GenomeNet

Database: PDB
Entry: 6BOX
LinkDB: 6BOX
Original site: 6BOX 
HEADER    TRANSFERASE                             21-NOV-17   6BOX              
TITLE     STRUCTURE OF THE S. POMBE CLR4 CATALYTIC DOMAIN BOUND TO SAH          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC;  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CRYPTIC LOCI REGULATOR 4,HISTONE H3-K9 METHYLTRANSFERASE,H3-
COMPND   5 K9-HMTASE,LYSINE N-METHYLTRANSFERASE 1;                              
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC    
SOURCE   3 24843);                                                              
SOURCE   4 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 284812;                                              
SOURCE   6 STRAIN: 972 / ATCC 24843;                                            
SOURCE   7 GENE: CLR4, KMT1, SPBC428.08C;                                       
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METHYLTRANSFERASE, SET DOMAIN, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.CURRIE,D.MOAZED                                                   
REVDAT   5   20-FEB-19 6BOX    1       REMARK                                   
REVDAT   4   05-SEP-18 6BOX    1       JRNL                                     
REVDAT   3   22-AUG-18 6BOX    1       JRNL                                     
REVDAT   2   15-AUG-18 6BOX    1       JRNL                                     
REVDAT   1   25-JUL-18 6BOX    0                                                
JRNL        AUTH   N.IGLESIAS,M.A.CURRIE,G.JIH,J.A.PAULO,N.SIUTI,M.KALOCSAY,    
JRNL        AUTH 2 S.P.GYGI,D.MOAZED                                            
JRNL        TITL   AUTOMETHYLATION-INDUCED CONFORMATIONAL SWITCH IN CLR4        
JRNL        TITL 2 (SUV39H) MAINTAINS EPIGENETIC STABILITY.                     
JRNL        REF    NATURE                        V. 560   504 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   30051891                                                     
JRNL        DOI    10.1038/S41586-018-0398-2                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 24906                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1268                            
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 54.2053 -  5.0160    1.00     2762   170  0.1970 0.2515        
REMARK   3     2  5.0160 -  3.9817    1.00     2730   139  0.1748 0.2035        
REMARK   3     3  3.9817 -  3.4785    1.00     2707   158  0.2043 0.2540        
REMARK   3     4  3.4785 -  3.1605    1.00     2724   142  0.2298 0.2692        
REMARK   3     5  3.1605 -  2.9340    1.00     2712   140  0.2655 0.3218        
REMARK   3     6  2.9340 -  2.7610    1.00     2701   139  0.2682 0.2996        
REMARK   3     7  2.7610 -  2.6227    1.00     2713   136  0.3028 0.3608        
REMARK   3     8  2.6227 -  2.5086    0.99     2668   131  0.3381 0.3574        
REMARK   3     9  2.5086 -  2.4120    0.71     1921   113  0.3955 0.4380        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.930           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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           4429                                  
REMARK   3   ANGLE     :  0.532           5993                                  
REMARK   3   CHIRALITY :  0.042            633                                  
REMARK   3   PLANARITY :  0.003            791                                  
REMARK   3   DIHEDRAL  : 21.454           1609                                  
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 6BOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231202.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24906                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.410                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.205                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1MVH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM CALCIUM ACETATE, 100 MM           
REMARK 280  IMIDAZOLE, PH 7.5, 15% PEG 8,000, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       62.81250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.62750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       62.81250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.62750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   188                                                      
