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Database: PDB
Entry: 1ZKK
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HEADER    TRANSFERASE                             03-MAY-05   1ZKK              
TITLE     CRYSTAL STRUCTURE OF HSET8 IN TERNARY COMPLEX WITH H4 PEPTIDE (16-24) 
TITLE    2 AND ADOHCY                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H4 LYSINE-20 SPECIFIC; 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 231-393;                        
COMPND   5 SYNONYM: HISTONE H4-K20 METHYLTRANSFERASE, H4-K20-HMTASE, SET DOMAIN-
COMPND   6 CONTAINING PROTEIN 8, PR/SET DOMAIN-CONTAINING PROTEIN 07, PR/SET07, 
COMPND   7 PR-SET7, SET8;                                                       
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: PEPTIDE CORRESPONDING TO RESIDUES 15-24 OF HISTONE H4;     
COMPND  12 CHAIN: E, F, G, H;                                                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SET8, PRSET7, SET07;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21-DE3PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS2;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: CHAIN E, F, G, H ARE SYNTHETIC PEPTIDE FROM NEW       
SOURCE  14 ENGLAND PEPTIDE CORRESPONDING TO RESIDUE 15-24 OF THE HISTONE H4     
KEYWDS    PSEUDO-KNOT, HISTONE H4, BETA-SHEET, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-F.COUTURE,E.COLLAZO,J.S.BRUNZELLE,R.C.TRIEVEL                      
REVDAT   4   11-OCT-17 1ZKK    1       REMARK                                   
REVDAT   3   24-FEB-09 1ZKK    1       VERSN                                    
REVDAT   2   05-JUL-05 1ZKK    1       JRNL                                     
REVDAT   1   07-JUN-05 1ZKK    0                                                
JRNL        AUTH   J.-F.COUTURE,E.COLLAZO,J.S.BRUNZELLE,R.C.TRIEVEL             
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSIS OF SET8, A HISTONE H4     
JRNL        TITL 2 LYS-20 METHYLTRANSFERASE                                     
JRNL        REF    GENES DEV.                    V.  19  1455 2005              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   15933070                                                     
JRNL        DOI    10.1101/GAD.1318405                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 117760                         
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6198                            
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8436                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 444                          
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5424                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 1007                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.04000                                              
REMARK   3    B12 (A**2) : 0.03000                                              
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): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.069         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.038         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.134         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5632 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7554 ; 1.278 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   668 ; 6.092 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   276 ;27.573 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1054 ;11.594 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;15.900 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   806 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4196 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2548 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3806 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   835 ; 0.115 ; 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):    85 ; 0.165 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    91 ; 0.096 ; 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):  3470 ; 0.986 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5344 ; 1.518 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2478 ; 2.162 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2210 ; 3.174 ; 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):  5948 ; 1.228 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  1008 ; 4.016 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5536 ; 2.540 ; 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000032824.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-04                          
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                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686, 0.9792, 0.9791             
REMARK 200  MONOCHROMATOR                  : DIAMOND 111                        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122425                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 32.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 34.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD, MOLECULAR REPLACEMENT   
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PENTAERYTHRITOL ETHOXYLATE, AMMONIUM     
REMARK 280  SULFATE, BIS-TRIS, PH 6.5, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 277K                                                    
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                                                       
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   186                                                      
REMARK 465     ALA A   187                                                      
REMARK 465     MET A   188                                                      
REMARK 465     GLY A   189                                                      
REMARK 465     SER A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     ARG A   192                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     ALA B   187                                                      
REMARK 465     MET B   188                                                      
