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Database: PDB
Entry: 2IVE
LinkDB: 2IVE
Original site: 2IVE 
HEADER    OXIDOREDUCTASE                          13-JUN-06   2IVE              
TITLE     STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM MYXOCOCCUS XANTHUS       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTOPORPHYRINOGEN OXIDASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PPO, PPOX;                                                  
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYXOCOCCUS XANTHUS;                             
SOURCE   3 ORGANISM_TAXID: 34;                                                  
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: JM109                                      
KEYWDS    OXIDOREDUCTASE, PROTOPORPHYRINOGEN OXIDASE, PORPHYRIN BIOSYNTHESIS,   
KEYWDS   2 CHLOROPHYLL BIOSYNTHESIS, FAD, PORPHYRIA, FLAVOPROTEIN, HEME         
KEYWDS   3 BIOSYNTHESIS, HAEM BIOSYNTHESIS                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.R.CORRADI,A.V.CORRIGALL,E.BOIX,C.G.MOHAN,E.D.STURROCK,P.N.MEISSNER, 
AUTHOR   2 K.R.ACHARYA                                                          
REVDAT   5   13-DEC-23 2IVE    1       REMARK                                   
REVDAT   4   24-FEB-09 2IVE    1       VERSN                                    
REVDAT   3   13-DEC-06 2IVE    1       JRNL                                     
REVDAT   2   25-OCT-06 2IVE    1       JRNL                                     
REVDAT   1   17-OCT-06 2IVE    0                                                
JRNL        AUTH   H.R.CORRADI,A.V.CORRIGALL,E.BOIX,C.G.MOHAN,E.D.STURROCK,     
JRNL        AUTH 2 P.N.MEISSNER,K.R.ACHARYA                                     
JRNL        TITL   CRYSTAL STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM         
JRNL        TITL 2 MYXOCOCCUS XANTHUS AND ITS COMPLEX WITH THE INHIBITOR        
JRNL        TITL 3 ACIFLUORFEN.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 281 38625 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17046834                                                     
JRNL        DOI    10.1074/JBC.M606640200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40498                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 857                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2914                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6648                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 217                                     
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.04000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.496         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.323         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.262         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.894        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.889                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.849                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6920 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9399 ; 1.122 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   897 ; 4.828 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   270 ;29.385 ;21.852       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1007 ;17.243 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    74 ;16.514 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1078 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5194 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3062 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4622 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   277 ; 0.118 ; 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):    50 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.114 ; 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):  4543 ; 0.269 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6992 ; 0.484 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2673 ; 0.431 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2407 ; 0.764 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS. RESIDUES 87-93 IN BOTH MOLECULES COULD NOT BE            
REMARK   3  MODELLED VERY ACCURATELY DUE TO LOTS OF NOISE IN THE MAPS           
REMARK   4                                                                      
REMARK   4 2IVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290029093.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41382                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, MOLREP                                        
REMARK 200 STARTING MODEL: PDB ENTRY 1SEZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL PH 7.5, 1.5M AMMONIUM      
REMARK 280  SULPHATE, 20% GLYCEROL, 1% PEG 4000, PH 7.50                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
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   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       74.28300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       74.28300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       74.28300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       74.28300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       74.28300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       74.28300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       74.28300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       74.28300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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 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 B2052  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 PROTOPORPHYRINOGEN OXIDASE IS RESPONSIBLE FOR THE CATALYTIC          
REMARK 400  OXIDATION OF PROTOPORPHYRINOGEN IX.                                 
