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Database: PDB
Entry: 3S8P
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HEADER    TRANSFERASE                             30-MAY-11   3S8P              
TITLE     CRYSTAL STRUCTURE OF THE SET DOMAIN OF HUMAN HISTONE-LYSINE N-        
TITLE    2 METHYLTRANSFERASE SUV420H1 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SUV420H1;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN;                                                
COMPND   5 SYNONYM: LYSINE N-METHYLTRANSFERASE 5B, SUPPRESSOR OF VARIEGATION 4- 
COMPND   6 20 HOMOLOG 1, SU(VAR)4-20 HOMOLOG 1, SUV4-20H1;                      
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 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: CGI-85, KMT5B, SUV420H1;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-(DE3)-V2R-PRARE2;                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    SET DOMAIN, HISTONE METHYLTRANSFERASE, TRANSCRIPTION REGULATION,      
KEYWDS   2 HISTONE LYSINE, SAM, METHYLATION, NUCLEUS, CHROMOSOME, STRUCTURAL    
KEYWDS   3 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.LAM,H.ZENG,P.LOPPNAU,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,            
AUTHOR   2 A.M.EDWARDS,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)          
REVDAT   3   08-NOV-17 3S8P    1       REMARK                                   
REVDAT   2   15-JAN-14 3S8P    1       JRNL   VERSN                             
REVDAT   1   06-JUL-11 3S8P    0                                                
JRNL        AUTH   H.WU,A.SIARHEYEVA,H.ZENG,R.LAM,A.DONG,X.H.WU,Y.LI,           
JRNL        AUTH 2 M.SCHAPIRA,M.VEDADI,J.MIN                                    
JRNL        TITL   CRYSTAL STRUCTURES OF THE HUMAN HISTONE H4K20                
JRNL        TITL 2 METHYLTRANSFERASES SUV420H1 AND SUV420H2.                    
JRNL        REF    FEBS LETT.                    V. 587  3859 2013              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   24396869                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.6.0081                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 52470                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2672                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3600                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.56                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 213                          
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3700                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 270                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.04000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.114         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.654         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3849 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5188 ; 1.241 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   475 ; 5.768 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   189 ;34.867 ;24.550       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   667 ;14.048 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;21.408 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   554 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2933 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    72        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4580  44.2000   7.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0327 T22:   0.0315                                     
REMARK   3      T33:   0.0154 T12:  -0.0084                                     
REMARK   3      T13:  -0.0009 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2520 L22:   0.6402                                     
REMARK   3      L33:   0.7129 L12:  -0.3530                                     
REMARK   3      L13:   0.2735 L23:  -0.2711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0126 S12:  -0.1788 S13:   0.0427                       
REMARK   3      S21:   0.0005 S22:   0.0260 S23:  -0.0009                       
REMARK   3      S31:   0.0033 S32:  -0.0154 S33:  -0.0385                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    71        B   333                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1700  18.9260 -18.5090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0330 T22:   0.0166                                     
REMARK   3      T33:   0.0105 T12:   0.0076                                     
REMARK   3      T13:   0.0068 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9920 L22:   0.7695                                     
REMARK   3      L33:   1.0606 L12:   0.2704                                     
REMARK   3      L13:   0.3268 L23:   0.6376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0121 S12:   0.1207 S13:   0.0337                       
REMARK   3      S21:  -0.0213 S22:   0.0060 S23:  -0.0267                       
REMARK   3      S31:  -0.0520 S32:   0.0116 S33:  -0.0181                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT. U VALUES WITH TLS ADDED.                                 
