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Database: PDB
Entry: 2BVJ
LinkDB: 2BVJ
Original site: 2BVJ 
HEADER    OXIDOREDUCTASE                          28-JUN-05   2BVJ              
TITLE     LIGAND-FREE STRUCTURE OF CYTOCHROME P450 PIKC (CYP107L1)              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 MONOOXYGENASE;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYTOCHROME P450 PIKC CYP107L1, CYTOCHROME P450 HYDROXYLASE  
COMPND   5 PIKC;                                                                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;                        
SOURCE   3 ORGANISM_TAXID: 54571;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);                               
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    CYTOCHROME P450, PIKC, CYP107L1, MACROLIDE MONOOXYGENASE, ANTIBIOTIC  
KEYWDS   2 BIOSYNTHESIS, HEME, IRON, METAL-BINDING, MONOOXYGENASE,              
KEYWDS   3 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.H.SHERMAN,S.LI,L.V.YERMALITSKAYA,Y.KIM,J.A.SMITH,M.R.WATERMAN,      
AUTHOR   2 L.M.PODUST                                                           
REVDAT   4   13-DEC-23 2BVJ    1       LINK                                     
REVDAT   3   24-FEB-09 2BVJ    1       VERSN                                    
REVDAT   2   06-SEP-06 2BVJ    1       JRNL                                     
REVDAT   1   03-JUL-06 2BVJ    0                                                
JRNL        AUTH   D.H.SHERMAN,S.LI,L.V.YERMALITSKAYA,Y.KIM,J.A.SMITH,          
JRNL        AUTH 2 M.R.WATERMAN,L.M.PODUST                                      
JRNL        TITL   THE STRUCTURAL BASIS FOR SUBSTRATE ANCHORING, ACTIVE SITE    
JRNL        TITL 2 SELECTIVITY, AND PRODUCT FORMATION BY P450 PIKC FROM         
JRNL        TITL 3 STREPTOMYCES VENEZUELAE.                                     
JRNL        REF    J.BIOL.CHEM.                  V. 281 26289 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16825192                                                     
JRNL        DOI    10.1074/JBC.M605478200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 65959.720                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 53812                          
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 SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5448                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6800                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.60                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 806                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6046                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 315                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.53000                                             
REMARK   3    B22 (A**2) : -1.73000                                             
REMARK   3    B33 (A**2) : 9.26000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.50000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.940                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.180 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.810 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.970 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.790 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 51.38                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED REGIONS WERE OMMITED FROM      
REMARK   3  THE STRUCTURE                                                       
REMARK   4                                                                      
REMARK   4 2BVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290024623.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI (220) DOUBLE CRYSTAL            
REMARK 200  OPTICS                         : SAGITTAL FOCUSING CRYSTAL AND      
REMARK 200                                   VERTICALLY FOCUSING DOUBLE MIRROR  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55910                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1OXA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000; 0.1 M HEPES, PH 7.5; 0.5   
REMARK 280  MM DTT, PH 7.50                                                     
