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Database: PDB
Entry: 2VE4
LinkDB: 2VE4
Original site: 2VE4 
HEADER    OXIDOREDUCTASE                          16-OCT-07   2VE4              
TITLE     SUBSTRATE FREE CYANOBACTERIAL CYP120A1                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE CYTOCHROME P450 120;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYTOCHROME P450 ENZYME;                                     
COMPND   5 EC: 1.14.-.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;                              
SOURCE   3 ORGANISM_TAXID: 1148;                                                
SOURCE   4 STRAIN: PCC 6803;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)                                 
KEYWDS    OXIDOREDUCTASE, MONOOXYGENASE, METAL-BINDING, HEME, IRON              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KUHNEL,N.KE,S.G.SLIGAR,M.A.SCHULER,I.SCHLICHTING                    
REVDAT   3   16-MAR-11 2VE4    1       VERSN                                    
REVDAT   2   24-FEB-09 2VE4    1       VERSN                                    
REVDAT   1   29-APR-08 2VE4    0                                                
JRNL        AUTH   K.KUHNEL,N.KE,M.J.CRYLE,S.G.SLIGAR,M.A.SCHULER,              
JRNL        AUTH 2 I.SCHLICHTING                                                
JRNL        TITL   CRYSTAL STRUCTURES OF SUBSTRATE-FREE AND RETINOIC            
JRNL        TITL 2 ACID-BOUND CYANOBACTERIAL CYTOCHROME P450 CYP120A1.          
JRNL        REF    BIOCHEMISTRY                  V.  47  6552 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18512957                                                     
JRNL        DOI    10.1021/BI800328S                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 39760                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.304                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2092                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2575                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 135                          
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6897                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 161                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.26000                                             
REMARK   3    B22 (A**2) : 0.78000                                              
REMARK   3    B33 (A**2) : -0.66000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.18000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.449         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.315         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.260         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.165        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7187 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9792 ; 1.441 ; 2.013       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   861 ; 6.651 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   335 ;38.464 ;23.910       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1181 ;19.223 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    49 ;19.659 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1045 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5561 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3294 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4796 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   285 ; 0.178 ; 0.200       
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):    37 ; 0.170 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.126 ; 0.200       
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):  4437 ; 0.659 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6975 ; 1.113 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3102 ; 1.395 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2813 ; 2.207 ; 4.500       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VE4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34162.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40633                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 5.2                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% ETHYLENE GLYCOL, 7% PEG               
REMARK 280  3350, 0.1 M TRIS PH7.5                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       76.82000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.08500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       76.82000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.08500            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2038  LIES ON A SPECIAL POSITION.                          