REMARK   4                                                                      
REMARK   4 3S8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000065901.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97904                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52506                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
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     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50900                            
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: SAD                          
REMARK 200 SOFTWARE USED: SHARP, DM 6.1                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M SODIUM FORMATE, 0.1 M BISTRIS      
REMARK 280  PROPANE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLN A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     ARG A    65                                                      
REMARK 465     TYR A    66                                                      
REMARK 465     VAL A    67                                                      
REMARK 465     PRO A    68                                                      
REMARK 465     SER A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     GLY A    71                                                      
REMARK 465     SER A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     PHE A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     SER A   107                                                      
REMARK 465     ARG A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     ARG A   111                                                      
REMARK 465     HIS A   112                                                      
REMARK 465     PHE A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     LYS A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ASP A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     PHE A   119                                                      
REMARK 465     SER A   120                                                      
REMARK 465     HIS A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     ASN A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     VAL A   125                                                      
REMARK 465     ARG A   126                                                      
REMARK 465     PHE A   127                                                      
REMARK 465     ARG A   128                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     ILE A   130                                                      
REMARK 465     LYS A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     GLN B    63                                                      
REMARK 465     SER B    64                                                      
REMARK 465     ARG B    65                                                      
REMARK 465     TYR B    66                                                      
REMARK 465     VAL B    67                                                      
REMARK 465     PRO B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     SER B    70                                                      
REMARK 465     SER B   103                                                      
REMARK 465     ALA B   104                                                      
REMARK 465     PHE B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     SER B   107                                                      
REMARK 465     ARG B   108                                                      
REMARK 465     SER B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     ARG B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     PHE B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     LYS B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     PHE B   119                                                      
REMARK 465     SER B   120                                                      
REMARK 465     HIS B   121                                                      
REMARK 465     ASN B   122                                                      
REMARK 465     ASN B   123                                                      
REMARK 465     PRO B   124                                                      
