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Database: PDB
Entry: 3T3Z
LinkDB: 3T3Z
Original site: 3T3Z 
HEADER    OXIDOREDUCTASE                          25-JUL-11   3T3Z              
TITLE     HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH PILOCARPINE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 2E1;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 31-492;                                       
COMPND   5 SYNONYM: 4-NITROPHENOL 2-HYDROXYLASE, CYPIIE1, CYTOCHROME P450-J;    
COMPND   6 EC: 1.14.13.-;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP2E, CYP2E1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOPP3;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKK2E1DH                                  
KEYWDS    CYP2E1, CYTOCHROME P450 2E1, P450 2E1, HEME PROTEIN, MONOOXYGENASE,   
KEYWDS   2 DRUG METABOLISM, XENOBIOTIC METABOLISM, ENDOPLASMIC RETICULUM,       
KEYWDS   3 MEMBRANE, OXIDOREDUCTASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.MENEELY,N.M.DEVORE,E.E.SCOTT                                      
REVDAT   4   29-JUL-20 3T3Z    1       COMPND REMARK SEQADV HET                 
REVDAT   4 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   4 3                   1       SITE   ATOM                              
REVDAT   3   08-NOV-17 3T3Z    1       REMARK                                   
REVDAT   2   06-JUN-12 3T3Z    1       JRNL                                     
REVDAT   1   07-DEC-11 3T3Z    0                                                
JRNL        AUTH   N.M.DEVORE,K.M.MENEELY,A.G.BART,E.S.STEPHENS,K.P.BATTAILE,   
JRNL        AUTH 2 E.E.SCOTT                                                    
JRNL        TITL   STRUCTURAL COMPARISON OF CYTOCHROMES P450 2A6, 2A13, AND 2E1 
JRNL        TITL 2 WITH PILOCARPINE.                                            
JRNL        REF    FEBS J.                       V. 279  1621 2012              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   22051186                                                     
JRNL        DOI    10.1111/J.1742-4658.2011.08412.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 6.1.13                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 97337                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5103                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6193                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 316                          
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15148                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 324                                     
REMARK   3   SOLVENT ATOMS            : 714                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.372         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.277         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.198         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.392         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15953 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21681 ; 1.629 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1858 ; 6.131 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   751 ;35.422 ;23.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2710 ;17.232 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   116 ;20.128 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2307 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12184 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9317 ; 0.857 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15178 ; 1.544 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6636 ; 2.485 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6500 ; 3.793 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3T3Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000067007.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : SAGITALLY FOCUSED SECOND           
REMARK 200                                   CRYSTAL, VERTICAL FOCUSING VIA A   
REMARK 200                                   ONE-METER, PT/PD-COATED            
REMARK 200                                   CYLINDRICALLY FOCUSING MIRROR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102444                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 3.760                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.04                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER MR                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG MME 2000, 12% ISOPROPANOL, AND    
REMARK 280  0.1 M NAHEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      129.72650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.86325            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      194.58975            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      100.63800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, H                            
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    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     HIS A   495                                                      
REMARK 465     HIS A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     MET B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     HIS B   495                                                      
REMARK 465     HIS B   496                                                      
