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Database: PDB
Entry: 6CHI
LinkDB: 6CHI
Original site: 6CHI 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 22-FEB-18   6CHI              
TITLE     HUMAN CYTOCHROME P450 17A1 IN COMPLEX WITH INHIBITOR: ABIRATERONE C6  
TITLE    2 AMIDE                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 24-508;                                           
COMPND   5 SYNONYM: 17-ALPHA-HYDROXYPROGESTERONE ALDOLASE,CYPXVII,CYTOCHROME    
COMPND   6 P450 17A1,CYTOCHROME P450-C17,CYTOCHROME P450C17,STEROID 17-ALPHA-   
COMPND   7 MONOOXYGENASE;                                                       
COMPND   8 EC: 1.14.14.19,1.14.14.32;                                           
COMPND   9 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: CYP17A1, CYP17, S17AH;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOCHROME P450, P450, CYP17A1, P450C17, P450 17A1, MONOOXYGENASE,    
KEYWDS   2 17A-HYDROXYLASE, HEME PROTEIN, CYTOCHROME P450 OXIDOREDUCTASE,       
KEYWDS   3 MEMBRANE, MICROSOME, ENDOPLASMIC RETICULUM, OXIDOREDUCTASE-          
KEYWDS   4 OXIDOREDUCTASE INHIBITOR, OXIDOREDUCTASE, OXIDOREDUCTASE-            
KEYWDS   5 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.E.SCOTT                                                             
REVDAT   3   01-JAN-20 6CHI    1       REMARK                                   
REVDAT   2   27-JUN-18 6CHI    1       JRNL                                     
REVDAT   1   06-JUN-18 6CHI    0                                                
JRNL        AUTH   C.FEHL,C.D.VOGT,R.YADAV,K.LI,E.E.SCOTT,J.AUBE                
JRNL        TITL   STRUCTURE-BASED DESIGN OF INHIBITORS WITH IMPROVED           
JRNL        TITL 2 SELECTIVITY FOR STEROIDOGENIC CYTOCHROME P450 17A1 OVER      
JRNL        TITL 3 CYTOCHROME P450 21A2.                                        
JRNL        REF    J. MED. CHEM.                 V.  61  4946 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29792703                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00419                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155:0000)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 64151                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3244                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.6767 -  7.6546    0.99     2825   163  0.1477 0.1694        
REMARK   3     2  7.6546 -  6.0834    1.00     2756   140  0.1711 0.2341        
REMARK   3     3  6.0834 -  5.3166    1.00     2706   131  0.1768 0.1954        
REMARK   3     4  5.3166 -  4.8315    1.00     2683   164  0.1478 0.1791        
REMARK   3     5  4.8315 -  4.4858    1.00     2667   156  0.1339 0.1959        
REMARK   3     6  4.4858 -  4.2216    1.00     2631   158  0.1506 0.2333        
REMARK   3     7  4.2216 -  4.0104    1.00     2683   138  0.1557 0.2146        
REMARK   3     8  4.0104 -  3.8360    1.00     2661   142  0.1683 0.2359        
REMARK   3     9  3.8360 -  3.6885    1.00     2647   143  0.1817 0.2386        
REMARK   3    10  3.6885 -  3.5613    1.00     2614   156  0.1993 0.2584        
REMARK   3    11  3.5613 -  3.4500    1.00     2629   156  0.2128 0.2610        
REMARK   3    12  3.4500 -  3.3514    1.00     2676   124  0.2115 0.2535        
REMARK   3    13  3.3514 -  3.2633    1.00     2649   141  0.2264 0.3065        
REMARK   3    14  3.2633 -  3.1837    1.00     2636   124  0.2257 0.2848        
REMARK   3    15  3.1837 -  3.1113    1.00     2663   141  0.2347 0.3190        
REMARK   3    16  3.1113 -  3.0451    1.00     2662   122  0.2535 0.3551        
REMARK   3    17  3.0451 -  2.9843    1.00     2582   152  0.2721 0.3683        
REMARK   3    18  2.9843 -  2.9280    1.00     2657   126  0.2808 0.3720        
REMARK   3    19  2.9280 -  2.8757    1.00     2624   136  0.2687 0.3493        
REMARK   3    20  2.8757 -  2.8270    1.00     2622   144  0.2568 0.3108        
REMARK   3    21  2.8270 -  2.7814    1.00     2622   121  0.2620 0.3187        
REMARK   3    22  2.7814 -  2.7386    1.00     2635   149  0.2754 0.3546        
REMARK   3    23  2.7386 -  2.6983    0.91     2377   117  0.3038 0.3862        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.240           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          15604                                  
REMARK   3   ANGLE     :  0.562          21210                                  
REMARK   3   CHIRALITY :  0.041           2380                                  
REMARK   3   PLANARITY :  0.002           2676                                  
REMARK   3   DIHEDRAL  : 12.841           9376                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232769.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64275                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.698                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.673                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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: 3SWZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.175 M TRIS, PH 8.5 CONTAINING 35%      
