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Database: PDB
Entry: 3SMT
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Original site: 3SMT 
HEADER    TRANSFERASE                             28-JUN-11   3SMT              
TITLE     CRYSTAL STRUCTURE OF HUMAN SET DOMAIN-CONTAINING PROTEIN3             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET DOMAIN-CONTAINING PROTEIN 3;                            
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: SETD3, C14ORF154;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)V2RPRARE;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    SETD3, HISTONE METHYLTRANSFERASE, HISTONE MODIFICATION, LYSINE, POST- 
KEYWDS   2 TRANSLATIONAL MODIFICATION, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS 
KEYWDS   3 CONSORTIUM, SGC, TRANSFERASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,J.R.WALKER,P.LOPPNAU,C.BOUNTRA,J.WEIGELT,               
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM 
AUTHOR   3 (SGC)                                                                
REVDAT   2   08-NOV-17 3SMT    1       REMARK                                   
REVDAT   1   20-JUL-11 3SMT    0                                                
JRNL        AUTH   H.ZENG,A.DONG,J.R.WALKER,P.LOPPNAU,C.BOUNTRA,J.WEIGELT,      
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,H.WU                        
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN SET DOMAIN-CONTAINING PROTEIN3    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 40086                          
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)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.208                          
REMARK   3   FREE R VALUE                      : 0.259                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 824                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.04                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.09                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2897                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2360                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2847                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2353                   
REMARK   3   BIN FREE R VALUE                        : 0.2791                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 1.73                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 50                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3645                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 301                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.29400                                             
REMARK   3    B22 (A**2) : -1.29400                                             
REMARK   3    B33 (A**2) : 2.58800                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.284               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3837   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5218   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1298   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 97     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 563    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3831   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 501    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4728   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.94                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.94                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066396.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VERIMAX HR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40192                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.90                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 40.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.94200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.94200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.760                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG4000, 0.2 M CALCIUM ACETATE,     
REMARK 280  0.1 M SODIUM CACODALYTE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 297K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       27.85667            
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       55.71333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       55.71333            
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       27.85667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.71333            
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     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     PRO A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     GLN A   224                                                      
REMARK 465     THR A   225                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     GLU A   493                                                      
REMARK 465     GLU A   494                                                      
REMARK 465     LYS A   495                                                      
REMARK 465     ALA A   496                                                      
REMARK 465     PRO A   497                                                      
