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Database: PDB
Entry: 3TG5
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HEADER    TRANSFERASE                             17-AUG-11   3TG5              
TITLE     STRUCTURE OF SMYD2 IN COMPLEX WITH P53 AND SAH                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HSKM-B, HISTONE METHYLTRANSFERASE SMYD2, LYSINE N-          
COMPND   5 METHYLTRANSFERASE 3C, SET AND MYND DOMAIN-CONTAINING PROTEIN 2;      
COMPND   6 EC: 2.1.1.-, 2.1.1.43;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 365-375;                                      
COMPND  12 SYNONYM: ANTIGEN NY-CO-13, PHOSPHOPROTEIN P53, TUMOR SUPPRESSOR P53; 
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: SMYD2, KMT3C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: THIS SEQUENCE IS SYNTHESIZED                          
KEYWDS    SET DOMAIN, METHYLTRANSFERASE, CO FACTOR BINDING, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.ZHAO,L.WANG                                                         
REVDAT   2   14-SEP-11 3TG5    1       JRNL                                     
REVDAT   1   31-AUG-11 3TG5    0                                                
JRNL        AUTH   L.WANG,L.LI,H.ZHANG,X.LUO,J.DAI,S.ZHOU,J.GU,J.ZHU,P.ATADJA,  
JRNL        AUTH 2 C.LU,E.LI,K.ZHAO                                             
JRNL        TITL   STRUCTURE OF HUMAN SMYD2 REVEALS THE BASIS OF P53 TUMOR      
JRNL        TITL 2 SUPPRESSOR METHYLATION                                       
JRNL        REF    J.BIOL.CHEM.                               2011              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   21880715                                                     
JRNL        DOI    10.1074/JBC.M111.262410                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 19311                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1042                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1322                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3472                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.29000                                             
REMARK   3    B22 (A**2) : -0.28000                                             
REMARK   3    B33 (A**2) : 1.57000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.270         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.192         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.732         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.891                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.864                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3581 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4823 ; 0.988 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   431 ; 4.799 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   166 ;37.240 ;24.277       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   658 ;15.752 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;11.692 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   515 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2681 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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 3TG5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067440.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97922                            
REMARK 200  MONOCHROMATOR                  : TOROIDAL MIRROR                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20928                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3TG4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 25% PEG 3350,       
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 293K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       26.68000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.62500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.83500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.62500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.68000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.83500            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLU A   431                                                      
REMARK 465     SER A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS B   365                                                      
REMARK 465     SER B   366                                                      
REMARK 465     SER B   367                                                      
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     HIS A 163    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE A 166    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS A    51     O    HOH A   484              2.04            
REMARK 500   OE1  GLU A   266     O    HOH A   464              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   496     O    HOH A   636     4455     1.66            
REMARK 500   O    HOH A   513     O    HOH A   525     3544     2.08            
REMARK 500   ND1  HIS A   397     O    HOH A   636     4455     2.16            
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    LEU A 164   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLU A 189   O   -  C   -  N   ANGL. DEV. =   9.8 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    ASN A  75     -159.85   -162.55                                   
REMARK 500    ASP A 188     -158.41    -86.54                                   
REMARK 500    VAL A 277       51.32   -110.17                                   
REMARK 500    TYR A 311      -34.95   -130.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A 164        21.5      L          L   OUTSIDE RANGE           
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 523        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A 529        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH A 548        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A 564        DISTANCE =  9.35 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 438  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  90   SG  110.5                                              
REMARK 620 3 HIS A  86   NE2 100.8 103.4                                        
REMARK 620 4 CYS A  68   SG  106.6 136.8  90.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 436  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 262   SG                                                     
REMARK 620 2 CYS A 267   SG  116.6                                              
REMARK 620 3 CYS A 209   SG  112.8  99.0                                        
REMARK 620 4 CYS A 264   SG  104.8 115.6 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 437  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  74   SG                                                     
REMARK 620 2 CYS A  55   SG   92.7                                              
REMARK 620 3 CYS A  78   SG  112.5  94.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 436                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 437                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 438                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TG4   RELATED DB: PDB                                   
DBREF  3TG5 A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
DBREF  3TG5 B  365   375  UNP    P04637   P53_HUMAN      365    375             
SEQRES   1 A  433  MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 A  433  SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO          
