GenomeNet

Database: PDB
Entry: 3KH4
LinkDB: 3KH4
Original site: 3KH4 
HEADER    OXIDOREDUCTASE                          30-OCT-09   3KH4              
TITLE     CRYSTAL STRUCTURE OF HUMAN CU/ZN SUPEROXIDE DISMUTASE RECOMBINANTLY   
TITLE    2 PRODUCED IN LEISHMANIA TARANTOLAE; P6522 CRYSTAL FORM CONTAINING 6   
TITLE    3 CHAINS IN THE ASYMMETRIC UNIT                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
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;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: LEISHMANIA TARENTOLAE;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 5689;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: P10;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: CHROMOSOMAL INTEGRATION               
KEYWDS    EUKARYOTIC EXPRESSION, LEISHMANIA TARANTOLAE, AMYOTROPHIC LATERAL     
KEYWDS   2 SCLEROSIS, ANTIOXIDANT, DISEASE MUTATION, DISULFIDE BOND, METAL-     
KEYWDS   3 BINDING, NEURODEGENERATION, OXIDOREDUCTASE, PHOSPHOPROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.GAZDAG,W.BLANKENFELDT                                             
REVDAT   2   01-SEP-10 3KH4    1       JRNL                                     
REVDAT   1   11-AUG-10 3KH4    0                                                
JRNL        AUTH   E.M.GAZDAG,I.C.CIRSTEA,R.BREITLING,J.LUKES,W.BLANKENFELDT,   
JRNL        AUTH 2 K.ALEXANDROV                                                 
JRNL        TITL   PURIFICATION AND CRYSTALLIZATION OF HUMAN CU/ZN SUPEROXIDE   
JRNL        TITL 2 DISMUTASE RECOMBINANTLY PRODUCED IN THE PROTOZOAN LEISHMANIA 
JRNL        TITL 3 TARENTOLAE.                                                  
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  66   871 2010              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   20693657                                                     
JRNL        DOI    10.1107/S1744309110019330                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21168                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1088                            
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1451                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.2820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6660                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 90.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.44000                                             
REMARK   3    B22 (A**2) : -8.44000                                             
REMARK   3    B33 (A**2) : 12.65000                                             
REMARK   3    B12 (A**2) : -4.22000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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): 0.428         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.310         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.112        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6774 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4482 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9144 ; 1.434 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11034 ; 4.332 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   912 ; 7.179 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   288 ;40.163 ;25.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1110 ;18.979 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;11.035 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1008 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7818 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1224 ; 0.004 ; 0.020       
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):  4470 ; 0.447 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1950 ; 0.000 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7104 ; 0.933 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2304 ; 1.405 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2040 ; 2.630 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     153      1                      
REMARK   3           1     B      1       B     153      1                      
REMARK   3           1     C      1       C     153      1                      
REMARK   3           1     D      1       D     153      1                      
REMARK   3           1     E      1       E     153      1                      
REMARK   3           1     F      1       F     153      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1857 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1857 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1857 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1857 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1857 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1857 ; 0.040 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1857 ; 0.070 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1857 ; 0.070 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1857 ; 0.070 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1857 ; 0.060 ; 0.500           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1857 ; 0.060 ; 0.500           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1857 ; 0.060 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1880 -35.3838  16.2062              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2460 T22:   0.2065                                     
REMARK   3      T33:   0.0411 T12:  -0.0111                                     
