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Database: PDB
Entry: 4FM5
LinkDB: 4FM5
Original site: 4FM5 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 15-JUN-12   4FM5              
TITLE     X-RAY STRUCTURE OF DES-METHYLFLURBIPROFEN BOUND TO MURINE COX-2       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED           
COMPND   6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-         
COMPND   7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2    
COMPND   8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE       
COMPND   9 SYNTHASE 2, TIS10 PROTEIN;                                           
COMPND  10 EC: 1.14.99.1;                                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    MEMBRANE PROTEIN, CYCLOOXYGENASE, HEME BINDING, OXIDOREDUCTASE-       
KEYWDS   2 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XU,S.BANERJEE,M.A.WINDSOR,L.J.MARNETT                               
REVDAT   2   19-DEC-12 4FM5    1       JRNL                                     
REVDAT   1   29-AUG-12 4FM5    0                                                
JRNL        AUTH   M.A.WINDSOR,D.J.HERMANSON,P.J.KINGSLEY,S.XU,B.C.CREWS,W.HO,  
JRNL        AUTH 2 C.M.KEENAN,S.BANERJEE,K.A.SHARKEY,L.J.MARNETT                
JRNL        TITL   SUBSTRATE-SELECTIVE INHIBITION OF CYCLOOXYGENASE-2:          
JRNL        TITL 2 DEVELOPMENT AND EVALUATION OF ACHIRAL PROFEN PROBES.         
JRNL        REF    ACS MED CHEM LETT             V.   3   759 2012              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   22984634                                                     
JRNL        DOI    10.1021/ML3001616                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 70778                          
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) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3752                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.91                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3651                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 337                          
REMARK   3   BIN FREE R VALUE                    : 0.4021                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17896                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 472                                     
REMARK   3   SOLVENT ATOMS            : 186                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.97                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : 0.10000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.429         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.324         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.009        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19084 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A): 13140 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25932 ; 1.984 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 31864 ; 1.469 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2204 ; 6.326 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   896 ;41.374 ;24.107       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3104 ;19.641 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;19.588 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2748 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20828 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3988 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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                                                           
REMARK   4                                                                      
REMARK   4 4FM5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073071.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74531                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.15800                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.030                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3NT1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM EPPS PH 8.0, 20~25% PEG MME 550,   
REMARK 280  80~120 MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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   -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       90.81600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.84800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.81600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.84800            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     PHE A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     CYS A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     GLN A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     ASP A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     THR A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     THR A   592                                                      
REMARK 465     ILE A   593                                                      
REMARK 465     ASN A   594                                                      
REMARK 465     ALA A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     HIS A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ARG A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     ILE A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     VAL A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     MET B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     PHE B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     CYS B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     GLN B    30                                                      
REMARK 465     ALA B    31                                                      
REMARK 465     ASP B   584                                                      
REMARK 465     PRO B   585                                                      
REMARK 465     GLN B   586                                                      
REMARK 465     PRO B   587                                                      
REMARK 465     THR B   588                                                      
REMARK 465     LYS B   589                                                      
REMARK 465     THR B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     THR B   592                                                      
REMARK 465     ILE B   593                                                      
REMARK 465     ASN B   594                                                      
REMARK 465     ALA B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     SER B   598                                                      
REMARK 465     HIS B   599                                                      
REMARK 465     SER B   600                                                      
REMARK 465     ARG B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     ASP B   603                                                      
REMARK 465     ASP B   604                                                      