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     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     SER A   442                                                      
REMARK 465     LEU A   443                                                      
REMARK 465     MET A   444                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     LEU B   443                                                      
REMARK 465     MET B   444                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  71    CG   CD   CE   NZ                                   
REMARK 470     GLU A 162    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 163    CG   CD   CE   NZ                                   
REMARK 470     GLN A 288    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 291    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 361    CG   CD   CE   NZ                                   
REMARK 470     ASP A 434    CG   OD1  OD2                                       
REMARK 470     ARG A 437    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 439    CG   CD   CE   NZ                                   
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     LYS B 106    CG   CD   CE   NZ                                   
REMARK 470     GLU B 162    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 163    CG   CD   CE   NZ                                   
REMARK 470     GLU B 278    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 288    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 291    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 361    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG B    66     OG1  THR B    70              2.18            
REMARK 500   O    TRP A    80     NH1  ARG A    85              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A  22      -66.09     67.11                                   
REMARK 500    THR A  75      -61.27    -91.07                                   
REMARK 500    PRO A 187       57.61    -92.79                                   
REMARK 500    ASN A 190       55.36    -97.04                                   
REMARK 500    HIS A 256      -80.02    -64.96                                   
REMARK 500    LEU A 289       72.70    -69.35                                   
REMARK 500    ILE A 315       79.35   -117.27                                   
REMARK 500    LYS A 338      141.55    -33.17                                   
REMARK 500    PRO A 359        7.40    -66.36                                   
REMARK 500    PRO A 369      -29.12    -22.06                                   
REMARK 500    HIS A 375       40.72    -99.30                                   
REMARK 500    ASN A 435       43.15     38.34                                   
REMARK 500    LEU A 436       93.96     60.27                                   
REMARK 500    TRP B  22      -68.28     61.37                                   
REMARK 500    GLN B  41       42.82    -69.68                                   
REMARK 500    GLN B  42      -56.01   -161.18                                   
REMARK 500    PRO B 187       56.51    -93.02                                   
REMARK 500    HIS B 256      -78.11    -72.00                                   
REMARK 500    HIS B 273       76.27   -119.75                                   
REMARK 500    GLN B 288       57.84    -98.09                                   
REMARK 500    SER B 290     -156.18    -99.05                                   
REMARK 500    GLN B 291       32.01    -89.64                                   
REMARK 500    PRO B 369      -38.61    -19.31                                   
REMARK 500    PHE B 379       40.48     76.58                                   
REMARK 500    CYS B 391      120.09    -38.54                                   
REMARK 500    VAL B 426       71.05   -119.10                                   
REMARK 500    LEU B 436       81.07     57.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  437     VAL A  438                 -149.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 435        24.3      L          L   OUTSIDE RANGE           
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 A1442  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM A1442   ND                                                     
REMARK 620 2 CYS A 391   SG   96.6                                              
REMARK 620 3 HEM A1442   NA   89.0 103.1                                        
REMARK 620 4 HEM A1442   NB  170.4  92.1  85.1                                  