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    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     ALA A   210                                                      
REMARK 465     LEU A   211                                                      
REMARK 465     PRO A   212                                                      
REMARK 465     ALA A   213                                                      
REMARK 465     GLY A   465                                                      
REMARK 465     ASN A   466                                                      
REMARK 465     THR A   467                                                      
REMARK 465     SER A   468                                                      
REMARK 465     HIS A   469                                                      
REMARK 465     ALA A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     ALA B   210                                                      
REMARK 465     LEU B   211                                                      
REMARK 465     PRO B   212                                                      
REMARK 465     ALA B   213                                                      
REMARK 465     GLY B   214                                                      
REMARK 465     THR B   215                                                      
REMARK 465     ALA B   216                                                      
REMARK 465     THR B   467                                                      
REMARK 465     SER B   468                                                      
REMARK 465     HIS B   469                                                      
REMARK 465     ALA B   470                                                      
REMARK 465     PRO B   471                                                      
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     MET A  10    CG   SD   CE                                        
REMARK 470     GLN A 206    CD   OE1  NE2                                       
REMARK 470     ARG A 207    CD   NE   CZ   NH1  NH2                             
REMARK 470     MET B  10    CG   SD   CE                                        
REMARK 470     ASP B 258    CG   OD1  OD2                                       
REMARK 470     ARG B 432    CD   NE   CZ   NH1  NH2                             
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASP A   89   CG   OD1  OD2                                       
REMARK 480     LYS A   93   CG   CD   CE   NZ                                   
REMARK 480     ARG A  134   NE   CZ   NH1  NH2                                  
REMARK 480     THR A  215   CB   OG1  CG2                                       
REMARK 480     LYS A  218   CD   CE   NZ                                        
REMARK 480     ARG A  256   NE   CZ   NH1  NH2                                  
REMARK 480     ARG A  262   NE   CZ   NH1  NH2                                  
REMARK 480     ARG A  270   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  290   CD   CE   NZ                                        
REMARK 480     ASP B   89   CG   OD1  OD2                                       
REMARK 480     LYS B   93   CG   CD   CE   NZ                                   
REMARK 480     GLN B  203   CG   CD   OE1  NE2                                  
REMARK 480     GLN B  206   CD   OE1  NE2                                       
REMARK 480     ARG B  207   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLN B  208   CG   CD   OE1  NE2                                  
REMARK 480     ARG B  262   NE   CZ   NH1  NH2                                  
REMARK 480     LYS B  290   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   CB   ALA A    92     CA   GLY A   328              2.18            
REMARK 500   CB   ALA A    88     O    LEU A   223              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 262   CD    ARG A 262   NE      0.118                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 217   C   -  N   -  CA  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    PRO B  90   C   -  N   -  CD  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    GLN B 206   CG  -  CD  -  OE1 ANGL. DEV. = -12.2 DEGREES          
