITH H4 PEPTIDE (16-   
REMARK 900 24) AND ADOHCY                                                       
REMARK 900 RELATED ID: 3F9X   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN   
REMARK 900 METHYLTRANSFERASES, SET8-Y334F / H4-LYS20ME2 / ADOHCY                
REMARK 900 RELATED ID: 3F9Y   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN   
REMARK 900 METHYLTRANSFERASES, SET8-Y334F / H4-LYS20ME1 / ADOHCY                
REMARK 900 RELATED ID: 3F9Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN   
REMARK 900 METHYLTRANSFERASES, SET8-Y245F / H4-LYS20 / ADOHCY                   
DBREF  3F9W A  191   352  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  3F9W B  191   352  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  3F9W C  191   352  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  3F9W D  191   352  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  3F9W E   15    24  UNP    P62805   H4_HUMAN        16     25             
DBREF  3F9W F   15    24  UNP    P62805   H4_HUMAN        16     25             
DBREF  3F9W G   15    24  UNP    P62805   H4_HUMAN        16     25             
DBREF  3F9W H   15    24  UNP    P62805   H4_HUMAN        16     25             
SEQADV 3F9W GLY A  187  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W ALA A  188  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W MET A  189  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W GLY A  190  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W PHE A  334  UNP  Q9NQR1    TYR   375 ENGINEERED                     
SEQADV 3F9W GLY B  187  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W ALA B  188  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W MET B  189  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W GLY B  190  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W PHE B  334  UNP  Q9NQR1    TYR   375 ENGINEERED                     
SEQADV 3F9W GLY C  187  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W ALA C  188  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W MET C  189  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W GLY C  190  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W PHE C  334  UNP  Q9NQR1    TYR   375 ENGINEERED                     
SEQADV 3F9W GLY D  187  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W ALA D  188  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W MET D  189  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W GLY D  190  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9W PHE D  334  UNP  Q9NQR1    TYR   375 ENGINEERED                     
SEQRES   1 A  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 A  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 A  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 A  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 A  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 A  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 A  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 A  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 A  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS GLY          
SEQRES  10 A  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 A  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 A  166  GLU GLU LEU LEU PHE ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 A  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 B  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 B  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 B  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 B  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 B  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 B  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 B  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 B  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 B  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS GLY          
SEQRES  10 B  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 B  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 B  166  GLU GLU LEU LEU PHE ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 B  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 C  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 C  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 C  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 C  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 C  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 C  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 C  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 C  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 C  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS GLY          
SEQRES  10 C  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 C  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 C  166  GLU GLU LEU LEU PHE ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 C  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 D  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 D  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 D  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 D  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 D  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 D  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 D  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 D  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 D  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS GLY          
SEQRES  10 D  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 D  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 D  166  GLU GLU LEU LEU PHE ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 D  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 E   10  ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP                      
SEQRES   1 F   10  ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP                      
SEQRES   1 G   10  ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP                      
SEQRES   1 H   10  ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP                      
HET    SAH  A 801      26                                                       
HET    SAH  B 801      26                                                       
HET    SAH  C 801      26                                                       
HET    SAH  D 801      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   9  SAH    4(C14 H20 N6 O5 S)                                           
FORMUL  13  HOH   *1022(H2 O)                                                   
HELIX    1   1 SER A  194  GLY A  213  1                                  20    
HELIX    2   2 ILE A  252  ALA A  263  1                                  12    
HELIX    3   3 LEU A  293  ILE A  297  5                                   5    
HELIX    4   4 SER A  340  HIS A  347  1                                   8    