REMARK 620 5 HEM A1442   NC   98.3  83.0 170.0  86.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B1443  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM B1443   NC                                                     
REMARK 620 2 CYS B 391   SG   89.7                                              
REMARK 620 3 HEM B1443   NB   86.4  89.8                                        
REMARK 620 4 HEM B1443   ND   94.4 102.0 168.2                                  
REMARK 620 5 HEM B1443   NA  166.0 101.6  85.4  91.3                            
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 A1442                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B1443                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VE3   RELATED DB: PDB                                   
REMARK 900  RETINOIC ACID BOUND CYANOBACTERIAL CYP120A1                         
DBREF  2VE4 A    1   444  UNP    Q59990   CP120_SYNY3      1    444             
DBREF  2VE4 B    1   444  UNP    Q59990   CP120_SYNY3      1    444             
SEQRES   1 A  444  MET ILE THR SER PRO THR ASN LEU ASN SER LEU PRO ILE          
SEQRES   2 A  444  PRO PRO GLY ASP PHE GLY LEU PRO TRP LEU GLY GLU THR          
SEQRES   3 A  444  LEU ASN PHE LEU ASN ASP GLY ASP PHE GLY LYS LYS ARG          
SEQRES   4 A  444  GLN GLN GLN PHE GLY PRO ILE PHE LYS THR ARG LEU PHE          
SEQRES   5 A  444  GLY LYS ASN VAL ILE PHE ILE SER GLY ALA LEU ALA ASN          
SEQRES   6 A  444  ARG PHE LEU PHE THR LYS GLU GLN GLU THR PHE GLN ALA          
SEQRES   7 A  444  THR TRP PRO LEU SER THR ARG ILE LEU LEU GLY PRO ASN          
SEQRES   8 A  444  ALA LEU ALA THR GLN MET GLY GLU ILE HIS ARG SER ARG          
SEQRES   9 A  444  ARG LYS ILE LEU TYR GLN ALA PHE LEU PRO ARG THR LEU          
SEQRES  10 A  444  ASP SER TYR LEU PRO LYS MET ASP GLY ILE VAL GLN GLY          
SEQRES  11 A  444  TYR LEU GLU GLN TRP GLY LYS ALA ASN GLU VAL ILE TRP          
SEQRES  12 A  444  TYR PRO GLN LEU ARG ARG MET THR PHE ASP VAL ALA ALA          
SEQRES  13 A  444  THR LEU PHE MET GLY GLU LYS VAL SER GLN ASN PRO GLN          
SEQRES  14 A  444  LEU PHE PRO TRP PHE GLU THR TYR ILE GLN GLY LEU PHE          
SEQRES  15 A  444  SER LEU PRO ILE PRO LEU PRO ASN THR LEU PHE GLY LYS          
SEQRES  16 A  444  SER GLN ARG ALA ARG ALA LEU LEU LEU ALA GLU LEU GLU          
SEQRES  17 A  444  LYS ILE ILE LYS ALA ARG GLN GLN GLN PRO PRO SER GLU          
SEQRES  18 A  444  GLU ASP ALA LEU GLY ILE LEU LEU ALA ALA ARG ASP ASP          
SEQRES  19 A  444  ASN ASN GLN PRO LEU SER LEU PRO GLU LEU LYS ASP GLN          
SEQRES  20 A  444  ILE LEU LEU LEU LEU PHE ALA GLY HIS GLU THR LEU THR          
SEQRES  21 A  444  SER ALA LEU SER SER PHE CYS LEU LEU LEU GLY GLN HIS          
SEQRES  22 A  444  SER ASP ILE ARG GLU ARG VAL ARG GLN GLU GLN ASN LYS          
SEQRES  23 A  444  LEU GLN LEU SER GLN GLU LEU THR ALA GLU THR LEU LYS          
SEQRES  24 A  444  LYS MET PRO TYR LEU ASP GLN VAL LEU GLN GLU VAL LEU          
SEQRES  25 A  444  ARG LEU ILE PRO PRO VAL GLY GLY GLY PHE ARG GLU LEU          
SEQRES  26 A  444  ILE GLN ASP CYS GLN PHE GLN GLY PHE HIS PHE PRO LYS          
SEQRES  27 A  444  GLY TRP LEU VAL SER TYR GLN ILE SER GLN THR HIS ALA          
SEQRES  28 A  444  ASP PRO ASP LEU TYR PRO ASP PRO GLU LYS PHE ASP PRO          
SEQRES  29 A  444  GLU ARG PHE THR PRO ASP GLY SER ALA THR HIS ASN PRO          
SEQRES  30 A  444  PRO PHE ALA HIS VAL PRO PHE GLY GLY GLY LEU ARG GLU          
SEQRES  31 A  444  CYS LEU GLY LYS GLU PHE ALA ARG LEU GLU MET LYS LEU          
SEQRES  32 A  444  PHE ALA THR ARG LEU ILE GLN GLN PHE ASP TRP THR LEU          
SEQRES  33 A  444  LEU PRO GLY GLN ASN LEU GLU LEU VAL VAL THR PRO SER          
SEQRES  34 A  444  PRO ARG PRO LYS ASP ASN LEU ARG VAL LYS LEU HIS SER          
SEQRES  35 A  444  LEU MET                                                      
SEQRES   1 B  444  MET ILE THR SER PRO THR ASN LEU ASN SER LEU PRO ILE          
SEQRES   2 B  444  PRO PRO GLY ASP PHE GLY LEU PRO TRP LEU GLY GLU THR          
SEQRES   3 B  444  LEU ASN PHE LEU ASN ASP GLY ASP PHE GLY LYS LYS ARG          
SEQRES   4 B  444  GLN GLN GLN PHE GLY PRO ILE PHE LYS THR ARG LEU PHE          
SEQRES   5 B  444  GLY LYS ASN VAL ILE PHE ILE SER GLY ALA LEU ALA ASN          
SEQRES   6 B  444  ARG PHE LEU PHE THR LYS GLU GLN GLU THR PHE GLN ALA          
SEQRES   7 B  444  THR TRP PRO LEU SER THR ARG ILE LEU LEU GLY PRO ASN          
SEQRES   8 B  444  ALA LEU ALA THR GLN MET GLY GLU ILE HIS ARG SER ARG          
SEQRES   9 B  444  ARG LYS ILE LEU TYR GLN ALA PHE LEU PRO ARG THR LEU          
