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Entry: 1SPD
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HEADER    OXIDOREDUCTASE                          21-JUL-93   1SPD              
TITLE     AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN         
TITLE    2 SUPEROXIDE DISMUTASE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.PARGE,J.A.TAINER                                                  
REVDAT   4   29-FEB-12 1SPD    1       JRNL   VERSN                             
REVDAT   3   24-FEB-09 1SPD    1       VERSN                                    
REVDAT   2   01-APR-03 1SPD    1       JRNL                                     
REVDAT   1   30-APR-94 1SPD    0                                                
JRNL        AUTH   H.X.DENG,A.HENTATI,J.A.TAINER,Z.IQBAL,A.CAYABYAB,W.Y.HUNG,   
JRNL        AUTH 2 E.D.GETZOFF,P.HU,B.HERZFELDT,R.P.ROOS,C.WARNER,G.DENG,       
JRNL        AUTH 3 E.SORIANO,C.SMYTH,H.E.PARGE,A.AHMED,A.D.ROSES,R.A.HALLEWELL, 
JRNL        AUTH 4 M.A.PERICAK-VANCE,T.SIDDIQUE                                 
JRNL        TITL   AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN      
JRNL        TITL 2 CU,ZN SUPEROXIDE DISMUTASE.                                  
JRNL        REF    SCIENCE                       V. 261  1047 1993              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   8351519                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ, X-PLOR                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,BRUNGER                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 5.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2226                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       35.77500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       35.77500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       35.77500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL   
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO          
REMARK 300 CHAIN *B*.                                                           
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL B    14     N    GLN B    15              1.74            
REMARK 500   O    ASP A   125     NZ   LYS A   128              2.05            
REMARK 500   ND1  HIS A    80     OD2  ASP A    83              2.09            
REMARK 500   ND1  HIS B    46     NE2  HIS B    63              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A   2   CB    THR A   2   OG1     0.125                       
REMARK 500    GLU A  24   CD    GLU A  24   OE2     0.071                       
REMARK 500    GLY A  27   CA    GLY A  27   C       0.101                       
REMARK 500    GLY A  41   CA    GLY A  41   C       0.106                       
REMARK 500    GLY A  44   N     GLY A  44   CA      0.093                       
REMARK 500    GLY A  56   CA    GLY A  56   C       0.111                       
REMARK 500    GLY A  72   N     GLY A  72   CA     -0.095                       
REMARK 500    HIS A  80   CG    HIS A  80   CD2     0.087                       
REMARK 500    HIS A  80   CE1   HIS A  80   NE2    -0.093                       
REMARK 500    SER A  98   CB    SER A  98   OG      0.079                       
REMARK 500    HIS A 120   NE2   HIS A 120   CD2    -0.072                       
REMARK 500    GLY B  12   CA    GLY B  12   C       0.116                       
REMARK 500    VAL B  14   C     GLN B  15   N      -0.210                       
REMARK 500    ILE B  17   N     ILE B  17   CA      0.122                       
REMARK 500    GLY B  27   N     GLY B  27   CA      0.095                       
REMARK 500    GLY B  33   N     GLY B  33   CA      0.178                       
REMARK 500    GLY B  41   N     GLY B  41   CA      0.125                       
REMARK 500    HIS B  63   CE1   HIS B  63   NE2    -0.067                       
REMARK 500    HIS B  71   CG    HIS B  71   CD2     0.073                       
REMARK 500    HIS B  80   CE1   HIS B  80   NE2    -0.085                       
REMARK 500    GLU B 132   CD    GLU B 132   OE2     0.080                       
REMARK 500    GLY B 150   N     GLY B 150   CA      0.133                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA A   1   CB  -  CA  -  C   ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ALA A   1   CA  -  C   -  O   ANGL. DEV. =  17.7 DEGREES          
REMARK 500    THR A   2   N   -  CA  -  CB  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    THR A   2   OG1 -  CB  -  CG2 ANGL. DEV. =  15.0 DEGREES          
REMARK 500    THR A   2   CA  -  CB  -  OG1 ANGL. DEV. = -13.1 DEGREES          
REMARK 500    THR A   2   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ALA A   1   CA  -  C   -  N   ANGL. DEV. = -17.6 DEGREES          