REMARK   3      T13:   0.0874 T23:   0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8655 L22:   7.3103                                     
REMARK   3      L33:   2.6896 L12:   0.6540                                     
REMARK   3      L13:   0.2053 L23:  -1.4116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1068 S12:   0.1620 S13:   0.0159                       
REMARK   3      S21:  -0.2823 S22:   0.0404 S23:  -0.0846                       
REMARK   3      S31:   0.1157 S32:  -0.1577 S33:   0.0664                       
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     1        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7200  -7.2764  16.4854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2797 T22:   0.1406                                     
REMARK   3      T33:   0.1920 T12:  -0.0360                                     
REMARK   3      T13:   0.0747 T23:   0.1288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6428 L22:   4.9351                                     
REMARK   3      L33:   4.5987 L12:  -0.5283                                     
REMARK   3      L13:  -0.3909 L23:   0.5378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0060 S12:   0.2531 S13:   0.4279                       
REMARK   3      S21:  -0.1449 S22:   0.0494 S23:   0.0679                       
REMARK   3      S31:  -0.2402 S32:   0.1853 S33:  -0.0554                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1534 -62.8182  16.0965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3244 T22:   0.3779                                     
REMARK   3      T33:   0.2983 T12:   0.0321                                     
REMARK   3      T13:   0.0217 T23:   0.1339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0936 L22:   6.1090                                     
REMARK   3      L33:   1.5459 L12:  -2.1316                                     
REMARK   3      L13:  -0.3708 L23:   0.4391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2539 S12:   0.1976 S13:  -0.2738                       
REMARK   3      S21:  -0.1149 S22:  -0.1000 S23:   0.2018                       
REMARK   3      S31:  -0.2134 S32:  -0.0046 S33:  -0.1538                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4514 -76.9018  17.1263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2501 T22:   0.2607                                     
REMARK   3      T33:   0.1647 T12:   0.0332                                     
REMARK   3      T13:  -0.0712 T23:   0.0643                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4505 L22:   6.2711                                     
REMARK   3      L33:   3.2117 L12:  -1.3879                                     
REMARK   3      L13:   0.2650 L23:  -0.1527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0083 S12:   0.0554 S13:   0.0809                       
REMARK   3      S21:  -0.0526 S22:  -0.0107 S23:  -0.0999                       
REMARK   3      S31:   0.1699 S32:  -0.0504 S33:   0.0190                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6236 -62.9948  16.5580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2930 T22:   0.2862                                     
REMARK   3      T33:   0.0931 T12:  -0.0548                                     
REMARK   3      T13:   0.0743 T23:   0.1109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9923 L22:   7.2983                                     
REMARK   3      L33:   2.2062 L12:   3.3145                                     
REMARK   3      L13:   1.0280 L23:   0.6191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1012 S12:   0.2566 S13:  -0.3693                       
REMARK   3      S21:  -0.2615 S22:  -0.0246 S23:  -0.3401                       
REMARK   3      S31:   0.1414 S32:   0.2307 S33:   0.1258                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.8178 -77.3172  17.4908              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2474 T22:   0.2393                                     
REMARK   3      T33:   0.1123 T12:  -0.0572                                     
REMARK   3      T13:  -0.0032 T23:   0.0878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0208 L22:   4.7563                                     
REMARK   3      L33:   2.9501 L12:   1.1792                                     
REMARK   3      L13:  -0.2283 L23:  -0.5861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0264 S12:   0.1958 S13:  -0.4040                       
REMARK   3      S21:  -0.3508 S22:  -0.0103 S23:  -0.1362                       
REMARK   3      S31:  -0.1429 S32:  -0.1137 S33:   0.0367                       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES: RESIDUAL ONLY                                             
REMARK   4                                                                      
REMARK   4 3KH4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055985.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2-5.2                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : SI(111)                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21168                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.17200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-25% (W/V) PEG4000, 0.1 M NAOAC, PH    
REMARK 280  4.2-5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      285.51200            
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      142.75600            
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      214.13400            
