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Database: PDB
Entry: 4NKW
LinkDB: 4NKW
Original site: 4NKW 
HEADER    OXIDOREDUCTASE, LYASE                   13-NOV-13   4NKW              
TITLE     HUMAN STEROIDOGENIC CYTOCHROME P450 17A1 MUTANT A105L WITH SUBSTRATE  
TITLE    2 PREGNENOLONE                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: 17-ALPHA-HYDROXYPROGESTERONE ALDOLASE, CYPXVII, CYTOCHROME  
COMPND   5 P450 17A1, CYTOCHROME P450-C17, CYTOCHROME P450C17, STEROID 17-ALPHA-
COMPND   6 MONOOXYGENASE;                                                       
COMPND   7 EC: 1.14.99.9, 4.1.2.30;                                             
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP17, CYP17A1, S17AH;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI17A1DELTA19H                        
KEYWDS    HEME PROTEIN, MONOOXYGENASE, STEROID 17ALPHA-HYDROXYLASE, STEROID     
KEYWDS   2 C17,20 LYASE, NADPH-CYTOCHROME P450 REDUCTASE, CYTOCHROME B5,        
KEYWDS   3 ENDOPLASMIC RETICULUM MEMBRANE, OXIDOREDUCTASE, LYASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.E.SCOTT,E.P.PETRUNAK                                                
REVDAT   2   03-DEC-14 4NKW    1       JRNL                                     
REVDAT   1   22-OCT-14 4NKW    0                                                
JRNL        AUTH   E.M.PETRUNAK,N.M.DEVORE,P.R.PORUBSKY,E.E.SCOTT               
JRNL        TITL   STRUCTURES OF HUMAN STEROIDOGENIC CYTOCHROME P450 17A1 WITH  
JRNL        TITL 2 SUBSTRATES.                                                  
JRNL        REF    J.BIOL.CHEM.                  V. 289 32952 2014              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   25301938                                                     
JRNL        DOI    10.1074/JBC.M114.610998                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 79236                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3978                            
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 39.1129 -  7.5730    0.99     2903   158  0.1607 0.1726        
REMARK   3     2  7.5730 -  6.0180    1.00     2780   154  0.2038 0.2564        
REMARK   3     3  6.0180 -  5.2593    1.00     2759   143  0.2052 0.2504        
REMARK   3     4  5.2593 -  4.7794    1.00     2743   147  0.1733 0.2196        
REMARK   3     5  4.7794 -  4.4373    1.00     2745   137  0.1621 0.2146        
REMARK   3     6  4.4373 -  4.1760    1.00     2730   133  0.1656 0.2316        
REMARK   3     7  4.1760 -  3.9671    1.00     2723   141  0.1701 0.2144        
REMARK   3     8  3.9671 -  3.7946    1.00     2703   138  0.1708 0.2341        
REMARK   3     9  3.7946 -  3.6486    1.00     2699   150  0.1774 0.2361        
REMARK   3    10  3.6486 -  3.5228    1.00     2702   157  0.1804 0.2544        
REMARK   3    11  3.5228 -  3.4127    1.00     2668   163  0.1843 0.2383        
REMARK   3    12  3.4127 -  3.3152    1.00     2683   153  0.1875 0.2560        
REMARK   3    13  3.3152 -  3.2280    1.00     2712   147  0.1935 0.2848        
REMARK   3    14  3.2280 -  3.1492    1.00     2696   147  0.2006 0.2675        
REMARK   3    15  3.1492 -  3.0777    1.00     2678   116  0.2060 0.3013        
REMARK   3    16  3.0777 -  3.0122    1.00     2701   151  0.2087 0.2836        
REMARK   3    17  3.0122 -  2.9520    1.00     2696   138  0.2213 0.3045        
REMARK   3    18  2.9520 -  2.8963    1.00     2665   142  0.2193 0.3041        
REMARK   3    19  2.8963 -  2.8446    1.00     2686   159  0.2244 0.3149        
REMARK   3    20  2.8446 -  2.7964    1.00     2656   140  0.2232 0.2771        
REMARK   3    21  2.7964 -  2.7513    1.00     2685   142  0.2124 0.3260        
REMARK   3    22  2.7513 -  2.7089    1.00     2677   133  0.2166 0.2894        
REMARK   3    23  2.7089 -  2.6691    1.00     2693   130  0.2216 0.2960        
REMARK   3    24  2.6691 -  2.6315    1.00     2674   142  0.2428 0.3040        
REMARK   3    25  2.6315 -  2.5960    1.00     2652   138  0.2553 0.3401        
REMARK   3    26  2.5960 -  2.5623    1.00     2721   121  0.2648 0.3555        
REMARK   3    27  2.5623 -  2.5302    1.00     2644   132  0.2588 0.3493        
REMARK   3    28  2.5302 -  2.4998    0.82     2184   126  0.2556 0.3295        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.110           
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      :  0.008          15477                                  
REMARK   3   ANGLE     :  1.185          21035                                  
REMARK   3   CHIRALITY :  0.061           2372                                  
REMARK   3   PLANARITY :  0.005           2650                                  
REMARK   3   DIHEDRAL  : 15.575           5742                                  
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 4NKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083331.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-13                          
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                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.24                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : FLAT COLLIMATING RH COATED         