REMARK 465     HIS B   497                                                      
REMARK 465     MET C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     LYS C    24                                                      
REMARK 465     LYS C    25                                                      
REMARK 465     THR C    26                                                      
REMARK 465     SER C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     LYS C    29                                                      
REMARK 465     GLY C    30                                                      
REMARK 465     HIS C   495                                                      
REMARK 465     HIS C   496                                                      
REMARK 465     HIS C   497                                                      
REMARK 465     MET D    22                                                      
REMARK 465     ALA D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     LYS D    25                                                      
REMARK 465     THR D    26                                                      
REMARK 465     SER D    27                                                      
REMARK 465     SER D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     GLY D    30                                                      
REMARK 465     HIS D   495                                                      
REMARK 465     HIS D   496                                                      
REMARK 465     HIS D   497                                                      
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  41      -58.77     67.96                                   
REMARK 500    ASN A  44       32.72    -94.26                                   
REMARK 500    ASN A  52       67.47   -153.79                                   
REMARK 500    ILE A 114      -62.99   -120.35                                   
REMARK 500    LEU A 171      -66.44   -100.72                                   
REMARK 500    THR A 301      -60.85    -97.66                                   
REMARK 500    THR A 362       61.51     37.67                                   
REMARK 500    ASN A 367     -165.36     66.88                                   
REMARK 500    ASN A 416     -155.45    -88.39                                   
REMARK 500    SER A 431     -170.02     67.51                                   
REMARK 500    ILE B  41      -61.55     74.20                                   
REMARK 500    ASN B  44       33.48    -98.03                                   
REMARK 500    GLN B 141       43.16   -108.23                                   
REMARK 500    LEU B 171      -62.93    -94.18                                   
REMARK 500    PRO B 259       -7.29    -56.94                                   
REMARK 500    LYS B 275       38.58    -75.09                                   
REMARK 500    GLU B 276      -11.58   -159.59                                   
REMARK 500    LYS B 277      -37.13    -36.99                                   
REMARK 500    VAL B 364       77.48   -116.92                                   
REMARK 500    ASN B 367     -169.11     62.69                                   
REMARK 500    SER B 431     -168.71     63.56                                   
REMARK 500    CYS B 437      124.20    -37.66                                   
REMARK 500    ILE C  41      -55.29     73.98                                   
REMARK 500    GLN C 141       31.25    -92.67                                   
REMARK 500    PRO C 259       -2.14    -49.59                                   
REMARK 500    ASP C 264     -165.23   -161.12                                   
REMARK 500    THR C 362       63.91     33.69                                   
REMARK 500    VAL C 364       73.76   -118.85                                   
REMARK 500    ASN C 367     -168.04     60.17                                   
REMARK 500    ASN C 416     -152.40    -96.71                                   
REMARK 500    SER C 431     -164.86     64.69                                   
REMARK 500    ILE D  41      -56.90     80.95                                   
REMARK 500    ASN D  52       70.22   -152.02                                   
REMARK 500    GLN D 141       30.36    -97.65                                   
REMARK 500    LYS D 160       -1.63    -58.88                                   
REMARK 500    LEU D 171      -63.72    -91.43                                   
REMARK 500    PRO D 259        0.86    -53.31                                   
REMARK 500    THR D 362       61.13     35.67                                   
REMARK 500    ASN D 367     -171.12     66.12                                   
REMARK 500    ASN D 416     -152.06    -96.23                                   
REMARK 500    SER D 431     -166.92     60.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 437   SG                                                     
REMARK 620 2 HEM A 500   NA   99.2                                              
REMARK 620 3 HEM A 500   NB   81.3  91.7                                        
REMARK 620 4 HEM A 500   NC   82.6 176.8  91.2                                  
REMARK 620 5 HEM A 500   ND   98.7  88.4 179.9  88.8                            