SEQRES  10 B  444  ASP SER TYR LEU PRO LYS MET ASP GLY ILE VAL GLN GLY          
SEQRES  11 B  444  TYR LEU GLU GLN TRP GLY LYS ALA ASN GLU VAL ILE TRP          
SEQRES  12 B  444  TYR PRO GLN LEU ARG ARG MET THR PHE ASP VAL ALA ALA          
SEQRES  13 B  444  THR LEU PHE MET GLY GLU LYS VAL SER GLN ASN PRO GLN          
SEQRES  14 B  444  LEU PHE PRO TRP PHE GLU THR TYR ILE GLN GLY LEU PHE          
SEQRES  15 B  444  SER LEU PRO ILE PRO LEU PRO ASN THR LEU PHE GLY LYS          
SEQRES  16 B  444  SER GLN ARG ALA ARG ALA LEU LEU LEU ALA GLU LEU GLU          
SEQRES  17 B  444  LYS ILE ILE LYS ALA ARG GLN GLN GLN PRO PRO SER GLU          
SEQRES  18 B  444  GLU ASP ALA LEU GLY ILE LEU LEU ALA ALA ARG ASP ASP          
SEQRES  19 B  444  ASN ASN GLN PRO LEU SER LEU PRO GLU LEU LYS ASP GLN          
SEQRES  20 B  444  ILE LEU LEU LEU LEU PHE ALA GLY HIS GLU THR LEU THR          
SEQRES  21 B  444  SER ALA LEU SER SER PHE CYS LEU LEU LEU GLY GLN HIS          
SEQRES  22 B  444  SER ASP ILE ARG GLU ARG VAL ARG GLN GLU GLN ASN LYS          
SEQRES  23 B  444  LEU GLN LEU SER GLN GLU LEU THR ALA GLU THR LEU LYS          
SEQRES  24 B  444  LYS MET PRO TYR LEU ASP GLN VAL LEU GLN GLU VAL LEU          
SEQRES  25 B  444  ARG LEU ILE PRO PRO VAL GLY GLY GLY PHE ARG GLU LEU          
SEQRES  26 B  444  ILE GLN ASP CYS GLN PHE GLN GLY PHE HIS PHE PRO LYS          
SEQRES  27 B  444  GLY TRP LEU VAL SER TYR GLN ILE SER GLN THR HIS ALA          
SEQRES  28 B  444  ASP PRO ASP LEU TYR PRO ASP PRO GLU LYS PHE ASP PRO          
SEQRES  29 B  444  GLU ARG PHE THR PRO ASP GLY SER ALA THR HIS ASN PRO          
SEQRES  30 B  444  PRO PHE ALA HIS VAL PRO PHE GLY GLY GLY LEU ARG GLU          
SEQRES  31 B  444  CYS LEU GLY LYS GLU PHE ALA ARG LEU GLU MET LYS LEU          
SEQRES  32 B  444  PHE ALA THR ARG LEU ILE GLN GLN PHE ASP TRP THR LEU          
SEQRES  33 B  444  LEU PRO GLY GLN ASN LEU GLU LEU VAL VAL THR PRO SER          
SEQRES  34 B  444  PRO ARG PRO LYS ASP ASN LEU ARG VAL LYS LEU HIS SER          
SEQRES  35 B  444  LEU MET                                                      
HET    HEM  A1442      43                                                       
HET    HEM  B1443      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  HOH   *161(H2 O)                                                    
HELIX    1   1 GLU A   25  ASP A   32  1                                   8    
HELIX    2   2 ASP A   34  GLY A   44  1                                  11    
HELIX    3   3 GLY A   61  PHE A   69  1                                   9    
HELIX    4   4 LYS A   71  THR A   75  1                                   5    
HELIX    5   5 PRO A   81  GLY A   89  1                                   9    
HELIX    6   6 ALA A   92  GLN A   96  5                                   5    
HELIX    7   7 MET A   97  TYR A  109  1                                  13    
HELIX    8   8 GLN A  110  PHE A  112  5                                   3    
HELIX    9   9 LEU A  113  SER A  119  1                                   7    
HELIX   10  10 TYR A  120  ALA A  138  1                                  19    
HELIX   11  11 TRP A  143  GLY A  161  1                                  19    
HELIX   12  12 GLY A  161  GLN A  166  1                                   6    
HELIX   13  13 GLN A  169  GLY A  180  1                                  12    
HELIX   14  14 THR A  191  GLN A  216  1                                  26    
HELIX   15  15 ASP A  223  ALA A  231  1                                   9    
HELIX   16  16 SER A  240  LEU A  270  1                                  31    
HELIX   17  17 HIS A  273  LYS A  286  1                                  14    
HELIX   18  18 THR A  294  LYS A  299  1                                   6    
HELIX   19  19 MET A  301  ILE A  315  1                                  15    
HELIX   20  20 GLN A  345  HIS A  350  1                                   6    
HELIX   21  21 ASP A  363  THR A  368  5                                   6    
HELIX   22  22 GLY A  386  GLU A  390  5                                   5    
HELIX   23  23 GLY A  393  PHE A  412  1                                  20    
HELIX   24  24 GLU B   25  ASP B   32  1                                   8    
HELIX   25  25 ARG B   39  GLY B   44  1                                   6    
HELIX   26  26 GLY B   61  PHE B   69  1                                   9    
HELIX   27  27 LYS B   71  THR B   75  1                                   5    
HELIX   28  28 PRO B   81  GLY B   89  1                                   9    
HELIX   29  29 MET B   97  TYR B  109  1                                  13    