REMARK 200                                   MIRROR, TOROIDAL FOCUSING MIRROR   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79261                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.110                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
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 ENTRY 3SWZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 150 MM MAGNESIUM        
REMARK 280  CHLORIDE HEXAHYDRATE, 25% PEG4000, 6% GLYCEROL, PH 8.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       43.03300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.88050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.31350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.88050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.03300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.31350            
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 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 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     SER A    30                                                      
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     ALA A   504                                                      
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     SER B    30                                                      
REMARK 465     ASP B   274                                                      
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     GLN B   282                                                      
REMARK 465     ALA B   504                                                      
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     LYS C    29                                                      
REMARK 465     SER C    30                                                      
REMARK 465     ASN C   277                                                      
REMARK 465     ALA C   278                                                      
REMARK 465     GLY C   279                                                      
REMARK 465     PRO C   280                                                      
REMARK 465     ASP C   281                                                      
REMARK 465     GLN C   282                                                      
REMARK 465     ALA C   504                                                      
REMARK 465     GLU C   505                                                      
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     LYS D    29                                                      
REMARK 465     SER D    30                                                      
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   282                                                      
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: 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      -80.80   -111.81                                   
REMARK 500    ARG A 109       39.97     81.21                                   
REMARK 500    ASP A 137     -156.84   -164.81                                   
REMARK 500    ASN A 185       17.52     57.68                                   
REMARK 500    ASP A 212     -141.45    -73.36                                   
REMARK 500    SER A 288      173.60    -55.82                                   
REMARK 500    VAL A 336      -37.62   -130.90                                   
REMARK 500    LEU A 370     -134.91     43.43                                   
REMARK 500    SER A 379     -158.15   -166.24                                   
REMARK 500    LYS A 481     -157.85   -115.40                                   
REMARK 500    ILE B  87      -79.99   -106.88                                   
REMARK 500    ILE B 112      -60.42   -103.36                                   
REMARK 500    ASN B 185       13.53     54.54                                   
REMARK 500    ASP B 212     -150.65    -80.01                                   
REMARK 500    VAL B 215       98.99    -65.04                                   
REMARK 500    ILE B 223      -68.12    -97.74                                   
REMARK 500    LEU B 370     -130.62     36.81                                   
REMARK 500    SER B 379     -158.26   -154.03                                   
REMARK 500    LYS B 481     -158.18   -110.55                                   
REMARK 500    ASN C 108       54.30     71.25                                   
REMARK 500    ILE C 112      -62.21   -122.06                                   
REMARK 500    ASP C 212     -151.11   -137.51                                   
REMARK 500    ASN C 226     -161.14   -100.68                                   
REMARK 500    VAL C 336      -46.87   -133.46                                   
REMARK 500    LEU C 370     -137.53     50.88                                   
REMARK 500    SER C 379     -152.74   -157.39                                   
REMARK 500    LYS C 481     -164.83   -106.41                                   
REMARK 500    ILE D  87      -76.07   -106.74                                   
REMARK 500    ILE D 112      -54.87   -123.48                                   
REMARK 500    SER D 117       39.07    -77.87                                   
REMARK 500    SER D 210      177.62    179.70                                   