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    SER A  30       10.60    -69.04                                   
REMARK 500    ALA A  78       12.03    -69.57                                   
REMARK 500    ALA A  87      129.19    -33.20                                   
REMARK 500    ALA A  88       84.89    -63.51                                   
REMARK 500    ASP A  89     -146.05    -67.48                                   
REMARK 500    PRO A  90     -112.04    -77.83                                   
REMARK 500    ALA A  91     -137.01     43.35                                   
REMARK 500    ARG A 193      -65.99     71.49                                   
REMARK 500    GLN A 208       57.52   -110.88                                   
REMARK 500    THR A 215       70.12    140.12                                   
REMARK 500    ALA A 216      178.82    112.49                                   
REMARK 500    PRO A 217     -164.96   -106.28                                   
REMARK 500    THR A 225     -159.12   -146.44                                   
REMARK 500    GLU A 257       90.51   -178.85                                   
REMARK 500    ASP A 258       74.57     49.87                                   
REMARK 500    GLU A 267     -100.69   -104.86                                   
REMARK 500    LEU A 410       79.30   -106.50                                   
REMARK 500    TYR A 443      -76.84   -100.38                                   
REMARK 500    ASN B  80       71.71     31.88                                   
REMARK 500    ALA B  88       76.67     54.59                                   
REMARK 500    ASP B  89     -114.05   -103.92                                   
REMARK 500    PRO B  90     -167.44     -6.21                                   
REMARK 500    ARG B 193      -59.52     69.58                                   
REMARK 500    ASP B 258      -99.92    -42.54                                   
REMARK 500    HIS B 268      -42.68     67.79                                   
REMARK 500    LEU B 410       72.68   -108.63                                   
REMARK 500    TYR B 443      -78.21   -106.54                                   
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 ALA A   88     ASP A   89                 -149.75                    
REMARK 500 ASP A   89     PRO A   90                 -131.60                    
REMARK 500 ALA A   92     LYS A   93                  145.86                    
REMARK 500 ILE A  345     HIS A  346                   57.02                    
REMARK 500 ASP B   89     PRO B   90                 -106.87                    
REMARK 500 GLY B  269     ARG B  270                   76.45                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A2114                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN A4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B2114                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN B4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN B4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B3006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B3007                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IVD   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM MYXOCOCCUS XANTHUS      
REMARK 900 WITH ACIFLUORFEN                                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST MET IN THE PPOX SEQUENCE WAS REPLACED BY THE               
REMARK 999  HIS TAG IN THE CONSTRUCT, BUT THIS RESIDUE WAS NOT                  
REMARK 999  OBSERVED IN THE STRUCTURE                                           
DBREF  2IVE A   -6     3  PDB    2IVE     2IVE            -6      3             
DBREF  2IVE A    4   471  UNP    P56601   PPOX_MYXXA       4    471             
DBREF  2IVE B   -6     3  PDB    2IVE     2IVE            -6      3             
DBREF  2IVE B    4   471  UNP    P56601   PPOX_MYXXA       4    471             
SEQRES   1 A  478  MET ASP HIS HIS HIS HIS HIS HIS HIS HIS MET PRO ARG          
SEQRES   2 A  478  THR THR GLY MET ASN VAL ALA VAL VAL GLY GLY GLY ILE          