REMARK 500    LYS A   3   CD  -  CE  -  NZ  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ALA A   4   CA  -  C   -  N   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ALA A   4   O   -  C   -  N   ANGL. DEV. =  19.6 DEGREES          
REMARK 500    VAL A   5   C   -  N   -  CA  ANGL. DEV. = -23.5 DEGREES          
REMARK 500    CYS A   6   O   -  C   -  N   ANGL. DEV. =  10.3 DEGREES          
REMARK 500    LEU A   8   CA  -  CB  -  CG  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    LYS A   9   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    LEU A   8   O   -  C   -  N   ANGL. DEV. =  14.8 DEGREES          
REMARK 500    LYS A   9   CA  -  C   -  N   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    VAL A  14   N   -  CA  -  CB  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    VAL A  14   CA  -  CB  -  CG1 ANGL. DEV. = -14.3 DEGREES          
REMARK 500    VAL A  14   CA  -  CB  -  CG2 ANGL. DEV. =  13.7 DEGREES          
REMARK 500    GLN A  15   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    GLN A  15   C   -  N   -  CA  ANGL. DEV. = -17.4 DEGREES          
REMARK 500    PHE A  20   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ASN A  19   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    PHE A  20   C   -  N   -  CA  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    GLU A  24   CA  -  C   -  O   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    GLY A  27   C   -  N   -  CA  ANGL. DEV. = -26.6 DEGREES          
REMARK 500    PRO A  28   N   -  CA  -  C   ANGL. DEV. =  24.9 DEGREES          
REMARK 500    PRO A  28   CA  -  C   -  O   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    PRO A  28   CA  -  C   -  N   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    VAL A  29   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    VAL A  29   O   -  C   -  N   ANGL. DEV. =  12.2 DEGREES          
REMARK 500    VAL A  31   CA  -  C   -  N   ANGL. DEV. = -14.0 DEGREES          
REMARK 500    TRP A  32   O   -  C   -  N   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    SER A  34   O   -  C   -  N   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    LEU A  38   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    THR A  39   C   -  N   -  CA  ANGL. DEV. =  23.8 DEGREES          
REMARK 500    HIS A  43   CA  -  CB  -  CG  ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LEU A  42   O   -  C   -  N   ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PHE A  45   CA  -  C   -  N   ANGL. DEV. = -16.0 DEGREES          
REMARK 500    HIS A  48   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    GLU A  49   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    PHE A  50   O   -  C   -  N   ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ASP A  52   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ASP A  52   CB  -  CG  -  OD2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    CYS A  57   C   -  N   -  CA  ANGL. DEV. =  22.0 DEGREES          
REMARK 500    SER A  59   N   -  CA  -  CB  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ALA A  60   N   -  CA  -  CB  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    PRO A  62   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO A  62   O   -  C   -  N   ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ASN A  65   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     253 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    THR A   2      157.68     69.04                                   
REMARK 500    LYS A   3      104.25    -24.21                                   
REMARK 500    CYS A   6      136.36    176.94                                   
REMARK 500    LYS A  23     -142.23    -82.16                                   
REMARK 500    GLU A  24      115.52     -3.67                                   
REMARK 500    SER A  25      -81.97     14.62                                   
REMARK 500    PRO A  28       96.50    -58.39                                   
REMARK 500    GLU A  40      178.19    -59.77                                   
REMARK 500    PHE A  45       88.49   -158.93                                   
REMARK 500    ALA A  55       80.06   -155.39                                   
REMARK 500    PRO A  62     -163.47    -72.45                                   
REMARK 500    PHE A  64      104.95    -40.50                                   
REMARK 500    PRO A  66      -45.93      6.22                                   
REMARK 500    SER A  68       97.73    -54.56                                   
REMARK 500    ASP A  76     -159.98    -93.06                                   
REMARK 500    LEU A  84     -106.68    -83.29                                   
REMARK 500    ASP A  90     -144.35    -97.07                                   
REMARK 500    ASP A  92       48.82     35.12                                   