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     LYS A  22    CG   CD   CE   NZ                                   
REMARK 470     ILE A  24    CG1  CG2  CD1                                       
REMARK 470     LEU A  25    CG   CD1  CD2                                       
REMARK 470     ASN A  26    CG   OD1  ND2                                       
REMARK 470     LEU A  32    CD1  CD2                                            
REMARK 470     GLN A  33    CG   CD   OE1  NE2                                  
REMARK 470     SER A  37    OG                                                  
REMARK 470     LYS A  44    CE   NZ                                             
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  52    CD1                                                 
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ILE A  59    CG1  CG2  CD1                                       
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LYS A  62    CG   CD   CE   NZ                                   
REMARK 470     LYS A  64    CG   CD   CE   NZ                                   
REMARK 470     LYS A  73    CG   CD   CE   NZ                                   
REMARK 470     LYS A  83    CD   CE   NZ                                        
REMARK 470     LYS A 101    CD   CE   NZ                                        
REMARK 470     GLU A 102    OE1  OE2                                            
REMARK 470     LYS A 125    CG   CD   CE   NZ                                   
REMARK 470     VAL A 137    CG1  CG2                                            
REMARK 470     LEU A 141    CG   CD1  CD2                                       
REMARK 470     GLN A 144    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 146    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 202    CD1                                                 
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     HIS A 228    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 230    CG   OD1  ND2                                       
REMARK 470     LYS A 231    CG   CD   CE   NZ                                   
REMARK 470     LYS A 235    CD   CE   NZ                                        
REMARK 470     ASP A 236    CG   OD1  OD2                                       
REMARK 470     GLU A 260    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 265    CG1  CG2                                            
REMARK 470     LEU A 289    CG   CD1  CD2                                       
REMARK 470     GLU A 290    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 303    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 339    CD   CE   NZ                                        
REMARK 470     LYS A 344    CD   CE   NZ                                        
REMARK 470     GLU A 414    CD   OE1  OE2                                       
REMARK 470     LYS A 441    CD   CE   NZ                                        
REMARK 470     LYS A 452    CD   CE   NZ                                        
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    LYS A  64       36.66    -98.59                                   
REMARK 500    GLU A 116        0.38     80.16                                   
REMARK 500    LEU A 272      -63.06     75.45                                   
REMARK 500    THR A 314       45.97    -82.24                                   
REMARK 500    ASP A 405       97.61    -69.80                                   
REMARK 500    PHE A 415       70.97   -119.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 A 4001                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARS A 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARS A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1001                
DBREF  3SMT A    1   497  UNP    Q86TU7   SETD3_HUMAN      2    498             
SEQRES   1 A  497  GLY LYS LYS SER ARG VAL LYS THR GLN LYS SER GLY THR          
SEQRES   2 A  497  GLY ALA THR ALA THR VAL SER PRO LYS GLU ILE LEU ASN          
SEQRES   3 A  497  LEU THR SER GLU LEU LEU GLN LYS CYS SER SER PRO ALA          
SEQRES   4 A  497  PRO GLY PRO GLY LYS GLU TRP GLU GLU TYR VAL GLN ILE          
SEQRES   5 A  497  ARG THR LEU VAL GLU LYS ILE ARG LYS LYS GLN LYS GLY          
SEQRES   6 A  497  LEU SER VAL THR PHE ASP GLY LYS ARG GLU ASP TYR PHE          
SEQRES   7 A  497  PRO ASP LEU MSE LYS TRP ALA SER GLU ASN GLY ALA SER          
SEQRES   8 A  497  VAL GLU GLY PHE GLU MSE VAL ASN PHE LYS GLU GLU GLY          
SEQRES   9 A  497  PHE GLY LEU ARG ALA THR ARG ASP ILE LYS ALA GLU GLU          
SEQRES  10 A  497  LEU PHE LEU TRP VAL PRO ARG LYS LEU LEU MSE THR VAL          
SEQRES  11 A  497  GLU SER ALA LYS ASN SER VAL LEU GLY PRO LEU TYR SER          
SEQRES  12 A  497  GLN ASP ARG ILE LEU GLN ALA MSE GLY ASN ILE ALA LEU          
SEQRES  13 A  497  ALA PHE HIS LEU LEU CYS GLU ARG ALA SER PRO ASN SER          
SEQRES  14 A  497  PHE TRP GLN PRO TYR ILE GLN THR LEU PRO SER GLU TYR          
SEQRES  15 A  497  ASP THR PRO LEU TYR PHE GLU GLU ASP GLU VAL ARG TYR          
SEQRES  16 A  497  LEU GLN SER THR GLN ALA ILE HIS ASP VAL PHE SER GLN          
SEQRES  17 A  497  TYR LYS ASN THR ALA ARG GLN TYR ALA TYR PHE TYR LYS          
SEQRES  18 A  497  VAL ILE GLN THR HIS PRO HIS ALA ASN LYS LEU PRO LEU          
SEQRES  19 A  497  LYS ASP SER PHE THR TYR GLU ASP TYR ARG TRP ALA VAL          
SEQRES  20 A  497  SER SER VAL MSE THR ARG GLN ASN GLN ILE PRO THR GLU          