SEQRES   3 A  478  SER GLY LEU ALA VAL ALA HIS HIS LEU ARG SER ARG GLY          
SEQRES   4 A  478  THR ASP ALA VAL LEU LEU GLU SER SER ALA ARG LEU GLY          
SEQRES   5 A  478  GLY ALA VAL GLY THR HIS ALA LEU ALA GLY TYR LEU VAL          
SEQRES   6 A  478  GLU GLN GLY PRO ASN SER PHE LEU ASP ARG GLU PRO ALA          
SEQRES   7 A  478  THR ARG ALA LEU ALA ALA ALA LEU ASN LEU GLU GLY ARG          
SEQRES   8 A  478  ILE ARG ALA ALA ASP PRO ALA ALA LYS ARG ARG TYR VAL          
SEQRES   9 A  478  TYR THR ARG GLY ARG LEU ARG SER VAL PRO ALA SER PRO          
SEQRES  10 A  478  PRO ALA PHE LEU ALA SER ASP ILE LEU PRO LEU GLY ALA          
SEQRES  11 A  478  ARG LEU ARG VAL ALA GLY GLU LEU PHE SER ARG ARG ALA          
SEQRES  12 A  478  PRO GLU GLY VAL ASP GLU SER LEU ALA ALA PHE GLY ARG          
SEQRES  13 A  478  ARG HIS LEU GLY HIS ARG ALA THR GLN VAL LEU LEU ASP          
SEQRES  14 A  478  ALA VAL GLN THR GLY ILE TYR ALA GLY ASP VAL GLU GLN          
SEQRES  15 A  478  LEU SER VAL ALA ALA THR PHE PRO MET LEU VAL LYS MET          
SEQRES  16 A  478  GLU ARG GLU HIS ARG SER LEU ILE LEU GLY ALA ILE ARG          
SEQRES  17 A  478  ALA GLN LYS ALA GLN ARG GLN ALA ALA LEU PRO ALA GLY          
SEQRES  18 A  478  THR ALA PRO LYS LEU SER GLY ALA LEU SER THR PHE ASP          
SEQRES  19 A  478  GLY GLY LEU GLN VAL LEU ILE ASP ALA LEU ALA ALA SER          
SEQRES  20 A  478  LEU GLY ASP ALA ALA HIS VAL GLY ALA ARG VAL GLU GLY          
SEQRES  21 A  478  LEU ALA ARG GLU ASP GLY GLY TRP ARG LEU ILE ILE GLU          
SEQRES  22 A  478  GLU HIS GLY ARG ARG ALA GLU LEU SER VAL ALA GLN VAL          
SEQRES  23 A  478  VAL LEU ALA ALA PRO ALA HIS ALA THR ALA LYS LEU LEU          
SEQRES  24 A  478  ARG PRO LEU ASP ASP ALA LEU ALA ALA LEU VAL ALA GLY          
SEQRES  25 A  478  ILE ALA TYR ALA PRO ILE ALA VAL VAL HIS LEU GLY PHE          
SEQRES  26 A  478  ASP ALA GLY THR LEU PRO ALA PRO ASP GLY PHE GLY PHE          
SEQRES  27 A  478  LEU VAL PRO ALA GLU GLU GLN ARG ARG MET LEU GLY ALA          
SEQRES  28 A  478  ILE HIS ALA SER THR THR PHE PRO PHE ARG ALA GLU GLY          
SEQRES  29 A  478  GLY ARG VAL LEU TYR SER CYS MET VAL GLY GLY ALA ARG          
SEQRES  30 A  478  GLN PRO GLY LEU VAL GLU GLN ASP GLU ASP ALA LEU ALA          
SEQRES  31 A  478  ALA LEU ALA ARG GLU GLU LEU LYS ALA LEU ALA GLY VAL          
SEQRES  32 A  478  THR ALA ARG PRO SER PHE THR ARG VAL PHE ARG TRP PRO          
SEQRES  33 A  478  LEU GLY ILE PRO GLN TYR ASN LEU GLY HIS LEU GLU ARG          
SEQRES  34 A  478  VAL ALA ALA ILE ASP ALA ALA LEU GLN ARG LEU PRO GLY          
SEQRES  35 A  478  LEU HIS LEU ILE GLY ASN ALA TYR LYS GLY VAL GLY LEU          
SEQRES  36 A  478  ASN ASP CYS ILE ARG ASN ALA ALA GLN LEU ALA ASP ALA          
SEQRES  37 A  478  LEU VAL ALA GLY ASN THR SER HIS ALA PRO                      
SEQRES   1 B  478  MET ASP HIS HIS HIS HIS HIS HIS HIS HIS MET PRO ARG          
SEQRES   2 B  478  THR THR GLY MET ASN VAL ALA VAL VAL GLY GLY GLY ILE          
SEQRES   3 B  478  SER GLY LEU ALA VAL ALA HIS HIS LEU ARG SER ARG GLY          
SEQRES   4 B  478  THR ASP ALA VAL LEU LEU GLU SER SER ALA ARG LEU GLY          
SEQRES   5 B  478  GLY ALA VAL GLY THR HIS ALA LEU ALA GLY TYR LEU VAL          
SEQRES   6 B  478  GLU GLN GLY PRO ASN SER PHE LEU ASP ARG GLU PRO ALA          
SEQRES   7 B  478  THR ARG ALA LEU ALA ALA ALA LEU ASN LEU GLU GLY ARG          
SEQRES   8 B  478  ILE ARG ALA ALA ASP PRO ALA ALA LYS ARG ARG TYR VAL          
SEQRES   9 B  478  TYR THR ARG GLY ARG LEU ARG SER VAL PRO ALA SER PRO          
SEQRES  10 B  478  PRO ALA PHE LEU ALA SER ASP ILE LEU PRO LEU GLY ALA          
SEQRES  11 B  478  ARG LEU ARG VAL ALA GLY GLU LEU PHE SER ARG ARG ALA          
SEQRES  12 B  478  PRO GLU GLY VAL ASP GLU SER LEU ALA ALA PHE GLY ARG          
SEQRES  13 B  478  ARG HIS LEU GLY HIS ARG ALA THR GLN VAL LEU LEU ASP          
SEQRES  14 B  478  ALA VAL GLN THR GLY ILE TYR ALA GLY ASP VAL GLU GLN          
SEQRES  15 B  478  LEU SER VAL ALA ALA THR PHE PRO MET LEU VAL LYS MET          
SEQRES  16 B  478  GLU ARG GLU HIS ARG SER LEU ILE LEU GLY ALA ILE ARG          
SEQRES  17 B  478  ALA GLN LYS ALA GLN ARG GLN ALA ALA LEU PRO ALA GLY          