REMARK 465     PRO A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     LEU A   194                                                      
REMARK 465     ASP A   371                                                      
REMARK 465     LYS A   372                                                      
REMARK 465     ASN A   373                                                      
REMARK 465     TYR A   374                                                      
REMARK 465     ASP A   375                                                      
REMARK 465     ASP A   376                                                      
REMARK 465     ASP A   377                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     ILE A   379                                                      
REMARK 465     ASP A   390                                                      
REMARK 465     ALA A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     VAL A   460                                                      
REMARK 465     GLN A   461                                                      
REMARK 465     SER A   462                                                      
REMARK 465     GLN A   463                                                      
REMARK 465     LYS A   464                                                      
REMARK 465     SER A   465                                                      
REMARK 465     GLN A   466                                                      
REMARK 465     GLN A   467                                                      
REMARK 465     ASN A   468                                                      
REMARK 465     ARG A   469                                                      
REMARK 465     ILE A   470                                                      
REMARK 465     SER A   471                                                      
REMARK 465     LYS A   472                                                      
REMARK 465     GLY A   490                                                      
REMARK 465     GLY B   188                                                      
REMARK 465     PRO B   189                                                      
REMARK 465     LEU B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     SER B   192                                                      
REMARK 465     LYS B   193                                                      
REMARK 465     LEU B   194                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     LYS B   372                                                      
REMARK 465     ASN B   373                                                      
REMARK 465     TYR B   374                                                      
REMARK 465     ASP B   375                                                      
REMARK 465     ASP B   376                                                      
REMARK 465     ASP B   377                                                      
REMARK 465     GLY B   378                                                      
REMARK 465     LYS B   455                                                      
REMARK 465     ASP B   456                                                      
REMARK 465     PHE B   457                                                      
REMARK 465     SER B   458                                                      
REMARK 465     PRO B   459                                                      
REMARK 465     VAL B   460                                                      
REMARK 465     GLN B   461                                                      
REMARK 465     SER B   462                                                      
REMARK 465     GLN B   463                                                      
REMARK 465     LYS B   464                                                      
REMARK 465     SER B   465                                                      
REMARK 465     GLN B   466                                                      
REMARK 465     GLN B   467                                                      
REMARK 465     ASN B   468                                                      
REMARK 465     ARG B   469                                                      
REMARK 465     ILE B   470                                                      
REMARK 465     SER B   471                                                      