HELIX    5   5 PRO A  348  HIS A  352  5                                   5    
HELIX    6   6 SER B  194  GLY B  213  1                                  20    
HELIX    7   7 ILE B  252  ALA B  263  1                                  12    
HELIX    8   8 LEU B  293  ILE B  297  5                                   5    
HELIX    9   9 SER B  340  HIS B  347  1                                   8    
HELIX   10  10 PRO B  348  HIS B  352  5                                   5    
HELIX   11  11 SER C  194  GLY C  213  1                                  20    
HELIX   12  12 ILE C  252  ALA C  263  1                                  12    
HELIX   13  13 LEU C  293  ILE C  297  5                                   5    
HELIX   14  14 SER C  340  HIS C  347  1                                   8    
HELIX   15  15 PRO C  348  HIS C  352  5                                   5    
HELIX   16  16 SER D  194  GLY D  213  1                                  20    
HELIX   17  17 ILE D  252  ALA D  263  1                                  12    
HELIX   18  18 LEU D  293  ILE D  297  5                                   5    
HELIX   19  19 SER D  340  HIS D  347  1                                   8    
HELIX   20  20 PRO D  348  HIS D  352  5                                   5    
SHEET    1   A 2 MET A 218  ILE A 223  0                                        
SHEET    2   A 2 GLY A 227  ALA A 232 -1  O  ILE A 231   N  LYS A 219           
SHEET    1   B 3 PHE A 241  TYR A 245  0                                        
SHEET    2   B 3 VAL A 315  ALA A 322 -1  O  LEU A 320   N  VAL A 243           
SHEET    3   B 3 CYS A 305  ILE A 312 -1  N  HIS A 310   O  HIS A 317           
SHEET    1   C 4 ASP A 248  GLU A 251  0                                        
SHEET    2   C 4 LYS A 280  ASP A 285 -1  O  ASP A 285   N  ASP A 248           
SHEET    3   C 4 MET A 272  TYR A 277 -1  N  PHE A 275   O  TYR A 282           
SHEET    4   C 4 LYS F  20  VAL F  21  1  O  LYS F  20   N  TYR A 274           
SHEET    1   D 2 ASN A 298  HIS A 299  0                                        
SHEET    2   D 2 LEU A 333  PHE A 334  1  O  PHE A 334   N  ASN A 298           
SHEET    1   E 2 MET B 218  ILE B 223  0                                        
SHEET    2   E 2 GLY B 227  ALA B 232 -1  O  ILE B 231   N  LYS B 219           
SHEET    1   F 3 PHE B 241  GLU B 244  0                                        
SHEET    2   F 3 VAL B 315  ALA B 322 -1  O  LEU B 320   N  VAL B 243           
SHEET    3   F 3 CYS B 305  ILE B 312 -1  N  LYS B 308   O  ILE B 319           
SHEET    1   G 4 ASP B 248  GLU B 251  0                                        
SHEET    2   G 4 LYS B 280  ASP B 285 -1  O  ASP B 285   N  ASP B 248           
SHEET    3   G 4 MET B 272  TYR B 277 -1  N  TYR B 277   O  LYS B 280           
SHEET    4   G 4 LYS E  20  VAL E  21  1  O  LYS E  20   N  TYR B 274           
SHEET    1   H 2 ASN B 298  HIS B 299  0                                        
SHEET    2   H 2 LEU B 333  PHE B 334  1  O  PHE B 334   N  ASN B 298           
SHEET    1   I 2 MET C 218  ILE C 223  0                                        
SHEET    2   I 2 GLY C 227  ALA C 232 -1  O  ILE C 231   N  LYS C 219           
SHEET    1   J 3 PHE C 241  GLU C 244  0                                        
SHEET    2   J 3 VAL C 315  ALA C 322 -1  O  LEU C 320   N  VAL C 243           
SHEET    3   J 3 CYS C 305  ILE C 312 -1  N  HIS C 310   O  HIS C 317           
SHEET    1   K 4 ASP C 248  GLU C 251  0                                        
SHEET    2   K 4 LYS C 280  ASP C 285 -1  O  ASP C 285   N  ASP C 248           
SHEET    3   K 4 MET C 272  TYR C 277 -1  N  PHE C 275   O  TYR C 282           
SHEET    4   K 4 LYS G  20  VAL G  21  1  O  LYS G  20   N  TYR C 274           
SHEET    1   L 2 ASN C 298  HIS C 299  0                                        
SHEET    2   L 2 LEU C 333  PHE C 334  1  O  PHE C 334   N  ASN C 298           
SHEET    1   M 2 MET D 218  ILE D 223  0                                        
SHEET    2   M 2 GLY D 227  ALA D 232 -1  O  ILE D 231   N  LYS D 219           
SHEET    1   N 3 PHE D 241  TYR D 245  0                                        
SHEET    2   N 3 VAL D 315  ALA D 322 -1  O  LEU D 318   N  TYR D 245           
SHEET    3   N 3 CYS D 305  ILE D 312 -1  N  HIS D 310   O  HIS D 317           
SHEET    1   O 4 ASP D 248  GLU D 251  0                                        
SHEET    2   O 4 LYS D 280  ASP D 285 -1  O  ASP D 285   N  ASP D 248           
SHEET    3   O 4 MET D 272  TYR D 277 -1  N  PHE D 275   O  TYR D 282           
SHEET    4   O 4 LYS H  20  VAL H  21  1  O  LYS H  20   N  TYR D 274           
SHEET    1   P 2 ASN D 298  HIS D 299  0                                        
SHEET    2   P 2 LEU D 333  PHE D 334  1  O  PHE D 334   N  ASN D 298           
SITE     1 AC1 20 HOH A 100  HOH A 108  HOH A 148  HOH A 154                    
SITE     2 AC1 20 GLY A 225  LYS A 226  ARG A 228  CYS A 270                    
SITE     3 AC1 20 TYR A 271  ARG A 295  LEU A 296  ASN A 298                    
SITE     4 AC1 20 HIS A 299  TYR A 336  TRP A 349  HOH A 364                    
SITE     5 AC1 20 HOH A 387  HOH A 432  HIS F  18  LYS F  20                    
SITE     1 AC2 18 HOH B  76  GLY B 225  LYS B 226  ARG B 228                    
SITE     2 AC2 18 CYS B 270  TYR B 271  ARG B 295  LEU B 296                    
SITE     3 AC2 18 ASN B 298  HIS B 299  TYR B 336  TRP B 349                    
SITE     4 AC2 18 HOH B 364  HOH B 371  HOH B 382  HOH B 389                    
SITE     5 AC2 18 HIS E  18  LYS E  20                                          
SITE     1 AC3 19 HOH C 149  HOH C 171  GLY C 225  LYS C 226                    
SITE     2 AC3 19 ARG C 228  CYS C 270  TYR C 271  ARG C 295                    
SITE     3 AC3 19 LEU C 296  ASN C 298  HIS C 299  TYR C 336                    
SITE     4 AC3 19 TRP C 349  HOH C 377  HOH C 378  HOH C 408                    
SITE     5 AC3 19 HOH C 412  HIS G  18  LYS G  20                               
SITE     1 AC4 20 HOH B  26  HOH D  47  HOH D  55  GLY D 225                    
SITE     2 AC4 20 LYS D 226  ARG D 228  CYS D 270  TYR D 271                    
SITE     3 AC4 20 ARG D 295  LEU D 296  ASN D 298  HIS D 299                    
SITE     4 AC4 20 TYR D 336  TRP D 349  HOH D 380  HOH D 413                    
SITE     5 AC4 20 HOH D 576  ARG E  23  HIS H  18  LYS H  20                    
CRYST1   44.000   45.600   94.200  89.20  87.10  90.80 P 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      0.022727  0.000317 -0.001156        0.00000                         
SCALE2      0.000000  0.021932 -0.000322        0.00000                         
SCALE3      0.000000  0.000000  0.010630        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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