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Database: PDB
Entry: 4NKY
LinkDB: 4NKY
Original site: 4NKY 
HEADER    OXIDOREDUCTASE, LYASE                   13-NOV-13   4NKY              
TITLE     HUMAN STEROIDOGENIC CYTOCHROME P450 17A1 MUTANT A105L WITH SUBSTRATE  
TITLE    2 17ALPHA-HYDROXYPROGESTERONE                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP 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: 1.14.99.9, 4.1.2.30;                                             
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 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.M.PETRUNAK                                                
REVDAT   2   03-DEC-14 4NKY    1       JRNL                                     
REVDAT   1   22-OCT-14 4NKY    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.    2.55 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) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 75825                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3806                            
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 39.1575 -  7.6323    0.98     2842   160  0.1466 0.1813        
REMARK   3     2  7.6323 -  6.0652    0.99     2746   153  0.1852 0.2280        
REMARK   3     3  6.0652 -  5.3007    1.00     2731   167  0.1779 0.2449        
REMARK   3     4  5.3007 -  4.8170    1.00     2724   147  0.1462 0.2205        
REMARK   3     5  4.8170 -  4.4722    0.98     2689   129  0.1410 0.1798        
REMARK   3     6  4.4722 -  4.2089    0.99     2675   142  0.1489 0.2014        
REMARK   3     7  4.2089 -  3.9983    1.00     2739   110  0.1460 0.1824        
REMARK   3     8  3.9983 -  3.8244    1.00     2680   151  0.1503 0.2138        
REMARK   3     9  3.8244 -  3.6773    1.00     2707   143  0.1625 0.2612        
REMARK   3    10  3.6773 -  3.5505    1.00     2665   132  0.1761 0.2593        
REMARK   3    11  3.5505 -  3.4396    0.99     2666   162  0.1941 0.2906        
REMARK   3    12  3.4396 -  3.3413    0.99     2678   135  0.1902 0.2840        
REMARK   3    13  3.3413 -  3.2534    1.00     2691   121  0.1934 0.2352        
REMARK   3    14  3.2534 -  3.1740    1.00     2691   130  0.1927 0.2944        
REMARK   3    15  3.1740 -  3.1019    1.00     2668   153  0.2038 0.2739        
REMARK   3    16  3.1019 -  3.0359    1.00     2658   128  0.2105 0.3402        
REMARK   3    17  3.0359 -  2.9752    1.00     2662   157  0.2224 0.2916        
REMARK   3    18  2.9752 -  2.9191    1.00     2682   144  0.2217 0.3119        
REMARK   3    19  2.9191 -  2.8670    1.00     2633   149  0.2182 0.3327        
REMARK   3    20  2.8670 -  2.8184    1.00     2674   130  0.2317 0.2939        
REMARK   3    21  2.8184 -  2.7729    0.99     2595   164  0.2417 0.3227        
REMARK   3    22  2.7729 -  2.7303    1.00     2693   136  0.2419 0.3272        
REMARK   3    23  2.7303 -  2.6901    0.99     2646   133  0.2466 0.3360        
REMARK   3    24  2.6901 -  2.6523    1.00     2691   112  0.2516 0.3293        
REMARK   3    25  2.6523 -  2.6164    0.99     2630   150  0.2506 0.3011        
REMARK   3    26  2.6164 -  2.5824    0.99     2631   158  0.2608 0.3217        
REMARK   3    27  2.5824 -  2.5502    0.83     2232   110  0.2618 0.3203        
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)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.870           
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      :  0.007          15459                                  
REMARK   3   ANGLE     :  1.226          21015                                  
REMARK   3   CHIRALITY :  0.103           2367                                  
REMARK   3   PLANARITY :  0.004           2646                                  
REMARK   3   DIHEDRAL  : 14.344           5752                                  
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 4NKY 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 RCSB083333.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-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                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL SI(111)                    
REMARK 200  OPTICS                         : RH COATED MIRROR, K-B FOCUSING     
REMARK 200                                   MIRROR                             
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   : 76008                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.153                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
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) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
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   (%): 52.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 175 MM TRIS-HCL, 250 MM LITHIUM          
REMARK 280  SULFATE, 30% PEG3350, 3% GLYCEROL, PH 8.5, VAPOR DIFFUSION,         
REMARK 280  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       45.64250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.02250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.88900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.02250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.64250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.88900            
