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Database: PDB
Entry: 3OXG
LinkDB: 3OXG
Original site: 3OXG 
HEADER    TRANSFERASE                             21-SEP-10   3OXG              
TITLE     HUMAN LYSINE METHYLTRANSFERASE SMYD3 IN COMPLEX WITH ADOHCY (FORM III)
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET AND MYND DOMAIN-CONTAINING PROTEIN 3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 1;               
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 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: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    SMYD PROTEINS, MYND, SET DOMAIN, HISTONE LYSINE METHYLTRANSFERASE,    
KEYWDS   2 HISTONE METHYLATION, H3K4, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XU,J.WU,B.SUN,C.ZHONG,J.DING                                        
REVDAT   2   13-JUL-11 3OXG    1       JRNL                                     
REVDAT   1   23-FEB-11 3OXG    0                                                
JRNL        AUTH   S.XU,J.WU,B.SUN,C.ZHONG,J.DING                               
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL STUDIES OF HUMAN LYSINE           
JRNL        TITL 2 METHYLTRANSFERASE SMYD3 REVEAL THE IMPORTANT FUNCTIONAL      
JRNL        TITL 3 ROLES OF ITS POST-SET AND TPR DOMAINS AND THE REGULATION OF  
JRNL        TITL 4 ITS ACTIVITY BY DNA BINDING.                                 
JRNL        REF    NUCLEIC ACIDS RES.            V.  39  4438 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   21266482                                                     
JRNL        DOI    10.1093/NAR/GKR019                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.41 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) : 3.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 9353                           
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 487                             
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) : 3.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 624                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 37                           
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3397                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 97.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.08000                                             
REMARK   3    B22 (A**2) : -1.08000                                             
REMARK   3    B33 (A**2) : 1.62000                                              
REMARK   3    B12 (A**2) : -0.54000                                             
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): 0.538         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.430         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.340        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3489 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4698 ; 1.095 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   423 ; 4.919 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   163 ;37.669 ;23.865       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   658 ;17.200 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;17.355 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   515 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2600 ; 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):  2122 ; 0.478 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3422 ; 0.830 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1367 ; 0.631 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1276 ; 1.143 ; 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: U VALUES: REFINED INDIVIDUALLY            
REMARK   4                                                                      
REMARK   4 3OXG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061693.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
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) : 0.97908                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9395                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.13000                            
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) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 3OXF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENE GLYCOL MONOMETHYL       
REMARK 280  ETHER 550, 0.1M NACL, 0.1M BICINE, PH 9.0, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.40067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.80133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.10100            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       93.50167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       18.70033            
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     MET A   -35                                                      
REMARK 465     GLY A   -34                                                      
REMARK 465     SER A   -33                                                      
REMARK 465     SER A   -32                                                      
REMARK 465     HIS A   -31                                                      
REMARK 465     HIS A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     SER A   -25                                                      
REMARK 465     SER A   -24                                                      
REMARK 465     GLY A   -23                                                      
REMARK 465     LEU A   -22                                                      
REMARK 465     VAL A   -21                                                      
REMARK 465     PRO A   -20                                                      
REMARK 465     ARG A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     MET A   -15                                                      
REMARK 465     ALA A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     THR A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     GLN A    -8                                                      
REMARK 465     GLN A    -7                                                      
REMARK 465     MET A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA A   427                                                      
REMARK 465     SER A   428                                                      
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  13       -5.44   -143.38                                   
REMARK 500    ARG A  14       74.64   -114.11                                   
REMARK 500    ASN A  16     -164.31   -113.41                                   
REMARK 500    ASP A  50        7.22    -56.83                                   
