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Database: PDB
Entry: 5YJO
LinkDB: 5YJO
Original site: 5YJO 
HEADER    TRANSFERASE/INHIBITOR                   11-OCT-17   5YJO              
TITLE     CRYSTAL STRUCTURE OF SMYD3 IN COMPLEX WITH COVALENT INHIBITOR 4       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET AND MYND DOMAIN-CONTAINING PROTEIN 3,ZINC FINGER MYND   
COMPND   5 DOMAIN-CONTAINING PROTEIN 1;                                         
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 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                                         
KEYWDS    COVALENT INHIBITOR, METHYLTRANSFERASE, METHYLTRANSFERASE INHIBITOR,   
KEYWDS   2 TRANSFERASE-INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABURAJENDRAN,J.ANNA E                                              
REVDAT   1   17-OCT-18 5YJO    0                                                
JRNL        AUTH   N.BABURAJENDRAN,J.ANNA E                                     
JRNL        TITL   CRYSTAL STRUCTURE OF SMYD3 IN COMPLEX WITH COVALENT          
JRNL        TITL 2 INHIBITOR 4                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24817                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2027                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 31.6333 -  5.1398    0.99     1751   157  0.1659 0.1674        
REMARK   3     2  5.1398 -  4.0823    1.00     1688   149  0.1498 0.1823        
REMARK   3     3  4.0823 -  3.5671    1.00     1656   153  0.1650 0.2244        
REMARK   3     4  3.5671 -  3.2413    1.00     1643   140  0.1921 0.2247        
REMARK   3     5  3.2413 -  3.0092    1.00     1636   150  0.2131 0.2467        
REMARK   3     6  3.0092 -  2.8319    1.00     1631   147  0.2231 0.2588        
REMARK   3     7  2.8319 -  2.6901    1.00     1626   142  0.2066 0.2849        
REMARK   3     8  2.6901 -  2.5731    1.00     1614   142  0.2162 0.2771        
REMARK   3     9  2.5731 -  2.4741    0.99     1623   136  0.2129 0.2801        
REMARK   3    10  2.4741 -  2.3887    0.99     1597   148  0.2086 0.2510        
REMARK   3    11  2.3887 -  2.3141    0.99     1622   138  0.2034 0.2409        
REMARK   3    12  2.3141 -  2.2479    0.99     1598   133  0.2020 0.2734        
REMARK   3    13  2.2479 -  2.1888    0.99     1568   155  0.2084 0.2597        
REMARK   3    14  2.1888 -  2.1354    0.95     1537   137  0.2161 0.2647        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.85                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           3467                                  
REMARK   3   ANGLE     :  0.525           4681                                  
REMARK   3   CHIRALITY :  0.038            516                                  
REMARK   3   PLANARITY :  0.003            601                                  
REMARK   3   DIHEDRAL  :  6.279           2154                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5YJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005405.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5419                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24856                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.135                              
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     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.16500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
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: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE, 17% PEG3350,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
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       30.71400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.82400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.09050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.82400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.71400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.09050            
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: 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ARG A  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 281    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     LYS A 391    CG   CD   CE   NZ                                   
REMARK 470     ASP A 422    CG   OD1  OD2                                       
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       17.67   -144.84                                   
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 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  49   SG                                                     
REMARK 620 2 CYS A  52   SG  107.7                                              
REMARK 620 3 CYS A  71   SG  114.0 106.5                                        