SEQRES  18 B  478  THR ALA PRO LYS LEU SER GLY ALA LEU SER THR PHE ASP          
SEQRES  19 B  478  GLY GLY LEU GLN VAL LEU ILE ASP ALA LEU ALA ALA SER          
SEQRES  20 B  478  LEU GLY ASP ALA ALA HIS VAL GLY ALA ARG VAL GLU GLY          
SEQRES  21 B  478  LEU ALA ARG GLU ASP GLY GLY TRP ARG LEU ILE ILE GLU          
SEQRES  22 B  478  GLU HIS GLY ARG ARG ALA GLU LEU SER VAL ALA GLN VAL          
SEQRES  23 B  478  VAL LEU ALA ALA PRO ALA HIS ALA THR ALA LYS LEU LEU          
SEQRES  24 B  478  ARG PRO LEU ASP ASP ALA LEU ALA ALA LEU VAL ALA GLY          
SEQRES  25 B  478  ILE ALA TYR ALA PRO ILE ALA VAL VAL HIS LEU GLY PHE          
SEQRES  26 B  478  ASP ALA GLY THR LEU PRO ALA PRO ASP GLY PHE GLY PHE          
SEQRES  27 B  478  LEU VAL PRO ALA GLU GLU GLN ARG ARG MET LEU GLY ALA          
SEQRES  28 B  478  ILE HIS ALA SER THR THR PHE PRO PHE ARG ALA GLU GLY          
SEQRES  29 B  478  GLY ARG VAL LEU TYR SER CYS MET VAL GLY GLY ALA ARG          
SEQRES  30 B  478  GLN PRO GLY LEU VAL GLU GLN ASP GLU ASP ALA LEU ALA          
SEQRES  31 B  478  ALA LEU ALA ARG GLU GLU LEU LYS ALA LEU ALA GLY VAL          
SEQRES  32 B  478  THR ALA ARG PRO SER PHE THR ARG VAL PHE ARG TRP PRO          
SEQRES  33 B  478  LEU GLY ILE PRO GLN TYR ASN LEU GLY HIS LEU GLU ARG          
SEQRES  34 B  478  VAL ALA ALA ILE ASP ALA ALA LEU GLN ARG LEU PRO GLY          
SEQRES  35 B  478  LEU HIS LEU ILE GLY ASN ALA TYR LYS GLY VAL GLY LEU          
SEQRES  36 B  478  ASN ASP CYS ILE ARG ASN ALA ALA GLN LEU ALA ASP ALA          
SEQRES  37 B  478  LEU VAL ALA GLY ASN THR SER HIS ALA PRO                      
HET    FAD  A2114      53                                                       
HET    GOL  A3001       6                                                       
HET    GOL  A3002       6                                                       
HET    GOL  A3003       6                                                       
HET    TWN  A4002      25                                                       
HET    FAD  B2114      53                                                       
HET    GOL  B3005       6                                                       
HET    GOL  B3006       6                                                       
HET    GOL  B3007       6                                                       
HET    TWN  B4001      25                                                       
HET    TWN  B4003      25                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     TWN (3S)-3-[(2S,3S,4R)-3,4-DIMETHYLTETRAHYDROFURAN-2-                
HETNAM   2 TWN  YL]BUTYL LAURATE                                                
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  GOL    6(C3 H8 O3)                                                  
FORMUL   7  TWN    3(C22 H42 O3)                                                
FORMUL  14  HOH   *146(H2 O)                                                    
HELIX    1   1 GLY A   18  SER A   30  1                                  13    
HELIX    2   2 GLU A   69  ALA A   78  1                                  10    
HELIX    3   3 LEU A   81  GLY A   83  5                                   3    
HELIX    4   4 SER A  109  SER A  116  1                                   8    
HELIX    5   5 PRO A  120  GLY A  129  1                                  10    
HELIX    6   6 GLU A  130  SER A  133  5                                   4    
HELIX    7   7 SER A  143  LEU A  152  1                                  10    
HELIX    8   8 GLY A  153  TYR A  169  1                                  17    
HELIX    9   9 SER A  177  PHE A  182  1                                   6    
HELIX   10  10 PHE A  182  ARG A  193  1                                  12    
HELIX   11  11 SER A  194  ARG A  207  1                                  14    
HELIX   12  12 LEU A  230  GLY A  242  1                                  13    
HELIX   13  13 PRO A  284  ARG A  293  1                                  10    
HELIX   14  14 ASP A  296  GLY A  305  1                                  10    
HELIX   15  15 PRO A  334  GLN A  338  5                                   5    
HELIX   16  16 ALA A  347  PHE A  351  1                                   5    