REMARK 465     LYS B   472                                                      
REMARK 465     LEU B   473                                                      
REMARK 465     PHE B   489                                                      
REMARK 465     GLY B   490                                                      
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    ASP A 228     -152.12   -138.90                                   
REMARK 500    CYS A 262      -40.40   -148.06                                   
REMARK 500    SER A 263      -97.89     43.95                                   
REMARK 500    SER A 264     -157.09     57.74                                   
REMARK 500    ASN A 272       62.74   -118.34                                   
REMARK 500    ARG A 275      -36.73     80.04                                   
REMARK 500    THR A 355     -179.31   -171.02                                   
REMARK 500    ALA A 454      -70.81   -103.74                                   
REMARK 500    ARG A 474     -153.75   -125.59                                   
REMARK 500    ASP B 228     -151.84   -138.58                                   
REMARK 500    ASN B 272       61.55   -119.74                                   
REMARK 500    ASP B 283     -161.88    -78.17                                   
REMARK 500    PRO B 285       75.05    -69.79                                   
REMARK 500    THR B 355     -179.84   -170.63                                   
REMARK 500    THR B 380     -109.79   -148.24                                   
REMARK 500    TYR B 381       22.78     81.18                                   
REMARK 500    LEU B 385       62.26   -102.76                                   
REMARK 500    PHE B 388      -77.60   -104.98                                   
REMARK 500    ARG B 428       52.91    -91.25                                   
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 260   SG                                                     
REMARK 620 2 CYS A 262   SG   99.7                                              
REMARK 620 3 CYS A 268   SG  111.7  97.2                                        
REMARK 620 4 CYS A 276   SG  112.6 110.4 121.8                                  
REMARK 620 N                    1     2     3                                   
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 260   SG                                                     
REMARK 620 2 CYS A 278   SG  115.5                                              
REMARK 620 3 CYS A 307   SG  115.2 108.6                                        
REMARK 620 4 CYS A 311   SG  102.0  98.5 115.9                                  
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 268   SG                                                     
REMARK 620 2 CYS A 307   SG  104.7                                              
REMARK 620 3 CYS A 313   SG  112.0 115.3                                        
REMARK 620 4 CYS A 317   SG   95.1 123.6 104.2                                  
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 412   SG                                                     
REMARK 620 2 CYS A 477   SG  116.8                                              
REMARK 620 3 CYS A 479   SG  107.9 109.1                                        
REMARK 620 4 CYS A 484   SG  104.1 120.7  95.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 260   SG                                                     
REMARK 620 2 CYS B 278   SG  119.5                                              
REMARK 620 3 CYS B 307   SG  115.0 108.6                                        
REMARK 620 4 CYS B 311   SG  100.7  96.9 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 260   SG                                                     
REMARK 620 2 CYS B 262   SG   97.9                                              
REMARK 620 3 CYS B 268   SG  102.5  92.3                                        
REMARK 620 4 CYS B 276   SG  105.1 125.5 128.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 268   SG                                                     
REMARK 620 2 CYS B 307   SG  107.2                                              
REMARK 620 3 CYS B 313   SG  114.3 111.7                                        
REMARK 620 4 CYS B 317   SG  100.1 122.7 100.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 412   SG                                                     
REMARK 620 2 CYS B 477   SG  110.4                                              
