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Database: PDB
Entry: 4RSZ
LinkDB: 4RSZ
Original site: 4RSZ 
HEADER    ELECTRON TRANSPORT                      12-NOV-14   4RSZ              
TITLE     THE X-RAY STRUCTURE OF THE PRIMARY ADDUCT FORMED IN THE REACTION      
TITLE    2 BETWEEN CISPLATIN AND CYTOCHROME C                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A, B, C, D, E, F                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: DOMESTIC HORSE,EQUINE;                              
SOURCE   4 ORGANISM_TAXID: 9796                                                 
KEYWDS    ELECTRON TRANSPORT                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MERLINO                                                             
REVDAT   2   25-FEB-15 4RSZ    1       JRNL                                     
REVDAT   1   14-JAN-15 4RSZ    0                                                
JRNL        AUTH   G.FERRARO,L.MESSORI,A.MERLINO                                
JRNL        TITL   THE X-RAY STRUCTURE OF THE PRIMARY ADDUCTS FORMED IN THE     
JRNL        TITL 2 REACTION BETWEEN CISPLATIN AND CYTOCHROME C.                 
JRNL        REF    CHEM.COMMUN.(CAMB.)           V.  51  2559 2015              
JRNL        REFN                   ISSN 1359-7345                               
JRNL        PMID   25567806                                                     
JRNL        DOI    10.1039/C4CC09056J                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 104.22                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28987                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1544                            
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) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2124                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4938                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 347                                     
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.80000                                             
REMARK   3    B22 (A**2) : -0.80000                                             
REMARK   3    B33 (A**2) : 2.59000                                              
REMARK   3    B12 (A**2) : -0.40000                                             
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): 0.446         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.272         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.245         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.786        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5450 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5241 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7317 ; 1.845 ; 2.054       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12126 ; 1.431 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   622 ; 5.865 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   206 ;34.760 ;25.340       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1029 ;17.446 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;28.912 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   718 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6050 ; 0.017 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1189 ; 0.024 ; 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):  2500 ; 1.629 ; 1.947       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2499 ; 1.629 ; 1.948       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3118 ; 2.688 ; 2.911       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3119 ; 2.687 ; 2.910       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2950 ; 2.276 ; 2.106       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2903 ; 2.227 ; 2.085       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4152 ; 3.102 ; 2.985       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6874 ; 5.884 ;15.505       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6848 ; 5.848 ;15.448       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 15                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A     1   104       B     1    104     6285  0.11  0.05    
REMARK   3    2      A     1   104       C     1    104     6325  0.11  0.05    
REMARK   3    3      A     1   104       D     1    104     6209  0.11  0.05    
REMARK   3    4      A     1   104       E     1    104     6222  0.10  0.05    
REMARK   3    5      A     1   104       F     1    104     6294  0.11  0.05    
REMARK   3    6      B     1   104       C     1    104     6268  0.10  0.05    
REMARK   3    7      B     1   104       D     1    104     6243  0.09  0.05    
REMARK   3    8      B     1   104       E     1    104     6167  0.10  0.05    
REMARK   3    9      B     1   104       F     1    104     6281  0.09  0.05    
REMARK   3   10      C     1   104       D     1    104     6260  0.10  0.05    
REMARK   3   11      C     1   104       E     1    104     6234  0.09  0.05    
REMARK   3   12      C     1   104       F     1    104     6331  0.10  0.05    
REMARK   3   13      D     1   104       E     1    104     6242  0.10  0.05    
REMARK   3   14      D     1   104       F     1    104     6343  0.08  0.05    