REMARK 500    ARG A  51      -84.82   -132.92                                   
REMARK 500    GLU A  57      167.34    -45.92                                   
REMARK 500    LYS A  58       93.06     14.61                                   
REMARK 500    CYS A  62      121.05    -31.51                                   
REMARK 500    GLN A  64      -75.64    -72.55                                   
REMARK 500    VAL A  67      -54.84   -132.29                                   
REMARK 500    LYS A  94      122.23    -27.77                                   
REMARK 500    PRO A 117       65.43    -66.32                                   
REMARK 500    THR A 137     -158.21    -74.86                                   
REMARK 500    GLU A 189       20.56    -75.21                                   
REMARK 500    LEU A 243       56.15    -94.82                                   
REMARK 500    SER A 246      -36.04    -39.14                                   
REMARK 500    CYS A 258       51.92     71.39                                   
REMARK 500    PHE A 264      -60.79    -24.89                                   
REMARK 500    GLN A 269       60.69     36.99                                   
REMARK 500    LYS A 271        4.79     58.98                                   
REMARK 500    TRP A 302      -82.68     15.77                                   
REMARK 500    GLU A 303      -51.03    -27.96                                   
REMARK 500    ARG A 319      -60.36   -121.53                                   
REMARK 500    MET A 385       47.48    -96.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 430  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  83   NE2                                                    
REMARK 620 2 CYS A  87   SG  100.9                                              
REMARK 620 3 CYS A  62   SG   99.3 108.1                                        
REMARK 620 4 CYS A  65   SG  111.8 126.5 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 431  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 261   SG                                                     
REMARK 620 2 CYS A 263   SG  132.3                                              
REMARK 620 3 CYS A 208   SG  113.2  87.7                                        
REMARK 620 4 CYS A 266   SG  108.5 113.2  92.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 429  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  75   SG  117.2                                              
REMARK 620 3 CYS A  71   SG  104.3  90.0                                        
REMARK 620 4 CYS A  49   SG  110.3 106.2 128.3                                  
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 429                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 430                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 431                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 432                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3OXF   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE EXPERIMENTAL INFO OF UNIPROT (Q9H7B4, SMYD3_HUMAN) SHOWS         
REMARK 999 CONFLICTS K -> N, K -> R AT THE POSITIONS 13, 140 (IN REF.6:         
REMARK 999 AAH31010)                                                            
DBREF  3OXG A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 3OXG MET A  -35  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A  -34  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A  -33  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A  -32  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -31  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -30  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -29  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -28  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -27  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -26  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A  -25  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A  -24  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A  -23  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG LEU A  -22  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG VAL A  -21  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG PRO A  -20  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG ARG A  -19  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A  -18  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A  -17  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG HIS A  -16  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG MET A  -15  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG ALA A  -14  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A  -13  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG MET A  -12  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG THR A  -11  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A  -10  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A   -9  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLN A   -8  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLN A   -7  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG MET A   -6  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A   -5  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG ARG A   -4  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLY A   -3  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG SER A   -2  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG GLU A   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG PHE A    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXG ASN A   13  UNP  Q9H7B4    LYS    13 SEE REMARK 999                 
SEQADV 3OXG ARG A  140  UNP  Q9H7B4    LYS   140 SEE REMARK 999                 
SEQRES   1 A  464  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  464  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 A  464  GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET GLU PRO          
SEQRES   4 A  464  LEU LYS VAL GLU LYS PHE ALA THR ALA ASN ARG GLY ASN          
SEQRES   5 A  464  GLY LEU ARG ALA VAL THR PRO LEU ARG PRO GLY GLU LEU          
SEQRES   6 A  464  LEU PHE ARG SER ASP PRO LEU ALA TYR THR VAL CYS LYS          
SEQRES   7 A  464  GLY SER ARG GLY VAL VAL CYS ASP ARG CYS LEU LEU GLY          
SEQRES   8 A  464  LYS GLU LYS LEU MET ARG CYS SER GLN CYS ARG VAL ALA          
SEQRES   9 A  464  LYS TYR CYS SER ALA LYS CYS GLN LYS LYS ALA TRP PRO          
SEQRES  10 A  464  ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS SER CYS LYS          
SEQRES  11 A  464  PRO ARG TYR PRO PRO ASP SER VAL ARG LEU LEU GLY ARG          