REMARK 620 6 9PL A 501   N3  170.4  88.5  92.9  89.9  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 437   SG                                                     
REMARK 620 2 HEM B 500   NA   94.4                                              
REMARK 620 3 HEM B 500   NB   82.0  91.5                                        
REMARK 620 4 HEM B 500   NC   85.0 179.0  89.2                                  
REMARK 620 5 HEM B 500   ND   97.4  87.9 179.1  91.4                            
REMARK 620 6 9PL B 501   N3  175.4  88.9  94.7  91.7  85.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 437   SG                                                     
REMARK 620 2 HEM C 500   NA   96.6                                              
REMARK 620 3 HEM C 500   NB   84.6  95.2                                        
REMARK 620 4 HEM C 500   NC   84.2 178.8  85.8                                  
REMARK 620 5 HEM C 500   ND   95.1  84.9 179.7  94.2                            
REMARK 620 6 9PL C 501   N3  175.5  87.4  93.0  91.9  87.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 437   SG                                                     
REMARK 620 2 HEM D 500   NA   98.1                                              
REMARK 620 3 HEM D 500   NB   82.7  94.2                                        
REMARK 620 4 HEM D 500   NC   82.4 176.8  89.0                                  
REMARK 620 5 HEM D 500   ND   96.1  84.7 178.3  92.1                            
REMARK 620 6 9PL D 501   N3  173.8  86.2  92.6  93.5  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3E4E   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH THE INHIBITOR 4-           
REMARK 900 METHYLPYRAZOLE                                                       
REMARK 900 RELATED ID: 3E6I   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH THE INHIBITOR INDAZOLE     
REMARK 900 RELATED ID: 3LC4   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-          
REMARK 900 DODECANOIC ACID                                                      
REMARK 900 RELATED ID: 3KOH   RELATED DB: PDB                                   
REMARK 900 CYTOCHROME P450 2E1 WITH OMEGA-IMIDAZOLYL OCTANOIC ACID              
REMARK 900 RELATED ID: 3GPH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYTOCHROME P450 2E1 IN COMPLEX WITH OMEGA-IMIDAZOLYL-DECANOIC  
REMARK 900 ACID                                                                 
REMARK 900 RELATED ID: 3T3Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3T3R   RELATED DB: NDB                                   
REMARK 900 RELATED ID: 3T3S   RELATED DB: PDB                                   
DBREF  3T3Z A   32   493  UNP    P05181   CP2E1_HUMAN     31    492             
DBREF  3T3Z B   32   493  UNP    P05181   CP2E1_HUMAN     31    492             
DBREF  3T3Z C   32   493  UNP    P05181   CP2E1_HUMAN     31    492             
DBREF  3T3Z D   32   493  UNP    P05181   CP2E1_HUMAN     31    492             
SEQADV 3T3Z MET A   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z ALA A   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS A   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS A   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z THR A   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER A   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER A   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS A   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z GLY A   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS A   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS A  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS A  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS A  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS A  497  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z MET B   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z ALA B   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS B   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS B   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z THR B   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER B   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER B   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS B   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z GLY B   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS B   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS B  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS B  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS B  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS B  497  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z MET C   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z ALA C   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS C   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS C   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z THR C   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER C   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER C   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS C   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z GLY C   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS C   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS C  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS C  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS C  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS C  497  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z