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     GLY A   138                                                      
REMARK 465     ASP A   139                                                      
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     ASP C   137                                                      
REMARK 465     GLY C   138                                                      
REMARK 465     ASP C   139                                                      
REMARK 465     ASN C   277                                                      
REMARK 465     ALA C   278                                                      
REMARK 465     GLY C   279                                                      
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   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   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      -72.11   -122.82                                   
REMARK 500    ARG A 109       33.37     70.30                                   
REMARK 500    ILE A 112      -63.60   -121.77                                   
REMARK 500    LEU A 134       10.67    -69.90                                   
REMARK 500    ASP A 212     -117.99   -105.90                                   
REMARK 500    ASN A 272       41.04    -88.58                                   
REMARK 500    VAL A 336      -39.22   -130.84                                   
REMARK 500    LEU A 370     -149.30     46.40                                   
REMARK 500    SER A 379     -159.85   -140.88                                   
REMARK 500    ALA A 437      144.91   -173.07                                   
REMARK 500    LYS A 481     -158.74   -106.47                                   
REMARK 500    ALA A 502        4.00    -67.83                                   
REMARK 500    ASN B 108       70.59     69.60                                   
REMARK 500    ASP B 137      146.32   -173.11                                   
REMARK 500    GLN B 140       32.22    -91.57                                   
REMARK 500    PHE B 184       11.09   -140.18                                   
REMARK 500    ASP B 212     -125.84   -105.84                                   
REMARK 500    LEU B 217      -71.59    -50.22                                   
REMARK 500    ASN B 272       33.49    -73.18                                   
REMARK 500    VAL B 336      -46.78   -131.75                                   
REMARK 500    LEU B 370     -145.33     46.72                                   
REMARK 500    LEU B 433       57.97   -140.34                                   
REMARK 500    PRO B 468     -179.87    -60.42                                   
REMARK 500    LYS B 481     -157.68   -124.45                                   
REMARK 500    ALA B 502       44.51    -79.97                                   
REMARK 500    HIS C  46     -173.27     59.39                                   
REMARK 500    ILE C  87      -72.41   -108.69                                   
REMARK 500    ASN C 108       50.91     70.56                                   
REMARK 500    ARG C 109       30.91     71.47                                   
REMARK 500    ILE C 112      -59.71   -120.54                                   
REMARK 500    ASP C 212     -167.54   -173.92                                   
REMARK 500    ASN C 226       12.82   -140.24                                   
REMARK 500    LEU C 370     -143.21     51.29                                   
REMARK 500    LYS C 481     -161.73   -129.41                                   
REMARK 500    ILE D  87      -70.71   -109.64                                   
REMARK 500    ASN D 108       56.79     70.72                                   
REMARK 500    ASP D 137      119.71   -160.82                                   
REMARK 500    ASP D 212     -169.35   -164.29                                   
REMARK 500    ASN D 226     -163.98   -113.03                                   
REMARK 500    ASN D 272       34.18    -83.83                                   
REMARK 500    LEU D 370     -140.13     46.69                                   
REMARK 500    SER D 379     -159.33   -154.81                                   
REMARK 500    GLU D 383       -1.92     72.38                                   
REMARK 500    LEU D 433       56.03   -143.17                                   
REMARK 500    LYS D 481     -157.73   -137.49                                   
REMARK 500    ALA D 502       31.76    -86.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 442   SG                                                     
REMARK 620 2 HEM C 600   NA   95.2                                              
REMARK 620 3 HEM C 600   NB   86.9  89.5                                        
REMARK 620 4 HEM C 600   NC   92.6 172.1  89.7                                  
REMARK 620 5 HEM C 600   ND   99.9  88.1 173.0  91.8                            
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   99.2                                              
