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Database: PDB
Entry: 5XXG
LinkDB: 5XXG
Original site: 5XXG 
HEADER    TRANSFERASE/INHIBITOR                   03-JUL-17   5XXG              
TITLE     CRYSTAL STRUCTURE OF SMYD3 IN COMPLEX WITH COVALENT INHIBITOR 2       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SMYD3;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METHYLTRANSFERASE, COVALENT INHIBITOR, SMYD3, TRANSFERASE,            
KEYWDS   2 TRANSFERASE-INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABURAJENDRAN,E.A.JANSSON                                           
REVDAT   1   08-AUG-18 5XXG    0                                                
JRNL        AUTH   N.BABURAJENDRAN,E.A.JANSSON                                  
JRNL        TITL   CRYSTAL STRUCTURE OF SMYD3 IN COMPLEX WITH COVALENT          
JRNL        TITL 2 INHIBITOR 2                                                  
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) : 29.47                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24820                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2008                            
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 29.4686 -  5.1356    0.97     1719   150  0.1694 0.2147        
REMARK   3     2  5.1356 -  4.0797    0.99     1670   149  0.1512 0.1971        
REMARK   3     3  4.0797 -  3.5650    1.00     1665   139  0.1600 0.1987        
REMARK   3     4  3.5650 -  3.2395    1.00     1629   150  0.1873 0.2482        
REMARK   3     5  3.2395 -  3.0076    1.00     1635   149  0.1996 0.2370        
REMARK   3     6  3.0076 -  2.8304    0.99     1642   134  0.2157 0.2944        
REMARK   3     7  2.8304 -  2.6887    1.00     1614   147  0.2009 0.2643        
REMARK   3     8  2.6887 -  2.5718    1.00     1612   145  0.2034 0.2750        
REMARK   3     9  2.5718 -  2.4728    1.00     1624   131  0.2029 0.2796        
REMARK   3    10  2.4728 -  2.3875    1.00     1604   155  0.1981 0.2520        
REMARK   3    11  2.3875 -  2.3129    1.00     1628   137  0.2017 0.2979        
REMARK   3    12  2.3129 -  2.2468    1.00     1615   140  0.2068 0.2799        
REMARK   3    13  2.2468 -  2.1877    1.00     1600   146  0.2056 0.2862        
REMARK   3    14  2.1877 -  2.1343    0.96     1555   136  0.2066 0.3024        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.17                          
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      :  0.007           3488                                  
REMARK   3   ANGLE     :  0.867           4715                                  
REMARK   3   CHIRALITY :  0.050            519                                  
REMARK   3   PLANARITY :  0.005            608                                  
REMARK   3   DIHEDRAL  :  5.077           2995                                  
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 5XXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004327.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-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) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24864                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.140                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.16600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54700                            
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM ACETATE AND 17% PEG      
REMARK 280  3350, 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       30.64400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.64800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.18700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.64800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.64400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.18700            
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       16.14   -149.36                                   
REMARK 500    TYR A 124      134.42   -170.30                                   
REMARK 500    LYS A 271       -0.41     78.55                                   
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 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  49   SG                                                     
REMARK 620 2 CYS A  52   SG  106.9                                              
REMARK 620 3 CYS A  71   SG  113.3 110.7                                        
REMARK 620 4 CYS A  75   SG  108.4 115.4 102.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  62   SG                                                     
REMARK 620 2 CYS A  65   SG  112.0                                              
REMARK 620 3 HIS A  83   NE2 110.6 107.1                                        
REMARK 620 4 CYS A  87   SG  111.9 111.7 103.2                                  
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  115.7                                              
REMARK 620 3 CYS A 263   SG  111.4 103.7                                        