REMARK 465     VAL B   125                                                      
REMARK 465     ARG B   126                                                      
REMARK 465     PHE B   127                                                      
REMARK 465     SER B   334                                                      
REMARK 465     ARG B   335                                                      
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 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 135    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 142    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     GLU A 148    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     TRP A 162    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 162    CZ3  CH2                                            
REMARK 470     ARG A 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 165    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 168    CG   CD1  CD2                                       
REMARK 470     ARG A 276    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 131    CG   CD   CE   NZ                                   
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 138    CG   CD   CE   NZ                                   
REMARK 470     LYS B 155    CG   CD   CE   NZ                                   
REMARK 470     ARG B 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 165    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR B 166    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 167    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 168    CG   CD1  CD2                                       
REMARK 470     ASN B 169    CG   OD1  ND2                                       
REMARK 470     GLU B 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 333    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 220      128.13    -38.56                                   
REMARK 500    ASN A 221       -7.07     81.28                                   
REMARK 500    PHE A 312       65.62   -103.21                                   
REMARK 500    GLU B 148       19.80     59.40                                   
REMARK 500    ARG B 220      128.53    -38.98                                   
REMARK 500    ASN B 221       -3.69     78.67                                   
REMARK 500    PHE B 312       63.12   -103.24                                   
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 B 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 275   SG                                                     
REMARK 620 2 CYS B 324   SG  103.4                                              
REMARK 620 3 CYS B 321   SG  109.7 109.0                                        
REMARK 620 4 CYS B 319   SG  112.8 115.9 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 321   SG                                                     
REMARK 620 2 CYS A 319   SG  106.0                                              
REMARK 620 3 CYS A 275   SG  111.9 110.1                                        
REMARK 620 4 CYS A 324   SG  110.5 114.1 104.3                                  
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 400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 500                 
DBREF  3S8P A   63   335  UNP    Q4FZB7   SV421_HUMAN     63    335             
DBREF  3S8P B   63   335  UNP    Q4FZB7   SV421_HUMAN     63    335             
SEQRES   1 A  273  GLN SER ARG TYR VAL PRO SER SER GLY MSE SER ALA LYS          
SEQRES   2 A  273  GLU LEU CYS GLU ASN ASP ASP LEU ALA THR SER LEU VAL          
SEQRES   3 A  273  LEU ASP PRO TYR LEU GLY PHE GLN THR HIS LYS MSE ASN          
SEQRES   4 A  273  THR SER ALA PHE PRO SER ARG SER SER ARG HIS PHE SER          
SEQRES   5 A  273  LYS SER ASP SER PHE SER HIS ASN ASN PRO VAL ARG PHE          
SEQRES   6 A  273  ARG PRO ILE LYS GLY ARG GLN GLU GLU LEU LYS GLU VAL          
SEQRES   7 A  273  ILE GLU ARG PHE LYS LYS ASP GLU HIS LEU GLU LYS ALA          
SEQRES   8 A  273  PHE LYS CYS LEU THR SER GLY GLU TRP ALA ARG HIS TYR          
SEQRES   9 A  273  PHE LEU ASN LYS ASN LYS MSE GLN GLU LYS LEU PHE LYS          
SEQRES  10 A  273  GLU HIS VAL PHE ILE TYR LEU ARG MSE PHE ALA THR ASP          
SEQRES  11 A  273  SER GLY PHE GLU ILE LEU PRO CYS ASN ARG TYR SER SER          
SEQRES  12 A  273  GLU GLN ASN GLY ALA LYS ILE VAL ALA THR LYS GLU TRP          