REMARK 465     ILE B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     VAL B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     SER B   615                                                      
REMARK 465     THR B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     LEU B   618                                                      
REMARK 465     MET C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     PHE C    17                                                      
REMARK 465     ARG C    18                                                      
REMARK 465     ALA C    19                                                      
REMARK 465     VAL C    20                                                      
REMARK 465     LEU C    21                                                      
REMARK 465     LEU C    22                                                      
REMARK 465     CYS C    23                                                      
REMARK 465     ALA C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     LEU C    28                                                      
REMARK 465     SER C    29                                                      
REMARK 465     GLN C    30                                                      
REMARK 465     ALA C    31                                                      
REMARK 465     ASP C   584                                                      
REMARK 465     PRO C   585                                                      
REMARK 465     GLN C   586                                                      
REMARK 465     PRO C   587                                                      
REMARK 465     THR C   588                                                      
REMARK 465     LYS C   589                                                      
REMARK 465     THR C   590                                                      
REMARK 465     ALA C   591                                                      
REMARK 465     THR C   592                                                      
REMARK 465     ILE C   593                                                      
REMARK 465     ASN C   594                                                      
REMARK 465     ALA C   595                                                      
REMARK 465     SER C   596                                                      
REMARK 465     ALA C   597                                                      
REMARK 465     SER C   598                                                      
REMARK 465     HIS C   599                                                      
REMARK 465     SER C   600                                                      
REMARK 465     ARG C   601                                                      
REMARK 465     LEU C   602                                                      
REMARK 465     ASP C   603                                                      
REMARK 465     ASP C   604                                                      
REMARK 465     ILE C   605                                                      
REMARK 465     ASN C   606                                                      
REMARK 465     PRO C   607                                                      
REMARK 465     THR C   608                                                      
REMARK 465     VAL C   609                                                      
REMARK 465     LEU C   610                                                      
REMARK 465     ILE C   611                                                      
REMARK 465     LYS C   612                                                      
REMARK 465     ARG C   613                                                      
REMARK 465     ARG C   614                                                      
REMARK 465     SER C   615                                                      
REMARK 465     THR C   616                                                      
REMARK 465     GLU C   617                                                      
REMARK 465     LEU C   618                                                      
REMARK 465     MET D    15                                                      
REMARK 465     LEU D    16                                                      
REMARK 465     PHE D    17                                                      
REMARK 465     ARG D    18                                                      
REMARK 465     ALA D    19                                                      
REMARK 465     VAL D    20                                                      
REMARK 465     LEU D    21                                                      
REMARK 465     LEU D    22                                                      
REMARK 465     CYS D    23                                                      
REMARK 465     ALA D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     LEU D    26                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     LEU D    28                                                      
REMARK 465     SER D    29                                                      
REMARK 465     GLN D    30                                                      
REMARK 465     ALA D    31                                                      
REMARK 465     ASP D   584                                                      
REMARK 465     PRO D   585                                                      
REMARK 465     GLN D   586                                                      
REMARK 465     PRO D   587                                                      
REMARK 465     THR D   588                                                      
REMARK 465     LYS D   589                                                      
REMARK 465     THR D   590                                                      
REMARK 465     ALA D   591                                                      
REMARK 465     THR D   592                                                      
REMARK 465     ILE D   593                                                      
REMARK 465     ASN D   594                                                      
REMARK 465     ALA D   595                                                      
REMARK 465     SER D   596                                                      
REMARK 465     ALA D   597                                                      
REMARK 465     SER D   598                                                      
REMARK 465     HIS D   599                                                      
REMARK 465     SER D   600                                                      
REMARK 465     ARG D   601                                                      
REMARK 465     LEU D   602                                                      
REMARK 465     ASP D   603                                                      
REMARK 465     ASP D   604                                                      
REMARK 465     ILE D   605                                                      
REMARK 465     ASN D   606                                                      
REMARK 465     PRO D   607                                                      