REMARK 620 3 HEM B 600   NB   86.8  88.9                                        
REMARK 620 4 HEM B 600   NC   93.4 167.1  88.9                                  
REMARK 620 5 HEM B 600   ND  106.4  89.9 166.8  89.3                            
REMARK 620 N                    1     2     3     4                             
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   98.5                                              
REMARK 620 3 HEM D 600   NB   89.3  88.4                                        
REMARK 620 4 HEM D 600   NC   95.1 166.3  90.9                                  
REMARK 620 5 HEM D 600   ND  104.2  88.2 166.4  89.3                            
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  103.9                                              
REMARK 620 3 HEM A 600   NB   89.7  86.7                                        
REMARK 620 4 HEM A 600   NC   91.2 164.6  90.8                                  
REMARK 620 5 HEM A 600   ND  106.0  88.0 164.2  90.4                            
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 3QZ 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 3QZ 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 3QZ 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 3QZ 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: 4NKW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4NKX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4NKZ   RELATED DB: PDB                                   
DBREF  4NKY A   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  4NKY B   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  4NKY C   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  4NKY D   24   508  UNP    P05093   CP17A_HUMAN     24    508             
SEQADV 4NKY MET A   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY ALA A   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS A   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS A   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY THR A   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LEU A  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKY HIS A  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS A  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS A  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS A  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY MET B   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY ALA B   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS B   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS B   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY THR B   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LEU B  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKY HIS B  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS B  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS B  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS B  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY MET C   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY ALA C   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS C   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS C   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY THR C   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LEU C  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKY HIS C  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS C  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS C  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS C  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY MET D   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY ALA D   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS D   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LYS D   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY THR D   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY LEU D  105  UNP  P05093    ALA   105 ENGINEERED MUTATION            
SEQADV 4NKY HIS D  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS D  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY HIS D  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 4NKY 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    3QZ  A 601      54                                                       
HET    HEM  B 600      73                                                       
HET    3QZ  B 601      54                                                       
HET    HEM  C 600      73                                                       
HET    3QZ  C 601      54                                                       
HET    HEM  D 600      73                                                       
HET    3QZ  D 601      54                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     3QZ (9BETA)-17-HYDROXYPREGN-4-ENE-3,20-DIONE                         
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  3QZ    4(C21 H30 O3)                                                
FORMUL  13  HOH   *161(H2 O)                                                    
HELIX    1   1 HIS A   48  GLY A   61  1                                  14    
HELIX    2   2 HIS A   78  ILE A   87  1                                  10    