SEQRES  13 A  273  LYS ARG ASN ASP LYS ILE GLU LEU LEU VAL GLY CYS ILE          
SEQRES  14 A  273  ALA GLU LEU SER GLU ILE GLU GLU ASN MSE LEU LEU ARG          
SEQRES  15 A  273  HIS GLY GLU ASN ASP PHE SER VAL MSE TYR SER THR ARG          
SEQRES  16 A  273  LYS ASN CYS ALA GLN LEU TRP LEU GLY PRO ALA ALA PHE          
SEQRES  17 A  273  ILE ASN HIS ASP CYS ARG PRO ASN CYS LYS PHE VAL SER          
SEQRES  18 A  273  THR GLY ARG ASP THR ALA CYS VAL LYS ALA LEU ARG ASP          
SEQRES  19 A  273  ILE GLU PRO GLY GLU GLU ILE SER CYS TYR TYR GLY ASP          
SEQRES  20 A  273  GLY PHE PHE GLY GLU ASN ASN GLU PHE CYS GLU CYS TYR          
SEQRES  21 A  273  THR CYS GLU ARG ARG GLY THR GLY ALA PHE LYS SER ARG          
SEQRES   1 B  273  GLN SER ARG TYR VAL PRO SER SER GLY MSE SER ALA LYS          
SEQRES   2 B  273  GLU LEU CYS GLU ASN ASP ASP LEU ALA THR SER LEU VAL          
SEQRES   3 B  273  LEU ASP PRO TYR LEU GLY PHE GLN THR HIS LYS MSE ASN          
SEQRES   4 B  273  THR SER ALA PHE PRO SER ARG SER SER ARG HIS PHE SER          
SEQRES   5 B  273  LYS SER ASP SER PHE SER HIS ASN ASN PRO VAL ARG PHE          
SEQRES   6 B  273  ARG PRO ILE LYS GLY ARG GLN GLU GLU LEU LYS GLU VAL          
SEQRES   7 B  273  ILE GLU ARG PHE LYS LYS ASP GLU HIS LEU GLU LYS ALA          
SEQRES   8 B  273  PHE LYS CYS LEU THR SER GLY GLU TRP ALA ARG HIS TYR          
SEQRES   9 B  273  PHE LEU ASN LYS ASN LYS MSE GLN GLU LYS LEU PHE LYS          
SEQRES  10 B  273  GLU HIS VAL PHE ILE TYR LEU ARG MSE PHE ALA THR ASP          
SEQRES  11 B  273  SER GLY PHE GLU ILE LEU PRO CYS ASN ARG TYR SER SER          
SEQRES  12 B  273  GLU GLN ASN GLY ALA LYS ILE VAL ALA THR LYS GLU TRP          
SEQRES  13 B  273  LYS ARG ASN ASP LYS ILE GLU LEU LEU VAL GLY CYS ILE          
SEQRES  14 B  273  ALA GLU LEU SER GLU ILE GLU GLU ASN MSE LEU LEU ARG          
SEQRES  15 B  273  HIS GLY GLU ASN ASP PHE SER VAL MSE TYR SER THR ARG          
SEQRES  16 B  273  LYS ASN CYS ALA GLN LEU TRP LEU GLY PRO ALA ALA PHE          
SEQRES  17 B  273  ILE ASN HIS ASP CYS ARG PRO ASN CYS LYS PHE VAL SER          
SEQRES  18 B  273  THR GLY ARG ASP THR ALA CYS VAL LYS ALA LEU ARG ASP          
SEQRES  19 B  273  ILE GLU PRO GLY GLU GLU ILE SER CYS TYR TYR GLY ASP          
SEQRES  20 B  273  GLY PHE PHE GLY GLU ASN ASN GLU PHE CYS GLU CYS TYR          
SEQRES  21 B  273  THR CYS GLU ARG ARG GLY THR GLY ALA PHE LYS SER ARG          
MODRES 3S8P MSE A   72  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE A  100  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE A  173  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE A  188  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE A  241  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE A  253  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE B   72  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE B  100  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE B  173  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE B  188  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE B  241  MET  SELENOMETHIONINE                                   
MODRES 3S8P MSE B  253  MET  SELENOMETHIONINE                                   
HET    MSE  A  72       8                                                       
HET    MSE  A 100       8                                                       
HET    MSE  A 173       8                                                       
HET    MSE  A 188       8                                                       
HET    MSE  A 241       8                                                       
HET    MSE  A 253       8                                                       
HET    MSE  B  72       8                                                       
HET    MSE  B 100       8                                                       
HET    MSE  B 173       8                                                       
HET    MSE  B 188       8                                                       
HET    MSE  B 241      13                                                       
HET    MSE  B 253       8                                                       
HET     ZN  A 400       1                                                       
HET    SAM  A 500      27                                                       