REMARK 620 3 CYS B 479   SG  114.8 102.0                                        
REMARK 620 4 CYS B 484   SG  106.2 106.8 116.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 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 ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 505                 
DBREF  6BOX A  192   490  UNP    O60016   CLR4_SCHPO     192    490             
DBREF  6BOX B  192   490  UNP    O60016   CLR4_SCHPO     192    490             
SEQADV 6BOX GLY A  188  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX PRO A  189  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX LEU A  190  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX GLY A  191  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX GLY B  188  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX PRO B  189  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX LEU B  190  UNP  O60016              EXPRESSION TAG                 
SEQADV 6BOX GLY B  191  UNP  O60016              EXPRESSION TAG                 
SEQRES   1 A  303  GLY PRO LEU GLY SER LYS LEU ASP SER TYR THR HIS LEU          
SEQRES   2 A  303  SER PHE TYR GLU LYS ARG GLU LEU PHE ARG LYS LYS LEU          
SEQRES   3 A  303  ARG GLU ILE GLU GLY PRO GLU VAL THR LEU VAL ASN GLU          
SEQRES   4 A  303  VAL ASP ASP GLU PRO CYS PRO SER LEU ASP PHE GLN PHE          
SEQRES   5 A  303  ILE SER GLN TYR ARG LEU THR GLN GLY VAL ILE PRO PRO          
SEQRES   6 A  303  ASP PRO ASN PHE GLN SER GLY CYS ASN CYS SER SER LEU          
SEQRES   7 A  303  GLY GLY CYS ASP LEU ASN ASN PRO SER ARG CYS GLU CYS          
SEQRES   8 A  303  LEU ASP ASP LEU ASP GLU PRO THR HIS PHE ALA TYR ASP          
SEQRES   9 A  303  ALA GLN GLY ARG VAL ARG ALA ASP THR GLY ALA VAL ILE          
SEQRES  10 A  303  TYR GLU CYS ASN SER PHE CYS SER CYS SER MET GLU CYS          
SEQRES  11 A  303  PRO ASN ARG VAL VAL GLN ARG GLY ARG THR LEU PRO LEU          
SEQRES  12 A  303  GLU ILE PHE LYS THR LYS GLU LYS GLY TRP GLY VAL ARG          
SEQRES  13 A  303  SER LEU ARG PHE ALA PRO ALA GLY THR PHE ILE THR CYS          
SEQRES  14 A  303  TYR LEU GLY GLU VAL ILE THR SER ALA GLU ALA ALA LYS          
SEQRES  15 A  303  ARG ASP LYS ASN TYR ASP ASP ASP GLY ILE THR TYR LEU          
SEQRES  16 A  303  PHE ASP LEU ASP MET PHE ASP ASP ALA SER GLU TYR THR          
SEQRES  17 A  303  VAL ASP ALA GLN ASN TYR GLY ASP VAL SER ARG PHE PHE          
SEQRES  18 A  303  ASN HIS SER CYS SER PRO ASN ILE ALA ILE TYR SER ALA          
SEQRES  19 A  303  VAL ARG ASN HIS GLY PHE ARG THR ILE TYR ASP LEU ALA          
SEQRES  20 A  303  PHE PHE ALA ILE LYS ASP ILE GLN PRO LEU GLU GLU LEU          
SEQRES  21 A  303  THR PHE ASP TYR ALA GLY ALA LYS ASP PHE SER PRO VAL          
SEQRES  22 A  303  GLN SER GLN LYS SER GLN GLN ASN ARG ILE SER LYS LEU          
SEQRES  23 A  303  ARG ARG GLN CYS LYS CYS GLY SER ALA ASN CYS ARG GLY          
SEQRES  24 A  303  TRP LEU PHE GLY                                              
SEQRES   1 B  303  GLY PRO LEU GLY SER LYS LEU ASP SER TYR THR HIS LEU          
SEQRES   2 B  303  SER PHE TYR GLU LYS ARG GLU LEU PHE ARG LYS LYS LEU          
SEQRES   3 B  303  ARG GLU ILE GLU GLY PRO GLU VAL THR LEU VAL ASN GLU          
SEQRES   4 B  303  VAL ASP ASP GLU PRO CYS PRO SER LEU ASP PHE GLN PHE          
SEQRES   5 B  303  ILE SER GLN TYR ARG LEU THR GLN GLY VAL ILE PRO PRO          
SEQRES   6 B  303  ASP PRO ASN PHE GLN SER GLY CYS ASN CYS SER SER LEU          
SEQRES   7 B  303  GLY GLY CYS ASP LEU ASN ASN PRO SER ARG CYS GLU CYS          
SEQRES   8 B  303  LEU ASP ASP LEU ASP GLU PRO THR HIS PHE ALA TYR ASP          
SEQRES   9 B  303  ALA GLN GLY ARG VAL ARG ALA ASP THR GLY ALA VAL ILE          
SEQRES  10 B  303  TYR GLU CYS ASN SER PHE CYS SER CYS SER MET GLU CYS          
SEQRES  11 B  303  PRO ASN ARG VAL VAL GLN ARG GLY ARG THR LEU PRO LEU          
SEQRES  12 B  303  GLU ILE PHE LYS THR LYS GLU LYS GLY TRP GLY VAL ARG          
SEQRES  13 B  303  SER LEU ARG PHE ALA PRO ALA GLY THR PHE ILE THR CYS          
SEQRES  14 B  303  TYR LEU GLY GLU VAL ILE THR SER ALA GLU ALA ALA LYS          
SEQRES  15 B  303  ARG ASP LYS ASN TYR ASP ASP ASP GLY ILE THR TYR LEU          
SEQRES  16 B  303  PHE ASP LEU ASP MET PHE ASP ASP ALA SER GLU TYR THR          
SEQRES  17 B  303  VAL ASP ALA GLN ASN TYR GLY ASP VAL SER ARG PHE PHE          
SEQRES  18 B  303  ASN HIS SER CYS SER PRO ASN ILE ALA ILE TYR SER ALA          