MET D   22  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z ALA D   23  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS D   24  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS D   25  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z THR D   26  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER D   27  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z SER D   28  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS D   29  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z GLY D   30  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z LYS D   31  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS D  494  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS D  495  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS D  496  UNP  P05181              EXPRESSION TAG                 
SEQADV 3T3Z HIS D  497  UNP  P05181              EXPRESSION TAG                 
SEQRES   1 A  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 A  476  GLY PRO PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN          
SEQRES   3 A  476  LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU          
SEQRES   4 A  476  ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY          
SEQRES   5 A  476  SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL          
SEQRES   6 A  476  LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY          
SEQRES   7 A  476  ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG          
SEQRES   8 A  476  GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE          
SEQRES   9 A  476  ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET          
SEQRES  10 A  476  GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA          
SEQRES  11 A  476  HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN          
SEQRES  12 A  476  PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS          
SEQRES  13 A  476  ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP          
SEQRES  14 A  476  TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE          
SEQRES  15 A  476  ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN          
SEQRES  16 A  476  LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO          
SEQRES  17 A  476  GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL          
SEQRES  18 A  476  LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN          
SEQRES  19 A  476  SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS          
SEQRES  20 A  476  LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU          
SEQRES  21 A  476  ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA          
SEQRES  22 A  476  ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR          
SEQRES  23 A  476  LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU          
SEQRES  24 A  476  ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE          
SEQRES  25 A  476  GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU          
SEQRES  26 A  476  MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG          
SEQRES  27 A  476  PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA          
SEQRES  28 A  476  THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS          
SEQRES  29 A  476  GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR          
SEQRES  30 A  476  ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO          
SEQRES  31 A  476  GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER          
SEQRES  32 A  476  ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS          
SEQRES  33 A  476  ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU          
SEQRES  34 A  476  LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU          
SEQRES  35 A  476  VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE          
SEQRES  36 A  476  GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL          
SEQRES  37 A  476  ILE PRO ARG SER HIS HIS HIS HIS                              
SEQRES   1 B  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 B  476  GLY PRO PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN          
SEQRES   3 B  476  LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU          
SEQRES   4 B  476  ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY          
SEQRES   5 B  476  SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL          
SEQRES   6 B  476  LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY          
SEQRES   7 B  476  ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG          
SEQRES   8 B  476  GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE          
SEQRES   9 B  476  ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET          
SEQRES  10 B  476  GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA          
SEQRES  11 B  476  HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN          
SEQRES  12 B  476  PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS          
SEQRES  13 B  476  ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP          
SEQRES  14 B  476  TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE          
SEQRES  15 B  476  ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN          
SEQRES  16 B  476  LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO          
SEQRES  17 B  476  GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL          