HET     ZN  B 400       1                                                       
HET    SAM  B 500      27                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   7  HOH   *270(H2 O)                                                    
HELIX    1   1 SER A   73  GLY A   94  1                                  22    
HELIX    2   2 ARG A  133  GLU A  148  1                                  16    
HELIX    3   3 HIS A  149  THR A  158  1                                  10    
HELIX    4   4 GLY A  160  LEU A  168  1                                   9    
HELIX    5   5 ASN A  171  MSE A  188  1                                  18    
HELIX    6   6 PHE A  189  SER A  193  5                                   5    
HELIX    7   7 SER A  235  LEU A  243  1                                   9    
HELIX    8   8 GLY A  266  ILE A  271  5                                   6    
HELIX    9   9 GLY A  313  GLU A  317  5                                   5    
HELIX   10  10 CYS A  321  GLY A  328  1                                   8    
HELIX   11  11 THR A  329  LYS A  333  5                                   5    
HELIX   12  12 SER B   73  LEU B   89  1                                  17    
HELIX   13  13 LEU B   89  GLY B   94  1                                   6    
HELIX   14  14 GLY B  132  GLU B  148  1                                  17    
HELIX   15  15 HIS B  149  SER B  159  1                                  11    
HELIX   16  16 TRP B  162  LEU B  168  1                                   7    
HELIX   17  17 ASN B  171  MSE B  188  1                                  18    
HELIX   18  18 SER B  235  LEU B  243  1                                   9    
HELIX   19  19 GLY B  266  ILE B  271  5                                   6    
HELIX   20  20 GLY B  313  GLU B  317  5                                   5    
HELIX   21  21 CYS B  321  GLY B  328  1                                   8    
HELIX   22  22 THR B  329  LYS B  333  5                                   5    
SHEET    1   A 2 PHE A 195  CYS A 200  0                                        
SHEET    2   A 2 GLY A 209  ALA A 214 -1  O  VAL A 213   N  GLU A 196           
SHEET    1   B 5 VAL A 252  SER A 255  0                                        
SHEET    2   B 5 CYS A 260  LEU A 265 -1  O  CYS A 260   N  SER A 255           
SHEET    3   B 5 LYS A 223  LEU A 234 -1  N  CYS A 230   O  LEU A 265           
SHEET    4   B 5 THR A 288  ALA A 293 -1  O  VAL A 291   N  ILE A 224           
SHEET    5   B 5 CYS A 279  GLY A 285 -1  N  VAL A 282   O  CYS A 290           
SHEET    1   C 2 ASN A 272  HIS A 273  0                                        
SHEET    2   C 2 SER A 304  CYS A 305  1  O  CYS A 305   N  ASN A 272           
SHEET    1   D 2 PHE B 195  CYS B 200  0                                        
SHEET    2   D 2 GLY B 209  ALA B 214 -1  O  VAL B 213   N  GLU B 196           
SHEET    1   E 5 VAL B 252  SER B 255  0                                        
SHEET    2   E 5 CYS B 260  LEU B 265 -1  O  CYS B 260   N  SER B 255           
SHEET    3   E 5 LYS B 223  LEU B 234 -1  N  CYS B 230   O  LEU B 265           
SHEET    4   E 5 THR B 288  ALA B 293 -1  O  VAL B 291   N  ILE B 224           
SHEET    5   E 5 CYS B 279  GLY B 285 -1  N  VAL B 282   O  CYS B 290           
SHEET    1   F 2 ASN B 272  HIS B 273  0                                        
SHEET    2   F 2 SER B 304  CYS B 305  1  O  CYS B 305   N  ASN B 272           
LINK         C   MSE A  72                 N   SER A  73     1555   1555  1.33  
LINK         C   LYS A  99                 N   MSE A 100     1555   1555  1.33  
LINK         C   MSE A 100                 N   ASN A 101     1555   1555  1.34  
LINK         C   LYS A 172                 N   MSE A 173     1555   1555  1.33  
LINK         C   MSE A 173                 N   GLN A 174     1555   1555  1.33  
LINK         C   ARG A 187                 N   MSE A 188     1555   1555  1.33  
LINK         C   MSE A 188                 N   PHE A 189     1555   1555  1.33  
LINK         C   ASN A 240                 N   MSE A 241     1555   1555  1.33  
LINK         C   MSE A 241                 N   LEU A 242     1555   1555  1.34  
LINK         C   VAL A 252                 N   MSE A 253     1555   1555  1.33  
LINK         C   MSE A 253                 N   TYR A 254     1555   1555  1.33  
LINK         C   GLY B  71                 N   MSE B  72     1555   1555  1.33  