HELIX   30  30 GLN B  110  PHE B  112  5                                   3    
HELIX   31  31 LEU B  113  LYS B  137  1                                  25    
HELIX   32  32 TRP B  143  GLY B  161  1                                  19    
HELIX   33  33 LYS B  163  ASN B  167  5                                   5    
HELIX   34  34 GLN B  169  GLY B  180  1                                  12    
HELIX   35  35 THR B  191  GLN B  215  1                                  25    
HELIX   36  36 ASP B  223  ALA B  230  1                                   8    
HELIX   37  37 SER B  240  HIS B  273  1                                  34    
HELIX   38  38 HIS B  273  LEU B  287  1                                  15    
HELIX   39  39 THR B  294  LYS B  299  1                                   6    
HELIX   40  40 MET B  301  ILE B  315  1                                  15    
HELIX   41  41 ILE B  346  HIS B  350  1                                   5    
HELIX   42  42 ASP B  363  THR B  368  5                                   6    
HELIX   43  43 GLY B  386  GLU B  390  5                                   5    
HELIX   44  44 GLY B  393  PHE B  412  1                                  20    
SHEET    1  AA 5 PHE A  47  LEU A  51  0                                        
SHEET    2  AA 5 LYS A  54  PHE A  58 -1  O  LYS A  54   N  LEU A  51           
SHEET    3  AA 5 LEU A 341  TYR A 344  1  O  LEU A 341   N  ILE A  57           
SHEET    4  AA 5 GLY A 321  LEU A 325 -1  O  GLY A 321   N  TYR A 344           
SHEET    5  AA 5 PHE A  76  GLN A  77 -1  O  GLN A  77   N  GLU A 324           
SHEET    1  AB 3 VAL A 141  ILE A 142  0                                        
SHEET    2  AB 3 ARG A 437  LEU A 440 -1  O  VAL A 438   N  VAL A 141           
SHEET    3  AB 3 TRP A 414  LEU A 416 -1  O  THR A 415   N  LYS A 439           
SHEET    1  AC 2 CYS A 329  PHE A 331  0                                        
SHEET    2  AC 2 PHE A 334  PHE A 336 -1  O  PHE A 334   N  PHE A 331           
SHEET    1  AD 2 LEU A 424  VAL A 425  0                                        
SHEET    2  AD 2 ARG A 431  PRO A 432 -1  O  ARG A 431   N  VAL A 425           
SHEET    1  BA 5 PHE B  47  LEU B  51  0                                        
SHEET    2  BA 5 LYS B  54  SER B  60 -1  O  LYS B  54   N  LEU B  51           
SHEET    3  BA 5 LEU B 341  GLN B 345  1  O  LEU B 341   N  ILE B  57           
SHEET    4  BA 5 GLY B 320  LEU B 325 -1  O  GLY B 321   N  TYR B 344           
SHEET    5  BA 5 PHE B  76  ALA B  78 -1  O  GLN B  77   N  GLU B 324           
SHEET    1  BB 3 VAL B 141  ILE B 142  0                                        
SHEET    2  BB 3 ARG B 437  HIS B 441 -1  O  VAL B 438   N  VAL B 141           
SHEET    3  BB 3 ASP B 413  LEU B 416 -1  O  ASP B 413   N  HIS B 441           
SHEET    1  BC 2 CYS B 329  PHE B 331  0                                        
SHEET    2  BC 2 PHE B 334  PHE B 336 -1  O  PHE B 334   N  PHE B 331           
SHEET    1  BD 2 LEU B 424  VAL B 426  0                                        
SHEET    2  BD 2 PRO B 430  PRO B 432 -1  O  ARG B 431   N  VAL B 425           
LINK        FE   HEM A1442                 SG  CYS A 391     1555   1555  2.36  
LINK        FE   HEM B1443                 SG  CYS B 391     1555   1555  2.36  
CISPEP   1 THR A  427    PRO A  428          0        -0.83                     
CISPEP   2 THR B  427    PRO B  428          0        -6.92                     
SITE     1 AC1 20 LEU A  93  HIS A 101  ARG A 105  ALA A 254                    
SITE     2 AC1 20 GLY A 255  THR A 258  LEU A 259  VAL A 318                    
SITE     3 AC1 20 ARG A 323  TYR A 344  ILE A 346  PRO A 383                    
SITE     4 AC1 20 PHE A 384  GLY A 385  ARG A 389  CYS A 391                    
SITE     5 AC1 20 GLY A 393  PHE A 396  ALA A 397  HOH A2075                    
SITE     1 AC2 20 LEU B  93  HIS B 101  ARG B 105  PHE B 159                    
SITE     2 AC2 20 LEU B 251  ALA B 254  GLY B 255  THR B 258                    
SITE     3 AC2 20 PRO B 317  VAL B 318  ARG B 323  TYR B 344                    
SITE     4 AC2 20 PRO B 383  PHE B 384  GLY B 385  ARG B 389                    
SITE     5 AC2 20 CYS B 391  GLY B 393  PHE B 396  HOH B2084                    
CRYST1  153.640  122.170   64.920  90.00 115.00  90.00 C 1 2 1       8          
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      0.006509  0.000000  0.003035        0.00000                         
SCALE2      0.000000  0.008185  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016996        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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