REMARK   3   15      E     1   104       F     1    104     6248  0.09  0.05    
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   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -90.9794  -0.3117  18.3381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2665 T22:   0.1786                                     
REMARK   3      T33:   0.2037 T12:   0.0338                                     
REMARK   3      T13:  -0.0527 T23:  -0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7688 L22:   1.4210                                     
REMARK   3      L33:   0.3832 L12:   0.0159                                     
REMARK   3      L13:   0.0191 L23:   0.6297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0585 S12:  -0.0358 S13:  -0.2311                       
REMARK   3      S21:  -0.1775 S22:  -0.0949 S23:   0.1336                       
REMARK   3      S31:  -0.2033 S32:  -0.0296 S33:   0.1534                       
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   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -73.1461  18.1040  20.0515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4296 T22:   0.1043                                     
REMARK   3      T33:   0.2751 T12:  -0.0454                                     
REMARK   3      T13:   0.0293 T23:  -0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6454 L22:   1.5331                                     
REMARK   3      L33:   0.3965 L12:   0.9320                                     
REMARK   3      L13:   1.0414 L23:   0.4425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4309 S12:  -0.2249 S13:   0.2145                       
REMARK   3      S21:  -0.6802 S22:   0.2465 S23:  -0.1584                       
REMARK   3      S31:  -0.2353 S32:  -0.0114 S33:   0.1844                       
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   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -66.0765  -6.3671  15.9623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2787 T22:   0.1683                                     
REMARK   3      T33:   0.4756 T12:  -0.0147                                     
REMARK   3      T13:   0.2814 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6244 L22:   1.7783                                     
REMARK   3      L33:   0.4601 L12:   0.0397                                     
REMARK   3      L13:  -0.4866 L23:   0.2049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0345 S12:  -0.0498 S13:  -0.2128                       
REMARK   3      S21:  -0.5747 S22:   0.0442 S23:  -0.7270                       
REMARK   3      S31:  -0.1030 S32:  -0.0334 S33:  -0.0097                       
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   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):-104.6333 -16.3125  34.8594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1308 T22:   0.3379                                     
REMARK   3      T33:   0.1908 T12:  -0.1286                                     
REMARK   3      T13:   0.0595 T23:  -0.1635                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0940 L22:   2.2049                                     
REMARK   3      L33:   0.2286 L12:   0.5242                                     
REMARK   3      L13:   0.6655 L23:   0.4337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3172 S12:  -0.4243 S13:   0.3914                       
REMARK   3      S21:   0.1662 S22:  -0.4033 S23:   0.1807                       
REMARK   3      S31:   0.1383 S32:  -0.1470 S33:   0.0861                       
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   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -90.2994  31.4375  35.6297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3034 T22:   0.6550                                     
REMARK   3      T33:   0.2698 T12:   0.1639                                     
REMARK   3      T13:  -0.1803 T23:  -0.3436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4221 L22:   1.6841                                     
REMARK   3      L33:   0.2523 L12:  -3.2503                                     
REMARK   3      L13:  -1.2684 L23:   0.6343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7533 S12:  -1.6493 S13:   0.9217                       
REMARK   3      S21:   0.3260 S22:   0.9238 S23:  -0.4829                       
REMARK   3      S31:   0.1664 S32:   0.3131 S33:  -0.1705                       
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   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -84.8421 -32.0314  31.2018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2912 T22:   0.2131                                     
REMARK   3      T33:   0.5851 T12:   0.0112                                     
REMARK   3      T13:   0.0725 T23:   0.2808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0217 L22:   0.7142                                     
REMARK   3      L33:   1.4049 L12:   0.7520                                     
REMARK   3      L13:   0.3244 L23:  -0.6546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3096 S12:  -0.6375 S13:  -0.8887                       
REMARK   3      S21:  -0.0021 S22:  -0.1852 S23:  -0.3824                       