SEQRES  18 B  476  LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN          
SEQRES  19 B  476  SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS          
SEQRES  20 B  476  LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU          
SEQRES  21 B  476  ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA          
SEQRES  22 B  476  ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR          
SEQRES  23 B  476  LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU          
SEQRES  24 B  476  ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE          
SEQRES  25 B  476  GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU          
SEQRES  26 B  476  MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG          
SEQRES  27 B  476  PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA          
SEQRES  28 B  476  THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS          
SEQRES  29 B  476  GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR          
SEQRES  30 B  476  ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO          
SEQRES  31 B  476  GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER          
SEQRES  32 B  476  ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS          
SEQRES  33 B  476  ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU          
SEQRES  34 B  476  LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU          
SEQRES  35 B  476  VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE          
SEQRES  36 B  476  GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL          
SEQRES  37 B  476  ILE PRO ARG SER HIS HIS HIS HIS                              
SEQRES   1 C  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 C  476  GLY PRO PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN          
SEQRES   3 C  476  LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU          
SEQRES   4 C  476  ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY          
SEQRES   5 C  476  SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL          
SEQRES   6 C  476  LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY          
SEQRES   7 C  476  ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG          
SEQRES   8 C  476  GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE          
SEQRES   9 C  476  ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET          
SEQRES  10 C  476  GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA          
SEQRES  11 C  476  HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN          
SEQRES  12 C  476  PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS          
SEQRES  13 C  476  ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP          
SEQRES  14 C  476  TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE          
SEQRES  15 C  476  ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN          
SEQRES  16 C  476  LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO          
SEQRES  17 C  476  GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL          
SEQRES  18 C  476  LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN          
SEQRES  19 C  476  SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS          
SEQRES  20 C  476  LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU          
SEQRES  21 C  476  ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA          
SEQRES  22 C  476  ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR          
SEQRES  23 C  476  LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU          
SEQRES  24 C  476  ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE          
SEQRES  25 C  476  GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU          
SEQRES  26 C  476  MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG          
SEQRES  27 C  476  PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA          
SEQRES  28 C  476  THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS          
SEQRES  29 C  476  GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR          
SEQRES  30 C  476  ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO          
SEQRES  31 C  476  GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER          
SEQRES  32 C  476  ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS          
SEQRES  33 C  476  ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU          
SEQRES  34 C  476  LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU          
SEQRES  35 C  476  VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE          
SEQRES  36 C  476  GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL          
SEQRES  37 C  476  ILE PRO ARG SER HIS HIS HIS HIS                              
SEQRES   1 D  476  MET ALA LYS LYS THR SER SER LYS GLY LYS LEU PRO PRO          
SEQRES   2 D  476  GLY PRO PHE PRO LEU PRO ILE ILE GLY ASN LEU PHE GLN          
SEQRES   3 D  476  LEU GLU LEU LYS ASN ILE PRO LYS SER PHE THR ARG LEU          
SEQRES   4 D  476  ALA GLN ARG PHE GLY PRO VAL PHE THR LEU TYR VAL GLY          
SEQRES   5 D  476  SER GLN ARG MET VAL VAL MET HIS GLY TYR LYS ALA VAL          
SEQRES   6 D  476  LYS GLU ALA LEU LEU ASP TYR LYS ASP GLU PHE SER GLY          
SEQRES   7 D  476  ARG GLY ASP LEU PRO ALA PHE HIS ALA HIS ARG ASP ARG          
SEQRES   8 D  476  GLY ILE ILE PHE ASN ASN GLY PRO THR TRP LYS ASP ILE          