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      109.09500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.08550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      109.09500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.08550            
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: PQS                                                   
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: PQS                                                   
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ARG A   409                                                      
REMARK 465     GLU A   410                                                      
REMARK 465     ALA A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     ARG A   414                                                      
REMARK 465     THR A   415                                                      
REMARK 465     GLY A   416                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     THR B    82                                                      
REMARK 465     GLU B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     GLU B    85                                                      
REMARK 465     ALA B    86                                                      
REMARK 465     ALA B    87                                                      
REMARK 465     ARG B   409                                                      
REMARK 465     GLU B   410                                                      
REMARK 465     ALA B   411                                                      
REMARK 465     GLY B   412                                                      
REMARK 465     ARG B   413                                                      
REMARK 465     ARG B   414                                                      
REMARK 465     THR B   415                                                      
REMARK 465     GLY B   416                                                      
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     ARG A  34    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  51    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     ARG A 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 180    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 182    CG   OD1  OD2                                       
REMARK 470     GLU A 300    CG   CD   OE1  OE2                                  
REMARK 470     GLY A 408    CA   C    O                                         
REMARK 470     ARG B  75    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B  81    CG   CD1  CD2                                       
REMARK 470     LEU B  88    CG   CD1  CD2                                       
REMARK 470     ASN B  89    CG   OD1  ND2                                       
REMARK 470     LYS B 105    CG   CD   CE   NZ                                   
REMARK 470     PHE B 178    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 186    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 188    CG   CD   OE1  NE2                                  
REMARK 470     THR B 189    OG1  CG2                                            
REMARK 470     MET B 191    CG   SD   CE                                        
REMARK 470     GLN B 208    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 209    CG   OD1  OD2                                       
REMARK 470     GLU B 223    CG   CD   OE1  OE2                                  
REMARK 470     GLY B 408    CA   C    O                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   C1   BME A  1409     C1   BME A  1409     2556     1.58            
REMARK 500   C1   BME B  1409     C1   BME B  1409     2557     1.77            
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    GLU A  94       48.10    -97.61                                   
REMARK 500    LEU A 148      -55.69   -145.80                                   
REMARK 500    VAL A 179      -74.39    -54.24                                   
REMARK 500    PHE A 180       71.24   -111.24                                   
REMARK 500    ASP A 183      138.64   -171.85                                   
REMARK 500    ASP A 209       50.15   -107.67                                   