REMARK 465     GLY B   189                                                      
REMARK 465     SER B   190                                                      
REMARK 465     SER B   191                                                      
REMARK 465     GLY C   186                                                      
REMARK 465     ALA C   187                                                      
REMARK 465     MET C   188                                                      
REMARK 465     GLY C   189                                                      
REMARK 465     SER C   190                                                      
REMARK 465     SER C   191                                                      
REMARK 465     ARG C   192                                                      
REMARK 465     GLY D   186                                                      
REMARK 465     ALA D   187                                                      
REMARK 465     MET D   188                                                      
REMARK 465     GLY D   189                                                      
REMARK 465     SER D   190                                                      
REMARK 465     SER D   191                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     ASP E    24                                                      
REMARK 465     ALA F    15                                                      
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 B 192    CG   CD   NE   CZ   NH1  NH2                        
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    CB   CG   CD   CE   NZ                              
REMARK 470     LYS G  16    CG   CD   CE   NZ                                   
REMARK 470     LYS H  16    CB   CG   CD   CE   NZ                              
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER A  200   OG                                                  
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   C    HIS A   352     O    HOH A  3006              1.68            
REMARK 500   O    HOH A  3014     O    HOH C  2935              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 302   CB    CYS A 302   SG      1.459                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 302   CA  -  CB  -  SG  ANGL. DEV. =  16.3 DEGREES          
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 B 242      -60.66   -104.14                                   
REMARK 500    LEU B 278     -122.21     53.96                                   
REMARK 500    VAL C 242      -63.79   -105.40                                   
REMARK 500    ALA D 286       31.78    -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 2800                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 2801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 2802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 2803                
DBREF  1ZKK A  190   352  UNP    Q9NQR1   SET07_HUMAN    231    393             
DBREF  1ZKK B  190   352  UNP    Q9NQR1   SET07_HUMAN    231    393             
DBREF  1ZKK C  190   352  UNP    Q9NQR1   SET07_HUMAN    231    393             
DBREF  1ZKK D  190   352  UNP    Q9NQR1   SET07_HUMAN    231    393             
DBREF  1ZKK E   15    24  PDB    1ZKK     1ZKK            15     24             
DBREF  1ZKK F   15    24  PDB    1ZKK     1ZKK            15     24             
DBREF  1ZKK G   15    24  PDB    1ZKK     1ZKK            15     24             
DBREF  1ZKK H   15    24  PDB    1ZKK     1ZKK            15     24             
SEQADV 1ZKK GLY A  186  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK ALA A  187  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK MET A  188  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY A  189  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY B  186  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK ALA B  187  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK MET B  188  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY B  189  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY C  186  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK ALA C  187  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK MET C  188  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY C  189  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY D  186  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK ALA D  187  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK MET D  188  UNP  Q9NQR1              CLONING ARTIFACT               
SEQADV 1ZKK GLY D  189  UNP  Q9NQR1              CLONING ARTIFACT               
SEQRES   1 A  167  GLY ALA MET GLY SER SER ARG LYS SER LYS ALA GLU LEU          
SEQRES   2 A  167  GLN SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU          
SEQRES   3 A  167  SER GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP          
SEQRES   4 A  167  GLY LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER          
SEQRES   5 A  167  ARG GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE          
SEQRES   6 A  167  GLU ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA          
SEQRES   7 A  167  GLN ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN          
SEQRES   8 A  167  TYR LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU          
SEQRES   9 A  167  THR ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS          
SEQRES  10 A  167  GLY ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL          
SEQRES  11 A  167  PRO HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA          
SEQRES  12 A  167  GLY GLU GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS          
SEQRES  13 A  167  ALA SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                  
SEQRES   1 B  167  GLY ALA MET GLY SER SER ARG LYS SER LYS ALA GLU LEU          
SEQRES   2 B  167  GLN SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU          
SEQRES   3 B  167  SER GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP          
SEQRES   4 B  167  GLY LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER          
SEQRES   5 B  167  ARG GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE          