REMARK   3      S31:  -0.2096 S32:  -0.1561 S33:  -0.1244                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4RSZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087757.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR571                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30538                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 104.220                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.400                             
REMARK 200  R MERGE                    (I) : 0.10900                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB CODE 1HRC                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: A NEW CRYSTAL FORM OF HORSE HEART        
REMARK 280  CYTOCHROME C THAT CO-CRYSTALLIZED WITH NITRATE AND SULPHATE IONS    
REMARK 280  HAS BEEN OBTAINED. CRYSTALLIZATION WAS PREPARED BY USING THE        
REMARK 280  HANGING-DROP VAPOUR DIFFUSION METHOD IN LINBRO PLATES AND A         
REMARK 280  RESERVOIR CONTAINED 3.5 M AMMONIUM SULPHATE, 0.6 M SODIUM           
REMARK 280  NITRATE. THE DROPLETS CONSISTED OF 1 MICROLITER PROTEIN (30 MG/ML   
REMARK 280  IN WATER) AND 1 MICROLITER OF RESERVOIR. THEY WERE EQUILIBRATED     
REMARK 280  AGAINST A 500 MICROLITERS RESERVOIR SOLUTION AT 20 C. THESE         
REMARK 280  CONDITIONS PRODUCED WELL SHAPED RED CRYSTALS AFTER 1 MONTH. THESE   
REMARK 280  CRYSTALS HAVE BEEN SOAKED FOR 24 H IN A SOLUTION CONSISTING OF      
REMARK 280  0.005 M CISPLATIN IN 2.0 M AMMONIUM SULPHATE AND 0.4 M SODIUM       
REMARK 280  NITRATE. TO PREPARE THIS SOLUTION, CISPLATIN WAS FIRST DISSOLVED    
REMARK 280  IN 5 MM SODIUM ACETATE BUFFER AT PH 5.0. , VAPOR DIFFUSION,         
REMARK 280  HANGING DROP, TEMPERATURE 300K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3                              
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                                                                      
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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7                                     
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -232.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1 -0.500000  0.866025  0.000000     -180.51600            
REMARK 350   BIOMT2   1 -0.866025 -0.500000  0.000000     -104.22096            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000      -36.67300            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -36.67300            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  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   SG   CYS E    14     CBB  HEM E   201              1.92            
REMARK 500   OE1  GLU B    61     N1   CPT B   203              2.13            
REMARK 500   OG1  THR F    40     O    HOH F   310              2.14            
REMARK 500   OE1  GLU A   104     O    HOH A   302              2.19            
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    GLU E  92   CG    GLU E  92   CD      0.175                       
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    GLU E  92   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.6 DEGREES          
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    LYS A  27     -142.95   -105.27                                   
REMARK 500    ASN A  70       84.66   -166.03                                   
REMARK 500    LYS B  27     -141.75   -105.90                                   
REMARK 500    ASN B  70       82.46   -164.95                                   
REMARK 500    LYS C  27     -143.67   -103.74                                   
REMARK 500    ASN C  70       83.52   -165.70                                   
REMARK 500    LYS D  27     -158.30   -123.48                                   
REMARK 500    ASN D  70       83.82   -165.35                                   
REMARK 500    LYS E  27     -144.34   -104.13                                   
REMARK 500    ASN E  70       83.04   -165.86                                   
REMARK 500    LYS F  22       25.51    -63.27                                   
REMARK 500    LYS F  27     -151.71   -112.24                                   
REMARK 500    ASN F  70       83.81   -166.29                                   
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                             CPT F 203  PT1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F  61   OE2                                                    
REMARK 620 2 CPT F 203   N1  175.7                                              
REMARK 620 3 CPT F 203  CL1   89.1  89.2                                        
REMARK 620 4 MET F  65   SD  117.9  63.3 152.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CPT A 202  PT1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  61   OE2                                                    
REMARK 620 2 CPT A 202   N1  158.0                                              
REMARK 620 3 CPT A 202   N2   92.2  95.9                                        
REMARK 620 4 MET A  65   SD   98.9  67.2 157.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  18   NE2                                                    
REMARK 620 2 HEM F 201   NA   90.3                                              
REMARK 620 3 HEM F 201   NB   86.1  90.9                                        