SEQRES  21 A  497  ASP GLY SER ARG VAL THR LEU ALA LEU ILE PRO LEU TRP          
SEQRES  22 A  497  ASP MSE CYS ASN HIS THR ASN GLY LEU ILE THR THR GLY          
SEQRES  23 A  497  TYR ASN LEU GLU ASP ASP ARG CYS GLU CYS VAL ALA LEU          
SEQRES  24 A  497  GLN ASP PHE ARG ALA GLY GLU GLN ILE TYR ILE PHE TYR          
SEQRES  25 A  497  GLY THR ARG SER ASN ALA GLU PHE VAL ILE HIS SER GLY          
SEQRES  26 A  497  PHE PHE PHE ASP ASN ASN SER HIS ASP ARG VAL LYS ILE          
SEQRES  27 A  497  LYS LEU GLY VAL SER LYS SER ASP ARG LEU TYR ALA MSE          
SEQRES  28 A  497  LYS ALA GLU VAL LEU ALA ARG ALA GLY ILE PRO THR SER          
SEQRES  29 A  497  SER VAL PHE ALA LEU HIS PHE THR GLU PRO PRO ILE SER          
SEQRES  30 A  497  ALA GLN LEU LEU ALA PHE LEU ARG VAL PHE CYS MSE THR          
SEQRES  31 A  497  GLU GLU GLU LEU LYS GLU HIS LEU LEU GLY ASP SER ALA          
SEQRES  32 A  497  ILE ASP ARG ILE PHE THR LEU GLY ASN SER GLU PHE PRO          
SEQRES  33 A  497  VAL SER TRP ASP ASN GLU VAL LYS LEU TRP THR PHE LEU          
SEQRES  34 A  497  GLU ASP ARG ALA SER LEU LEU LEU LYS THR TYR LYS THR          
SEQRES  35 A  497  THR ILE GLU GLU ASP LYS SER VAL LEU LYS ASN HIS ASP          
SEQRES  36 A  497  LEU SER VAL ARG ALA LYS MSE ALA ILE LYS LEU ARG LEU          
SEQRES  37 A  497  GLY GLU LYS GLU ILE LEU GLU LYS ALA VAL LYS SER ALA          
SEQRES  38 A  497  ALA VAL ASN ARG GLU TYR TYR ARG GLN GLN MSE GLU GLU          
SEQRES  39 A  497  LYS ALA PRO                                                  
MODRES 3SMT MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A   97  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  128  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  151  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  251  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  275  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  351  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  389  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  462  MET  SELENOMETHIONINE                                   
MODRES 3SMT MSE A  492  MET  SELENOMETHIONINE                                   
HET    MSE  A  82       8                                                       
HET    MSE  A  97       8                                                       
HET    MSE  A 128       8                                                       
HET    MSE  A 151       8                                                       
HET    MSE  A 251       8                                                       
HET    MSE  A 275       8                                                       
HET    MSE  A 351       8                                                       
HET    MSE  A 389       8                                                       
HET    MSE  A 462       8                                                       
HET    MSE  A 492       8                                                       
HET    SAM  A1000      27                                                       
HET    ARS  A 498       1                                                       
HET    ARS  A 499       1                                                       
HET    PG4  A4001       7                                                       
HET    ACT  A 500       4                                                       
HET    ACT  A1001       4                                                       
HET    UNX  A 501       1                                                       
HET    UNX  A 502       1                                                       
HET    UNX  A 503       1                                                       
HET    UNX  A 504       1                                                       
HET    UNX  A 505       1                                                       
HET    UNX  A 506       1                                                       
HET    UNX  A 507       1                                                       
HET    UNX  A 508       1                                                       
HET    UNX  A 509       1                                                       
HET    UNX  A 510       1                                                       
HET    UNX  A 511       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     ARS ARSENIC                                                          
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     ACT ACETATE ION                                                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  ARS    2(AS)                                                        
FORMUL   5  PG4    C8 H18 O5                                                    
FORMUL   6  ACT    2(C2 H3 O2 1-)                                               
FORMUL   8  UNX    11(X)                                                        
FORMUL  19  HOH   *301(H2 O)                                                    
HELIX    1   1 SER A   20  CYS A   35  1                                  16    
HELIX    2   2 LYS A   44  LYS A   62  1                                  19    
HELIX    3   3 LYS A   73  ASP A   76  5                                   4    
HELIX    4   4 TYR A   77  ASN A   88  1                                  12    
HELIX    5   5 LYS A  125  LEU A  127  5                                   3    
HELIX    6   6 VAL A  130  ASN A  135  1                                   6    