REMARK 620 4 CYS A  75   SG  108.7 116.4 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  62   SG                                                     
REMARK 620 2 CYS A  65   SG  109.2                                              
REMARK 620 3 HIS A  83   NE2 114.3 109.2                                        
REMARK 620 4 CYS A  87   SG  110.4 110.3 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 208   SG                                                     
REMARK 620 2 CYS A 261   SG  114.4                                              
REMARK 620 3 CYS A 263   SG  109.6 108.4                                        
REMARK 620 4 CYS A 266   SG  101.8 111.9 110.5                                  
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8W0 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 505                 
DBREF  5YJO A    3   425  UNP    Q9H7B4   SMYD3_HUMAN      3    425             
SEQADV 5YJO ASN A   13  UNP  Q9H7B4    LYS    13 ENGINEERED MUTATION            
SEQADV 5YJO ARG A  140  UNP  Q9H7B4    LYS   140 ENGINEERED MUTATION            
SEQRES   1 A  423  PRO LEU LYS VAL GLU LYS PHE ALA THR ALA ASN ARG GLY          
SEQRES   2 A  423  ASN GLY LEU ARG ALA VAL THR PRO LEU ARG PRO GLY GLU          
SEQRES   3 A  423  LEU LEU PHE ARG SER ASP PRO LEU ALA TYR THR VAL CYS          
SEQRES   4 A  423  LYS GLY SER ARG GLY VAL VAL CYS ASP ARG CYS LEU LEU          
SEQRES   5 A  423  GLY LYS GLU LYS LEU MET ARG CYS SER GLN CYS ARG VAL          
SEQRES   6 A  423  ALA LYS TYR CYS SER ALA LYS CYS GLN LYS LYS ALA TRP          
SEQRES   7 A  423  PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS SER CYS          
SEQRES   8 A  423  LYS PRO ARG TYR PRO PRO ASP SER VAL ARG LEU LEU GLY          
SEQRES   9 A  423  ARG VAL VAL PHE LYS LEU MET ASP GLY ALA PRO SER GLU          
SEQRES  10 A  423  SER GLU LYS LEU TYR SER PHE TYR ASP LEU GLU SER ASN          
SEQRES  11 A  423  ILE ASN LYS LEU THR GLU ASP ARG LYS GLU GLY LEU ARG          
SEQRES  12 A  423  GLN LEU VAL MET THR PHE GLN HIS PHE MET ARG GLU GLU          
SEQRES  13 A  423  ILE GLN ASP ALA SER GLN LEU PRO PRO ALA PHE ASP LEU          
SEQRES  14 A  423  PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN SER PHE THR          
SEQRES  15 A  423  ILE CYS ASN ALA GLU MET GLN GLU VAL GLY VAL GLY LEU          
SEQRES  16 A  423  TYR PRO SER ILE SER LEU LEU ASN HIS SER CYS ASP PRO          
SEQRES  17 A  423  ASN CYS SER ILE VAL PHE ASN GLY PRO HIS LEU LEU LEU          
SEQRES  18 A  423  ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU LEU THR          
SEQRES  19 A  423  ILE CYS TYR LEU ASP MET LEU MET THR SER GLU GLU ARG          
SEQRES  20 A  423  ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU CYS ASP          
SEQRES  21 A  423  CYS PHE ARG CYS GLN THR GLN ASP LYS ASP ALA ASP MET          
SEQRES  22 A  423  LEU THR GLY ASP GLU GLN VAL TRP LYS GLU VAL GLN GLU          
SEQRES  23 A  423  SER LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS TRP LYS          
SEQRES  24 A  423  TRP GLU GLN VAL LEU ALA MET CYS GLN ALA ILE ILE SER          
SEQRES  25 A  423  SER ASN SER GLU ARG LEU PRO ASP ILE ASN ILE TYR GLN          
SEQRES  26 A  423  LEU LYS VAL LEU ASP CYS ALA MET ASP ALA CYS ILE ASN          
SEQRES  27 A  423  LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY THR ARG          
SEQRES  28 A  423  THR MET GLU PRO TYR ARG ILE PHE PHE PRO GLY SER HIS          
SEQRES  29 A  423  PRO VAL ARG GLY VAL GLN VAL MET LYS VAL GLY LYS LEU          
SEQRES  30 A  423  GLN LEU HIS GLN GLY MET PHE PRO GLN ALA MET LYS ASN          
SEQRES  31 A  423  LEU ARG LEU ALA PHE ASP ILE MET ARG VAL THR HIS GLY          
SEQRES  32 A  423  ARG GLU HIS SER LEU ILE GLU ASP LEU ILE LEU LEU LEU          
SEQRES  33 A  423  GLU GLU CYS ASP ALA ASN ILE                                  
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    8W0  A 504      31                                                       
HET    SAM  A 505      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     8W0 PROPYL (3~{S})-4-[[(6~{R})-6-(AMINOMETHYL)-5,6,7,8-              
HETNAM   2 8W0  TETRAHYDROACRIDIN-3-YL]CARBONYL]-3-METHYL-PIPERAZINE-           
HETNAM   3 8W0  1-CARBOXYLATE                                                   
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  8W0    C24 H32 N4 O3                                                
FORMUL   6  SAM    C15 H22 N6 O5 S                                              
FORMUL   7  HOH   *158(H2 O)                                                    
HELIX    1 AA1 LYS A   42  ARG A   45  5                                   4    
HELIX    2 AA2 SER A   72  ALA A   79  1                                   8    
HELIX    3 AA3 ALA A   79  CYS A   93  1                                  15    
HELIX    4 AA4 PRO A   99  GLY A  115  1                                  17    