REMARK 280  PEG 3350, 3% GLYCEROL, AND 0.250-0.275 M LITHIUM SULFATE, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.71200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.94550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.05400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.94550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.71200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       77.05400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     ASP A   274                                                      
REMARK 465     ASN A   275                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     ASN A   277                                                      
REMARK 465     ALA A   278                                                      
REMARK 465     GLY A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     ASP A   281                                                      
REMARK 465     GLN A   282                                                      
REMARK 465     GLU A   505                                                      
REMARK 465     GLY A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     THR A   508                                                      
REMARK 465     HIS A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     HIS A   512                                                      
REMARK 465     MET B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     TYR B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     ASN B   275                                                      
REMARK 465     GLY B   276                                                      
REMARK 465     ASN B   277                                                      
REMARK 465     ALA B   278                                                      
REMARK 465     GLY B   279                                                      
REMARK 465     PRO B   280                                                      
REMARK 465     ASP B   281                                                      
REMARK 465     GLU B   505                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     THR B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     HIS B   510                                                      
REMARK 465     HIS B   511                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     MET C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     LYS C    22                                                      
REMARK 465     THR C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     LYS C    26                                                      
REMARK 465     TYR C    27                                                      
REMARK 465     PRO C    28                                                      
REMARK 465     ASN C   277                                                      
REMARK 465     GLY C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     THR C   508                                                      
REMARK 465     HIS C   509                                                      
REMARK 465     HIS C   510                                                      
REMARK 465     HIS C   511                                                      
REMARK 465     HIS C   512                                                      
REMARK 465     MET D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     TYR D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     ASN D   275                                                      
REMARK 465     GLY D   276                                                      
REMARK 465     ASN D   277                                                      
REMARK 465     ALA D   278                                                      
REMARK 465     GLY D   279                                                      
REMARK 465     PRO D   280                                                      
REMARK 465     ASP D   281                                                      
REMARK 465     GLN D   503                                                      
REMARK 465     ALA D   504                                                      
REMARK 465     GLU D   505                                                      
REMARK 465     GLY D   506                                                      
REMARK 465     SER D   507                                                      
REMARK 465     THR D   508                                                      
REMARK 465     HIS D   509                                                      
REMARK 465     HIS D   510                                                      
REMARK 465     HIS D   511                                                      
REMARK 465     HIS D   512                                                      
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    VAL A 218   C     PRO A 219   N       0.130                       
REMARK 500    VAL B 218   C     PRO B 219   N       0.151                       
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    ILE A  87      -77.19   -113.45                                   
REMARK 500    ASN A 108       62.37     64.59                                   
REMARK 500    ASP A 137      131.80    -37.19                                   
REMARK 500    SER A 210      140.13   -172.79                                   
REMARK 500    ASP A 212     -131.31     61.34                                   
