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Database: PDB
Entry: 3BO5
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HEADER    TRANSFERASE                             17-DEC-07   3BO5              
TITLE     CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN HISTONE-LYSINE 
TITLE    2 N-METHYLTRANSFERASE SETMAR                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HISTONE-LYSINE N-METHYLTRANSFERASE DOMAIN: RESIDUES 2-290; 
COMPND   5 SYNONYM: SET DOMAIN AND MARINER TRANSPOSASE FUSION GENE-CONTAINING   
COMPND   6 PROTEIN, METNASE, HSMAR1 [INCLUDES: HISTONE-LYSINE N-                
COMPND   7 METHYLTRANSFERASE, AND MARINER TRANSPOSASE HSMAR1];                  
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETMAR;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P15B                                      
KEYWDS    TRANSFERASE, SET DOMAIN, METHYLTRANSFERASE, SETMAR, CHROMATIN         
KEYWDS   2 REGULATOR, DNA DAMAGE, DNA REPAIR, DNA-BINDING, NUCLEUS, STRUCTURAL  
KEYWDS   3 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.V.LUNIN,H.WU,H.REN,E.DOBROVETSKY,J.WEIGELT,C.H.ARROWSMITH,          
AUTHOR   2 A.M.EDWARDS,A.BOCHKAREV,J.MIN,A.N.PLOTNIKOV,STRUCTURAL GENOMICS      
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   3   13-JUL-11 3BO5    1       VERSN                                    
REVDAT   2   24-FEB-09 3BO5    1       VERSN                                    
REVDAT   1   22-JAN-08 3BO5    0                                                
JRNL        AUTH   H.WU,V.V.LUNIN,H.REN,E.DOBROVETSKY,J.WEIGELT,C.H.ARROWSMITH, 
JRNL        AUTH 2 A.M.EDWARDS,A.BOCHKAREV,J.MIN,A.N.PLOTNIKOV                  
JRNL        TITL   THE CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN   
JRNL        TITL 2 HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR IN COMPLEX WITH    
JRNL        TITL 3 ADOHCY.                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 30096                          
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) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1606                            
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) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1880                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2088                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 304                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.59000                                              
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : 0.12000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.33000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.462         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2218 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3016 ; 2.057 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   278 ; 6.461 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    97 ;34.774 ;23.402       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   357 ;12.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;14.138 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   329 ; 0.149 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1698 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1092 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1517 ; 0.327 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   289 ; 0.153 ; 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):    79 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.206 ; 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):  1389 ; 1.466 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2217 ; 2.294 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   921 ; 2.990 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   793 ; 4.437 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3BO5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045757.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793143, 1.2832396               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31726                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M AMMONIUM ACETATE,    
REMARK 280  0.1 M BIS-TRIS PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE   
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.91350            
REMARK 290   SMTRY3   2  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ILE A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     TYR A   187                                                      
REMARK 465     ASN A   188                                                      
REMARK 465     GLY A   189                                                      
REMARK 465     GLN A   190                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  12    CD   OE1  OE2                                       
REMARK 470     GLN A  55    CD   OE1  NE2                                       