REMARK 500    LEU A 228      108.30   -161.26                                   
REMARK 500    HIS A 245      -34.44   -154.36                                   
REMARK 500    CYS A 354      115.42    -32.71                                   
REMARK 500    TRP A 405       37.95   -149.06                                   
REMARK 500    LEU B 148      -56.76   -141.50                                   
REMARK 500    VAL B 179      -47.75   -142.35                                   
REMARK 500    PHE B 180       68.36   -113.49                                   
REMARK 500    ALA B 187      -79.03    -43.70                                   
REMARK 500    GLN B 208      162.02    175.00                                   
REMARK 500    HIS B 245      -80.21    -95.62                                   
REMARK 500    GLU B 287       59.48   -140.35                                   
REMARK 500    ASN B 392      118.36    177.64                                   
REMARK 500    TRP B 405       25.57   -141.35                                   
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 A1408  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 354   SG                                                     
REMARK 620 2 HEM A1408   NA   96.7                                              
REMARK 620 3 HEM A1408   NB   84.0  91.4                                        
REMARK 620 4 HEM A1408   NC   81.9 178.3  89.5                                  
REMARK 620 5 HEM A1408   ND   98.2  89.1 177.7  90.1                            
REMARK 620 6 HOH A2087   O   167.1  89.6  84.6  92.0  93.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B1408  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 354   SG                                                     
REMARK 620 2 HEM B1408   NA   99.3                                              
REMARK 620 3 HEM B1408   NB   87.4  91.3                                        
REMARK 620 4 HEM B1408   NC   83.5 177.1  88.7                                  
REMARK 620 5 HEM B1408   ND   96.7  89.7 175.6  90.0                            
REMARK 620 6 HOH B2101   O   167.7  80.4  80.4  96.8  95.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A1408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A1409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A1410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B1408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B1409                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C6H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)     
REMARK 900 RELATED ID: 2C7X   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NARBOMYCIN-BOUND CYTOCHROME P450 PIKC           
REMARK 900 (CYP107L1)                                                           
REMARK 900 RELATED ID: 2CA0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)     
REMARK 900 RELATED ID: 2CD8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FIRST 20 RESIDUES INCLUDING 6X HIS-TAG  AND THROMBIN                 
REMARK 999 CLEAVAGE SITE ARE FROM THE CLONING VECTOR PET28A                     
DBREF  2BVJ A  -19     0  PDB    2BVJ     2BVJ           -19      0             
DBREF  2BVJ A    1   416  UNP    O87605   O87605_9ACTO     1    416             
DBREF  2BVJ B  -19     0  PDB    2BVJ     2BVJ           -19      0             
DBREF  2BVJ B    1   416  UNP    O87605   O87605_9ACTO     1    416             
SEQRES   1 A  436  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  436  LEU VAL PRO ARG GLY SER HIS MET ARG ARG THR GLN GLN          
SEQRES   3 A  436  GLY THR THR ALA SER PRO PRO VAL LEU ASP LEU GLY ALA          
SEQRES   4 A  436  LEU GLY GLN ASP PHE ALA ALA ASP PRO TYR PRO THR TYR          
SEQRES   5 A  436  ALA ARG LEU ARG ALA GLU GLY PRO ALA HIS ARG VAL ARG          
SEQRES   6 A  436  THR PRO GLU GLY ASP GLU VAL TRP LEU VAL VAL GLY TYR          
SEQRES   7 A  436  ASP ARG ALA ARG ALA VAL LEU ALA ASP PRO ARG PHE SER          
SEQRES   8 A  436  LYS ASP TRP ARG ASN SER THR THR PRO LEU THR GLU ALA          
SEQRES   9 A  436  GLU ALA ALA LEU ASN HIS ASN MET LEU GLU SER ASP PRO          
SEQRES  10 A  436  PRO ARG HIS THR ARG LEU ARG LYS LEU VAL ALA ARG GLU          
SEQRES  11 A  436  PHE THR MET ARG ARG VAL GLU LEU LEU ARG PRO ARG VAL          
SEQRES  12 A  436  GLN GLU ILE VAL ASP GLY LEU VAL ASP ALA MET LEU ALA          