REMARK 500    GLU A 100       57.18   -150.68                                   
REMARK 500    SER A 105     -164.30   -107.56                                   
REMARK 500    LEU A 106       13.42   -143.30                                   
REMARK 500    SER A 107       88.19    171.20                                   
REMARK 500    ASP A 109     -112.15     51.72                                   
REMARK 500    HIS A 110       64.87    -65.70                                   
REMARK 500    LEU A 126       19.45     44.02                                   
REMARK 500    LYS A 128       -4.63    -56.95                                   
REMARK 500    SER A 134      -69.94    -92.21                                   
REMARK 500    THR A 135      -31.86    -30.34                                   
REMARK 500    LYS A 136      -78.00    -72.20                                   
REMARK 500    ASN A 139        4.38     59.21                                   
REMARK 500    ALA A 140       46.36    -62.60                                   
REMARK 500    ALA A 152     -137.07    -81.29                                   
REMARK 500    GLN B  15      111.34    -34.04                                   
REMARK 500    GLN B  22      125.21    174.59                                   
REMARK 500    LYS B  23     -153.28   -126.54                                   
REMARK 500    GLU B  24       54.47     24.01                                   
REMARK 500    SER B  25      -30.83     59.92                                   
REMARK 500    ASN B  26       54.27   -161.13                                   
REMARK 500    ASN B  53       33.46   -149.15                                   
REMARK 500    SER B  68       40.80     82.65                                   
REMARK 500    LYS B  70     -159.36   -104.78                                   
REMARK 500    HIS B  80      -72.77     -8.58                                   
REMARK 500    VAL B  81      -38.65    143.96                                   
REMARK 500    ASP B  90      127.10    -36.71                                   
REMARK 500    LYS B  91      -67.88     14.63                                   
REMARK 500    ILE B 104       50.81    -93.10                                   
REMARK 500    SER B 107     -116.06   -158.69                                   
REMARK 500    ASP B 109      162.94     81.57                                   
REMARK 500    HIS B 110       16.79     55.73                                   
REMARK 500    ASP B 125       42.88    -91.92                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE A  17        46.6      L          L   OUTSIDE RANGE           
REMARK 500    PRO A  28        20.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN A  65        24.6      L          L   OUTSIDE RANGE           
REMARK 500    SER A  68        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN A  86        53.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 110        46.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  40        22.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  67        24.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS B  71        24.3      L          L   OUTSIDE RANGE           
REMARK 500    PRO B  74        45.7      L          L   OUTSIDE RANGE           
REMARK 500    LYS B  91        23.9      L          L   OUTSIDE RANGE           
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                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 120   NE2                                                    
REMARK 620 2 HIS A  46   ND1  78.2                                              
REMARK 620 3 HIS A  63   NE2 167.5  89.6                                        
REMARK 620 4 HIS A  48   NE2  91.8 139.6  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 HIS A  63   ND1 143.8                                              
REMARK 620 3 HIS A  80   ND1 113.0 102.3                                        
REMARK 620 4 ASP A  83   OD2  75.8 116.3  62.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 120   NE2                                                    
REMARK 620 2 HIS B  63   NE2 147.7                                              
REMARK 620 3 HIS B  46   ND1  95.4  59.5                                        
REMARK 620 4 HIS B  48   NE2  98.4  83.0 125.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 ASP B  83   OD2 146.3                                              
REMARK 620 3 HIS B  80   ND1 124.7  71.7                                        
REMARK 620 4 HIS B  71   ND1 128.8  77.4  85.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CUA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZNA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CUB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