REMARK 500    THR D 260       19.89   -140.79                                   
REMARK 500    LEU D 370     -133.85     44.23                                   
REMARK 500    SER D 379     -159.04   -166.38                                   
REMARK 500    ALA D 421      -71.48    -59.39                                   
REMARK 500    GLN D 424      136.14     71.14                                   
REMARK 500    SER D 431       54.01   -107.03                                   
REMARK 500    LEU D 433       56.60   -147.60                                   
REMARK 500    ALA D 437      161.05    179.87                                   
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 D 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 442   SG                                                     
REMARK 620 2 HEM D 600   NA  101.0                                              
REMARK 620 3 HEM D 600   NB   92.6  86.0                                        
REMARK 620 4 HEM D 600   NC   90.3 168.5  91.2                                  
REMARK 620 5 HEM D 600   ND   99.6  91.6 167.8  88.7                            
REMARK 620 N                    1     2     3     4                             
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 CYS B 442   SG                                                     
REMARK 620 2 HEM B 600   NA   95.9                                              
REMARK 620 3 HEM B 600   NB   81.3  86.8                                        
REMARK 620 4 HEM B 600   NC   91.0 170.3  87.6                                  
REMARK 620 5 HEM B 600   ND  108.3  90.9 170.4  93.3                            
REMARK 620 N                    1     2     3     4                             
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 CYS C 442   SG                                                     
REMARK 620 2 HEM C 600   NA  105.8                                              
REMARK 620 3 HEM C 600   NB   92.0  90.4                                        
REMARK 620 4 HEM C 600   NC   89.2 164.8  87.2                                  
REMARK 620 5 HEM C 600   ND  101.8  88.8 165.8  89.9                            
REMARK 620 N                    1     2     3     4                             
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   99.7                                              
REMARK 620 3 HEM A 600   NB   83.8  86.5                                        
REMARK 620 4 HEM A 600   NC   94.0 165.7  90.6                                  
REMARK 620 5 HEM A 600   ND  109.9  90.2 166.3  89.2                            
REMARK 620 N                    1     2     3     4                             
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 PLO 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 PLO 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 PLO 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 PLO D 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RUK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 CYP17A1 IN COMPLEX WITH ABIRATERONE            
REMARK 900 RELATED ID: 3SWZ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 17A1 IN COMPLEX WITH TOK-001                   
REMARK 900 RELATED ID: 4NKV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4NKX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4NKY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4NKZ   RELATED DB: PDB                                   
DBREF  4NKW A   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  4NKW B   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  4NKW C   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  4NKW D   24   508  UNP    P05093   CP17A_HUMAN     24    508             
SEQADV 4NKW MET A   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW ALA A   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS A   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS A   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW THR A   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LEU A  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKW HIS A  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS A  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS A  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS A  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW MET B   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW ALA B   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS B   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS B   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW THR B   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LEU B  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKW HIS B  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS B  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS B  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS B  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW MET C   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW ALA C   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS C   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS C   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW THR C   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LEU C  