SEQRES  13 A  436  ALA PRO ASP GLY ARG ALA ASP LEU MET GLU SER LEU ALA          
SEQRES  14 A  436  TRP PRO LEU PRO ILE THR VAL ILE SER GLU LEU LEU GLY          
SEQRES  15 A  436  VAL PRO GLU PRO ASP ARG ALA ALA PHE ARG VAL TRP THR          
SEQRES  16 A  436  ASP ALA PHE VAL PHE PRO ASP ASP PRO ALA GLN ALA GLN          
SEQRES  17 A  436  THR ALA MET ALA GLU MET SER GLY TYR LEU SER ARG LEU          
SEQRES  18 A  436  ILE ASP SER LYS ARG GLY GLN ASP GLY GLU ASP LEU LEU          
SEQRES  19 A  436  SER ALA LEU VAL ARG THR SER ASP GLU ASP GLY SER ARG          
SEQRES  20 A  436  LEU THR SER GLU GLU LEU LEU GLY MET ALA HIS ILE LEU          
SEQRES  21 A  436  LEU VAL ALA GLY HIS GLU THR THR VAL ASN LEU ILE ALA          
SEQRES  22 A  436  ASN GLY MET TYR ALA LEU LEU SER HIS PRO ASP GLN LEU          
SEQRES  23 A  436  ALA ALA LEU ARG ALA ASP MET THR LEU LEU ASP GLY ALA          
SEQRES  24 A  436  VAL GLU GLU MET LEU ARG TYR GLU GLY PRO VAL GLU SER          
SEQRES  25 A  436  ALA THR TYR ARG PHE PRO VAL GLU PRO VAL ASP LEU ASP          
SEQRES  26 A  436  GLY THR VAL ILE PRO ALA GLY ASP THR VAL LEU VAL VAL          
SEQRES  27 A  436  LEU ALA ASP ALA HIS ARG THR PRO GLU ARG PHE PRO ASP          
SEQRES  28 A  436  PRO HIS ARG PHE ASP ILE ARG ARG ASP THR ALA GLY HIS          
SEQRES  29 A  436  LEU ALA PHE GLY HIS GLY ILE HIS PHE CYS ILE GLY ALA          
SEQRES  30 A  436  PRO LEU ALA ARG LEU GLU ALA ARG ILE ALA VAL ARG ALA          
SEQRES  31 A  436  LEU LEU GLU ARG CYS PRO ASP LEU ALA LEU ASP VAL SER          
SEQRES  32 A  436  PRO GLY GLU LEU VAL TRP TYR PRO ASN PRO MET ILE ARG          
SEQRES  33 A  436  GLY LEU LYS ALA LEU PRO ILE ARG TRP ARG ARG GLY ARG          
SEQRES  34 A  436  GLU ALA GLY ARG ARG THR GLY                                  
SEQRES   1 B  436  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  436  LEU VAL PRO ARG GLY SER HIS MET ARG ARG THR GLN GLN          
SEQRES   3 B  436  GLY THR THR ALA SER PRO PRO VAL LEU ASP LEU GLY ALA          
SEQRES   4 B  436  LEU GLY GLN ASP PHE ALA ALA ASP PRO TYR PRO THR TYR          
SEQRES   5 B  436  ALA ARG LEU ARG ALA GLU GLY PRO ALA HIS ARG VAL ARG          
SEQRES   6 B  436  THR PRO GLU GLY ASP GLU VAL TRP LEU VAL VAL GLY TYR          
SEQRES   7 B  436  ASP ARG ALA ARG ALA VAL LEU ALA ASP PRO ARG PHE SER          
SEQRES   8 B  436  LYS ASP TRP ARG ASN SER THR THR PRO LEU THR GLU ALA          
SEQRES   9 B  436  GLU ALA ALA LEU ASN HIS ASN MET LEU GLU SER ASP PRO          
SEQRES  10 B  436  PRO ARG HIS THR ARG LEU ARG LYS LEU VAL ALA ARG GLU          
SEQRES  11 B  436  PHE THR MET ARG ARG VAL GLU LEU LEU ARG PRO ARG VAL          
SEQRES  12 B  436  GLN GLU ILE VAL ASP GLY LEU VAL ASP ALA MET LEU ALA          
SEQRES  13 B  436  ALA PRO ASP GLY ARG ALA ASP LEU MET GLU SER LEU ALA          
SEQRES  14 B  436  TRP PRO LEU PRO ILE THR VAL ILE SER GLU LEU LEU GLY          
SEQRES  15 B  436  VAL PRO GLU PRO ASP ARG ALA ALA PHE ARG VAL TRP THR          
SEQRES  16 B  436  ASP ALA PHE VAL PHE PRO ASP ASP PRO ALA GLN ALA GLN          
SEQRES  17 B  436  THR ALA MET ALA GLU MET SER GLY TYR LEU SER ARG LEU          
SEQRES  18 B  436  ILE ASP SER LYS ARG GLY GLN ASP GLY GLU ASP LEU LEU          
SEQRES  19 B  436  SER ALA LEU VAL ARG THR SER ASP GLU ASP GLY SER ARG          
SEQRES  20 B  436  LEU THR SER GLU GLU LEU LEU GLY MET ALA HIS ILE LEU          
SEQRES  21 B  436  LEU VAL ALA GLY HIS GLU THR THR VAL ASN LEU ILE ALA          
SEQRES  22 B  436  ASN GLY MET TYR ALA LEU LEU SER HIS PRO ASP GLN LEU          
SEQRES  23 B  436  ALA ALA LEU ARG ALA ASP MET THR LEU LEU ASP GLY ALA          
SEQRES  24 B  436  VAL GLU GLU MET LEU ARG TYR GLU GLY PRO VAL GLU SER          
SEQRES  25 B  436  ALA THR TYR ARG PHE PRO VAL GLU PRO VAL ASP LEU ASP          
SEQRES  26 B  436  GLY THR VAL ILE PRO ALA GLY ASP THR VAL LEU VAL VAL          
SEQRES  27 B  436  LEU ALA ASP ALA HIS ARG THR PRO GLU ARG PHE PRO ASP          
SEQRES  28 B  436  PRO HIS ARG PHE ASP ILE ARG ARG ASP THR ALA GLY HIS          
SEQRES  29 B  436  LEU ALA PHE GLY HIS GLY ILE HIS PHE CYS ILE GLY ALA          
SEQRES  30 B  436  PRO LEU ALA ARG LEU GLU ALA ARG ILE ALA VAL ARG ALA          
SEQRES  31 B  436  LEU LEU GLU ARG CYS PRO ASP LEU ALA LEU ASP VAL SER          