SEQRES  19 B  303  VAL ARG ASN HIS GLY PHE ARG THR ILE TYR ASP LEU ALA          
SEQRES  20 B  303  PHE PHE ALA ILE LYS ASP ILE GLN PRO LEU GLU GLU LEU          
SEQRES  21 B  303  THR PHE ASP TYR ALA GLY ALA LYS ASP PHE SER PRO VAL          
SEQRES  22 B  303  GLN SER GLN LYS SER GLN GLN ASN ARG ILE SER LYS LEU          
SEQRES  23 B  303  ARG ARG GLN CYS LYS CYS GLY SER ALA ASN CYS ARG GLY          
SEQRES  24 B  303  TRP LEU PHE GLY                                              
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET    SAH  A 505      45                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET     ZN  B 504       1                                                       
HET    SAH  B 505      45                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL   7  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  13  HOH   *58(H2 O)                                                     
HELIX    1 AA1 SER A  201  GLU A  215  1                                  15    
HELIX    2 AA2 ASP A  253  GLN A  257  5                                   5    
HELIX    3 AA3 CYS A  276  ASP A  280  5                                   5    
HELIX    4 AA4 ARG A  320  GLY A  325  1                                   6    
HELIX    5 AA5 THR A  363  ARG A  370  1                                   8    
HELIX    6 AA6 ASP A  403  PHE A  408  5                                   6    
HELIX    7 AA7 SER B  201  GLU B  215  1                                  15    
HELIX    8 AA8 ASP B  253  GLN B  257  5                                   5    
HELIX    9 AA9 ASN B  272  ASP B  280  5                                   9    
HELIX   10 AB1 ARG B  320  GLY B  325  1                                   6    
HELIX   11 AB2 THR B  363  ASP B  371  1                                   9    
HELIX   12 AB3 ASP B  403  PHE B  408  5                                   6    
HELIX   13 AB4 ASP B  450  ALA B  454  5                                   5    
SHEET    1 AA1 3 VAL A 221  VAL A 224  0                                        
SHEET    2 AA1 3 LEU A 330  LYS A 334  1  O  ILE A 332   N  THR A 222           
SHEET    3 AA1 3 TRP A 340  SER A 344 -1  O  GLY A 341   N  PHE A 333           
SHEET    1 AA2 2 GLN A 238  PHE A 239  0                                        
SHEET    2 AA2 2 TYR A 401  GLY A 402  1  O  GLY A 402   N  GLN A 238           
SHEET    1 AA3 4 ARG A 244  LEU A 245  0                                        
SHEET    2 AA3 4 GLU A 360  ILE A 362  1  O  VAL A 361   N  ARG A 244           
SHEET    3 AA3 4 THR A 395  ASP A 397 -1  O  ASP A 397   N  GLU A 360           
SHEET    4 AA3 4 LEU A 382  ASP A 384 -1  N  PHE A 383   O  VAL A 396           
SHEET    1 AA4 4 VAL A 303  TYR A 305  0                                        
SHEET    2 AA4 4 ILE A 416  VAL A 422  1  O  VAL A 422   N  ILE A 304           
SHEET    3 AA4 4 ASP A 432  ALA A 437 -1  O  ALA A 434   N  TYR A 419           
SHEET    4 AA4 4 PHE A 353  TYR A 357 -1  N  THR A 355   O  PHE A 435           
SHEET    1 AA5 2 ASN A 409  HIS A 410  0                                        
SHEET    2 AA5 2 THR A 448  PHE A 449  1  O  PHE A 449   N  ASN A 409           
SHEET    1 AA6 3 VAL B 221  VAL B 224  0                                        
SHEET    2 AA6 3 LEU B 330  LYS B 334  1  O  ILE B 332   N  THR B 222           
SHEET    3 AA6 3 TRP B 340  SER B 344 -1  O  GLY B 341   N  PHE B 333           
SHEET    1 AA7 2 GLN B 238  PHE B 239  0                                        
SHEET    2 AA7 2 TYR B 401  GLY B 402  1  O  GLY B 402   N  GLN B 238           
SHEET    1 AA8 4 ARG B 244  LEU B 245  0                                        
SHEET    2 AA8 4 GLU B 360  ILE B 362  1  O  VAL B 361   N  ARG B 244           
SHEET    3 AA8 4 THR B 395  ASP B 397 -1  O  ASP B 397   N  GLU B 360           
SHEET    4 AA8 4 LEU B 382  ASP B 384 -1  N  PHE B 383   O  VAL B 396           
SHEET    1 AA9 4 VAL B 303  TYR B 305  0                                        
SHEET    2 AA9 4 ILE B 416  VAL B 422  1  O  VAL B 422   N  ILE B 304           
SHEET    3 AA9 4 ASP B 432  ALA B 437 -1  O  ALA B 434   N  TYR B 419           
SHEET    4 AA9 4 PHE B 353  TYR B 357 -1  N  THR B 355   O  PHE B 435           
SHEET    1 AB1 2 ASN B 409  HIS B 410  0                                        
SHEET    2 AB1 2 THR B 448  PHE B 449  1  O  PHE B 449   N  ASN B 409           
LINK         SG  CYS A 260                ZN    ZN A 504     1555   1555  2.46  