REMARK 470     ASP A  90    CG   OD1  OD2                                       
REMARK 470     TYR A  97    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 171    CG   CD   OE1  NE2                                  
REMARK 470     THR A 172    OG1  CG2                                            
REMARK 470     LYS A 173    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A    65     O    SER A   288     2747     2.15            
REMARK 500   O    HOH A   606     O    HOH A   689     2646     2.15            
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    ASP A 247   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 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 A  64      -31.40   -141.52                                   
REMARK 500    ASN A 105     -167.18   -124.44                                   
REMARK 500    VAL A 118      -67.39   -137.23                                   
REMARK 500    VAL A 151      -62.53   -105.77                                   
REMARK 500    ILE A 223      -93.77   -127.96                                   
REMARK 500    ALA A 282       -1.04     75.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 702        DISTANCE =  5.62 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  61   SG                                                     
REMARK 620 2 CYS A  75   SG  114.9                                              
REMARK 620 3 CYS A 104   SG  114.1 110.5                                        
REMARK 620 4 CYS A 108   SG   99.2 101.6 115.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  61   SG                                                     
REMARK 620 2 CYS A  63   SG  106.7                                              
REMARK 620 3 CYS A  68   SG  107.5 104.2                                        
REMARK 620 4 CYS A  73   SG  112.0 114.9 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  68   SG                                                     
REMARK 620 2 CYS A 104   SG  110.2                                              
REMARK 620 3 CYS A 110   SG  107.2 107.3                                        
REMARK 620 4 CYS A 114   SG  106.6 111.7 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 212   SG                                                     
REMARK 620 2 CYS A 273   SG  114.4                                              
REMARK 620 3 CYS A 275   SG  107.0 105.5                                        
REMARK 620 4 CYS A 280   SG  110.9 107.0 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307                 
DBREF  3BO5 A    1   289  UNP    Q53H47   SETMR_HUMAN      2    290             
SEQADV 3BO5 GLY A    0  UNP  Q53H47              EXPRESSION TAG                 
SEQADV 3BO5 ALA A  259  UNP  Q53H47    GLU   260 ENGINEERED                     
SEQADV 3BO5 SER A  260  UNP  Q53H47    ASP   261 ENGINEERED                     
SEQRES   1 A  290  GLY ALA GLU PHE LYS GLU LYS PRO GLU ALA PRO THR GLU          
SEQRES   2 A  290  GLN LEU ASP VAL ALA CYS GLY GLN GLU ASN LEU PRO VAL          
SEQRES   3 A  290  GLY ALA TRP PRO PRO GLY ALA ALA PRO ALA PRO PHE GLN          
SEQRES   4 A  290  TYR THR PRO ASP HIS VAL VAL GLY PRO GLY ALA ASP ILE          
SEQRES   5 A  290  ASP PRO THR GLN ILE THR PHE PRO GLY CYS ILE CYS VAL          
SEQRES   6 A  290  LYS THR PRO CYS LEU PRO GLY THR CYS SER CYS LEU ARG          
SEQRES   7 A  290  HIS GLY GLU ASN TYR ASP ASP ASN SER CYS LEU ARG ASP          
SEQRES   8 A  290  ILE GLY SER GLY GLY LYS TYR ALA GLU PRO VAL PHE GLU          
SEQRES   9 A  290  CYS ASN VAL LEU CYS ARG CYS SER ASP HIS CYS ARG ASN          
SEQRES  10 A  290  ARG VAL VAL GLN LYS GLY LEU GLN PHE HIS PHE GLN VAL          
SEQRES  11 A  290  PHE LYS THR HIS LYS LYS GLY TRP GLY LEU ARG THR LEU          
SEQRES  12 A  290  GLU PHE ILE PRO LYS GLY ARG PHE VAL CYS GLU TYR ALA          
SEQRES  13 A  290  GLY GLU VAL LEU GLY PHE SER GLU VAL GLN ARG ARG ILE          
SEQRES  14 A  290  HIS LEU GLN THR LYS SER ASP SER ASN TYR ILE ILE ALA          
SEQRES  15 A  290  ILE ARG GLU HIS VAL TYR ASN GLY GLN VAL MET GLU THR          
SEQRES  16 A  290  PHE VAL ASP PRO THR TYR ILE GLY ASN ILE GLY ARG PHE          
SEQRES  17 A  290  LEU ASN HIS SER CYS GLU PRO ASN LEU LEU MET ILE PRO          
SEQRES  18 A  290  VAL ARG ILE ASP SER MET VAL PRO LYS LEU ALA LEU PHE          
SEQRES  19 A  290  ALA ALA LYS ASP ILE VAL PRO GLU GLU GLU LEU SER TYR          
SEQRES  20 A  290  ASP TYR SER GLY ARG TYR LEU ASN LEU THR VAL SER ALA          
SEQRES  21 A  290  SER LYS GLU ARG LEU ASP HIS GLY LYS LEU ARG LYS PRO          
SEQRES  22 A  290  CYS TYR CYS GLY ALA LYS SER CYS THR ALA PHE LEU PRO          
SEQRES  23 A  290  PHE ASP SER SER                                              
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET     ZN  A 304       1                                                       
HET    SAH  A 305      26                                                       