SEQRES  32 B  436  PRO GLY GLU LEU VAL TRP TYR PRO ASN PRO MET ILE ARG          
SEQRES  33 B  436  GLY LEU LYS ALA LEU PRO ILE ARG TRP ARG ARG GLY ARG          
SEQRES  34 B  436  GLU ALA GLY ARG ARG THR GLY                                  
HET    HEM  A1408      43                                                       
HET    BME  A1409       4                                                       
HET    DTT  A1410       8                                                       
HET    HEM  B1408      43                                                       
HET    BME  B1409       4                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETSYN     HEM HEME                                                             
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  BME    2(C2 H6 O S)                                                 
FORMUL   5  DTT    C4 H10 O2 S2                                                 
FORMUL   8  HOH   *315(H2 O)                                                    
HELIX    1   1 LEU A   20  ASP A   27  1                                   8    
HELIX    2   2 PRO A   28  GLY A   39  1                                  12    
HELIX    3   3 GLY A   57  ASP A   67  1                                  11    
HELIX    4   4 ASP A   73  SER A   77  5                                   5    
HELIX    5   5 THR A   82  ASN A   89  1                                   8    
HELIX    6   6 PRO A   98  ALA A  108  1                                  11    
HELIX    7   7 ARG A  109  PHE A  111  5                                   3    
HELIX    8   8 THR A  112  LEU A  118  1                                   7    
HELIX    9   9 LEU A  119  LEU A  135  1                                  17    
HELIX   10  10 LEU A  144  LEU A  148  1                                   5    
HELIX   11  11 TRP A  150  LEU A  161  1                                  12    
HELIX   12  12 PRO A  164  ASP A  167  5                                   4    
HELIX   13  13 ARG A  168  PHE A  180  1                                  13    
HELIX   14  14 ASP A  183  ARG A  206  1                                  24    
HELIX   15  15 ASP A  212  ASP A  224  1                                  13    
HELIX   16  16 THR A  229  ALA A  243  1                                  15    
HELIX   17  17 HIS A  245  SER A  261  1                                  17    
HELIX   18  18 HIS A  262  ASP A  272  1                                  11    
HELIX   19  19 LEU A  275  GLY A  288  1                                  14    
HELIX   20  20 VAL A  318  HIS A  323  1                                   6    
HELIX   21  21 GLY A  356  CYS A  375  1                                  20    
HELIX   22  22 SER A  383  LEU A  387  5                                   5    
HELIX   23  23 GLY B   18  LEU B   20  5                                   3    
HELIX   24  24 GLY B   21  ASP B   27  1                                   7    
HELIX   25  25 PRO B   28  GLY B   39  1                                  12    
HELIX   26  26 GLY B   57  ASP B   67  1                                  11    
HELIX   27  27 ASP B   73  SER B   77  5                                   5    
HELIX   28  28 ASN B   91  SER B   95  5                                   5    
HELIX   29  29 PRO B   98  ARG B  109  1                                  12    
HELIX   30  30 THR B  112  LEU B  119  1                                   8    
HELIX   31  31 LEU B  119  LEU B  135  1                                  17    
HELIX   32  32 LEU B  144  LEU B  148  1                                   5    
HELIX   33  33 TRP B  150  LEU B  161  1                                  12    
HELIX   34  34 PRO B  164  PHE B  178  1                                  15    
HELIX   35  35 ASP B  183  ARG B  206  1                                  24    
HELIX   36  36 ASP B  212  THR B  220  1                                   9    
HELIX   37  37 THR B  229  HIS B  245  1                                  17    
HELIX   38  38 HIS B  245  SER B  261  1                                  17    
HELIX   39  39 HIS B  262  ASP B  272  1                                  11    
HELIX   40  40 LEU B  275  GLY B  288  1                                  14    
HELIX   41  41 VAL B  318  HIS B  323  1                                   6    