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKW HIS C  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS C  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS C  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS C  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW MET D   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW ALA D   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS D   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LYS D   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW THR D   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW LEU D  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKW HIS D  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS D  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW HIS D  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKW 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 LEU 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 LEU 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 LEU 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 LEU 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    PLO  A 601      55                                                       
HET    HEM  B 600      73                                                       
HET    PLO  B 601      55                                                       
HET    HEM  C 600      73                                                       
HET    PLO  C 601      55                                                       
HET    HEM  D 600      73                                                       
HET    PLO  D 601      55                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     PLO (3BETA)-3-HYDROXYPREGN-5-EN-20-ONE                               
HETSYN     HEM HEME                                                             
HETSYN     PLO PREGNENOLONE                                                     
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  PLO    4(C21 H32 O2)                                                
FORMUL  13  HOH   *87(H2 O)                                                     
HELIX    1   1 HIS A   48  LEU A   56  1                                   9    
HELIX    2   2 LEU A   56  GLY A   61  1                                   6    
HELIX    3   3 HIS A   78  ILE A   87  1                                  10    
HELIX    4   4 LYS A   89  SER A   94  5                                   6    
HELIX    5   5 MET A   99  SER A  106  1                                   8    
HELIX    6   6 GLY A  118  PHE A  132  1                                  15    
HELIX    7   7 ALA A  133  LYS A  136  5                                   4    
HELIX    8   8 ASP A  137  GLN A  140  5                                   4    
HELIX    9   9 LYS A  141  HIS A  160  1                                  20    
HELIX   10  10 ILE A  167  ASN A  185  1                                  19    
HELIX   11  11 PRO A  193  SER A  210  1                                  18    
HELIX   12  12 PRO A  219  ILE A  223  5                                   5    
HELIX   13  13 LYS A  227  PHE A  254  1                                  28    
HELIX   14  14 ASN A  261  SER A  273  1                                  13    
HELIX   15  15 ASP A  283  LEU A  287  5                                   5    
HELIX   16  16 SER A  288  HIS A  320  1                                  33    
HELIX   17  17 ASN A  321  VAL A  336  1                                  16    
HELIX   18  18 THR A  343  ASN A  348  5                                   6    
HELIX   19  19 LEU A  350  ARG A  364  1                                  15    
HELIX   20  20 ASN A  395  ASN A  402  1                                   8    
HELIX   21  21 MET A  413  LEU A  418  5                                   6    
HELIX   22  22 ALA A  437  SER A  441  5                                   5    
HELIX   23  23 GLY A  444  ARG A  462  1                                  19    
HELIX   24  24 ARG A  496  ALA A  502  1                                   7    
HELIX   25  25 HIS B   48  LEU B   56  1                                   9    
HELIX   26  26 LEU B   56  GLY B   61  1                                   6    
HELIX   27  27 HIS B   78  ILE B   87  1                                  10    
HELIX   28  28 MET B   99  SER B  106  1                                   8    
HELIX   29  29 GLY B  118  PHE B  132  1                                  15    
HELIX   30  30 ALA B  133  LYS B  136  5                                   4    
HELIX   31  31 LYS B  141  HIS B  160  1                                  20    
HELIX   32  32 ILE B  167  ASN B  185  1                                  19    
HELIX   33  33 PRO B  193  SER B  210  1                                  18    
HELIX   34  34 PRO B  219  ILE B  223  5                                   5    
HELIX   35  35 LYS B  227  PHE B  254  1                                  28    
HELIX   36  36 ASN B  261  SER B  273  1                                  13    
HELIX   37  37 SER B  284  LEU B  287  5                                   4    
HELIX   38  38 SER B  288  ASN B  321  1                                  34    
HELIX   39  39 ASN B  321  VAL B  336  1                                  16    