REMARK 620 4 HEM F 201   NC   89.2 179.5  88.8                                  
REMARK 620 5 HEM F 201   ND   93.5  90.1 178.9  90.2                            
REMARK 620 6 MET F  80   SD  177.2  87.8  96.0  92.6  84.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 HEM B 201   NA   90.7                                              
REMARK 620 3 HEM B 201   NB   88.1  92.0                                        
REMARK 620 4 HEM B 201   NC   88.3 178.5  86.8                                  
REMARK 620 5 HEM B 201   ND   91.4  89.0 178.9  92.2                            
REMARK 620 6 MET B  80   SD  171.2  85.0  99.7  96.1  80.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  18   NE2                                                    
REMARK 620 2 HEM D 201   NA   87.4                                              
REMARK 620 3 HEM D 201   NB   86.3  89.9                                        
REMARK 620 4 HEM D 201   NC   91.8 178.7  89.1                                  
REMARK 620 5 HEM D 201   ND   93.3  90.9 179.2  90.2                            
REMARK 620 6 MET D  80   SD  171.5  84.3  95.3  96.5  85.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  18   NE2                                                    
REMARK 620 2 HEM C 201   NA   85.3                                              
REMARK 620 3 HEM C 201   NB   88.2  88.9                                        
REMARK 620 4 HEM C 201   NC   94.2 178.7  90.0                                  
REMARK 620 5 HEM C 201   ND   91.3  91.4 179.4  89.7                            
REMARK 620 6 MET C  80   SD  170.1  86.1  96.5  94.6  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  18   NE2                                                    
REMARK 620 2 HEM E 201   NA   89.4                                              
REMARK 620 3 HEM E 201   NB   84.0  91.1                                        
REMARK 620 4 HEM E 201   NC   89.8 179.0  88.2                                  
REMARK 620 5 HEM E 201   ND   95.3  89.5 179.1  91.2                            
REMARK 620 6 MET E  80   SD  175.5  86.1  95.9  94.6  84.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 HEM A 201   NA   88.7                                              
REMARK 620 3 HEM A 201   NB   85.9  91.3                                        
REMARK 620 4 HEM A 201   NC   90.0 178.7  88.3                                  
REMARK 620 5 HEM A 201   ND   93.8  89.4 179.3  91.1                            
REMARK 620 6 MET A  80   SD  174.7  86.7  96.9  94.6  83.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CPT D 202  PT1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET D  65   SD                                                     
REMARK 620 2 CPT D 202   N1  177.2                                              
REMARK 620 3 CPT D 202   N2  105.5  77.2                                        
REMARK 620 4 CPT D 202  CL1   73.3 103.9 178.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CPT B 203  PT1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET B  65   SD                                                     
REMARK 620 2 CPT B 203   N1  177.5                                              
REMARK 620 3 CPT B 203   N2   70.0 107.5                                        
REMARK 620 4 CPT B 203  CL1  111.3  71.1 178.6                                  
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 HEM A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT F 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 205                 
DBREF  4RSZ A    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  4RSZ B    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  4RSZ C    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  4RSZ D    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  4RSZ E    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  4RSZ F    1   104  UNP    P00004   CYC_HORSE        2    105             
SEQRES   1 A  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 A  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 A  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 A  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 A  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 A  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 A  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 A  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 B  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 B  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 B  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 B  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 B  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 B  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 B  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 B  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 C  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 C  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 C  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 C  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 C  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 C  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 C  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 