SEQRES   9 D  476  ARG ARG PHE SER LEU THR THR LEU ARG ASN TYR GLY MET          
SEQRES  10 D  476  GLY LYS GLN GLY ASN GLU SER ARG ILE GLN ARG GLU ALA          
SEQRES  11 D  476  HIS PHE LEU LEU GLU ALA LEU ARG LYS THR GLN GLY GLN          
SEQRES  12 D  476  PRO PHE ASP PRO THR PHE LEU ILE GLY CYS ALA PRO CYS          
SEQRES  13 D  476  ASN VAL ILE ALA ASP ILE LEU PHE ARG LYS HIS PHE ASP          
SEQRES  14 D  476  TYR ASN ASP GLU LYS PHE LEU ARG LEU MET TYR LEU PHE          
SEQRES  15 D  476  ASN GLU ASN PHE HIS LEU LEU SER THR PRO TRP LEU GLN          
SEQRES  16 D  476  LEU TYR ASN ASN PHE PRO SER PHE LEU HIS TYR LEU PRO          
SEQRES  17 D  476  GLY SER HIS ARG LYS VAL ILE LYS ASN VAL ALA GLU VAL          
SEQRES  18 D  476  LYS GLU TYR VAL SER GLU ARG VAL LYS GLU HIS HIS GLN          
SEQRES  19 D  476  SER LEU ASP PRO ASN CYS PRO ARG ASP LEU THR ASP CYS          
SEQRES  20 D  476  LEU LEU VAL GLU MET GLU LYS GLU LYS HIS SER ALA GLU          
SEQRES  21 D  476  ARG LEU TYR THR MET ASP GLY ILE THR VAL THR VAL ALA          
SEQRES  22 D  476  ASP LEU PHE PHE ALA GLY THR GLU THR THR SER THR THR          
SEQRES  23 D  476  LEU ARG TYR GLY LEU LEU ILE LEU MET LYS TYR PRO GLU          
SEQRES  24 D  476  ILE GLU GLU LYS LEU HIS GLU GLU ILE ASP ARG VAL ILE          
SEQRES  25 D  476  GLY PRO SER ARG ILE PRO ALA ILE LYS ASP ARG GLN GLU          
SEQRES  26 D  476  MET PRO TYR MET ASP ALA VAL VAL HIS GLU ILE GLN ARG          
SEQRES  27 D  476  PHE ILE THR LEU VAL PRO SER ASN LEU PRO HIS GLU ALA          
SEQRES  28 D  476  THR ARG ASP THR ILE PHE ARG GLY TYR LEU ILE PRO LYS          
SEQRES  29 D  476  GLY THR VAL VAL VAL PRO THR LEU ASP SER VAL LEU TYR          
SEQRES  30 D  476  ASP ASN GLN GLU PHE PRO ASP PRO GLU LYS PHE LYS PRO          
SEQRES  31 D  476  GLU HIS PHE LEU ASN GLU ASN GLY LYS PHE LYS TYR SER          
SEQRES  32 D  476  ASP TYR PHE LYS PRO PHE SER THR GLY LYS ARG VAL CYS          
SEQRES  33 D  476  ALA GLY GLU GLY LEU ALA ARG MET GLU LEU PHE LEU LEU          
SEQRES  34 D  476  LEU CYS ALA ILE LEU GLN HIS PHE ASN LEU LYS PRO LEU          
SEQRES  35 D  476  VAL ASP PRO LYS ASP ILE ASP LEU SER PRO ILE HIS ILE          
SEQRES  36 D  476  GLY PHE GLY CYS ILE PRO PRO ARG TYR LYS LEU CYS VAL          
SEQRES  37 D  476  ILE PRO ARG SER HIS HIS HIS HIS                              
HET    GLC  E   1      11                                                       
HET    FRU  E   2      12                                                       
HET    GLC  F   1      11                                                       
HET    FRU  F   2      12                                                       
HET    GLC  G   1      11                                                       
HET    FRU  G   2      12                                                       
HET    GLC  H   1      11                                                       
HET    FRU  H   2      12                                                       
HET    HEM  A 500      43                                                       
HET    9PL  A 501      15                                                       
HET    HEM  B 500      43                                                       
HET    9PL  B 501      15                                                       
HET    HEM  C 500      43                                                       
HET    9PL  C 501      15                                                       
HET    HEM  D 500      43                                                       
HET    9PL  D 501      15                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     FRU BETA-D-FRUCTOFURANOSE                                            
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     9PL (3S,4R)-3-ETHYL-4-[(1-METHYL-1H-IMIDAZOL-5-YL)                   
HETNAM   2 9PL  METHYL]DIHYDROFURAN-2(3H)-ONE                                   
HETSYN     HEM HEME                                                             
HETSYN     9PL PILOCARPINE                                                      
FORMUL   5  GLC    4(C6 H12 O6)                                                 
FORMUL   5  FRU    4(C6 H12 O6)                                                 
FORMUL   9  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  10  9PL    4(C11 H16 N2 O2)                                             
FORMUL  17  HOH   *714(H2 O)                                                    
HELIX    1   1 ASN A   44  LEU A   48  5                                   5    
HELIX    2   2 GLU A   49  LYS A   51  5                                   3    
HELIX    3   3 ASN A   52  GLY A   65  1                                  14    
HELIX    4   4 GLY A   82  ASP A   92  1                                  11    
HELIX    5   5 LEU A  103  HIS A  107  5                                   5    
HELIX    6   6 THR A  121  MET A  138  1                                  18    
HELIX    7   7 GLY A  142  LYS A  160  1                                  19    
HELIX    8   8 PRO A  168  GLY A  173  1                                   6    
HELIX    9   9 GLY A  173  ARG A  186  1                                  14    
HELIX   10  10 ASP A  193  LEU A  210  1                                  18    
HELIX   11  11 THR A  212  PHE A  221  1                                  10    