HELIX   17  17 PRO A  352  ARG A  354  5                                   3    
HELIX   18  18 GLN A  371  GLN A  377  5                                   7    
HELIX   19  19 ASP A  378  ALA A  394  1                                  17    
HELIX   20  20 GLY A  418  GLN A  431  1                                  14    
HELIX   21  21 GLY A  447  VAL A  463  1                                  17    
HELIX   22  22 GLY B   18  GLY B   32  1                                  15    
HELIX   23  23 GLU B   69  LEU B   79  1                                  11    
HELIX   24  24 LEU B   81  GLY B   83  5                                   3    
HELIX   25  25 SER B  109  SER B  116  1                                   8    
HELIX   26  26 PRO B  120  GLY B  129  1                                  10    
HELIX   27  27 GLU B  130  SER B  133  5                                   4    
HELIX   28  28 SER B  143  LEU B  152  1                                  10    
HELIX   29  29 GLY B  153  ALA B  170  1                                  18    
HELIX   30  30 SER B  177  PHE B  182  1                                   6    
HELIX   31  31 PHE B  182  ARG B  193  1                                  12    
HELIX   32  32 SER B  194  ARG B  207  1                                  14    
HELIX   33  33 LEU B  230  GLY B  242  1                                  13    
HELIX   34  34 PRO B  284  ARG B  293  1                                  10    
HELIX   35  35 ASP B  296  GLY B  305  1                                  10    
HELIX   36  36 PRO B  334  GLN B  338  5                                   5    
HELIX   37  37 ALA B  347  PHE B  351  1                                   5    
HELIX   38  38 PRO B  352  ARG B  354  5                                   3    
HELIX   39  39 GLN B  371  GLN B  377  5                                   7    
HELIX   40  40 ASP B  378  GLY B  395  1                                  18    
HELIX   41  41 GLY B  418  GLN B  431  1                                  14    
HELIX   42  42 GLY B  447  GLY B  465  1                                  19    
SHEET    1  AA 5 ALA A 245  VAL A 247  0                                        
SHEET    2  AA 5 ALA A  35  GLU A  39  1  O  LEU A  37   N  HIS A 246           
SHEET    3  AA 5 VAL A  12  VAL A  15  1  O  VAL A  12   N  VAL A  36           
SHEET    4  AA 5 GLN A 278  LEU A 281  1  O  GLN A 278   N  ALA A  13           
SHEET    5  AA 5 LEU A 436  LEU A 438  1  O  HIS A 437   N  LEU A 281           
SHEET    1  AB 2 THR A  50  LEU A  53  0                                        
SHEET    2  AB 2 TYR A  56  GLU A  59 -1  O  TYR A  56   N  LEU A  53           
SHEET    1  AC 3 PHE A  65  LEU A  66  0                                        
SHEET    2  AC 3 LEU A 223  PHE A 226 -1  O  SER A 224   N  PHE A  65           
SHEET    3  AC 3 ILE A  85  ALA A  87 -1  O  ARG A  86   N  THR A 225           
SHEET    1  AD 7 ARG A 102  SER A 105  0                                        
SHEET    2  AD 7 TYR A  96  THR A  99 -1  O  VAL A  97   N  ARG A 104           
SHEET    3  AD 7 PHE A 331  LEU A 332  1  O  LEU A 332   N  TYR A  98           
SHEET    4  AD 7 GLY A 343  HIS A 346 -1  O  ALA A 344   N  PHE A 331           
SHEET    5  AD 7 VAL A 360  GLY A 367 -1  O  SER A 363   N  ILE A 345           
SHEET    6  AD 7 TYR A 308  PHE A 318 -1  O  ALA A 312   N  VAL A 366           
SHEET    7  AD 7 PHE A 402  PRO A 413 -1  O  PHE A 402   N  GLY A 317           
SHEET    1  AE 3 ARG A 250  ARG A 256  0                                        
SHEET    2  AE 3 TRP A 261  GLU A 266 -1  O  ARG A 262   N  ALA A 255           
SHEET    3  AE 3 ARG A 271  VAL A 276 -1  O  ALA A 272   N  ILE A 265           
SHEET    1  BA 5 ALA B 245  VAL B 247  0                                        
SHEET    2  BA 5 ASP B  34  GLU B  39  1  O  LEU B  37   N  HIS B 246           
SHEET    3  BA 5 ASN B  11  VAL B  15  1  O  VAL B  12   N  VAL B  36           
SHEET    4  BA 5 GLN B 278  LEU B 281  1  O  GLN B 278   N  ALA B  13           
SHEET    5  BA 5 LEU B 436  LEU B 438  1  O  HIS B 437   N  LEU B 281           
SHEET    1  BB 2 THR B  50  LEU B  53  0                                        