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       71.37800            
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      356.89000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      285.51200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      142.75600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       71.37800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      214.13400            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      356.89000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 3                                                       
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: 1340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP B    90     NZ   LYS D    91    10455     1.75            
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    ASN A  26       12.54     57.06                                   
REMARK 500    ALA A  55       68.08   -112.85                                   
REMARK 500    ASP A  90      169.17    -35.77                                   
REMARK 500    SER A  98      114.75   -164.21                                   
REMARK 500    LYS A 136      -59.89   -126.72                                   
REMARK 500    ASN B  26       15.69     56.56                                   
REMARK 500    ALA B  55       68.74   -112.38                                   
REMARK 500    ASP B  90      169.33    -36.63                                   
REMARK 500    LYS B 136      -61.00   -125.09                                   
REMARK 500    ASN C  26       14.54     56.07                                   
REMARK 500    ALA C  55       69.22   -113.74                                   
REMARK 500    ASP C  90      169.95    -33.01                                   
REMARK 500    SER C  98      117.95   -165.71                                   
REMARK 500    LYS C 136      -61.44   -123.69                                   
REMARK 500    ASN D  26       15.57     55.34                                   
REMARK 500    ALA D  55       69.83   -113.31                                   
REMARK 500    ASP D  90      170.36    -33.08                                   
REMARK 500    SER D  98      118.06   -164.64                                   
REMARK 500    LYS D 136      -59.06   -127.16                                   
REMARK 500    ASN E  26       16.50     53.71                                   
REMARK 500    ALA E  55       70.06   -112.97                                   
REMARK 500    ASP E  90      171.83    -33.88                                   
REMARK 500    SER E  98      118.84   -163.21                                   
REMARK 500    LYS E 136      -57.74   -124.45                                   
REMARK 500    ASN F  26       12.93     55.21                                   
REMARK 500    ALA F  55       68.74   -113.44                                   
REMARK 500    ASP F  90      168.90    -34.23                                   
REMARK 500    SER F  98      116.62   -162.44                                   
REMARK 500    LYS F 136      -59.86   -125.95                                   
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  46   ND1                                                    
REMARK 620 2 HIS A 120   NE2  96.0                                              
REMARK 620 3 HIS A  48   NE2 123.1  93.7                                        
REMARK 620 N                    1     2                                         
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  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 111.0                                              
REMARK 620 3 HIS A  80   ND1 116.1 122.1                                        
REMARK 620 4 ASP A  83   OD1  90.6  90.1 120.2                                  
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 HIS B  71   ND1 105.3                                              
REMARK 620 3 HIS B  80   ND1 113.5 126.1                                        
REMARK 620 4 ASP B  83   OD1  85.6  87.8 129.7                                  
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  48   NE2  94.5                                              
REMARK 620 3 HIS B  46   ND1  81.3 103.2                                        
REMARK 620 4 HIS B  63   NE2 152.7 109.7  81.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 112.0                                              
REMARK 620 3 HIS C 120   NE2  88.0  95.5                                        
REMARK 620 4 HIS C  63   NE2  85.2 111.3 153.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 114.2                                              
REMARK 620 3 HIS C  80   ND1 112.0 123.1                                        
REMARK 620 4 ASP C  83   OD1  89.8  93.6 118.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D 120   NE2  95.7                                              
REMARK 620 3 HIS D  48   NE2 113.8  91.3                                        
REMARK 620 4 HIS D  63   NE2  88.1 161.1 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 117.3                                              
REMARK 620 3 HIS D  80   ND1 114.3 121.5                                        
REMARK 620 4 ASP D  83   OD1  86.3  93.1 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  48   NE2                                                    
REMARK 620 2 HIS E 120   NE2  97.8                                              
REMARK 620 3 HIS E  46   ND1 114.7  85.9                                        