HELIX   12  12 PHE A  221  HIS A  226  1                                   6    
HELIX   13  13 SER A  231  SER A  256  1                                  26    
HELIX   14  14 ASP A  264  LYS A  275  1                                  12    
HELIX   15  15 THR A  285  TYR A  318  1                                  34    
HELIX   16  16 TYR A  318  ILE A  333  1                                  16    
HELIX   17  17 ALA A  340  GLU A  346  5                                   7    
HELIX   18  18 MET A  347  THR A  362  1                                  16    
HELIX   19  19 LEU A  393  TYR A  398  1                                   6    
HELIX   20  20 LYS A  410  LEU A  415  5                                   6    
HELIX   21  21 GLY A  439  HIS A  457  1                                  19    
HELIX   22  22 ASP A  465  ILE A  469  5                                   5    
HELIX   23  23 ASN B   44  LEU B   48  5                                   5    
HELIX   24  24 GLU B   49  LYS B   51  5                                   3    
HELIX   25  25 ASN B   52  GLY B   65  1                                  14    
HELIX   26  26 GLY B   82  ASP B   92  1                                  11    
HELIX   27  27 LEU B  103  HIS B  107  5                                   5    
HELIX   28  28 THR B  121  MET B  138  1                                  18    
HELIX   29  29 GLY B  142  THR B  161  1                                  20    
HELIX   30  30 PRO B  168  GLY B  173  1                                   6    
HELIX   31  31 GLY B  173  ARG B  186  1                                  14    
HELIX   32  32 ASP B  193  LEU B  210  1                                  18    
HELIX   33  33 THR B  212  PHE B  221  1                                  10    
HELIX   34  34 PHE B  221  HIS B  226  1                                   6    
HELIX   35  35 SER B  231  SER B  256  1                                  26    
HELIX   36  36 ASP B  264  LYS B  275  1                                  12    
HELIX   37  37 THR B  285  TYR B  318  1                                  34    
HELIX   38  38 TYR B  318  ILE B  333  1                                  16    
HELIX   39  39 ALA B  340  GLU B  346  5                                   7    
HELIX   40  40 MET B  347  THR B  362  1                                  16    
HELIX   41  41 LEU B  393  TYR B  398  1                                   6    
HELIX   42  42 LYS B  410  LEU B  415  5                                   6    
HELIX   43  43 GLY B  439  HIS B  457  1                                  19    
HELIX   44  44 ASP B  465  ILE B  469  5                                   5    
HELIX   45  45 ASN C   44  LEU C   48  5                                   5    
HELIX   46  46 ASN C   52  GLY C   65  1                                  14    
HELIX   47  47 GLY C   82  ASP C   92  1                                  11    
HELIX   48  48 LEU C  103  HIS C  107  5                                   5    
HELIX   49  49 THR C  121  MET C  138  1                                  18    
HELIX   50  50 GLY C  142  LYS C  160  1                                  19    
HELIX   51  51 PRO C  168  GLY C  173  1                                   6    
HELIX   52  52 GLY C  173  ARG C  186  1                                  14    
HELIX   53  53 ASP C  193  LEU C  210  1                                  18    
HELIX   54  54 THR C  212  PHE C  221  1                                  10    
HELIX   55  55 PHE C  221  HIS C  226  1                                   6    
HELIX   56  56 GLY C  230  SER C  256  1                                  27    
HELIX   57  57 ASP C  264  LYS C  275  1                                  12    
HELIX   58  58 THR C  285  TYR C  318  1                                  34    
HELIX   59  59 TYR C  318  ILE C  333  1                                  16    
HELIX   60  60 ALA C  340  GLU C  346  5                                   7    
HELIX   61  61 MET C  347  THR C  362  1                                  16    
HELIX   62  62 LEU C  393  TYR C  398  1                                   6    
HELIX   63  63 LYS C  410  LEU C  415  5                                   6    
HELIX   64  64 GLY C  439  HIS C  457  1                                  19    
HELIX   65  65 ASP C  465  ILE C  469  5                                   5    
HELIX   66  66 ASN D   44  LEU D   48  5                                   5    
HELIX   67  67 ASN D   52  GLY D   65  1                                  14    
HELIX   68  68 GLY D   82  ASP D   92  1                                  11    
HELIX   69  69 LEU D  103  HIS D  107  5                                   5    
HELIX   70  70 THR D  121  TYR D  136  1                                  16    
HELIX   71  71 GLY D  142  LYS D  160  1                                  19    
HELIX   72  72 PRO D  168  GLY D  173  1                                   6    
HELIX   73  73 GLY D  173  ARG D  186  1                                  14    
HELIX   74  74 ASP D  193  LEU D  210  1                                  18    
HELIX   75  75 THR D  212  PHE D  221  1                                  10    
HELIX   76  76 PHE D  221  HIS D  226  1                                   6    
HELIX   77  77 SER D  231  SER D  256  1                                  26    
HELIX   78  78 ASP D  264  LYS D  275  1                                  12    
HELIX   79  79 THR D  285  TYR D  318  1                                  34    