HELIX   42  42 GLY B  356  CYS B  375  1                                  20    
HELIX   43  43 SER B  383  LEU B  387  5                                   5    
SHEET    1  AA 4 LEU A  15  ASP A  16  0                                        
SHEET    2  AA 4 ALA A  41  ARG A  45  1  O  ARG A  43   N  LEU A  15           
SHEET    3  AA 4 GLU A  51  VAL A  55 -1  O  VAL A  52   N  VAL A  44           
SHEET    4  AA 4 VAL A 315  VAL A 317  1  O  LEU A 316   N  VAL A  55           
SHEET    1  AB 2 PHE A  70  SER A  71  0                                        
SHEET    2  AB 2 PHE A 297  PRO A 298 -1  O  PHE A 297   N  SER A  71           
SHEET    1  AC 3 ARG A 141  ASP A 143  0                                        
SHEET    2  AC 3 PRO A 402  ARG A 404 -1  O  ILE A 403   N  ALA A 142           
SHEET    3  AC 3 ALA A 379  LEU A 380 -1  O  ALA A 379   N  ARG A 404           
SHEET    1  AD 2 VAL A 302  LEU A 304  0                                        
SHEET    2  AD 2 THR A 307  ILE A 309 -1  O  THR A 307   N  LEU A 304           
SHEET    1  BA 4 LEU B  15  ASP B  16  0                                        
SHEET    2  BA 4 ALA B  41  ARG B  45  1  N  ARG B  45   O  LEU B  15           
SHEET    3  BA 4 GLU B  51  VAL B  55 -1  O  VAL B  52   N  VAL B  44           
SHEET    4  BA 4 VAL B 315  VAL B 317  1  O  LEU B 316   N  VAL B  55           
SHEET    1  BB 2 PHE B  70  SER B  71  0                                        
SHEET    2  BB 2 PHE B 297  PRO B 298 -1  O  PHE B 297   N  SER B  71           
SHEET    1  BC 3 ARG B 141  ASP B 143  0                                        
SHEET    2  BC 3 PRO B 402  ARG B 404 -1  O  ILE B 403   N  ALA B 142           
SHEET    3  BC 3 ALA B 379  LEU B 380 -1  O  ALA B 379   N  ARG B 404           
SHEET    1  BD 2 VAL B 302  LEU B 304  0                                        
SHEET    2  BD 2 THR B 307  ILE B 309 -1  O  THR B 307   N  LEU B 304           
LINK         SG  CYS A 354                FE   HEM A1408     1555   1555  2.63  
LINK        FE   HEM A1408                 O   HOH A2087     1555   1555  2.99  
LINK         SG  CYS B 354                FE   HEM B1408     1555   1555  2.68  
LINK        FE   HEM B1408                 O   HOH B2101     1555   1555  2.88  
CISPEP   1 PRO A   97    PRO A   98          0         0.23                     
CISPEP   2 PRO B   97    PRO B   98          0         0.18                     
SITE     1 AC1 26 LYS A  72  MET A  92  LEU A  93  HIS A 100                    
SITE     2 AC1 26 ARG A 104  PHE A 111  ALA A 243  GLY A 244                    
SITE     3 AC1 26 THR A 247  THR A 248  LEU A 251  PRO A 289                    
SITE     4 AC1 26 ALA A 293  THR A 294  ARG A 296  ALA A 346                    
SITE     5 AC1 26 PHE A 347  GLY A 348  ILE A 351  HIS A 352                    
SITE     6 AC1 26 CYS A 354  ILE A 355  GLY A 356  ALA A 360                    
SITE     7 AC1 26 HOH A2087  HOH A2144                                          
SITE     1 AC2  5 LEU A 135  ARG A 374  CYS A 375  TRP A 405                    
SITE     2 AC2  5 HOH A2143                                                     
SITE     1 AC3  7 ARG A 120  ASP A 277  ARG A 365  ARG A 369                    
SITE     2 AC3  7 HOH A2098  GLY B  21  GLN B  22                               
SITE     1 AC4 24 LYS B  72  MET B  92  LEU B  93  HIS B 100                    
SITE     2 AC4 24 ARG B 104  PHE B 111  LEU B 240  ALA B 243                    
SITE     3 AC4 24 GLY B 244  THR B 247  THR B 248  LEU B 251                    
SITE     4 AC4 24 ALA B 293  THR B 294  ARG B 296  ALA B 346                    
SITE     5 AC4 24 PHE B 347  GLY B 348  HIS B 352  CYS B 354                    
SITE     6 AC4 24 ILE B 355  ALA B 360  HOH B2101  HOH B2140                    
SITE     1 AC5  6 LEU B 135  ARG B 374  CYS B 375  TRP B 405                    
SITE     2 AC5  6 HOH B2168  HOH B2169                                          
CRYST1  218.190   64.171   73.593  90.00 107.15  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      0.004583  0.000000  0.001414        0.00000                         
SCALE2      0.000000  0.015583  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014221        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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