C  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 D  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 D  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 D  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 D  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 D  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 D  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 D  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 D  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 E  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 E  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 E  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 E  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 E  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 E  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 E  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 E  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 F  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 F  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 F  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 F  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 F  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 F  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 F  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 F  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
HET    HEM  A 201      43                                                       
HET    CPT  A 202       3                                                       
HET    NO3  A 203       4                                                       
HET    NO3  A 204       4                                                       
HET    HEM  B 201      43                                                       
HET    SO4  B 202       5                                                       
HET    CPT  B 203       4                                                       
HET    NO3  B 204       4                                                       
HET    NO3  B 205       4                                                       
HET    NO3  B 206       4                                                       
HET    HEM  C 201      43                                                       
HET    NO3  C 202       4                                                       
HET    NO3  C 203       4                                                       
HET    NO3  C 204       4                                                       
HET    NO3  C 205       4                                                       
HET    HEM  D 201      43                                                       
HET    CPT  D 202       4                                                       
HET    NO3  D 203       4                                                       
HET    NO3  D 204       4                                                       
HET    HEM  E 201      43                                                       
HET    CPT  E 202       1                                                       
HET    NO3  E 203       4                                                       
HET    NO3  E 204       4                                                       
HET    NO3  E 205       4                                                       
HET    HEM  F 201      43                                                       
HET    SO4  F 202       5                                                       
HET    CPT  F 203       3                                                       
HET    NO3  F 204       4                                                       
HET    NO3  F 205       4                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CPT CISPLATIN                                                        
HETNAM     NO3 NITRATE ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETSYN     HEM HEME                                                             
HETSYN     CPT DIAMMINE(DICHLORO)PLATINUM                                       
FORMUL   7  HEM    6(C34 H32 FE N4 O4)                                          
FORMUL   8  CPT    5(CL2 H6 N2 PT)                                              
FORMUL   9  NO3    16(N O3 1-)                                                  
FORMUL  12  SO4    2(O4 S 2-)                                                   
FORMUL  36  HOH   *127(H2 O)                                                    
HELIX    1   1 ASP A    2  CYS A   14  1                                  13    
HELIX    2   2 THR A   49  LYS A   55  1                                   7    
HELIX    3   3 LYS A   60  ASN A   70  1                                  11    
HELIX    4   4 ASN A   70  ILE A   75  1                                   6    
HELIX    5   5 LYS A   87  THR A  102  1                                  16    
HELIX    6   6 ASP B    2  CYS B   14  1                                  13    
HELIX    7   7 THR B   49  LYS B   55  1                                   7    
HELIX    8   8 LYS B   60  ASN B   70  1                                  11    
HELIX    9   9 ASN B   70  ILE B   75  1                                   6    
HELIX   10  10 LYS B   87  THR B  102  1                                  16    