LINK         SG  CYS A 260                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 262                ZN    ZN A 504     1555   1555  2.58  
LINK         SG  CYS A 268                ZN    ZN A 504     1555   1555  2.30  
LINK         SG  CYS A 268                ZN    ZN A 503     1555   1555  2.57  
LINK         SG  CYS A 276                ZN    ZN A 504     1555   1555  2.32  
LINK         SG  CYS A 278                ZN    ZN A 502     1555   1555  2.34  
LINK         SG  CYS A 307                ZN    ZN A 502     1555   1555  2.26  
LINK         SG  CYS A 307                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A 311                ZN    ZN A 502     1555   1555  2.33  
LINK         SG  CYS A 313                ZN    ZN A 503     1555   1555  2.26  
LINK         SG  CYS A 317                ZN    ZN A 503     1555   1555  2.43  
LINK         SG  CYS A 412                ZN    ZN A 501     1555   1555  2.49  
LINK         SG  CYS A 477                ZN    ZN A 501     1555   1555  2.47  
LINK         SG  CYS A 479                ZN    ZN A 501     1555   1555  2.26  
LINK         SG  CYS A 484                ZN    ZN A 501     1555   1555  2.41  
LINK         SG  CYS B 260                ZN    ZN B 503     1555   1555  2.41  
LINK         SG  CYS B 260                ZN    ZN B 504     1555   1555  2.58  
LINK         SG  CYS B 262                ZN    ZN B 504     1555   1555  2.69  
LINK         SG  CYS B 268                ZN    ZN B 504     1555   1555  2.23  
LINK         SG  CYS B 268                ZN    ZN B 502     1555   1555  2.45  
LINK         SG  CYS B 276                ZN    ZN B 504     1555   1555  2.27  
LINK         SG  CYS B 278                ZN    ZN B 503     1555   1555  2.41  
LINK         SG  CYS B 307                ZN    ZN B 503     1555   1555  2.30  
LINK         SG  CYS B 307                ZN    ZN B 502     1555   1555  2.35  
LINK         SG  CYS B 311                ZN    ZN B 503     1555   1555  2.36  
LINK         SG  CYS B 313                ZN    ZN B 502     1555   1555  2.30  
LINK         SG  CYS B 317                ZN    ZN B 502     1555   1555  2.53  
LINK         SG  CYS B 412                ZN    ZN B 501     1555   1555  2.49  
LINK         SG  CYS B 477                ZN    ZN B 501     1555   1555  2.24  
LINK         SG  CYS B 479                ZN    ZN B 501     1555   1555  2.26  
LINK         SG  CYS B 484                ZN    ZN B 501     1555   1555  2.50  
SITE     1 AC1  4 CYS A 412  CYS A 477  CYS A 479  CYS A 484                    
SITE     1 AC2  5 CYS A 260  CYS A 278  CYS A 307  CYS A 311                    
SITE     2 AC2  5  ZN A 504                                                     
SITE     1 AC3  4 CYS A 268  CYS A 307  CYS A 313  CYS A 317                    
SITE     1 AC4  5 CYS A 260  CYS A 262  CYS A 268  CYS A 276                    
SITE     2 AC4  5  ZN A 502                                                     
SITE     1 AC5 13 LYS A 338  GLY A 339  TRP A 340  TYR A 381                    
SITE     2 AC5 13 ARG A 406  PHE A 407  ASN A 409  HIS A 410                    
SITE     3 AC5 13 TYR A 451  GLN A 476  CYS A 477  LYS A 478                    
SITE     4 AC5 13 PHE A 489                                                     
SITE     1 AC6  4 CYS B 412  CYS B 477  CYS B 479  CYS B 484                    
SITE     1 AC7  4 CYS B 268  CYS B 307  CYS B 313  CYS B 317                    
SITE     1 AC8  5 CYS B 260  CYS B 278  CYS B 307  CYS B 311                    
SITE     2 AC8  5  ZN B 504                                                     
SITE     1 AC9  5 CYS B 260  CYS B 262  CYS B 268  CYS B 276                    
SITE     2 AC9  5  ZN B 503                                                     
SITE     1 AD1 16 LYS B 338  GLY B 339  TRP B 340  THR B 380                    
SITE     2 AD1 16 TYR B 381  ARG B 406  PHE B 408  ASN B 409                    
SITE     3 AD1 16 HIS B 410  TYR B 451  ARG B 475  GLN B 476                    
SITE     4 AD1 16 CYS B 477  LYS B 478  CYS B 479  HOH B 622                    
CRYST1  125.625   71.255   87.239  90.00 120.37  90.00 C 1 2 1       8          
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      0.007960  0.000000  0.004665        0.00000                         
SCALE2      0.000000  0.014034  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013286        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system