REMARK 620 4 HIS E  63   NE2 113.4 148.5  85.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1 103.7                                              
REMARK 620 3 HIS E  80   ND1 115.0 133.2                                        
REMARK 620 4 ASP E  83   OD1  80.5  88.3 122.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F 120   NE2  96.5                                              
REMARK 620 3 HIS F  48   NE2 115.5  96.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 117.2                                              
REMARK 620 3 HIS F  80   ND1 108.5 124.6                                        
REMARK 620 4 ASP F  83   OD1  85.5  97.5 116.2                                  
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 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                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KH3   RELATED DB: PDB                                   
REMARK 900 P212121 CRYSTAL FORM                                                 
DBREF  3KH4 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH4 B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH4 C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH4 D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH4 E    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH4 F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   7   CU    6(CU 2+)                                                     
FORMUL   8   ZN    6(ZN 2+)                                                     
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  CYS A  111  5                                   5    
HELIX    3   3 GLU A  132  LYS A  136  5                                   5    
HELIX    4   4 ALA B   55  GLY B   61  5                                   7    
HELIX    5   5 SER B  107  CYS B  111  5                                   5    
HELIX    6   6 GLU B  132  LYS B  136  5                                   5    
HELIX    7   7 ALA C   55  GLY C   61  5                                   7    
HELIX    8   8 SER C  107  CYS C  111  5                                   5    
HELIX    9   9 GLU C  133  GLY C  138  1                                   6    
HELIX   10  10 ALA D   55  GLY D   61  5                                   7    
HELIX   11  11 SER D  107  CYS D  111  5                                   5    
HELIX   12  12 GLU D  133  GLY D  138  1                                   6    
HELIX   13  13 ALA E   55  GLY E   61  5                                   7    
HELIX   14  14 SER E  107  CYS E  111  5                                   5    
HELIX   15  15 GLU E  133  GLY E  138  1                                   6    
HELIX   16  16 ALA F   55  GLY F   61  5                                   7    
HELIX   17  17 SER F  107  CYS F  111  5                                   5    
HELIX   18  18 GLU F  133  GLY F  138  1                                   6    
SHEET    1   A 5 VAL A  94  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  31   O  ILE A  99           
SHEET    3   A 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LEU A   8 -1  N  ALA A   4   O  PHE A  20           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  VAL A  47 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  VAL A 118   N  HIS A  46           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  VAL B  31   O  ILE B  99           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LEU B   8 -1  N  ALA B   4   O  PHE B  20           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  VAL B  47 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  VAL B 118   N  HIS B  46           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  ILE C  35   O  ALA C  95           
SHEET    3   E 5 GLN C  15  GLU C  21 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 LYS C   3  LEU C   8 -1  N  ALA C   4   O  PHE C  20           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  VAL C  47 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  VAL C 118   N  HIS C  46           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  ILE D  35   O  ALA D  95           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  VAL D  47 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  VAL D 118   N  HIS D  46           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1   I 5 ALA E  95  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  LYS E  36 -1  N  VAL E  31   O  ILE E  99           
SHEET    3   I 5 GLN E  15  GLU E  21 -1  N  ASN E  19   O  TRP E  32           
SHEET    4   I 5 LYS E   3  LEU E   8 -1  N  ALA E   4   O  PHE E  20           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  VAL E  47 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  VAL E 119 -1  O  VAL E 118   N  HIS E  46           
SHEET    4   J 4 ALA E 145  VAL E 148 -1  O  GLY E 147   N  LEU E 117           
SHEET    1   K 5 ALA F  95  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  LYS F  36 -1  N  ILE F  35   O  ALA F  95           
SHEET    3   K 5 GLN F  15  GLU F  21 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   K 5 LYS F   3  LEU F   8 -1  N  ALA F   4   O  PHE F  20           
SHEET    5   K 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  VAL F  47 -1  N  GLY F  41   O  ALA F  89           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  VAL F 118   N  HIS F  46           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  GLY F 147   N  LEU F 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.08  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.07  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.08  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.10  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.10  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.09  