REMARK 500    LEU A 217      -71.53    -46.58                                   
REMARK 500    LEU A 370     -154.15     48.90                                   
REMARK 500    SER A 379     -159.58   -150.17                                   
REMARK 500    GLN A 408       70.23     49.69                                   
REMARK 500    SER A 431       70.62   -104.67                                   
REMARK 500    LYS A 481     -156.51   -121.31                                   
REMARK 500    ILE B  87      -71.97   -110.43                                   
REMARK 500    ILE B 112      -58.00   -123.42                                   
REMARK 500    ASP B 137     -167.74   -164.32                                   
REMARK 500    GLN B 140       40.35    -94.70                                   
REMARK 500    ASP B 212     -133.52   -115.32                                   
REMARK 500    SER B 273     -112.63     64.38                                   
REMARK 500    VAL B 336      -37.92   -130.96                                   
REMARK 500    LEU B 370     -139.56     45.56                                   
REMARK 500    SER B 379     -156.22   -155.24                                   
REMARK 500    GLU B 383       -6.64     74.43                                   
REMARK 500    SER B 431       55.18    -90.31                                   
REMARK 500    LYS B 481     -159.70   -126.56                                   
REMARK 500    ALA B 502       40.67    -82.48                                   
REMARK 500    ASN C 108       56.92     70.44                                   
REMARK 500    ILE C 112      -62.58   -124.15                                   
REMARK 500    PHE C 135       35.85    -85.57                                   
REMARK 500    ASP C 139      175.83    -55.18                                   
REMARK 500    ASP C 212     -159.56   -149.94                                   
REMARK 500    SER C 258       83.73   -155.53                                   
REMARK 500    ASP C 281     -169.85    -72.77                                   
REMARK 500    LEU C 370     -141.09     49.56                                   
REMARK 500    SER C 379     -157.47   -145.59                                   
REMARK 500    SER C 431       55.93    -96.96                                   
REMARK 500    LYS C 481     -159.72   -141.45                                   
REMARK 500    ALA C 504      -77.39    -56.80                                   
REMARK 500    HIS D  46       -0.29     64.85                                   
REMARK 500    ASN D 108       53.96     71.41                                   
REMARK 500    ARG D 109       30.34     74.25                                   
REMARK 500    ILE D 112      -57.25   -128.79                                   
REMARK 500    LEU D 134       39.19    -83.46                                   
REMARK 500    ASP D 212     -165.98   -160.08                                   
REMARK 500    PRO D 225       44.81    -79.91                                   
REMARK 500    LYS D 227       54.71   -117.13                                   
REMARK 500    LEU D 370     -142.14     59.05                                   
REMARK 500    GLU D 383      -19.94     84.85                                   
REMARK 500    SER D 431       47.00    -77.28                                   
REMARK 500    GLU D 501       82.59    -63.51                                   
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                             HEM A 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 442   SG                                                     
REMARK 620 2 HEM A 600   NA   98.8                                              
REMARK 620 3 HEM A 600   NB   84.0  89.3                                        
REMARK 620 4 HEM A 600   NC   83.2 178.0  91.3                                  
REMARK 620 5 HEM A 600   ND   96.1  91.2 179.5  88.2                            
REMARK 620 6 3NX A 601   N32 169.0  84.0  85.4  94.2  94.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 3NX B 601   N32                                                    
REMARK 620 2 HEM B 600   NA   85.3                                              
REMARK 620 3 HEM B 600   NB   80.8  88.9                                        
REMARK 620 4 HEM B 600   NC   95.2 179.5  91.4                                  
REMARK 620 5 HEM B 600   ND  100.9  91.2 178.3  88.5                            
REMARK 620 6 CYS B 442   SG  161.8  93.4  81.1  86.2  97.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 3NX C 601   N32                                                    
REMARK 620 2 HEM C 600   NA   82.2                                              
REMARK 620 3 HEM C 600   NB   81.5  90.6                                        
REMARK 620 4 HEM C 600   NC   89.7 171.7  90.0                                  
REMARK 620 5 HEM C 600   ND   90.8  90.6 172.0  87.8                            
REMARK 620 6 CYS C 442   SG  166.9 106.8  88.7  81.4  98.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 442   SG                                                     
REMARK 620 2 HEM D 600   NA   98.4                                              
REMARK 620 3 HEM D 600   NB   82.7  89.4                                        