REMARK 620 4 CYS A 266   SG  102.6 112.3 111.4                                  
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 8HR A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM 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 ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS STATE THAT THE GENEBANK ACCESSION NUMBER IS AAH31010.1 FOR   
REMARK 999 THIS SEQUENCE.                                                       
DBREF  5XXG A    3   425  PDB    5XXG     5XXG             3    425             
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    8HR  A 501      30                                                       
HET    SAM  A 502      27                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  A 505       1                                                       
HETNAM     8HR PROPYL 4-(4-CHLORANYL-2-PHENYL-QUINOLIN-7-YL)                    
HETNAM   2 8HR  CARBONYLPIPERAZINE-1-CARBOXYLATE                                
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
FORMUL   2  8HR    C24 H24 CL N3 O3                                             
FORMUL   3  SAM    C15 H22 N6 O5 S                                              
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *157(H2 O)                                                    
HELIX    1 AA1 LYS A   42  ARG A   45  5                                   4    
HELIX    2 AA2 SER A   72  CYS A   93  1                                  22    
HELIX    3 AA3 PRO A   99  GLY A  115  1                                  17    
HELIX    4 AA4 SER A  118  LYS A  122  5                                   5    
HELIX    5 AA5 SER A  125  LEU A  129  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  SER A  182  1                                  13    
HELIX   10 AB1 SER A  200  LEU A  204  5                                   5    
HELIX   11 AB2 THR A  245  CYS A  258  1                                  14    
HELIX   12 AB3 CYS A  263  THR A  268  1                                   6    
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  LEU A  341  1                                  18    
HELIX   17 AB8 LEU A  343  PHE A  362  1                                  20    
HELIX   18 AB9 HIS A  366  GLN A  383  1                                  18    
HELIX   19 AC1 MET A  385  HIS A  404  1                                  20    
HELIX   20 AC2 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 PHE A 183  CYS A 186 -1  N  PHE A 183   O  GLY A 196           
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 504     1555   1555  2.42  
LINK         SG  CYS A  52                ZN    ZN A 504     1555   1555  2.38  
LINK         SG  CYS A  62                ZN    ZN A 505     1555   1555  2.35  
LINK         SG  CYS A  65                ZN    ZN A 505     1555   1555  2.38  
LINK         SG  CYS A  71                ZN    ZN A 504     1555   1555  2.35  
LINK         SG  CYS A  75                ZN    ZN A 504     1555   1555  2.20  
LINK         NE2 HIS A  83                ZN    ZN A 505     1555   1555  2.09  
LINK         SG  CYS A  87                ZN    ZN A 505     1555   1555  2.28  
LINK         SG  CYS A 186                 CAJ 8HR A 501     1555   1555  1.75  
LINK         SG  CYS A 208                ZN    ZN A 503     1555   1555  2.30  
LINK         SG  CYS A 261                ZN    ZN A 503     1555   1555  2.28  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A 266                ZN    ZN A 503     1555   1555  2.34  
CISPEP   1 LYS A   94    PRO A   95          0         2.11                     
SITE     1 AC1 19 ASN A 181  SER A 182  PHE A 183  THR A 184                    
SITE     2 AC1 19 CYS A 186  MET A 190  SER A 202  ILE A 214                    
SITE     3 AC1 19 PHE A 216  CYS A 238  TYR A 239  TYR A 257                    
SITE     4 AC1 19 VAL A 368  SAM A 502  HOH A 601  HOH A 627                    
SITE     5 AC1 19 HOH A 642  HOH A 694  HOH A 748                               
SITE     1 AC2 22 ARG A  14  ASN A  16  TYR A 124  GLU A 130                    
SITE     2 AC2 22 ASN A 132  CYS A 180  ASN A 181  SER A 202                    
SITE     3 AC2 22 LEU A 203  LEU A 204  ASN A 205  HIS A 206                    
SITE     4 AC2 22 TYR A 239  TYR A 257  PHE A 259  8HR A 501                    
SITE     5 AC2 22 HOH A 605  HOH A 611  HOH A 666  HOH A 707                    
SITE     6 AC2 22 HOH A 720  HOH A 728                                          
SITE     1 AC3  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC4  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC5  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
CRYST1   61.288   66.374  107.296  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      0.016316  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015066  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009320        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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