REMARK 465     THR D   608                                                      
REMARK 465     VAL D   609                                                      
REMARK 465     LEU D   610                                                      
REMARK 465     ILE D   611                                                      
REMARK 465     LYS D   612                                                      
REMARK 465     ARG D   613                                                      
REMARK 465     ARG D   614                                                      
REMARK 465     SER D   615                                                      
REMARK 465     THR D   616                                                      
REMARK 465     GLU D   617                                                      
REMARK 465     LEU D   618                                                      
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   O5   NAG C   703     O4   NAG C   704              1.74            
REMARK 500   CD2  LEU D   294     CG2  VAL D   295              1.79            
REMARK 500   O5   NAG A   703     O4   NAG A   704              1.86            
REMARK 500   OH   TYR B   355     O1   DF0 B   705              1.96            
REMARK 500   O    LEU C   123     NH2  ARG C   469              2.02            
REMARK 500   O5   NAG D   702     O4   NAG D   703              2.02            
REMARK 500   O5   NAG B   702     O4   NAG B   703              2.02            
REMARK 500   O    LEU B   123     NH2  ARG B   469              2.06            
REMARK 500   O    LEU A   123     NH2  ARG A   469              2.06            
REMARK 500   O    LEU D   123     NH2  ARG D   469              2.08            
REMARK 500   C8'  BOG A   701     O    HOH A   831              2.11            
REMARK 500   O    PHE D   142     NH2  ARG D   376              2.12            
REMARK 500   NH2  ARG A   245     OE2  GLU A   326              2.14            
REMARK 500   NH1  ARG B   216     O7   NAG B   702              2.15            
REMARK 500   O    PHE B   142     NH2  ARG B   376              2.16            
REMARK 500   C1D  HEM D   704     O    HOH D   814              2.16            
REMARK 500   NH2  ARG C   245     OE2  GLU C   326              2.16            
REMARK 500   NH2  ARG D   245     OE2  GLU D   326              2.18            
REMARK 500   CG   GLU B   398     NE2  GLN B   421              2.18            
REMARK 500   O    PHE C   142     NH2  ARG C   376              2.18            
REMARK 500   ND1  HIS A   214     O    HOH A   829              2.19            
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    TYR B 134   CE1   TYR B 134   CZ     -0.095                       
REMARK 500    HIS C 351   CG    HIS C 351   CD2     0.061                       
REMARK 500    TYR D 136   CE1   TYR D 136   CZ     -0.096                       
REMARK 500    TYR D 147   CG    TYR D 147   CD2    -0.119                       
REMARK 500    TYR D 147   CG    TYR D 147   CD1    -0.117                       
REMARK 500    TYR D 147   CE1   TYR D 147   CZ     -0.146                       
REMARK 500    TYR D 147   CZ    TYR D 147   CE2    -0.108                       
REMARK 500    TYR D 348   CG    TYR D 348   CD2    -0.126                       
REMARK 500    TYR D 348   CG    TYR D 348   CD1    -0.097                       
REMARK 500    TYR D 348   CE1   TYR D 348   CZ     -0.137                       
REMARK 500    TYR D 348   CZ    TYR D 348   CE2    -0.090                       
REMARK 500    GLY D 574   C     GLY D 574   O      -0.121                       
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    ARG A 376   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 467   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B  43   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    LEU B 534   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG C  43   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    CYS D 575   N   -  CA  -  C   ANGL. DEV. = -16.5 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    THR A 129      -82.34   -113.42                                   
REMARK 500    ASP A 158       52.51   -102.83                                   
REMARK 500    ARG A 185      -63.53    -92.78                                   
REMARK 500    TRP A 387       43.13    -93.17                                   
REMARK 500    GLU A 398     -121.31     46.59                                   
REMARK 500    LEU A 494      -64.10    -95.65                                   
REMARK 500    CYS A 575       62.33     36.34                                   
REMARK 500    ARG B  60       14.97     58.19                                   
REMARK 500    THR B 129      -76.41   -118.37                                   
REMARK 500    PRO B 153      151.79    -47.45                                   
REMARK 500    ASP B 158       59.19    -98.95                                   
REMARK 500    MET B 163       39.08    -86.57                                   
REMARK 500    ARG B 185      -63.81    -97.34                                   
REMARK 500    GLU B 290        0.31    -64.56                                   
REMARK 500    TRP B 387       53.36    -95.40                                   
REMARK 500    GLU B 398     -119.29     48.39                                   
REMARK 500    LEU B 494      -63.09   -100.91                                   
REMARK 500    CYS B 575       59.41     35.28                                   
REMARK 500    ARG C  60       16.09     59.37                                   
REMARK 500    THR C 129      -82.12   -116.49                                   
REMARK 500    ASP C 158       54.45    -99.50                                   
REMARK 500    ARG C 185      -72.99    -97.72                                   
REMARK 500    TRP C 387       47.10    -97.71                                   
REMARK 500    ILE C 397      -99.55    -88.97                                   
REMARK 500    GLU C 398      -93.32    -90.91                                   
REMARK 500    TYR C 409       27.69     42.65                                   
REMARK 500    LEU C 494      -61.73    -94.58                                   
REMARK 500    CYS C 575       59.90     34.87                                   
REMARK 500    ARG D  60       11.83     59.46                                   
REMARK 500    THR D 129      -75.99   -125.65                                   
REMARK 500    ASP D 158       54.43   -101.09                                   
REMARK 500    ARG D 185      -63.80    -91.76                                   
REMARK 500    VAL D 287      -60.35   -106.30                                   
REMARK 500    TRP D 387       49.55    -89.43                                   
REMARK 500    GLU D 398     -119.37     50.07                                   
REMARK 500    LEU D 494      -60.64   -102.28                                   
REMARK 500    CYS D 575       68.78   -169.78                                   
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 B 704  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 HEM B 704   NA  109.5                                              