HELIX   40  40 THR B  343  ARG B  349  5                                   7    
HELIX   41  41 LEU B  350  ARG B  364  1                                  15    
HELIX   42  42 ASN B  395  HIS B  400  1                                   6    
HELIX   43  43 MET B  413  LEU B  418  5                                   6    
HELIX   44  44 ALA B  437  SER B  441  5                                   5    
HELIX   45  45 GLY B  444  ARG B  462  1                                  19    
HELIX   46  46 ARG B  496  ALA B  502  1                                   7    
HELIX   47  47 HIS C   48  GLY C   61  1                                  14    
HELIX   48  48 HIS C   78  ILE C   87  1                                  10    
HELIX   49  49 MET C   99  SER C  106  1                                   8    
HELIX   50  50 GLY C  118  THR C  131  1                                  14    
HELIX   51  51 PHE C  132  LYS C  136  5                                   5    
HELIX   52  52 LYS C  141  THR C  159  1                                  19    
HELIX   53  53 ILE C  167  ASN C  185  1                                  19    
HELIX   54  54 PRO C  193  LEU C  209  1                                  17    
HELIX   55  55 LYS C  227  PHE C  254  1                                  28    
HELIX   56  56 ASN C  261  ASN C  275  1                                  15    
HELIX   57  57 ASP C  283  LEU C  287  5                                   5    
HELIX   58  58 SER C  288  LEU C  319  1                                  32    
HELIX   59  59 ASN C  321  VAL C  336  1                                  16    
HELIX   60  60 THR C  343  ARG C  349  5                                   7    
HELIX   61  61 LEU C  350  ARG C  364  1                                  15    
HELIX   62  62 ASN C  395  ASN C  402  1                                   8    
HELIX   63  63 MET C  413  LEU C  418  5                                   6    
HELIX   64  64 ALA C  437  SER C  441  5                                   5    
HELIX   65  65 GLY C  444  ARG C  462  1                                  19    
HELIX   66  66 ARG C  496  GLU C  501  1                                   6    
HELIX   67  67 HIS D   48  GLY D   61  1                                  14    
HELIX   68  68 HIS D   78  ILE D   87  1                                  10    
HELIX   69  69 MET D   99  SER D  106  1                                   8    
HELIX   70  70 GLY D  118  THR D  131  1                                  14    
HELIX   71  71 PHE D  132  LYS D  136  5                                   5    
HELIX   72  72 ASP D  137  GLN D  140  5                                   4    
HELIX   73  73 LYS D  141  THR D  159  1                                  19    
HELIX   74  74 ILE D  167  ASN D  185  1                                  19    
HELIX   75  75 PRO D  193  SER D  210  1                                  18    
HELIX   76  76 LYS D  227  PHE D  254  1                                  28    
HELIX   77  77 ASN D  261  GLY D  276  1                                  16    
HELIX   78  78 SER D  284  LEU D  287  5                                   4    
HELIX   79  79 SER D  288  LEU D  319  1                                  32    
HELIX   80  80 ASN D  321  VAL D  336  1                                  16    
HELIX   81  81 THR D  343  ARG D  349  5                                   7    
HELIX   82  82 LEU D  350  ARG D  364  1                                  15    
HELIX   83  83 ASN D  395  ASN D  402  1                                   8    
HELIX   84  84 MET D  413  LEU D  418  5                                   6    
HELIX   85  85 ALA D  437  SER D  441  5                                   5    
HELIX   86  86 GLY D  444  ARG D  462  1                                  19    
HELIX   87  87 ARG D  496  ALA D  502  1                                   7    
SHEET    1   A 5 LEU A  36  LEU A  40  0                                        
SHEET    2   A 5 ILE D  63  MET D  68  1  O  ARG D  67   N  LEU A  40           
SHEET    3   A 5 LYS D  71  VAL D  76 -1  O  ILE D  75   N  TYR D  64           
SHEET    4   A 5 GLU D 391  ILE D 394  1  O  GLU D 391   N  VAL D  74           
SHEET    5   A 5 HIS D 373  LYS D 374 -1  N  HIS D 373   O  VAL D 392           
SHEET    1   B 5 HIS A 373  LYS A 374  0                                        
SHEET    2   B 5 GLU A 391  ILE A 394 -1  O  VAL A 392   N  HIS A 373           
SHEET    3   B 5 LYS A  71  VAL A  76  1  N  VAL A  76   O  ILE A 393           
SHEET    4   B 5 ILE A  63  MET A  68 -1  N  VAL A  66   O  THR A  73           
SHEET    5   B 5 LEU D  36  LEU D  40  1  O  VAL D  37   N  SER A  65           
SHEET    1   C 3 GLN A 163  ILE A 165  0                                        
SHEET    2   C 3 VAL A 491  VAL A 495 -1  O  VAL A 491   N  ILE A 165           
SHEET    3   C 3 PHE A 463  GLU A 466 -1  N  ASP A 464   O  LYS A 494           
SHEET    1   D 2 SER A 379  ILE A 381  0                                        
SHEET    2   D 2 PHE A 384  VAL A 386 -1  O  VAL A 386   N  SER A 379           
SHEET    1   E 2 ILE A 479  PRO A 480  0                                        
SHEET    2   E 2 PHE A 484  LEU A 485 -1  O  LEU A 485   N  ILE A 479           
SHEET    1   F 5 LEU B  36  LEU B  40  0                                        