LINK         C   MSE B  72                 N   SER B  73     1555   1555  1.33  
LINK         C   LYS B  99                 N   MSE B 100     1555   1555  1.33  
LINK         C   MSE B 100                 N   ASN B 101     1555   1555  1.34  
LINK         C   LYS B 172                 N   MSE B 173     1555   1555  1.33  
LINK         C   MSE B 173                 N   GLN B 174     1555   1555  1.33  
LINK         C   ARG B 187                 N   MSE B 188     1555   1555  1.33  
LINK         C   MSE B 188                 N   PHE B 189     1555   1555  1.33  
LINK         C   ASN B 240                 N   MSE B 241     1555   1555  1.33  
LINK         C   MSE B 241                 N   LEU B 242     1555   1555  1.33  
LINK         C   VAL B 252                 N   MSE B 253     1555   1555  1.33  
LINK         C   MSE B 253                 N   TYR B 254     1555   1555  1.33  
LINK         SG  CYS B 275                ZN    ZN B 400     1555   1555  2.19  
LINK         SG  CYS A 321                ZN    ZN A 400     1555   1555  2.28  
LINK         SG  CYS A 319                ZN    ZN A 400     1555   1555  2.32  
LINK         SG  CYS B 324                ZN    ZN B 400     1555   1555  2.34  
LINK         SG  CYS B 321                ZN    ZN B 400     1555   1555  2.34  
LINK         SG  CYS B 319                ZN    ZN B 400     1555   1555  2.35  
LINK         SG  CYS A 275                ZN    ZN A 400     1555   1555  2.35  
LINK         SG  CYS A 324                ZN    ZN A 400     1555   1555  2.37  
SITE     1 AC1  4 CYS A 275  CYS A 319  CYS A 321  CYS A 324                    
SITE     1 AC2 20 HOH A  31  HIS A  98  TYR A 203  SER A 205                    
SITE     2 AC2 20 GLU A 206  GLY A 209  ALA A 210  PHE A 250                    
SITE     3 AC2 20 ALA A 269  PHE A 270  ILE A 271  ASN A 272                    
SITE     4 AC2 20 HIS A 273  TYR A 307  PHE A 312  CYS A 319                    
SITE     5 AC2 20 GLU A 320  CYS A 321  HOH A 436  ARG B 257                    
SITE     1 AC3  4 CYS B 275  CYS B 319  CYS B 321  CYS B 324                    
SITE     1 AC4 21 ARG A 257  HOH A 352  HOH B  14  HOH B  52                    
SITE     2 AC4 21 HIS B  98  TYR B 203  SER B 205  GLU B 206                    
SITE     3 AC4 21 GLY B 209  ALA B 210  PHE B 250  ALA B 269                    
SITE     4 AC4 21 PHE B 270  ILE B 271  ASN B 272  HIS B 273                    
SITE     5 AC4 21 TYR B 307  PHE B 312  CYS B 319  GLU B 320                    
SITE     6 AC4 21 CYS B 321                                                     
CRYST1   46.424   50.134   74.839 100.99 108.05  89.76 P 1           2          
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      0.021541 -0.000088  0.007144        0.00000                         
SCALE2      0.000000  0.019947  0.004052        0.00000                         
SCALE3      0.000000  0.000000  0.014341        0.00000                         
HETATM    1  N   MSE A  72      -9.949  39.283   3.480  1.00 44.08           N  
ANISOU    1  N   MSE A  72     5409   5584   5755   -297   -274    458       N  
HETATM    2  CA  MSE A  72      -9.772  40.740   3.183  1.00 38.65           C  
ANISOU    2  CA  MSE A  72     4738   4916   5031   -248   -234    403       C  
HETATM    3  C   MSE A  72      -9.572  41.004   1.696  1.00 36.83           C  
ANISOU    3  C   MSE A  72     4565   4626   4802   -239   -272    358       C  
HETATM    4  O   MSE A  72      -8.811  40.309   1.018  1.00 43.15           O  
ANISOU    4  O   MSE A  72     5421   5372   5601   -249   -306    333       O  
HETATM    5  CB  MSE A  72      -8.574  41.327   3.954  1.00 39.13           C  
ANISOU    5  CB  MSE A  72     4824   4999   5044   -214   -179    361       C  
HETATM    6  CG  MSE A  72      -8.865  41.659   5.412  1.00 38.48           C  
ANISOU    6  CG  MSE A  72     4682   4999   4937   -198   -128    387       C  
HETATM    7 SE   MSE A  72      -7.339  42.414   6.356  0.75 38.85          SE  
ANISOU    7 SE   MSE A  72     4763   5073   4925   -157    -75    322      SE  
HETATM    8  CE  MSE A  72      -6.127  40.871   6.225  1.00 38.24           C  
ANISOU    8  CE  MSE A  72     4732   4941   4855   -193   -111    338       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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