REMARK 620 4 HEM D 600   NC   82.4 179.0  91.2                                  
REMARK 620 5 HEM D 600   ND   97.8  90.3 179.4  89.1                            
REMARK 620 6 3NX D 601   N32 161.5  74.6  80.2 104.8  99.3                      
REMARK 620 N                    1     2     3     4     5                       
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 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3NX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3NX B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3NX C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3NX D 601                 
DBREF  6CHI A   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  6CHI B   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  6CHI C   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  6CHI D   24   508  UNP    P05093   CP17A_HUMAN     24    508             
SEQADV 6CHI MET A   19  UNP  P05093              INITIATING METHIONINE          
SEQADV 6CHI ALA A   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS A   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS A   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI THR A   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS A  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS A  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS A  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS A  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI MET B   19  UNP  P05093              INITIATING METHIONINE          
SEQADV 6CHI ALA B   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS B   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS B   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI THR B   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS B  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS B  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS B  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS B  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI MET C   19  UNP  P05093              INITIATING METHIONINE          
SEQADV 6CHI ALA C   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS C   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS C   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI THR C   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS C  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS C  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS C  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS C  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI MET D   19  UNP  P05093              INITIATING METHIONINE          
SEQADV 6CHI ALA D   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS D   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI LYS D   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI THR D   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS D  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS D  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS D  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 6CHI HIS D  512  UNP  P05093              EXPRESSION TAG                 
SEQRES   1 A  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 A  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 A  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 A  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 A  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 A  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 A  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 A  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 A  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 A  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 A  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 A  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 A  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 A  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 A  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 A  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 A  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 A  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 A  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 A  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 A  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 A  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 A  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 A  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 A  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 A  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 A  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 A  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 A  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 A  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 A  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 A  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 A  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 A  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 A  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 A  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 A  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 A  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 B  