HELIX   11  11 ASP C    2  CYS C   14  1                                  13    
HELIX   12  12 THR C   49  LYS C   55  1                                   7    
HELIX   13  13 LYS C   60  ASN C   70  1                                  11    
HELIX   14  14 ASN C   70  ILE C   75  1                                   6    
HELIX   15  15 LYS C   87  THR C  102  1                                  16    
HELIX   16  16 ASP D    2  CYS D   14  1                                  13    
HELIX   17  17 THR D   49  LYS D   55  1                                   7    
HELIX   18  18 LYS D   60  ASN D   70  1                                  11    
HELIX   19  19 ASN D   70  ILE D   75  1                                   6    
HELIX   20  20 LYS D   87  THR D  102  1                                  16    
HELIX   21  21 ASP E    2  CYS E   14  1                                  13    
HELIX   22  22 THR E   49  LYS E   55  1                                   7    
HELIX   23  23 LYS E   60  ASN E   70  1                                  11    
HELIX   24  24 ASN E   70  ILE E   75  1                                   6    
HELIX   25  25 LYS E   87  THR E  102  1                                  16    
HELIX   26  26 ASP F    2  CYS F   14  1                                  13    
HELIX   27  27 THR F   49  LYS F   55  1                                   7    
HELIX   28  28 LYS F   60  ASN F   70  1                                  11    
HELIX   29  29 ASN F   70  ILE F   75  1                                   6    
HELIX   30  30 LYS F   87  THR F  102  1                                  16    
LINK         OE2 GLU F  61                PT1  CPT F 203     1555   1555  1.83  
LINK         OE2 GLU A  61                PT1  CPT A 202     1555   1555  1.83  
LINK         NE2 HIS F  18                FE   HEM F 201     1555   1555  1.90  
LINK         NE2 HIS B  18                FE   HEM B 201     1555   1555  1.90  
LINK         NE2 HIS D  18                FE   HEM D 201     1555   1555  1.91  
LINK         NE2 HIS C  18                FE   HEM C 201     1555   1555  1.93  
LINK         NE2 HIS E  18                FE   HEM E 201     1555   1555  1.94  
LINK         NE2 HIS A  18                FE   HEM A 201     1555   1555  1.95  
LINK         SD  MET D  65                PT1  CPT D 202     1555   1555  2.23  
LINK         SD  MET A  65                PT1  CPT A 202     1555   1555  2.26  
LINK         SD  MET E  80                FE   HEM E 201     1555   1555  2.28  
LINK         SD  MET A  80                FE   HEM A 201     1555   1555  2.28  
LINK         SD  MET F  65                PT1  CPT F 203     1555   1555  2.28  
LINK         SD  MET E  65                PT1  CPT E 202     1555   1555  2.29  
LINK         SD  MET F  80                FE   HEM F 201     1555   1555  2.31  
LINK         SD  MET D  80                FE   HEM D 201     1555   1555  2.31  
LINK         SD  MET B  80                FE   HEM B 201     1555   1555  2.31  
LINK         SD  MET B  65                PT1  CPT B 203     1555   1555  2.33  
LINK         SD  MET C  80                FE   HEM C 201     1555   1555  2.35  
LINK         SG  CYS A  14                 CAB HEM A 201     1555   1555  1.77  
LINK         SG  CYS B  14                 CAB HEM B 201     1555   1555  1.65  
LINK         SG  CYS C  14                 CAB HEM C 201     1555   1555  1.73  
LINK         SG  CYS D  14                 CAB HEM D 201     1555   1555  1.74  
LINK         SG  CYS E  14                 CAB HEM E 201     1555   1555  1.68  
LINK         SG  CYS F  14                 CAB HEM F 201     1555   1555  1.76  
LINK         SG  CYS A  17                 CAC HEM A 201     1555   1555  1.82  
LINK         SG  CYS B  17                 CAC HEM B 201     1555   1555  1.79  
LINK         SG  CYS C  17                 CAC HEM C 201     1555   1555  1.83  
LINK         SG  CYS D  17                 CAC HEM D 201     1555   1555  1.75  
LINK         SG  CYS E  17                 CAC HEM E 201     1555   1555  1.72  
LINK         SG  CYS F  17                 CAC HEM F 201     1555   1555  1.81  
SITE     1 AC1 22 LYS A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC1 22 THR A  28  PRO A  30  ARG A  38  THR A  40                    
SITE     3 AC1 22 GLY A  41  TYR A  48  THR A  49  ASN A  52                    
SITE     4 AC1 22 TRP A  59  TYR A  67  LEU A  68  THR A  78                    
SITE     5 AC1 22 LYS A  79  MET A  80  ILE A  81  PHE A  82                    
SITE     6 AC1 22 LEU A  94  HOH A 305                                          
SITE     1 AC2  3 GLU A  61  MET A  65  GLU A  92                               
SITE     1 AC3  8 PHE A  10  THR A  19  VAL A  20  GLU A  21                    
SITE     2 AC3  8 HOH A 310  THR C  28  ILE C  81  HOH C 302                    
SITE     1 AC4  6 PHE A  82  ALA A  83  GLY A  84  LYS B   8                    
SITE     2 AC4  6 VAL B  11  GLN B  12                                          
SITE     1 AC5 21 LYS B  13  CYS B  14  GLN B  16  CYS B  17                    
SITE     2 AC5 21 HIS B  18  THR B  28  GLY B  29  PRO B  30                    
SITE     3 AC5 21 THR B  40  GLY B  41  TYR B  48  THR B  49                    
SITE     4 AC5 21 ASN B  52  TRP B  59  TYR B  67  LEU B  68                    