HET    GOL  A 306       6                                                       
HET    GOL  A 307       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    4(ZN 2+)                                                     
FORMUL   6  SAH    C14 H20 N6 O5 S                                              
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9  HOH   *304(H2 O)                                                    
HELIX    1   1 CYS A   73  ARG A   77  5                                   5    
HELIX    2   2 VAL A  118  GLY A  122  5                                   5    
HELIX    3   3 GLY A  160  HIS A  169  1                                  10    
HELIX    4   4 ILE A  204  LEU A  208  5                                   5    
SHEET    1   A 5 GLY A  26  TRP A  28  0                                        
SHEET    2   A 5 PHE A 127  LYS A 131  1  O  VAL A 129   N  GLY A  26           
SHEET    3   A 5 TRP A 137  THR A 141 -1  O  ARG A 140   N  GLN A 128           
SHEET    4   A 5 GLU A 243  TYR A 246 -1  O  LEU A 244   N  LEU A 139           
SHEET    5   A 5 ASN A 209  HIS A 210  1  N  ASN A 209   O  TYR A 246           
SHEET    1   B 4 GLN A  38  TYR A  39  0                                        
SHEET    2   B 4 MET A 192  GLY A 202  1  O  TYR A 200   N  GLN A  38           
SHEET    3   B 4 GLY A 156  LEU A 159 -1  N  GLU A 157   O  ASP A 197           
SHEET    4   B 4 VAL A  44  VAL A  45  1  N  VAL A  44   O  VAL A 158           
SHEET    1   C 5 GLN A  38  TYR A  39  0                                        
SHEET    2   C 5 MET A 192  GLY A 202  1  O  TYR A 200   N  GLN A  38           
SHEET    3   C 5 ILE A 180  GLU A 184 -1  N  ILE A 182   O  THR A 194           
SHEET    4   C 5 ALA A 259  ASP A 265 -1  O  GLU A 262   N  ALA A 181           
SHEET    5   C 5 ASP A 287  SER A 288  1  O  ASP A 287   N  ARG A 263           
SHEET    1   D 4 VAL A 101  PHE A 102  0                                        
SHEET    2   D 4 LEU A 216  ARG A 222  1  O  ARG A 222   N  VAL A 101           
SHEET    3   D 4 LYS A 229  ALA A 234 -1  O  LYS A 229   N  VAL A 221           
SHEET    4   D 4 PHE A 150  GLU A 153 -1  N  CYS A 152   O  LEU A 232           
LINK         SG  CYS A  61                ZN    ZN A 301     1555   1555  2.39  
LINK         SG  CYS A  61                ZN    ZN A 303     1555   1555  2.36  
LINK         SG  CYS A  63                ZN    ZN A 303     1555   1555  2.33  
LINK         SG  CYS A  68                ZN    ZN A 302     1555   1555  2.36  
LINK         SG  CYS A  68                ZN    ZN A 303     1555   1555  2.41  
LINK         SG  CYS A  73                ZN    ZN A 303     1555   1555  2.28  
LINK         SG  CYS A  75                ZN    ZN A 301     1555   1555  2.30  
LINK         SG  CYS A 104                ZN    ZN A 302     1555   1555  2.36  
LINK         SG  CYS A 104                ZN    ZN A 301     1555   1555  2.35  
LINK         SG  CYS A 108                ZN    ZN A 301     1555   1555  2.37  
LINK         SG  CYS A 110                ZN    ZN A 302     1555   1555  2.30  
LINK         SG  CYS A 114                ZN    ZN A 302     1555   1555  2.30  
LINK         SG  CYS A 212                ZN    ZN A 304     1555   1555  2.44  
LINK         SG  CYS A 273                ZN    ZN A 304     1555   1555  2.39  
LINK         SG  CYS A 275                ZN    ZN A 304     1555   1555  2.30  
LINK         SG  CYS A 280                ZN    ZN A 304     1555   1555  2.31  
CISPEP   1 TRP A   28    PRO A   29          0         4.89                     
SITE     1 AC1  4 CYS A  61  CYS A  75  CYS A 104  CYS A 108                    
SITE     1 AC2  4 CYS A  68  CYS A 104  CYS A 110  CYS A 114                    
SITE     1 AC3  4 CYS A  61  CYS A  63  CYS A  68  CYS A  73                    
SITE     1 AC4  4 CYS A 212  CYS A 273  CYS A 275  CYS A 280                    
SITE     1 AC5 21 LYS A 135  GLY A 136  TRP A 137  ASN A 177                    
SITE     2 AC5 21 TYR A 178  ARG A 206  ASN A 209  HIS A 210                    
SITE     3 AC5 21 TYR A 248  ARG A 263  PRO A 272  CYS A 273                    
SITE     4 AC5 21 TYR A 274  CYS A 275  LEU A 284  PHE A 286                    
SITE     5 AC5 21 HOH A 427  HOH A 473  HOH A 515  HOH A 524                    
SITE     6 AC5 21 HOH A 627                                                     
SITE     1 AC6  4 CYS A  63  VAL A  64  LYS A  65  THR A  66                    
SITE     1 AC7  4 ASN A  22  LYS A 121  GLN A 124  HOH A 642                    
CRYST1   41.396   67.827   44.637  90.00 105.93  90.00 P 1 21 1      2          
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      0.024157  0.000000  0.006893        0.00000                         
SCALE2      0.000000  0.014743  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023297        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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