HELIX   80  80 TYR D  318  ILE D  333  1                                  16    
HELIX   81  81 ALA D  340  GLU D  346  5                                   7    
HELIX   82  82 MET D  347  THR D  362  1                                  16    
HELIX   83  83 LEU D  393  TYR D  398  1                                   6    
HELIX   84  84 LYS D  410  LEU D  415  5                                   6    
HELIX   85  85 GLY D  439  HIS D  457  1                                  19    
HELIX   86  86 ASP D  465  ILE D  469  5                                   5    
SHEET    1   A 5 VAL A  67  VAL A  72  0                                        
SHEET    2   A 5 GLN A  75  MET A  80 -1  O  MET A  77   N  LEU A  70           
SHEET    3   A 5 VAL A 388  PRO A 391  1  O  VAL A 390   N  MET A  80           
SHEET    4   A 5 HIS A 370  GLU A 371 -1  N  HIS A 370   O  VAL A 389           
SHEET    5   A 5 GLY A  99  ARG A 100 -1  N  GLY A  99   O  GLU A 371           
SHEET    1   B 2 THR A 376  PHE A 378  0                                        
SHEET    2   B 2 TYR A 381  ILE A 383 -1  O  ILE A 383   N  THR A 376           
SHEET    1   C 2 PHE A 458  PRO A 462  0                                        
SHEET    2   C 2 LEU A 487  PRO A 491 -1  O  CYS A 488   N  LYS A 461           
SHEET    1   D 2 HIS A 475  ILE A 476  0                                        
SHEET    2   D 2 CYS A 480  ILE A 481 -1  O  ILE A 481   N  HIS A 475           
SHEET    1   E 5 VAL B  67  VAL B  72  0                                        
SHEET    2   E 5 GLN B  75  MET B  80 -1  O  MET B  77   N  LEU B  70           
SHEET    3   E 5 VAL B 388  PRO B 391  1  O  VAL B 390   N  VAL B  78           
SHEET    4   E 5 HIS B 370  GLU B 371 -1  N  HIS B 370   O  VAL B 389           
SHEET    5   E 5 GLY B  99  ARG B 100 -1  N  GLY B  99   O  GLU B 371           
SHEET    1   F 2 THR B 376  PHE B 378  0                                        
SHEET    2   F 2 TYR B 381  ILE B 383 -1  O  ILE B 383   N  THR B 376           
SHEET    1   G 2 PHE B 458  PRO B 462  0                                        
SHEET    2   G 2 LEU B 487  PRO B 491 -1  O  CYS B 488   N  LYS B 461           
SHEET    1   H 2 HIS B 475  ILE B 476  0                                        
SHEET    2   H 2 CYS B 480  ILE B 481 -1  O  ILE B 481   N  HIS B 475           
SHEET    1   I 5 VAL C  67  VAL C  72  0                                        
SHEET    2   I 5 GLN C  75  MET C  80 -1  O  MET C  77   N  LEU C  70           
SHEET    3   I 5 VAL C 388  PRO C 391  1  O  VAL C 390   N  VAL C  78           
SHEET    4   I 5 HIS C 370  GLU C 371 -1  N  HIS C 370   O  VAL C 389           
SHEET    5   I 5 GLY C  99  ARG C 100 -1  N  GLY C  99   O  GLU C 371           
SHEET    1   J 2 THR C 376  PHE C 378  0                                        
SHEET    2   J 2 TYR C 381  ILE C 383 -1  O  ILE C 383   N  THR C 376           
SHEET    1   K 2 PHE C 458  PRO C 462  0                                        
SHEET    2   K 2 LEU C 487  PRO C 491 -1  O  CYS C 488   N  LYS C 461           
SHEET    1   L 2 HIS C 475  ILE C 476  0                                        
SHEET    2   L 2 CYS C 480  ILE C 481 -1  O  ILE C 481   N  HIS C 475           
SHEET    1   M 5 VAL D  67  VAL D  72  0                                        
SHEET    2   M 5 GLN D  75  MET D  80 -1  O  MET D  77   N  LEU D  70           
SHEET    3   M 5 VAL D 388  PRO D 391  1  O  VAL D 390   N  VAL D  78           
SHEET    4   M 5 HIS D 370  GLU D 371 -1  N  HIS D 370   O  VAL D 389           
SHEET    5   M 5 GLY D  99  ARG D 100 -1  N  GLY D  99   O  GLU D 371           
SHEET    1   N 2 THR D 376  PHE D 378  0                                        
SHEET    2   N 2 TYR D 381  ILE D 383 -1  O  ILE D 383   N  THR D 376           
SHEET    1   O 2 PHE D 458  PRO D 462  0                                        
SHEET    2   O 2 LEU D 487  PRO D 491 -1  O  ILE D 490   N  ASN D 459           
SHEET    1   P 2 HIS D 475  ILE D 476  0                                        
SHEET    2   P 2 CYS D 480  ILE D 481 -1  O  ILE D 481   N  HIS D 475           
LINK         C1  GLC E   1                 O2  FRU E   2     1555   1555  1.45  
LINK         C1  GLC F   1                 O2  FRU F   2     1555   1555  1.44  
LINK         C1  GLC G   1                 O2  FRU G   2     1555   1555  1.42  
LINK         C1  GLC H   1                 O2  FRU H   2     1555   1555  1.45  
LINK         SG  CYS A 437                FE   HEM A 500     1555   1555  2.43  
LINK        FE   HEM A 500                 N3  9PL A 501     1555   1555  2.21  
LINK         SG  CYS B 437                FE   HEM B 500     1555   1555  2.39  
LINK        FE   HEM B 500                 N3  9PL B 501     1555   1555  2.18  
LINK         SG  CYS C 437                FE   HEM C 500     1555   1555  2.32  
LINK        FE   HEM C 500                 N3  9PL C 501     1555   1555  2.18  
LINK         SG  CYS D 437                FE   HEM D 500     1555   1555  2.37  
LINK        FE   HEM D 500                 N3  9PL D 501     1555   1555  2.21  
CRYST1  100.638  100.638  259.453  90.00  90.00  90.00 P 41         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      0.009937  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009937  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003854        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system