SITE     5 AC5 21 THR B  78  LYS B  79  MET B  80  LEU B  94                    
SITE     6 AC5 21 HOH B 307                                                     
SITE     1 AC6  4 LYS A  72  LYS B 100  GLU B 104  GLY E  23                    
SITE     1 AC7  5 GLU B  61  GLU B  62  MET B  65  GLU B  92                    
SITE     2 AC7  5 GLU E  62                                                     
SITE     1 AC8  8 THR A  28  ILE A  81  PHE B  10  THR B  19                    
SITE     2 AC8  8 VAL B  20  GLU B  21  HOH B 306  HOH B 318                    
SITE     1 AC9  6 PHE B  82  ALA B  83  GLY B  84  LYS C   8                    
SITE     2 AC9  6 VAL C  11  GLN C  12                                          
SITE     1 BC1  4 GLY B  41  PHE B  46  THR B  47  TYR B  48                    
SITE     1 BC2 22 LYS C  13  CYS C  14  GLN C  16  CYS C  17                    
SITE     2 BC2 22 HIS C  18  THR C  28  PRO C  30  ARG C  38                    
SITE     3 BC2 22 THR C  40  GLY C  41  TYR C  48  THR C  49                    
SITE     4 BC2 22 ASN C  52  TRP C  59  TYR C  67  LEU C  68                    
SITE     5 BC2 22 THR C  78  LYS C  79  MET C  80  ILE C  81                    
SITE     6 BC2 22 LEU C  94  HOH C 308                                          
SITE     1 BC3  8 THR B  28  ILE B  81  PHE C  10  THR C  19                    
SITE     2 BC3  8 VAL C  20  GLU C  21  HOH C 304  HOH C 305                    
SITE     1 BC4  6 LYS A   8  VAL A  11  GLN A  12  PHE C  82                    
SITE     2 BC4  6 ALA C  83  GLY C  84                                          
SITE     1 BC5  3 ALA B  83  GLU C   4  LYS C   7                               
SITE     1 BC6  3 PHE C  36  LYS C  99  LYS F  22                               
SITE     1 BC7 21 LYS D  13  CYS D  14  GLN D  16  CYS D  17                    
SITE     2 BC7 21 HIS D  18  THR D  28  GLY D  29  PRO D  30                    
SITE     3 BC7 21 ARG D  38  GLY D  41  TYR D  48  THR D  49                    
SITE     4 BC7 21 ASN D  52  TRP D  59  TYR D  67  LEU D  68                    
SITE     5 BC7 21 THR D  78  LYS D  79  MET D  80  LEU D  94                    
SITE     6 BC7 21 HOH D 301                                                     
SITE     1 BC8  5 GLU A  61  GLU D  61  GLU D  62  MET D  65                    
SITE     2 BC8  5 GLU D  92                                                     
SITE     1 BC9  8 PHE D  10  THR D  19  VAL D  20  GLU D  21                    
SITE     2 BC9  8 HOH D 310  HOH D 318  THR F  28  ILE F  81                    
SITE     1 CC1  6 PHE D  82  ALA D  83  GLY D  84  LYS E   8                    
SITE     2 CC1  6 VAL E  11  GLN E  12                                          
SITE     1 CC2 20 LYS E  13  CYS E  14  CYS E  17  HIS E  18                    
SITE     2 CC2 20 THR E  28  GLY E  29  ARG E  38  THR E  40                    
SITE     3 CC2 20 GLY E  41  TYR E  48  THR E  49  ASN E  52                    
SITE     4 CC2 20 TRP E  59  TYR E  67  LEU E  68  THR E  78                    
SITE     5 CC2 20 LYS E  79  MET E  80  LEU E  94  HOH E 301                    
SITE     1 CC3  1 MET E  65                                                     
SITE     1 CC4  7 HIS E  26  PRO E  30  ASN E  31  ALA E  43                    
SITE     2 CC4  7 PRO E  44  GLY E  45  PHE E  46                               
SITE     1 CC5  6 PHE E  82  ALA E  83  GLY E  84  LYS F   8                    
SITE     2 CC5  6 VAL F  11  GLN F  12                                          
SITE     1 CC6  7 THR D  28  ILE D  81  PHE E  10  THR E  19                    
SITE     2 CC6  7 VAL E  20  GLU E  21  HOH E 309                               
SITE     1 CC7 22 LYS F  13  CYS F  14  GLN F  16  CYS F  17                    
SITE     2 CC7 22 HIS F  18  THR F  28  GLY F  29  PRO F  30                    
SITE     3 CC7 22 ARG F  38  THR F  40  GLY F  41  TYR F  48                    
SITE     4 CC7 22 THR F  49  ASN F  52  TRP F  59  TYR F  67                    
SITE     5 CC7 22 THR F  78  LYS F  79  MET F  80  ILE F  81                    
SITE     6 CC7 22 LEU F  94  HOH F 311                                          
SITE     1 CC8 10 LYS D  25  LYS D  27  LYS E  25  LYS E  27                    
SITE     2 CC8 10 GLN F  16  LYS F  25  LYS F  27  HOH F 303                    
SITE     3 CC8 10 HOH F 304  HOH F 308                                          
SITE     1 CC9  3 GLU F  61  MET F  65  GLU F  92                               
SITE     1 DC1  7 THR E  28  ILE E  81  HOH E 312  THR F  19                    
SITE     2 DC1  7 VAL F  20  GLU F  21  HOH F 313                               
SITE     1 DC2  6 LYS D   8  VAL D  11  GLN D  12  PHE F  82                    
SITE     2 DC2  6 ALA F  83  GLY F  84                                          
CRYST1  120.344  120.344   36.673  90.00  90.00 120.00 P 3          18          
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      0.008310  0.004797  0.000000        0.00000                         
SCALE2      0.000000  0.009595  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027268        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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