SEQRES   3 A  433  PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 A  433  ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS          
SEQRES   5 A  433  GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 A  433  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS          
SEQRES   7 A  433  GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER          
SEQRES   8 A  433  PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU          
SEQRES   9 A  433  THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS          
SEQRES  10 A  433  ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA          
SEQRES  11 A  433  VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN          
SEQRES  12 A  433  GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU          
SEQRES  13 A  433  HIS HIS PHE TYR SER LYS HIS LEU GLY PHE PRO ASP ASN          
SEQRES  14 A  433  ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN          
SEQRES  15 A  433  GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY          
SEQRES  16 A  433  SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER          
SEQRES  17 A  433  CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU          
SEQRES  18 A  433  ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU          
SEQRES  19 A  433  GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR          
SEQRES  20 A  433  GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE          
SEQRES  21 A  433  THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 A  433  LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO          
SEQRES  23 A  433  LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG          
SEQRES  24 A  433  ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS          
SEQRES  25 A  433  SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN          
SEQRES  26 A  433  GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL TYR          
SEQRES  27 A  433  MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU          
SEQRES  28 A  433  TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN          
SEQRES  29 A  433  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR          
SEQRES  30 A  433  SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG          
SEQRES  31 A  433  LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS          
SEQRES  32 A  433  ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS          
SEQRES  33 A  433  GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU          
SEQRES  34 A  433  ILE GLU SER HIS                                              
SEQRES   1 B   11  HIS SER SER HIS LEU LYS SER LYS LYS GLY GLN                  
HET    GOL  A 434       6                                                       
HET    SAH  A 435      26                                                       
HET     ZN  A 436       1                                                       
HET     ZN  A 437       1                                                       
HET     ZN  A 438       1                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  SAH    C14 H20 N6 O5 S                                              
FORMUL   5   ZN    3(ZN 2+)                                                     
FORMUL   8  HOH   *209(H2 O)                                                    
HELIX    1   1 VAL A   45  ARG A   48  5                                   4    
HELIX    2   2 ASN A   75  LYS A   87  1                                  13    
HELIX    3   3 GLU A   89  GLY A   97  1                                   9    
HELIX    4   4 GLU A   98  TRP A  100  5                                   3    
HELIX    5   5 SER A  103  HIS A  119  1                                  17    
HELIX    6   6 ALA A  130  PHE A  134  5                                   5    
HELIX    7   7 ASP A  142  SER A  161  1                                  20    
HELIX    8   8 ASP A  168  GLY A  183  1                                  16    
HELIX    9   9 PRO A  246  PHE A  259  1                                  14    
HELIX   10  10 CYS A  264  LYS A  270  1                                   7    
HELIX   11  11 LYS A  272  VAL A  277  1                                   6    
HELIX   12  12 LYS A  287  LYS A  309  1                                  23    
HELIX   13  13 SER A  313  SER A  329  1                                  17    
HELIX   14  14 ASN A  336  MET A  353  1                                  18    
HELIX   15  15 ASP A  355  TYR A  374  1                                  20    
HELIX   16  16 SER A  378  LEU A  395  1                                  18    
HELIX   17  17 HIS A  397  GLY A  417  1                                  21    
HELIX   18  18 HIS A  420  ILE A  430  1                                  11    
SHEET    1   A 2 LEU A   9  SER A  14  0                                        
SHEET    2   A 2 GLY A  18  ALA A  23 -1  O  GLY A  18   N  SER A  14           
SHEET    1   B 3 LEU A  32  PRO A  37  0                                        
SHEET    2   B 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3   B 3 VAL A 213  LYS A 218 -1  N  THR A 216   O  GLU A 223           
SHEET    1   C 3 ALA A  40  LEU A  43  0                                        
SHEET    2   C 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3   C 3 PHE A 184  GLU A 187 -1  N  ILE A 186   O  GLY A 195           
SHEET    1   D 2 SER A  63  LYS A  64  0                                        
SHEET    2   D 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1   E 2 ASN A 206  HIS A 207  0                                        
SHEET    2   E 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
LINK         SG  CYS A  65                ZN    ZN A 438     1555   1555  2.15  
LINK         SG  CYS A 262                ZN    ZN A 436     1555   1555  2.28  
LINK         SG  CYS A 267                ZN    ZN A 436     1555   1555  2.33  
LINK         SG  CYS A  90                ZN    ZN A 438     1555   1555  2.40  
LINK         SG  CYS A 209                ZN    ZN A 436     1555   1555  2.41  
LINK         NE2 HIS A  86                ZN    ZN A 438     1555   1555  2.41  
LINK         SG  CYS A 264                ZN    ZN A 436     1555   1555  2.41  
LINK         SG  CYS A  74                ZN    ZN A 437     1555   1555  2.52  
LINK         SG  CYS A  55                ZN    ZN A 437     1555   1555  2.63  
LINK         SG  CYS A  68                ZN    ZN A 438     1555   1555  2.68  
LINK         SG  CYS A  78                ZN    ZN A 437     1555   1555  2.73  
SITE     1 AC1  7 PRO A 211  ILE A 214  SER A 378  LEU A 379                    
SITE     2 AC1  7 ASN A 380  HOH A 456  HOH A 461                               
SITE     1 AC2 19 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC2 19 HIS A 137  CYS A 181  ASN A 182  ALA A 203                    
SITE     3 AC2 19 LEU A 204  ASN A 206  HIS A 207  TYR A 240                    
SITE     4 AC2 19 TYR A 258  PHE A 260  HOH A 441  HOH A 446                    
SITE     5 AC2 19 HOH A 574  HOH A 596  HOH A 630                               
SITE     1 AC3  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC4  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC5  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
CRYST1   53.360   71.670  121.250  90.00  90.00  90.00 P 21 21 21    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      0.018741  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008247        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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