DBREF  1SPD A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SPD B    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQRES   1 A  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET    ACE  A   0       3                                                       
HET    ACE  B   0       3                                                       
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   1  ACE    2(C2 H4 O)                                                   
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
HELIX    1  HA GLU A  133  THR A  137  1                                   5    
HELIX    2  HB GLU B  133  THR B  137  1                                   5    
SHEET    1  SA 9 ALA A   4  LYS A   9  0                                        
SHEET    2  SA 9 GLN A  15  GLU A  21 -1  N  PHE A  20   O  ALA A   4           
SHEET    3  SA 9 VAL A  29  LYS A  30  1  N  LYS A  30   O  GLU A  21           
SHEET    4  SA 9 VAL A  94  ASP A 101 -1                                        
SHEET    5  SA 9 GLY A  85  ALA A  89  1                                        
SHEET    6  SA 9 GLY A  41  HIS A  48 -1  N  HIS A  43   O  VAL A  87           
SHEET    7  SA 9 ARG A 115  HIS A 120  1  N  VAL A 118   O  HIS A  46           
SHEET    8  SA 9 CYS A 146  GLY A 150 -1  N  GLY A 147   O  LEU A 117           
SHEET    9  SA 9 ALA A   4  LYS A   9  1  N  VAL A   7   O  VAL A 148           
SHEET    1  SB 9 ALA B   4  LYS B   9  0                                        
SHEET    2  SB 9 GLN B  15  GLU B  21 -1  N  PHE B  20   O  ALA B   4           
SHEET    3  SB 9 VAL B  29  LYS B  30  1  N  LYS B  30   O  GLU B  21           
SHEET    4  SB 9 VAL B  94  ASP B 101 -1                                        
SHEET    5  SB 9 GLY B  85  ALA B  89  1                                        
SHEET    6  SB 9 GLY B  41  HIS B  48 -1  N  HIS B  43   O  VAL B  87           
SHEET    7  SB 9 ARG B 115  HIS B 120  1  N  VAL B 118   O  HIS B  46           
SHEET    8  SB 9 CYS B 146  GLY B 150 -1  N  GLY B 147   O  LEU B 117           
SHEET    9  SB 9 ALA B   4  LYS B   9  1  N  VAL B   7   O  VAL B 148           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.10  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.06  
LINK         CH3 ACE A   0                 N   ALA A   1     1555   1555  1.49  
LINK         CH3 ACE B   0                 N   ALA B   1     1555   1555  1.58  
LINK         C   ACE A   0                 N   ALA A   1     1555   1555  1.85  
LINK        CU    CU A 154                 NE2 HIS A 120     1555   1555  2.08  
LINK        CU    CU A 154                 ND1 HIS A  46     1555   1555  2.05  
LINK        CU    CU A 154                 NE2 HIS A  63     1555   1555  2.09  
LINK        CU    CU A 154                 NE2 HIS A  48     1555   1555  2.13  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.13  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.05  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.08  
LINK        ZN    ZN A 155                 OD2 ASP A  83     1555   1555  1.95  
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.80  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  2.02  
LINK        CU    CU B 154                 NE2 HIS B  63     1555   1555  2.15  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.15  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  2.13  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.20  
LINK        ZN    ZN B 155                 OD2 ASP B  83     1555   1555  2.00  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  2.08  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.16  
SITE     1 CUA  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 ZNA  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 CUB  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 ZNB  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
CRYST1  113.570  113.570   71.550  90.00  90.00 120.00 P 63         12          
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      0.008805  0.005084  0.000000        0.00000                         
SCALE2      0.000000  0.010167  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013976        0.00000                         
MTRIX1   1 -0.998800  0.009900 -0.048600       57.20400    1                    
MTRIX2   1 -0.005600 -0.996200 -0.087200      -32.03400    1                    
MTRIX3   1 -0.049300 -0.086800  0.995000        0.28400    1                    
HETATM    1  C   ACE A   0      33.042 -11.070  24.499  1.00  8.74           C  
HETATM    2  O   ACE A   0      33.828 -10.864  24.277  1.00  9.48           O  
HETATM    3  CH3 ACE A   0      32.117 -11.386  24.809  1.00  8.49           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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