HELIX    3   3 MET A   99  SER A  106  1                                   8    
HELIX    4   4 GLY A  118  PHE A  132  1                                  15    
HELIX    5   5 ALA A  133  LYS A  136  5                                   4    
HELIX    6   6 LYS A  141  THR A  159  1                                  19    
HELIX    7   7 ILE A  167  ASN A  185  1                                  19    
HELIX    8   8 PRO A  193  SER A  210  1                                  18    
HELIX    9   9 PRO A  219  ILE A  223  5                                   5    
HELIX   10  10 LYS A  227  PHE A  254  1                                  28    
HELIX   11  11 ASN A  261  ASN A  272  1                                  12    
HELIX   12  12 ASP A  283  LEU A  287  5                                   5    
HELIX   13  13 SER A  288  ASN A  321  1                                  34    
HELIX   14  14 ASN A  321  VAL A  336  1                                  16    
HELIX   15  15 THR A  343  ARG A  349  5                                   7    
HELIX   16  16 LEU A  350  ARG A  364  1                                  15    
HELIX   17  17 ASN A  395  ASN A  402  1                                   8    
HELIX   18  18 MET A  413  LEU A  418  5                                   6    
HELIX   19  19 GLY A  444  ARG A  462  1                                  19    
HELIX   20  20 ARG A  496  ALA A  502  1                                   7    
HELIX   21  21 HIS B   48  LEU B   56  1                                   9    
HELIX   22  22 LEU B   56  GLY B   61  1                                   6    
HELIX   23  23 HIS B   78  ILE B   87  1                                  10    
HELIX   24  24 LYS B   89  SER B   94  5                                   6    
HELIX   25  25 MET B   99  SER B  106  1                                   8    
HELIX   26  26 GLY B  118  PHE B  132  1                                  15    
HELIX   27  27 ALA B  133  LYS B  136  5                                   4    
HELIX   28  28 LYS B  141  THR B  159  1                                  19    
HELIX   29  29 ILE B  167  ASN B  185  1                                  19    
HELIX   30  30 PRO B  193  SER B  210  1                                  18    
HELIX   31  31 PRO B  219  ILE B  223  5                                   5    
HELIX   32  32 LYS B  227  GLU B  252  1                                  26    
HELIX   33  33 ASN B  261  ASN B  272  1                                  12    
HELIX   34  34 ASP B  283  LEU B  287  5                                   5    
HELIX   35  35 SER B  288  ASN B  321  1                                  34    
HELIX   36  36 ASN B  321  VAL B  336  1                                  16    
HELIX   37  37 THR B  343  ARG B  349  5                                   7    
HELIX   38  38 LEU B  350  ARG B  364  1                                  15    
HELIX   39  39 ASN B  395  HIS B  400  1                                   6    
HELIX   40  40 MET B  413  LEU B  418  5                                   6    
HELIX   41  41 GLY B  444  ARG B  462  1                                  19    
HELIX   42  42 ARG B  496  ALA B  502  1                                   7    
HELIX   43  43 HIS C   48  LEU C   56  1                                   9    
HELIX   44  44 LEU C   56  GLY C   61  1                                   6    
HELIX   45  45 HIS C   78  ILE C   87  1                                  10    
HELIX   46  46 MET C   99  SER C  106  1                                   8    
HELIX   47  47 GLY C  118  LEU C  134  1                                  17    
HELIX   48  48 LYS C  141  THR C  159  1                                  19    
HELIX   49  49 ILE C  167  ASN C  185  1                                  19    
HELIX   50  50 PRO C  193  SER C  210  1                                  18    
HELIX   51  51 LYS C  227  GLU C  252  1                                  26    
HELIX   52  52 ASN C  261  ASN C  275  1                                  15    
HELIX   53  53 SER C  284  LEU C  287  5                                   4    
HELIX   54  54 SER C  288  HIS C  320  1                                  33    
HELIX   55  55 ASN C  321  VAL C  336  1                                  16    
HELIX   56  56 THR C  343  ARG C  349  5                                   7    
HELIX   57  57 LEU C  350  ARG C  364  1                                  15    
HELIX   58  58 ASN C  395  ASN C  402  1                                   8    
HELIX   59  59 MET C  413  LEU C  418  5                                   6    
HELIX   60  60 ALA C  437  SER C  441  5                                   5    
HELIX   61  61 GLY C  444  ARG C  462  1                                  19    
HELIX   62  62 ARG C  496  ALA C  502  1                                   7    
HELIX   63  63 HIS D   48  GLY D   61  1                                  14    
HELIX   64  64 HIS D   78  ILE D   87  1                                  10    
HELIX   65  65 MET D   99  SER D  106  1                                   8    
HELIX   66  66 GLY D  118  PHE D  132  1                                  15    