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 B  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 B  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 B  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 B  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 B  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 B  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 B  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 B  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 B  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 B  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 B  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 B  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 B  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 B  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 B  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 B  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 B  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 B  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 B  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 B  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 B  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 B  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 B  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 B  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 B  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 B  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 B  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 B  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 B  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 B  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 B  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 B  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 B  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 B  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 B  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 B  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 B  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 C  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 C  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 C  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 C  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 C  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 C  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 C  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 C  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 C  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 C  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 C  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 C  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 C  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 C  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 C  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 C  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 C  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 C  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 C  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 C  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 C  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 C  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 C  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 C  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 C  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 C  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 C  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 C  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 C  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 C  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 C  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 C  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 C  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 C  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 C  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 C  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 C  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 C  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 D  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 D  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 D  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 D  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 D  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 D  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 D  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 D  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 D  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 D  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 D  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 D  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 D  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 D  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 D  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 D  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 D  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 D  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 D  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 D  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 D  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 D  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 D  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 D  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 D  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 D  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 D  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 D  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 D  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 D  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 D  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 D  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 D  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 D  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 D  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 D  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 D  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 D  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
HET    HEM  A 600      73                                                       
HET    3NX  A 601      29                                                       
HET    HEM  B 600      73                                                       
HET    3NX  B 601      29                                                       
HET    HEM  C 600      73                                                       
HET    3NX  C 601      29                                                       
HET    HEM  D 600      73                                                       
HET    3NX  D 601      29                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     3NX 3-HYDROXY-17-(3-PYRIDYL)-ANDROST-5,16-DIEN-6-AMIDE               
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  3NX    4(C25 H32 N2 O2)                                             
FORMUL  13  HOH   *86(H2 O)                                                     
HELIX    1 AA1 HIS A   48  GLY A   61  1                                  14    
HELIX    2 AA2 HIS A   78  ILE A   87  1                                  10    
HELIX    3 AA3 LYS A   89  SER A   94  5                                   6    
HELIX    4 AA4 MET A   99  SER A  106  1                                   8    
HELIX    5 AA5 GLY A  118  LEU A  134  1                                  17    
HELIX    6 AA6 LYS A  141  THR A  159  1                                  19    
HELIX    7 AA7 ILE A  167  ASN A  185  1                                  19    
HELIX    8 AA8 ASP A  192  SER A  210  1                                  19    
HELIX    9 AA9 PRO A  219  PHE A  224  1                                   6    
HELIX   10 AB1 LYS A  227  PHE A  254  1                                  28    
HELIX   11 AB2 ASN A  261  SER A  273  1                                  13    
HELIX   12 AB3 ASP A  283  LEU A  287  5                                   5    
HELIX   13 AB4 SER A  288  ASN A  321  1                                  34    
HELIX   14 AB5 ASN A  321  VAL A  336  1                                  16    
HELIX   15 AB6 THR A  343  ARG A  349  5                                   7    
HELIX   16 AB7 LEU A  350  ARG A  364  1                                  15    
HELIX   17 AB8 ASN A  395  ASN A  402  1                                   8    
HELIX   18 AB9 MET A  413  LEU A  418  5                                   6    
HELIX   19 AC1 GLY A  444  ARG A  462  1                                  19    
HELIX   20 AC2 ARG A  496  ALA A  502  1                                   7    
HELIX   21 AC3 HIS B   48  GLY B   61  1                                  14    
HELIX   22 AC4 HIS B   78  ILE B   87  1                                  10    
HELIX   23 AC5 LYS B   89  SER B   94  5                                   6    
HELIX   24 AC6 MET B   99  SER B  106  1                                   8    
HELIX   25 AC7 GLY B  118  PHE B  135  1                                  18    
HELIX   26 AC8 LYS B  141  THR B  159  1                                  19    
HELIX   27 AC9 ILE B  167  ASN B  185  1                                  19    
HELIX   28 AD1 ASP B  192  SER B  210  1                                  19    
HELIX   29 AD2 PRO B  219  ILE B  223  5                                   5    
HELIX   30 AD3 LYS B  227  GLU B  252  1                                  26    
HELIX   31 AD4 ASN B  261  ASN B  272  1                                  12    
HELIX   32 AD5 SER B  284  LEU B  287  5                                   4    
HELIX   33 AD6 SER B  288  ASN B  321  1                                  34    
HELIX   34 AD7 ASN B  321  VAL B  336  1                                  16    
HELIX   35 AD8 THR B  343  ARG B  349  5                                   7    
HELIX   36 AD9 LEU B  350  ARG B  364  1                                  15    
HELIX   37 AE1 ASN B  395  ASN B  402  1                                   8    
HELIX   38 AE2 MET B  413  LEU B  418  5                                   6    
HELIX   39 AE3 ALA B  437  SER B  441  5                                   5    
HELIX   40 AE4 GLY B  444  ARG B  462  1                                  19    