LINK         ND1 HIS A  46                CU    CU A 154     1555   1555  2.14  
LINK         ND1 HIS A  63                ZN    ZN A 155     1555   1555  2.10  
LINK         ND1 HIS A  71                ZN    ZN A 155     1555   1555  2.11  
LINK         ND1 HIS A  80                ZN    ZN A 155     1555   1555  2.20  
LINK         OD1 ASP A  83                ZN    ZN A 155     1555   1555  1.81  
LINK         NE2 HIS A 120                CU    CU A 154     1555   1555  2.13  
LINK         ND1 HIS B  63                ZN    ZN B 155     1555   1555  2.23  
LINK         ND1 HIS B  71                ZN    ZN B 155     1555   1555  2.16  
LINK         ND1 HIS B  80                ZN    ZN B 155     1555   1555  2.08  
LINK         OD1 ASP B  83                ZN    ZN B 155     1555   1555  1.81  
LINK         NE2 HIS B 120                CU    CU B 154     1555   1555  2.16  
LINK         ND1 HIS C  46                CU    CU C 154     1555   1555  2.40  
LINK         NE2 HIS C  48                CU    CU C 154     1555   1555  2.39  
LINK         ND1 HIS C  63                ZN    ZN C 155     1555   1555  2.14  
LINK         ND1 HIS C  71                ZN    ZN C 155     1555   1555  2.05  
LINK         ND1 HIS C  80                ZN    ZN C 155     1555   1555  2.31  
LINK         OD1 ASP C  83                ZN    ZN C 155     1555   1555  1.79  
LINK         NE2 HIS C 120                CU    CU C 154     1555   1555  2.17  
LINK         ND1 HIS D  46                CU    CU D 154     1555   1555  2.14  
LINK         ND1 HIS D  63                ZN    ZN D 155     1555   1555  2.08  
LINK         ND1 HIS D  71                ZN    ZN D 155     1555   1555  1.98  
LINK         ND1 HIS D  80                ZN    ZN D 155     1555   1555  2.28  
LINK         OD1 ASP D  83                ZN    ZN D 155     1555   1555  1.82  
LINK         NE2 HIS D 120                CU    CU D 154     1555   1555  2.05  
LINK         NE2 HIS E  48                CU    CU E 154     1555   1555  2.30  
LINK         ND1 HIS E  63                ZN    ZN E 155     1555   1555  2.34  
LINK         ND1 HIS E  71                ZN    ZN E 155     1555   1555  2.10  
LINK         ND1 HIS E  80                ZN    ZN E 155     1555   1555  2.07  
LINK         OD1 ASP E  83                ZN    ZN E 155     1555   1555  1.93  
LINK         NE2 HIS E 120                CU    CU E 154     1555   1555  2.18  
LINK         ND1 HIS F  46                CU    CU F 154     1555   1555  2.23  
LINK         ND1 HIS F  63                ZN    ZN F 155     1555   1555  2.18  
LINK         ND1 HIS F  71                ZN    ZN F 155     1555   1555  1.91  
LINK         ND1 HIS F  80                ZN    ZN F 155     1555   1555  2.30  
LINK         OD1 ASP F  83                ZN    ZN F 155     1555   1555  1.84  
LINK         NE2 HIS F 120                CU    CU F 154     1555   1555  2.03  
LINK         ND1 HIS E  46                CU    CU E 154     1555   1555  2.40  
LINK         NE2 HIS A  48                CU    CU A 154     1555   1555  2.42  
LINK         NE2 HIS B  48                CU    CU B 154     1555   1555  2.43  
LINK         NE2 HIS F  48                CU    CU F 154     1555   1555  2.48  
LINK         NE2 HIS D  48                CU    CU D 154     1555   1555  2.56  
LINK         ND1 HIS B  46                CU    CU B 154     1555   1555  2.62  
LINK         NE2 HIS C  63                CU    CU C 154     1555   1555  2.64  
LINK         NE2 HIS D  63                CU    CU D 154     1555   1555  2.65  
LINK         NE2 HIS E  63                CU    CU E 154     1555   1555  2.66  
LINK         NE2 HIS B  63                CU    CU B 154     1555   1555  2.68  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  5 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     2 AC2  5 LYS A 136                                                     
SITE     1 AC3  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  5 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     2 AC4  5 LYS B 136                                                     
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  5 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     2 AC6  5 LYS C 136                                                     
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  5 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     2 AC8  5 LYS D 136                                                     
SITE     1 AC9  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC1  5 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     2 BC1  5 LYS E 136                                                     
SITE     1 BC2  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC3  5 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     2 BC3  5 LYS F 136                                                     
CRYST1  112.188  112.188  428.268  90.00  90.00 120.00 P 65 2 2     72          
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      0.008914  0.005146  0.000000        0.00000                         
SCALE2      0.000000  0.010293  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002335        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system