REMARK 620 3 HEM B 704   NB   98.9  83.5                                        
REMARK 620 4 HEM B 704   NC  111.4 139.1  87.7                                  
REMARK 620 5 HEM B 704   ND  104.2  85.5 156.7  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 704  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 388   NE2                                                    
REMARK 620 2 HEM D 704   NA  113.0                                              
REMARK 620 3 HEM D 704   NB   95.3  83.3                                        
REMARK 620 4 HEM D 704   NC  108.5 138.1  87.8                                  
REMARK 620 5 HEM D 704   ND  107.9  86.6 156.8  85.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 705  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 388   NE2                                                    
REMARK 620 2 HEM C 705   NA  107.0                                              
REMARK 620 3 HEM C 705   NB  102.3  83.3                                        
REMARK 620 4 HEM C 705   NC  115.3 137.7  87.0                                  
REMARK 620 5 HEM C 705   ND  100.0  86.5 157.3  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 705  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 705   NA  107.3                                              
REMARK 620 3 HEM A 705   NB   98.9  83.2                                        
REMARK 620 4 HEM A 705   NC  113.3 139.3  88.3                                  
REMARK 620 5 HEM A 705   ND  104.9  86.2 155.9  85.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DF0 A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DF0 B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DF0 C 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DF0 D 705                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RR3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NT1   RELATED DB: PDB                                   
DBREF  4FM5 A   15   618  UNP    Q05769   PGH2_MOUSE       1    604             
DBREF  4FM5 B   15   618  UNP    Q05769   PGH2_MOUSE       1    604             
DBREF  4FM5 C   15   618  UNP    Q05769   PGH2_MOUSE       1    604             
DBREF  4FM5 D   15   618  UNP    Q05769   PGH2_MOUSE       1    604             
SEQRES   1 A  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 A  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS          
SEQRES   3 A  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN          
SEQRES   4 A  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU          
SEQRES   5 A  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU          
SEQRES   6 A  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU          
SEQRES   7 A  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE          
SEQRES   8 A  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR          
SEQRES   9 A  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN          
SEQRES  10 A  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN          
SEQRES  11 A  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP          
SEQRES  12 A  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU          
SEQRES  13 A  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU          
SEQRES  14 A  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET          
SEQRES  15 A  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE          
SEQRES  16 A  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG          
SEQRES  17 A  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY          
SEQRES  18 A  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS          
SEQRES  19 A  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL          
SEQRES  20 A  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE          
SEQRES  21 A  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL          
SEQRES  22 A  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET          
SEQRES  23 A  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS          
SEQRES  24 A  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU          
SEQRES  25 A  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU          
SEQRES  26 A  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU          
SEQRES  27 A  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU          
SEQRES  28 A  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA          
SEQRES  29 A  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU          
SEQRES  30 A  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE          
SEQRES  31 A  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS          
SEQRES  32 A  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE          
SEQRES  33 A  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA          
SEQRES  34 A  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG          
SEQRES  35 A  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG          
SEQRES  36 A  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR          
SEQRES  37 A  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR          
SEQRES  38 A  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU          
SEQRES  39 A  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR          
SEQRES  40 A  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU          
SEQRES  41 A  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO          
SEQRES  42 A  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN          
SEQRES  43 A  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS          
SEQRES  44 A  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN          
SEQRES  45 A  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS          
SEQRES  46 A  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS          
SEQRES  47 A  604  ARG ARG SER THR GLU LEU                                      
SEQRES   1 B  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 B  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS          
SEQRES   3 B  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN          
SEQRES   4 B  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU          
SEQRES   5 B  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU          
SEQRES   6 B  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU          
SEQRES   7 B  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE          
SEQRES   8 B  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR          
SEQRES   9 B  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN          
SEQRES  10 B  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN          
SEQRES  11 B  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP          
SEQRES  12 B  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU          
SEQRES  13 B  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU          
SEQRES  14 B  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET          
SEQRES  15 B  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE          