HELIX   41 AE5 ARG B  496  ALA B  502  1                                   7    
HELIX   42 AE6 HIS C   48  GLY C   61  1                                  14    
HELIX   43 AE7 HIS C   78  ILE C   87  1                                  10    
HELIX   44 AE8 MET C   99  SER C  106  1                                   8    
HELIX   45 AE9 GLY C  118  PHE C  135  1                                  18    
HELIX   46 AF1 LYS C  141  THR C  159  1                                  19    
HELIX   47 AF2 ILE C  167  ASN C  185  1                                  19    
HELIX   48 AF3 ASP C  192  SER C  210  1                                  19    
HELIX   49 AF4 LYS C  227  PHE C  254  1                                  28    
HELIX   50 AF5 ASN C  261  SER C  273  1                                  13    
HELIX   51 AF6 ASP C  281  LEU C  287  5                                   7    
HELIX   52 AF7 SER C  288  ASN C  321  1                                  34    
HELIX   53 AF8 ASN C  321  VAL C  336  1                                  16    
HELIX   54 AF9 THR C  343  ARG C  349  5                                   7    
HELIX   55 AG1 LEU C  350  ARG C  364  1                                  15    
HELIX   56 AG2 ASN C  395  ASN C  402  1                                   8    
HELIX   57 AG3 MET C  413  LEU C  418  5                                   6    
HELIX   58 AG4 ALA C  437  SER C  441  5                                   5    
HELIX   59 AG5 GLY C  444  ARG C  462  1                                  19    
HELIX   60 AG6 ARG C  496  GLU C  505  1                                  10    
HELIX   61 AG7 HIS D   48  GLY D   61  1                                  14    
HELIX   62 AG8 HIS D   78  ILE D   87  1                                  10    
HELIX   63 AG9 MET D   99  SER D  106  1                                   8    
HELIX   64 AH1 GLY D  118  LEU D  134  1                                  17    
HELIX   65 AH2 LYS D  141  THR D  159  1                                  19    
HELIX   66 AH3 ILE D  167  ASN D  185  1                                  19    
HELIX   67 AH4 ASP D  192  LEU D  209  1                                  18    
HELIX   68 AH5 PRO D  219  ILE D  223  5                                   5    
HELIX   69 AH6 LYS D  227  PHE D  254  1                                  28    
HELIX   70 AH7 ASN D  261  ASN D  272  1                                  12    
HELIX   71 AH8 GLN D  282  LEU D  287  5                                   6    
HELIX   72 AH9 SER D  288  ASN D  321  1                                  34    
HELIX   73 AI1 ASN D  321  VAL D  336  1                                  16    
HELIX   74 AI2 THR D  343  ASN D  348  5                                   6    
HELIX   75 AI3 LEU D  350  ARG D  364  1                                  15    
HELIX   76 AI4 ASN D  395  HIS D  401  1                                   7    
HELIX   77 AI5 MET D  413  LEU D  418  5                                   6    
HELIX   78 AI6 ALA D  437  SER D  441  5                                   5    
HELIX   79 AI7 GLY D  444  PHE D  463  1                                  20    
HELIX   80 AI8 ARG D  496  GLU D  501  1                                   6    
SHEET    1 AA1 5 LEU A  36  LEU A  40  0                                        
SHEET    2 AA1 5 ILE D  63  MET D  68  1  O  SER D  65   N  VAL A  37           
SHEET    3 AA1 5 LYS D  71  VAL D  76 -1  O  LYS D  71   N  MET D  68           
SHEET    4 AA1 5 GLU D 391  ILE D 394  1  O  GLU D 391   N  VAL D  74           
SHEET    5 AA1 5 HIS D 373  LYS D 374 -1  N  HIS D 373   O  VAL D 392           
SHEET    1 AA2 5 HIS A 373  LYS A 374  0                                        
SHEET    2 AA2 5 GLU A 391  ILE A 394 -1  O  VAL A 392   N  HIS A 373           
SHEET    3 AA2 5 LYS A  71  VAL A  76  1  N  VAL A  74   O  ILE A 393           
SHEET    4 AA2 5 ILE A  63  MET A  68 -1  N  MET A  68   O  LYS A  71           
SHEET    5 AA2 5 LEU D  36  LEU D  40  1  O  GLY D  38   N  ARG A  67           
SHEET    1 AA3 3 GLN A 163  ILE A 165  0                                        
SHEET    2 AA3 3 VAL A 491  VAL A 495 -1  O  VAL A 491   N  ILE A 165           
SHEET    3 AA3 3 PHE A 463  GLU A 466 -1  N  ASP A 464   O  LYS A 494           
SHEET    1 AA4 2 SER A 379  ILE A 381  0                                        
SHEET    2 AA4 2 PHE A 384  VAL A 386 -1  O  VAL A 386   N  SER A 379           
SHEET    1 AA5 2 ILE A 479  PRO A 480  0                                        
SHEET    2 AA5 2 PHE A 484  LEU A 485 -1  O  LEU A 485   N  ILE A 479           
SHEET    1 AA6 5 LEU B  36  LEU B  40  0                                        
SHEET    2 AA6 5 ILE C  63  MET C  68  1  O  SER C  65   N  VAL B  37           
SHEET    3 AA6 5 LYS C  71  VAL C  76 -1  O  LYS C  71   N  MET C  68           
SHEET    4 AA6 5 GLU C 391  ILE C 394  1  O  ILE C 393   N  VAL C  76           
SHEET    5 AA6 5 HIS C 373  LYS C 374 -1  N  HIS C 373   O  VAL C 392           
SHEET    1 AA7 5 HIS B 373  LYS B 374  0                                        
SHEET    2 AA7 5 GLU B 391  ILE B 394 -1  O  VAL B 392   N  HIS B 373           
SHEET    3 AA7 5 LYS B  71  VAL B  76  1  N  VAL B  74   O  ILE B 393           
SHEET    4 AA7 5 ILE B  63  MET B  68 -1  N  MET B  68   O  LYS B  71           
SHEET    5 AA7 5 LEU C  36  LEU C  40  1  O  VAL C  37   N  SER B  65           