SEQRES   6 B  167  GLU ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA          
SEQRES   7 B  167  GLN ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN          
SEQRES   8 B  167  TYR LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU          
SEQRES   9 B  167  THR ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS          
SEQRES  10 B  167  GLY ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL          
SEQRES  11 B  167  PRO HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA          
SEQRES  12 B  167  GLY GLU GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS          
SEQRES  13 B  167  ALA SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                  
SEQRES   1 C  167  GLY ALA MET GLY SER SER ARG LYS SER LYS ALA GLU LEU          
SEQRES   2 C  167  GLN SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU          
SEQRES   3 C  167  SER GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP          
SEQRES   4 C  167  GLY LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER          
SEQRES   5 C  167  ARG GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE          
SEQRES   6 C  167  GLU ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA          
SEQRES   7 C  167  GLN ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN          
SEQRES   8 C  167  TYR LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU          
SEQRES   9 C  167  THR ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS          
SEQRES  10 C  167  GLY ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL          
SEQRES  11 C  167  PRO HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA          
SEQRES  12 C  167  GLY GLU GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS          
SEQRES  13 C  167  ALA SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                  
SEQRES   1 D  167  GLY ALA MET GLY SER SER ARG LYS SER LYS ALA GLU LEU          
SEQRES   2 D  167  GLN SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU          
SEQRES   3 D  167  SER GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP          
SEQRES   4 D  167  GLY LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER          
SEQRES   5 D  167  ARG GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE          
SEQRES   6 D  167  GLU ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA          
SEQRES   7 D  167  GLN ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN          
SEQRES   8 D  167  TYR LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU          
SEQRES   9 D  167  THR ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS          
SEQRES  10 D  167  GLY ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL          
SEQRES  11 D  167  PRO HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA          
SEQRES  12 D  167  GLY GLU GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS          
SEQRES  13 D  167  ALA 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  A2800      26                                                       
HET    SAH  B2801      26                                                       
HET    SAH  C2802      26                                                       
HET    SAH  D2803      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   9  SAH    4(C14 H20 N6 O5 S)                                           
FORMUL  13  HOH   *1007(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 E  20  VAL E  21  1  O  LYS E  20   N  TYR A 274           
SHEET    1   D 2 ASN A 298  HIS A 299  0                                        
SHEET    2   D 2 LEU A 333  TYR A 334  1  O  TYR 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  PHE B 275   O  TYR B 282           
SHEET    4   G 4 LYS F  20  VAL F  21  1  O  LYS F  20   N  TYR B 274           
SHEET    1   H 2 ASN B 298  HIS B 299  0                                        
SHEET    2   H 2 LEU B 333  TYR B 334  1  O  TYR 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  TYR C 334  1  O  TYR 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  TYR D 334  1  O  TYR D 334   N  ASN D 298           
SITE     1 AC1 20 GLY A 225  LYS A 226  ARG A 228  CYS A 270                    
SITE     2 AC1 20 TYR A 271  ARG A 295  LEU A 296  ASN A 298                    
SITE     3 AC1 20 HIS A 299  TYR A 336  TRP A 349  HOH A2829                    
SITE     4 AC1 20 HOH A2835  HOH A2863  HOH A2879  HOH A2901                    
SITE     5 AC1 20 HOH A2906  HIS E  18  LYS E  20  HOH G 186                    
SITE     1 AC2 19 GLY B 225  LYS B 226  ARG B 228  CYS B 270                    
SITE     2 AC2 19 TYR B 271  ARG B 295  LEU B 296  ASN B 298                    
SITE     3 AC2 19 HIS B 299  TYR B 336  TRP B 349  HOH B2825                    
SITE     4 AC2 19 HOH B2856  HOH B2862  HOH B2875  HOH B2898                    
SITE     5 AC2 19 HOH B2902  HIS F  18  LYS F  20                               
SITE     1 AC3 18 GLY C 225  LYS C 226  ARG C 228  CYS C 270                    
SITE     2 AC3 18 TYR C 271  ARG C 295  LEU C 296  ASN C 298                    
SITE     3 AC3 18 HIS C 299  TYR C 336  TRP C 349  HOH C2831                    
SITE     4 AC3 18 HOH C2841  HOH C2908  HOH C2921  HOH C2928                    
SITE     5 AC3 18 HIS G  18  LYS G  20                                          
SITE     1 AC4 20 HOH B2806  GLY D 225  LYS D 226  ARG D 228                    
SITE     2 AC4 20 CYS D 270  TYR D 271  ARG D 295  LEU D 296                    
SITE     3 AC4 20 ASN D 298  HIS D 299  TYR D 336  TRP D 349                    
SITE     4 AC4 20 HOH D2810  HOH D2826  HOH D2878  HOH D2889                    
SITE     5 AC4 20 HOH D2892  ARG F  23  HIS H  18  LYS H  20                    
CRYST1   43.960   45.775   94.435  89.22  87.07  90.72 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      0.022748  0.000287 -0.001167        0.00000                         
SCALE2      0.000000  0.021848 -0.000313        0.00000                         
SCALE3      0.000000  0.000000  0.010604        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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