HELIX   67  67 ALA D  133  LYS D  136  5                                   4    
HELIX   68  68 LYS D  141  THR D  159  1                                  19    
HELIX   69  69 ILE D  167  ASN D  185  1                                  19    
HELIX   70  70 ASP D  192  SER D  210  1                                  19    
HELIX   71  71 LYS D  227  LYS D  251  1                                  25    
HELIX   72  72 ASN D  261  ASN D  272  1                                  12    
HELIX   73  73 ASP D  283  LEU D  287  5                                   5    
HELIX   74  74 SER D  288  HIS D  320  1                                  33    
HELIX   75  75 ASN D  321  VAL D  336  1                                  16    
HELIX   76  76 THR D  343  ARG D  349  5                                   7    
HELIX   77  77 LEU D  350  ARG D  364  1                                  15    
HELIX   78  78 ASN D  395  ASN D  402  1                                   8    
HELIX   79  79 MET D  413  LEU D  418  5                                   6    
HELIX   80  80 GLY D  444  ARG D  462  1                                  19    
HELIX   81  81 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  SER D  65   N  VAL A  37           
SHEET    3   A 5 LYS D  71  VAL D  76 -1  O  LYS D  71   N  MET D  68           
SHEET    4   A 5 GLU D 391  ILE D 394  1  O  ILE D 393   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  74   O  GLU A 391           
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  LEU D  40   N  ARG A  67           
SHEET    1   C 3 SER A 164  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  74           
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  GLU B 391           
SHEET    4   G 5 ILE B  63  MET B  68 -1  N  VAL B  66   O  THR B  73           
SHEET    5   G 5 LEU C  36  LEU C  40  1  O  LEU C  40   N  ARG B  67           
SHEET    1   H 3 GLN B 163  ILE B 165  0                                        
SHEET    2   H 3 VAL B 491  VAL B 495 -1  O  ILE B 493   N  GLN B 163           
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 GLN C 163  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 C 442                FE   HEM C 600     1555   1555  2.49  
LINK         SG  CYS B 442                FE   HEM B 600     1555   1555  2.52  
LINK         SG  CYS D 442                FE   HEM D 600     1555   1555  2.57  
LINK         SG  CYS A 442                FE   HEM A 600     1555   1555  2.65  
SITE     1 AC1 19 ARG A  96  ILE A 112  ALA A 113  TRP A 121                    
SITE     2 AC1 19 ARG A 125  ILE A 299  ALA A 302  THR A 306                    
SITE     3 AC1 19 THR A 307  VAL A 366  LEU A 370  ILE A 371                    
SITE     4 AC1 19 HIS A 373  PRO A 434  PHE A 435  ARG A 440                    
SITE     5 AC1 19 CYS A 442  ALA A 448  3QZ A 601                               
SITE     1 AC2  8 ALA A 113  ASN A 202  ASP A 298  THR A 306                    
SITE     2 AC2  8 VAL A 366  VAL A 482  VAL A 483  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 179  ALA B 302  GLY B 303                    
SITE     3 AC3 18 THR B 306  VAL B 366  ILE B 371  HIS B 373                    
SITE     4 AC3 18 PRO B 434  PHE B 435  ARG B 440  CYS B 442                    
SITE     5 AC3 18 ALA B 448  3QZ B 601                                          
SITE     1 AC4 10 ALA B 113  ASN B 202  ILE B 205  ASP B 298                    
SITE     2 AC4 10 GLY B 301  THR B 306  VAL B 366  VAL B 482                    
SITE     3 AC4 10 VAL B 483  HEM B 600                                          
SITE     1 AC5 18 ARG C  96  ILE C 112  ALA C 113  TRP C 121                    
SITE     2 AC5 18 ARG C 125  ALA C 302  THR C 306  VAL C 366                    
SITE     3 AC5 18 LEU C 370  ILE C 371  HIS C 373  PRO C 434                    
SITE     4 AC5 18 PHE C 435  ARG C 440  CYS C 442  GLY C 444                    
SITE     5 AC5 18 ALA C 448  3QZ C 601                                          
SITE     1 AC6  8 ALA C 113  ASN C 202  ILE C 205  ASP C 298                    
SITE     2 AC6  8 THR C 306  VAL C 366  HEM C 600  HOH C 738                    
SITE     1 AC7 23 ARG D  96  ILE D 112  ALA D 113  TRP D 121                    
SITE     2 AC7 23 ARG D 125  ILE D 179  ALA D 302  GLY D 303                    
SITE     3 AC7 23 THR D 306  VAL D 310  VAL D 366  LEU D 370                    
SITE     4 AC7 23 ILE D 371  HIS D 373  PRO D 434  PHE D 435                    
SITE     5 AC7 23 ARG D 440  CYS D 442  GLY D 444  LEU D 447                    
SITE     6 AC7 23 ALA D 448  3QZ D 601  HOH D 702                               
SITE     1 AC8 11 ALA D 113  ASN D 202  ILE D 205  ILE D 206                    
SITE     2 AC8 11 ASP D 298  ALA D 302  THR D 306  VAL D 366                    
SITE     3 AC8 11 ILE D 371  VAL D 482  HEM D 600                               
CRYST1   91.285  151.778  168.045  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      0.010955  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006589  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005951        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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