SEQRES  12 A  464  VAL VAL PHE LYS LEU MET ASP GLY ALA PRO SER GLU SER          
SEQRES  13 A  464  GLU LYS LEU TYR SER PHE TYR ASP LEU GLU SER ASN ILE          
SEQRES  14 A  464  ASN LYS LEU THR GLU ASP ARG LYS GLU GLY LEU ARG GLN          
SEQRES  15 A  464  LEU VAL MET THR PHE GLN HIS PHE MET ARG GLU GLU ILE          
SEQRES  16 A  464  GLN ASP ALA SER GLN LEU PRO PRO ALA PHE ASP LEU PHE          
SEQRES  17 A  464  GLU ALA PHE ALA LYS VAL ILE CYS ASN SER PHE THR ILE          
SEQRES  18 A  464  CYS ASN ALA GLU MET GLN GLU VAL GLY VAL GLY LEU TYR          
SEQRES  19 A  464  PRO SER ILE SER LEU LEU ASN HIS SER CYS ASP PRO ASN          
SEQRES  20 A  464  CYS SER ILE VAL PHE ASN GLY PRO HIS LEU LEU LEU ARG          
SEQRES  21 A  464  ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU LEU THR ILE          
SEQRES  22 A  464  CYS TYR LEU ASP MET LEU MET THR SER GLU GLU ARG ARG          
SEQRES  23 A  464  LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU CYS ASP CYS          
SEQRES  24 A  464  PHE ARG CYS GLN THR GLN ASP LYS ASP ALA ASP MET LEU          
SEQRES  25 A  464  THR GLY ASP GLU GLN VAL TRP LYS GLU VAL GLN GLU SER          
SEQRES  26 A  464  LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS TRP LYS TRP          
SEQRES  27 A  464  GLU GLN VAL LEU ALA MET CYS GLN ALA ILE ILE SER SER          
SEQRES  28 A  464  ASN SER GLU ARG LEU PRO ASP ILE ASN ILE TYR GLN LEU          
SEQRES  29 A  464  LYS VAL LEU ASP CYS ALA MET ASP ALA CYS ILE ASN LEU          
SEQRES  30 A  464  GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY THR ARG THR          
SEQRES  31 A  464  MET GLU PRO TYR ARG ILE PHE PHE PRO GLY SER HIS PRO          
SEQRES  32 A  464  VAL ARG GLY VAL GLN VAL MET LYS VAL GLY LYS LEU GLN          
SEQRES  33 A  464  LEU HIS GLN GLY MET PHE PRO GLN ALA MET LYS ASN LEU          
SEQRES  34 A  464  ARG LEU ALA PHE ASP ILE MET ARG VAL THR HIS GLY ARG          
SEQRES  35 A  464  GLU HIS SER LEU ILE GLU ASP LEU ILE LEU LEU LEU GLU          
SEQRES  36 A  464  GLU CYS ASP ALA ASN ILE ARG ALA SER                          
HET     ZN  A 429       1                                                       
HET     ZN  A 430       1                                                       
HET     ZN  A 431       1                                                       
HET    SAH  A 432      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SAH    C14 H20 N6 O5 S                                              
HELIX    1   1 SER A   72  LYS A   94  1                                  23    
HELIX    2   2 PRO A   99  LEU A  112  1                                  14    
HELIX    3   3 SER A  118  LYS A  122  5                                   5    
HELIX    4   4 ASN A  132  LEU A  136  5                                   5    
HELIX    5   5 THR A  137  MET A  155  1                                  19    
HELIX    6   6 ASP A  170  ASN A  181  1                                  12    
HELIX    7   7 SER A  200  LEU A  204  5                                   5    
HELIX    8   8 THR A  245  TYR A  257  1                                  13    
HELIX    9   9 CYS A  263  THR A  268  1                                   6    
HELIX   10  10 LYS A  271  THR A  277  1                                   7    
HELIX   11  11 ASP A  279  HIS A  299  1                                  21    
HELIX   12  12 TRP A  302  ASN A  316  1                                  15    
HELIX   13  13 ASN A  324  GLY A  342  1                                  19    
HELIX   14  14 LEU A  343  THR A  352  1                                  10    
HELIX   15  15 THR A  354  PHE A  362  1                                   9    
HELIX   16  16 HIS A  366  GLY A  384  1                                  19    
HELIX   17  17 MET A  385  HIS A  404  1                                  20    
HELIX   18  18 HIS A  408  ALA A  423  1                                  16    
SHEET    1   A 2 VAL A   6  LYS A   8  0                                        
SHEET    2   A 2 LEU A  18  ALA A  20 -1  O  ARG A  19   N  GLU A   7           
SHEET    1   B 3 LEU A  29  SER A  33  0                                        
SHEET    2   B 3 HIS A 220  ALA A 225 -1  O  LEU A 221   N  SER A  33           
SHEET    3   B 3 CYS A 212  ASN A 217 -1  N  VAL A 215   O  LEU A 222           
SHEET    1   C 3 ALA A  37  VAL A  40  0                                        
SHEET    2   C 3 GLU A 192  LEU A 197 -1  O  VAL A 195   N  THR A  39           
SHEET    3   C 3 SER A 182  CYS A 186 -1  N  ILE A 185   O  GLY A 194           
SHEET    1   D 2 MET A  60  ARG A  61  0                                        
SHEET    2   D 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
SHEET    1   E 2 ASN A 205  HIS A 206  0                                        
SHEET    2   E 2 THR A 236  ILE A 237  1  O  ILE A 237   N  ASN A 205           
LINK         NE2 HIS A  83                ZN    ZN A 430     1555   1555  1.91  
LINK         SG  CYS A 261                ZN    ZN A 431     1555   1555  2.12  
LINK         SG  CYS A  52                ZN    ZN A 429     1555   1555  2.33  
LINK         SG  CYS A  75                ZN    ZN A 429     1555   1555  2.40  
LINK         SG  CYS A  87                ZN    ZN A 430     1555   1555  2.42  
LINK         SG  CYS A  62                ZN    ZN A 430     1555   1555  2.44  
LINK         SG  CYS A  71                ZN    ZN A 429     1555   1555  2.48  
LINK         SG  CYS A  49                ZN    ZN A 429     1555   1555  2.50  
LINK         SG  CYS A  65                ZN    ZN A 430     1555   1555  2.63  
LINK         SG  CYS A 263                ZN    ZN A 431     1555   1555  2.66  
LINK         SG  CYS A 208                ZN    ZN A 431     1555   1555  2.67  
LINK         SG  CYS A 266                ZN    ZN A 431     1555   1555  2.80  
CISPEP   1 LYS A   94    PRO A   95          0        -3.27                     
SITE     1 AC1  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC2  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC3  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC4 11 ARG A  14  ASN A  16  GLY A  17  TYR A 124                    
SITE     2 AC4 11 GLU A 130  ASN A 132  SER A 202  ASN A 205                    
SITE     3 AC4 11 HIS A 206  TYR A 257  PHE A 259                               
CRYST1  103.439  103.439  112.202  90.00  90.00 120.00 P 61          6          
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      0.009668  0.005582  0.000000        0.00000                         
SCALE2      0.000000  0.011163  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008912        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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