SHEET    2   F 5 ILE C  63  MET C  68  1  O  SER C  65   N  VAL B  37           
SHEET    3   F 5 LYS C  71  VAL C  76 -1  O  LYS C  71   N  MET C  68           
SHEET    4   F 5 GLU C 391  ILE C 394  1  O  ILE C 393   N  VAL C  76           
SHEET    5   F 5 HIS C 373  LYS C 374 -1  N  HIS C 373   O  VAL C 392           
SHEET    1   G 5 HIS B 373  LYS B 374  0                                        
SHEET    2   G 5 GLU B 391  ILE B 394 -1  O  VAL B 392   N  HIS B 373           
SHEET    3   G 5 LYS B  71  VAL B  76  1  N  VAL B  74   O  ILE B 393           
SHEET    4   G 5 ILE B  63  MET B  68 -1  N  TYR B  64   O  ILE B  75           
SHEET    5   G 5 LEU C  36  LEU C  40  1  O  VAL C  37   N  SER B  65           
SHEET    1   H 3 SER B 164  ILE B 165  0                                        
SHEET    2   H 3 VAL B 491  VAL B 495 -1  O  VAL B 491   N  ILE B 165           
SHEET    3   H 3 PHE B 463  GLU B 466 -1  N  ASP B 464   O  LYS B 494           
SHEET    1   I 2 SER B 379  ILE B 381  0                                        
SHEET    2   I 2 PHE B 384  VAL B 386 -1  O  VAL B 386   N  SER B 379           
SHEET    1   J 2 ILE B 479  PRO B 480  0                                        
SHEET    2   J 2 PHE B 484  LEU B 485 -1  O  LEU B 485   N  ILE B 479           
SHEET    1   K 3 SER C 164  ILE C 165  0                                        
SHEET    2   K 3 VAL C 491  VAL C 495 -1  O  VAL C 491   N  ILE C 165           
SHEET    3   K 3 PHE C 463  GLU C 466 -1  N  ASP C 464   O  LYS C 494           
SHEET    1   L 2 SER C 379  ILE C 381  0                                        
SHEET    2   L 2 PHE C 384  VAL C 386 -1  O  VAL C 386   N  SER C 379           
SHEET    1   M 2 ILE C 479  PRO C 480  0                                        
SHEET    2   M 2 PHE C 484  LEU C 485 -1  O  LEU C 485   N  ILE C 479           
SHEET    1   N 3 SER D 164  ILE D 165  0                                        
SHEET    2   N 3 VAL D 491  VAL D 495 -1  O  VAL D 491   N  ILE D 165           
SHEET    3   N 3 PHE D 463  GLU D 466 -1  N  ASP D 464   O  LYS D 494           
SHEET    1   O 2 SER D 379  ILE D 381  0                                        
SHEET    2   O 2 PHE D 384  VAL D 386 -1  O  VAL D 386   N  SER D 379           
SHEET    1   P 2 ILE D 479  PRO D 480  0                                        
SHEET    2   P 2 PHE D 484  LEU D 485 -1  O  LEU D 485   N  ILE D 479           
LINK         SG  CYS D 442                FE   HEM D 600     1555   1555  2.47  
LINK         SG  CYS B 442                FE   HEM B 600     1555   1555  2.48  
LINK         SG  CYS C 442                FE   HEM C 600     1555   1555  2.50  
LINK         SG  CYS A 442                FE   HEM A 600     1555   1555  2.51  
SITE     1 AC1 20 ARG A  96  ILE A 112  ALA A 113  TRP A 121                    
SITE     2 AC1 20 ARG A 125  ALA A 302  GLY A 303  THR A 306                    
SITE     3 AC1 20 VAL A 310  LEU A 370  ILE A 371  HIS A 373                    
SITE     4 AC1 20 PRO A 434  PHE A 435  ARG A 440  CYS A 442                    
SITE     5 AC1 20 ILE A 443  ALA A 448  PLO A 601  HOH A 704                    
SITE     1 AC2  9 LEU A 105  ALA A 113  ASN A 202  ILE A 205                    
SITE     2 AC2  9 LEU A 209  THR A 306  VAL A 366  ILE A 371                    
SITE     3 AC2  9 HEM A 600                                                     
SITE     1 AC3 18 ARG B  96  ILE B 112  ALA B 113  TRP B 121                    
SITE     2 AC3 18 ARG B 125  ILE B 299  ALA B 302  THR B 306                    
SITE     3 AC3 18 LEU B 370  ILE B 371  HIS B 373  PRO B 434                    
SITE     4 AC3 18 PHE B 435  ARG B 440  CYS B 442  ILE B 443                    
SITE     5 AC3 18 ALA B 448  PLO B 601                                          
SITE     1 AC4 10 LEU B 105  ALA B 113  ASN B 202  ILE B 205                    
SITE     2 AC4 10 ASP B 298  GLU B 305  THR B 306  VAL B 366                    
SITE     3 AC4 10 ILE B 371  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  ALA C 302  THR C 306  THR C 307                    
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 GLY C 444  ALA C 448  PLO C 601  HOH C 707                    
SITE     1 AC6  8 ALA C 113  ASN C 202  ILE C 205  THR C 306                    
SITE     2 AC6  8 ILE C 371  VAL C 482  VAL C 483  HEM C 600                    
SITE     1 AC7 20 ARG D  96  ILE D 112  ALA D 113  TRP D 121                    
SITE     2 AC7 20 ARG D 125  ALA D 302  GLY D 303  THR D 306                    
SITE     3 AC7 20 THR D 307  VAL D 366  LEU D 370  HIS D 373                    
SITE     4 AC7 20 PRO D 434  PHE D 435  ARG D 440  CYS D 442                    
SITE     5 AC7 20 ILE D 443  ALA D 448  PLO D 601  HOH D 708                    
SITE     1 AC8  7 ALA D 113  ASN D 202  THR D 306  ILE D 371                    
SITE     2 AC8  7 VAL D 482  VAL D 483  HEM D 600                               
CRYST1   86.066  152.627  173.761  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      0.011619  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006552  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005755        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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