SHEET    2  BB 2 TYR B  56  GLU B  59 -1  O  TYR B  56   N  LEU B  53           
SHEET    1  BC 3 PHE B  65  LEU B  66  0                                        
SHEET    2  BC 3 LEU B 223  PHE B 226 -1  O  SER B 224   N  PHE B  65           
SHEET    3  BC 3 ILE B  85  ARG B  86 -1  O  ARG B  86   N  THR B 225           
SHEET    1  BD 7 ARG B 102  VAL B 106  0                                        
SHEET    2  BD 7 ARG B  95  THR B  99 -1  O  ARG B  95   N  VAL B 106           
SHEET    3  BD 7 GLY B 330  LEU B 332  1  O  GLY B 330   N  TYR B  96           
SHEET    4  BD 7 GLY B 343  HIS B 346 -1  O  ALA B 344   N  PHE B 331           
SHEET    5  BD 7 VAL B 360  GLY B 367 -1  O  SER B 363   N  ILE B 345           
SHEET    6  BD 7 TYR B 308  PHE B 318 -1  O  ALA B 312   N  VAL B 366           
SHEET    7  BD 7 PHE B 402  PRO B 413 -1  O  PHE B 402   N  GLY B 317           
SHEET    1  BE 3 ALA B 249  ARG B 256  0                                        
SHEET    2  BE 3 TRP B 261  GLU B 267 -1  O  ARG B 262   N  ALA B 255           
SHEET    3  BE 3 ARG B 271  VAL B 276 -1  O  ALA B 272   N  ILE B 265           
SITE     1 AC1 27 VAL A  15  GLY A  16  GLY A  18  ILE A  19                    
SITE     2 AC1 27 SER A  20  LEU A  38  GLU A  39  SER A  40                    
SITE     3 AC1 27 SER A  41  GLY A  46  ALA A  47  GLY A  61                    
SITE     4 AC1 27 PRO A  62  ASN A  63  SER A  64  ALA A 249                    
SITE     5 AC1 27 VAL A 251  ALA A 282  ALA A 287  GLY A 440                    
SITE     6 AC1 27 ASN A 441  VAL A 446  GLY A 447  LEU A 448                    
SITE     7 AC1 27 HOH A2003  HOH A2072  TWN A4002                               
SITE     1 AC2 14 THR A 166  GLY A 167  ILE A 168  ALA A 170                    
SITE     2 AC2 14 ILE A 311  PHE A 329  GLY A 330  PHE A 331                    
SITE     3 AC2 14 LEU A 332  GLY A 343  ALA A 344  ILE A 345                    
SITE     4 AC2 14 MET A 365  FAD A2114                                          
SITE     1 AC3 27 VAL B  15  GLY B  16  GLY B  18  ILE B  19                    
SITE     2 AC3 27 SER B  20  LEU B  38  GLU B  39  SER B  40                    
SITE     3 AC3 27 GLY B  46  ALA B  47  GLY B  61  PRO B  62                    
SITE     4 AC3 27 ASN B  63  SER B  64  VAL B 251  ALA B 282                    
SITE     5 AC3 27 ALA B 283  PRO B 284  ALA B 287  GLY B 440                    
SITE     6 AC3 27 ASN B 441  GLY B 447  LEU B 448  HOH B2068                    
SITE     7 AC3 27 HOH B2069  HOH B2070  TWN B4003                               
SITE     1 AC4  4 LEU B 125  ARG B 126  GLY B 129  ARG B 134                    
SITE     1 AC5 11 THR B 166  GLY B 167  ILE B 168  PHE B 329                    
SITE     2 AC5 11 GLY B 330  PHE B 331  LEU B 332  ALA B 344                    
SITE     3 AC5 11 ILE B 345  MET B 365  FAD B2114                               
SITE     1 AC6  6 PRO A 120  LEU A 121  GLY A 122  ALA A 123                    
SITE     2 AC6  6 ARG A 201  HOH A2073                                          
SITE     1 AC7  8 GLY A 122  ALA A 123  ARG A 193  LEU A 197                    
SITE     2 AC7  8 ARG A 201  HOH A2026  HOH A2043  HOH A2074                    
SITE     1 AC8  2 ARG A 126  GLY A 129                                          
SITE     1 AC9  4 PRO B 120  GLY B 122  ARG B 201  HOH B2071                    
SITE     1 BC1  2 LEU A 125  LEU B 125                                          
SITE     1 BC2  7 GLY B 122  ALA B 123  ARG B 193  LEU B 197                    
SITE     2 BC2  7 ARG B 201  HOH B2032  HOH B2072                               
CRYST1  148.566  148.566  132.745  90.00  90.00  90.00 P 4 21 2     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006731  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006731  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007533        0.00000                         
MTRIX1   1 -0.684360  0.729080  0.010240       24.68063    1                    
MTRIX2   1  0.729150  0.684320  0.006900      -53.83945    1                    
MTRIX3   1 -0.001970  0.012190 -0.999920      111.49263    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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