SEQRES  16 B  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG          
SEQRES  17 B  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY          
SEQRES  18 B  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS          
SEQRES  19 B  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL          
SEQRES  20 B  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE          
SEQRES  21 B  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL          
SEQRES  22 B  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET          
SEQRES  23 B  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS          
SEQRES  24 B  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU          
SEQRES  25 B  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU          
SEQRES  26 B  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU          
SEQRES  27 B  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU          
SEQRES  28 B  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA          
SEQRES  29 B  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU          
SEQRES  30 B  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE          
SEQRES  31 B  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS          
SEQRES  32 B  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE          
SEQRES  33 B  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA          
SEQRES  34 B  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG          
SEQRES  35 B  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG          
SEQRES  36 B  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR          
SEQRES  37 B  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR          
SEQRES  38 B  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU          
SEQRES  39 B  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR          
SEQRES  40 B  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU          
SEQRES  41 B  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO          
SEQRES  42 B  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN          
SEQRES  43 B  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS          
SEQRES  44 B  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN          
SEQRES  45 B  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS          
SEQRES  46 B  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS          
SEQRES  47 B  604  ARG ARG SER THR GLU LEU                                      
SEQRES   1 C  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 C  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS          
SEQRES   3 C  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN          
SEQRES   4 C  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU          
SEQRES   5 C  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU          
SEQRES   6 C  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU          
SEQRES   7 C  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE          
SEQRES   8 C  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR          
SEQRES   9 C  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN          
SEQRES  10 C  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN          
SEQRES  11 C  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP          
SEQRES  12 C  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU          
SEQRES  13 C  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU          
SEQRES  14 C  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET          
SEQRES  15 C  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE          
SEQRES  16 C  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG          
SEQRES  17 C  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY          
SEQRES  18 C  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS          
SEQRES  19 C  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL          
SEQRES  20 C  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE          
SEQRES  21 C  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL          
SEQRES  22 C  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET          
SEQRES  23 C  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS          
SEQRES  24 C  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU          
SEQRES  25 C  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU          
SEQRES  26 C  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU          
SEQRES  27 C  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU          
SEQRES  28 C  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA          
SEQRES  29 C  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU          
SEQRES  30 C  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE          
SEQRES  31 C  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS          
SEQRES  32 C  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE          
SEQRES  33 C  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA          
SEQRES  34 C  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG          
SEQRES  35 C  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG          
SEQRES  36 C  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR          
SEQRES  37 C  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR          
SEQRES  38 C  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU          
SEQRES  39 C  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR          
SEQRES  40 C  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU          
SEQRES  41 C  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO          
SEQRES  42 C  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN          
SEQRES  43 C  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS          
SEQRES  44 C  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN          
SEQRES  45 C  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS          
SEQRES  46 C  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS          
SEQRES  47 C  604  ARG ARG SER THR GLU LEU                                      
SEQRES   1 D  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 D  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS          
SEQRES   3 D  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN          
SEQRES   4 D  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU          
SEQRES   5 D  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU          
SEQRES   6 D  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU          
SEQRES   7 D  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE          
SEQRES   8 D  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR          
SEQRES   9 D  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN          
SEQRES  10 D  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN          
SEQRES  11 D  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP          
SEQRES  12 D  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU          
SEQRES  13 D  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU          