HELIX    7   7 LEU A  138  ASP A  145  1                                   8    
HELIX    8   8 ASP A  145  MSE A  151  1                                   7    
HELIX    9   9 MSE A  151  ALA A  165  1                                  15    
HELIX   10  10 TRP A  171  GLN A  176  1                                   6    
HELIX   11  11 THR A  184  PHE A  188  5                                   5    
HELIX   12  12 GLU A  189  TYR A  195  1                                   7    
HELIX   13  13 GLN A  200  ILE A  223  1                                  24    
HELIX   14  14 THR A  239  GLN A  254  1                                  16    
HELIX   15  15 LEU A  272  CYS A  276  5                                   5    
HELIX   16  16 SER A  316  GLY A  325  1                                  10    
HELIX   17  17 LEU A  348  ALA A  359  1                                  12    
HELIX   18  18 SER A  377  CYS A  388  1                                  12    
HELIX   19  19 THR A  390  GLY A  400  1                                  11    
HELIX   20  20 SER A  418  THR A  439  1                                  22    
HELIX   21  21 THR A  443  LEU A  451  1                                   9    
HELIX   22  22 SER A  457  GLN A  490  1                                  34    
SHEET    1   A 4 PHE A  95  PHE A 100  0                                        
SHEET    2   A 4 GLY A 104  ALA A 109 -1  O  ARG A 108   N  GLU A  96           
SHEET    3   A 4 GLN A 307  ILE A 310 -1  O  ILE A 308   N  LEU A 107           
SHEET    4   A 4 ASN A 277  HIS A 278  1  N  ASN A 277   O  ILE A 310           
SHEET    1   B 3 LEU A 118  PRO A 123  0                                        
SHEET    2   B 3 ARG A 293  ALA A 298 -1  O  CYS A 296   N  LEU A 120           
SHEET    3   B 3 ILE A 283  ASN A 288 -1  N  GLY A 286   O  GLU A 295           
SHEET    1   C 3 MSE A 128  THR A 129  0                                        
SHEET    2   C 3 VAL A 265  LEU A 269 -1  O  LEU A 269   N  MSE A 128           
SHEET    3   C 3 ASN A 255  PRO A 258 -1  N  ILE A 257   O  THR A 266           
SHEET    1   D 2 ARG A 335  GLY A 341  0                                        
SHEET    2   D 2 SER A 364  HIS A 370 -1  O  PHE A 367   N  ILE A 338           
LINK         C   LEU A  81                 N   MSE A  82     1555   1555  1.34  
LINK         C   MSE A  82                 N   LYS A  83     1555   1555  1.36  
LINK         C   GLU A  96                 N   MSE A  97     1555   1555  1.34  
LINK         C   MSE A  97                 N   VAL A  98     1555   1555  1.34  
LINK         C   LEU A 127                 N   MSE A 128     1555   1555  1.33  
LINK         C   MSE A 128                 N   THR A 129     1555   1555  1.34  
LINK         C   ALA A 150                 N   MSE A 151     1555   1555  1.35  
LINK         C   MSE A 151                 N   GLY A 152     1555   1555  1.34  
LINK         C   VAL A 250                 N   MSE A 251     1555   1555  1.34  
LINK         C   MSE A 251                 N   THR A 252     1555   1555  1.36  
LINK         C   ASP A 274                 N   MSE A 275     1555   1555  1.36  
LINK         C   MSE A 275                 N   CYS A 276     1555   1555  1.37  
LINK         C   ALA A 350                 N   MSE A 351     1555   1555  1.35  
LINK         C   MSE A 351                 N   LYS A 352     1555   1555  1.35  
LINK         C   CYS A 388                 N   MSE A 389     1555   1555  1.33  
LINK         C   MSE A 389                 N   THR A 390     1555   1555  1.34  
LINK         C   LYS A 461                 N   MSE A 462     1555   1555  1.34  
LINK         C   MSE A 462                 N   ALA A 463     1555   1555  1.37  
LINK         C   GLN A 491                 N   MSE A 492     1555   1555  1.34  
CISPEP   1 GLU A  373    PRO A  374          0        -7.33                     
SITE     1 AC1 21 ARG A  74  GLU A 102  GLU A 103  PHE A 105                    
SITE     2 AC1 21 THR A 252  ARG A 253  ASP A 274  MSE A 275                    
SITE     3 AC1 21 CYS A 276  ASN A 277  HIS A 278  TYR A 312                    
SITE     4 AC1 21 SER A 324  PHE A 326  PHE A 328  HOH A 515                    
SITE     5 AC1 21 HOH A 545  HOH A 569  HOH A 603  HOH A 762                    
SITE     6 AC1 21 HOH A 794                                                     
SITE     1 AC2  1 CYS A 296                                                     
SITE     1 AC3  1 CYS A 294                                                     
SITE     1 AC4  8 PHE A 100  ARG A 108  GLY A 305  GLU A 306                    
SITE     2 AC4  8 GLN A 307  ASP A 455  HOH A 525  HOH A 718                    
SITE     1 AC5  6 PHE A 367  ALA A 368  SER A 377  GLN A 379                    
SITE     2 AC5  6 HOH A 753  HOH A 789                                          
SITE     1 AC6  6 LEU A 340  GLY A 341  PHE A 387  PHE A 428                    
SITE     2 AC6  6 ARG A 432  HOH A 655                                          
CRYST1  113.864  113.864   83.570  90.00  90.00 120.00 P 31 2 1      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      0.008782  0.005071  0.000000        0.00000                         
SCALE2      0.000000  0.010141  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011966        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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