HELIX    5 AA5 SER A  118  LYS A  122  5                                   5    
HELIX    6 AA6 ASN A  132  LEU A  136  5                                   5    
HELIX    7 AA7 THR A  137  MET A  155  1                                  19    
HELIX    8 AA8 ASP A  161  LEU A  165  5                                   5    
HELIX    9 AA9 ASP A  170  CYS A  180  1                                  11    
HELIX   10 AB1 SER A  200  LEU A  204  5                                   5    
HELIX   11 AB2 THR A  245  GLN A  256  1                                  12    
HELIX   12 AB3 CYS A  263  GLN A  269  1                                   7    
HELIX   13 AB4 LYS A  271  LEU A  276  1                                   6    
HELIX   14 AB5 ASP A  279  HIS A  299  1                                  21    
HELIX   15 AB6 LYS A  301  SER A  314  1                                  14    
HELIX   16 AB7 ASN A  324  GLY A  342  1                                  19    
HELIX   17 AB8 LEU A  343  THR A  354  1                                  12    
HELIX   18 AB9 THR A  354  PHE A  362  1                                   9    
HELIX   19 AC1 HIS A  366  GLY A  384  1                                  19    
HELIX   20 AC2 MET A  385  HIS A  404  1                                  20    
HELIX   21 AC3 HIS A  408  ILE A  425  1                                  18    
SHEET    1 AA1 4 VAL A   6  ALA A  10  0                                        
SHEET    2 AA1 4 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    3 AA1 4 GLU A 234  ILE A 237 -1  O  LEU A 235   N  LEU A  18           
SHEET    4 AA1 4 ASN A 205  HIS A 206  1  N  ASN A 205   O  ILE A 237           
SHEET    1 AA2 3 LEU A  29  SER A  33  0                                        
SHEET    2 AA2 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  LEU A  30           
SHEET    3 AA2 3 CYS A 212  ASN A 217 -1  N  SER A 213   O  ARG A 224           
SHEET    1 AA3 3 ALA A  37  VAL A  40  0                                        
SHEET    2 AA3 3 GLU A 192  LEU A 197 -1  O  LEU A 197   N  ALA A  37           
SHEET    3 AA3 3 SER A 182  CYS A 186 -1  N  ILE A 185   O  VAL A 193           
SHEET    1 AA4 2 MET A  60  ARG A  61  0                                        
SHEET    2 AA4 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
LINK         SG  CYS A  49                ZN    ZN A 502     1555   1555  2.36  
LINK         SG  CYS A  52                ZN    ZN A 502     1555   1555  2.33  
LINK         SG  CYS A  62                ZN    ZN A 501     1555   1555  2.35  
LINK         SG  CYS A  65                ZN    ZN A 501     1555   1555  2.31  
LINK         SG  CYS A  71                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A  75                ZN    ZN A 502     1555   1555  2.29  
LINK         NE2 HIS A  83                ZN    ZN A 501     1555   1555  2.05  
LINK         SG  CYS A  87                ZN    ZN A 501     1555   1555  2.27  
LINK         SG  CYS A 186                 CAJ 8W0 A 504     1555   1555  1.77  
LINK         SG  CYS A 208                ZN    ZN A 503     1555   1555  2.31  
LINK         SG  CYS A 261                ZN    ZN A 503     1555   1555  2.27  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS A 266                ZN    ZN A 503     1555   1555  2.33  
CISPEP   1 LYS A   94    PRO A   95          0         0.22                     
SITE     1 AC1  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC2  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC3  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC4 17 ASN A 181  SER A 182  PHE A 183  THR A 184                    
SITE     2 AC4 17 CYS A 186  MET A 190  ILE A 214  PHE A 216                    
SITE     3 AC4 17 CYS A 238  TYR A 239  ASP A 241  TYR A 257                    
SITE     4 AC4 17 SAM A 505  HOH A 603  HOH A 672  HOH A 694                    
SITE     5 AC4 17 HOH A 721                                                     
SITE     1 AC5 23 ARG A  14  ASN A  16  TYR A 124  GLU A 130                    
SITE     2 AC5 23 ASN A 132  CYS A 180  ASN A 181  SER A 202                    
SITE     3 AC5 23 LEU A 203  LEU A 204  ASN A 205  HIS A 206                    
SITE     4 AC5 23 TYR A 239  TYR A 257  PHE A 259  8W0 A 504                    
SITE     5 AC5 23 HOH A 604  HOH A 638  HOH A 653  HOH A 698                    
SITE     6 AC5 23 HOH A 711  HOH A 715  HOH A 723                               
CRYST1   61.428   66.181  107.648  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      0.016279  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015110  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009290        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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