SHEET    1 AA8 3 GLN B 163  ILE B 165  0                                        
SHEET    2 AA8 3 VAL B 491  VAL B 495 -1  O  ILE B 493   N  GLN B 163           
SHEET    3 AA8 3 PHE B 463  GLU B 466 -1  N  ASP B 464   O  LYS B 494           
SHEET    1 AA9 2 SER B 379  ILE B 381  0                                        
SHEET    2 AA9 2 PHE B 384  VAL B 386 -1  O  VAL B 386   N  SER B 379           
SHEET    1 AB1 2 ILE B 479  PRO B 480  0                                        
SHEET    2 AB1 2 PHE B 484  LEU B 485 -1  O  LEU B 485   N  ILE B 479           
SHEET    1 AB2 3 GLN C 163  ILE C 165  0                                        
SHEET    2 AB2 3 VAL C 491  VAL C 495 -1  O  VAL C 491   N  ILE C 165           
SHEET    3 AB2 3 PHE C 463  GLU C 466 -1  N  ASP C 464   O  LYS C 494           
SHEET    1 AB3 2 SER C 379  ILE C 381  0                                        
SHEET    2 AB3 2 PHE C 384  VAL C 386 -1  O  VAL C 386   N  SER C 379           
SHEET    1 AB4 2 ILE C 479  PRO C 480  0                                        
SHEET    2 AB4 2 PHE C 484  LEU C 485 -1  O  LEU C 485   N  ILE C 479           
SHEET    1 AB5 2 SER D 164  ILE D 165  0                                        
SHEET    2 AB5 2 VAL D 491  LYS D 492 -1  O  VAL D 491   N  ILE D 165           
SHEET    1 AB6 2 SER D 379  ILE D 381  0                                        
SHEET    2 AB6 2 PHE D 384  VAL D 386 -1  O  VAL D 386   N  SER D 379           
SHEET    1 AB7 2 ILE D 479  PRO D 480  0                                        
SHEET    2 AB7 2 PHE D 484  LEU D 485 -1  O  LEU D 485   N  ILE D 479           
LINK         SG  CYS A 442                FE   HEM A 600     1555   1555  2.70  
LINK        FE   HEM A 600                 N32 3NX A 601     1555   1555  2.49  
LINK        FE   HEM B 600                 N32 3NX B 601     1555   1555  2.53  
LINK        FE   HEM C 600                 N32 3NX C 601     1555   1555  2.52  
LINK         SG  CYS B 442                FE   HEM B 600     1555   1555  2.76  
LINK         SG  CYS C 442                FE   HEM C 600     1555   1555  2.81  
LINK         SG  CYS D 442                FE   HEM D 600     1555   1555  2.80  
LINK        FE   HEM D 600                 N32 3NX D 601     1555   1555  4.96  
SITE     1 AC1 20 ARG A  96  ILE A 112  ALA A 113  TRP A 121                    
SITE     2 AC1 20 ARG A 125  ILE A 299  ALA A 302  THR A 306                    
SITE     3 AC1 20 VAL A 310  VAL A 366  LEU A 370  ILE A 371                    
SITE     4 AC1 20 HIS A 373  PRO A 434  PHE A 435  ARG A 440                    
SITE     5 AC1 20 CYS A 442  ILE A 443  ALA A 448  3NX A 601                    
SITE     1 AC2 10 ALA A 105  ALA A 113  TYR A 201  ASN A 202                    
SITE     2 AC2 10 ILE A 205  ARG A 239  GLY A 297  ASP A 298                    
SITE     3 AC2 10 THR A 306  HEM A 600                                          
SITE     1 AC3 20 ARG B  96  ILE B 112  ALA B 113  TRP B 121                    
SITE     2 AC3 20 ARG B 125  ILE B 179  ALA B 302  GLY B 303                    
SITE     3 AC3 20 THR B 306  VAL B 310  VAL B 366  LEU B 370                    
SITE     4 AC3 20 ILE B 371  HIS B 373  PRO B 434  PHE B 435                    
SITE     5 AC3 20 ARG B 440  CYS B 442  ALA B 448  3NX B 601                    
SITE     1 AC4 12 ALA B 105  ALA B 113  TYR B 201  ASN B 202                    
SITE     2 AC4 12 ILE B 205  ARG B 239  GLY B 297  ASP B 298                    
SITE     3 AC4 12 GLU B 305  THR B 306  VAL B 482  HEM B 600                    
SITE     1 AC5 20 ARG C  96  ILE C 112  ALA C 113  TRP C 121                    
SITE     2 AC5 20 ARG C 125  ILE C 299  ALA C 302  THR C 306                    
SITE     3 AC5 20 VAL C 366  LEU C 370  ILE C 371  HIS C 373                    
SITE     4 AC5 20 PRO C 434  PHE C 435  ARG C 440  CYS C 442                    
SITE     5 AC5 20 ILE C 443  ALA C 448  3NX C 601  HOH C 705                    
SITE     1 AC6 11 ALA C 105  ALA C 113  PHE C 114  TYR C 201                    
SITE     2 AC6 11 ASN C 202  ILE C 205  ARG C 239  GLY C 297                    
SITE     3 AC6 11 ASP C 298  VAL C 482  HEM C 600                               
SITE     1 AC7 19 ARG D  96  ILE D 112  ALA D 113  TRP D 121                    
SITE     2 AC7 19 ARG D 125  ALA D 302  GLY D 303  THR D 306                    
SITE     3 AC7 19 VAL D 310  VAL D 366  LEU D 370  ILE D 371                    
SITE     4 AC7 19 HIS D 373  PRO D 434  PHE D 435  ARG D 440                    
SITE     5 AC7 19 CYS D 442  ALA D 448  3NX D 601                               
SITE     1 AC8 13 ALA D 105  ALA D 113  PHE D 114  TYR D 201                    
SITE     2 AC8 13 ASN D 202  ILE D 205  ARG D 239  GLY D 297                    
SITE     3 AC8 13 ASP D 298  THR D 306  VAL D 366  VAL D 482                    
SITE     4 AC8 13 HEM D 600                                                     
CRYST1   89.424  154.108  167.891  90.00  90.00  90.00 P 21 21 21   16          
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      0.011183  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006489  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005956        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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