SEQRES  14 D  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET          
SEQRES  15 D  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE          
SEQRES  16 D  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG          
SEQRES  17 D  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY          
SEQRES  18 D  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS          
SEQRES  19 D  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL          
SEQRES  20 D  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE          
SEQRES  21 D  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL          
SEQRES  22 D  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET          
SEQRES  23 D  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS          
SEQRES  24 D  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU          
SEQRES  25 D  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU          
SEQRES  26 D  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU          
SEQRES  27 D  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU          
SEQRES  28 D  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA          
SEQRES  29 D  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU          
SEQRES  30 D  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE          
SEQRES  31 D  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS          
SEQRES  32 D  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE          
SEQRES  33 D  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA          
SEQRES  34 D  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG          
SEQRES  35 D  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG          
SEQRES  36 D  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR          
SEQRES  37 D  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR          
SEQRES  38 D  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU          
SEQRES  39 D  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR          
SEQRES  40 D  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU          
SEQRES  41 D  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO          
SEQRES  42 D  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN          
SEQRES  43 D  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS          
SEQRES  44 D  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN          
SEQRES  45 D  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS          
SEQRES  46 D  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS          
SEQRES  47 D  604  ARG ARG SER THR GLU LEU                                      
MODRES 4FM5 ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4FM5 ASN D  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4FM5 ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4FM5 ASN C  144  ASN  GLYCOSYLATION SITE                                 
HET    BOG  A 701      20                                                       
HET    BOG  A 702      20                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    HEM  A 705      43                                                       
HET    DF0  A 706      17                                                       
HET    BOG  B 701      20                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    HEM  B 704      43                                                       
HET    DF0  B 705      17                                                       
HET    BOG  C 701      20                                                       
HET    BOG  C 702      20                                                       
HET    NAG  C 703      14                                                       
HET    NAG  C 704      14                                                       
HET    HEM  C 705      43                                                       
HET    DF0  C 706      17                                                       
HET    BOG  D 701      20                                                       
HET    NAG  D 702      14                                                       
HET    NAG  D 703      14                                                       
HET    HEM  D 704      43                                                       
HET    DF0  D 705      17                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     DF0 (2-FLUOROBIPHENYL-4-YL)ACETIC ACID                               
HETSYN     HEM HEME                                                             
HETSYN     DF0 DES-METHYLFLURBIPROFEN                                           
FORMUL   5  BOG    6(C14 H28 O6)                                                
FORMUL   7  NAG    8(C8 H15 N O6)                                               
FORMUL   8  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   9  DF0    4(C14 H11 F O2)                                              
FORMUL  23  HOH   *186(H2 O)                                                    
HELIX    1   1 GLU A   72  LYS A   82  1                                  11    
HELIX    2   2 THR A   84  HIS A   94  1                                  11    
HELIX    3   3 PHE A   95  ASN A  103  1                                   9    
HELIX    4   4 ILE A  105  TYR A  122  1                                  18    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  ARG A  245  1                                   9    
HELIX   10  10 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 PRO A  280  GLN A  284  5                                   5    
HELIX   12  12 VAL A  291  LEU A  294  5                                   4    
HELIX   13  13 VAL A  295  HIS A  320  1                                  26    
HELIX   14  14 GLY A  324  ASP A  347  1                                  24    
HELIX   15  15 ASP A  347  GLY A  354  1                                   8    
HELIX   16  16 ASP A  362  PHE A  367  5                                   6    
HELIX   17  17 ALA A  378  TYR A  385  1                                   8    
HELIX   18  18 HIS A  386  LEU A  391  5                                   6    
HELIX   19  19 SER A  403  LEU A  408  1                                   6    
HELIX   20  20 ASN A  411  GLN A  429  1                                  19    
HELIX   21  21 PRO A  441  ALA A  443  5                                   3    
HELIX   22  22 VAL A  444  MET A  458  1                                  15    
HELIX   23  23 SER A  462  PHE A  470  1                                   9    
HELIX   24  24 SER A  477  GLY A  483  1                                   7    
HELIX   25  25 LYS A  485  TYR A  495  1                                  11    
HELIX   26  26 ASP A  497  MET A  501  5                                   5    
HELIX   27  27 GLU A  502  GLU A  510  1                                   9    
HELIX   28  28 GLY A  519  GLY A  536  1                                  18    
HELIX   29  29 ASN A  537  SER A  541  5                                   5    
HELIX   30  30 LYS A  546  GLY A  551  5                                   6    
HELIX   31  31 GLY A  552  THR A  561  1                                  10    
HELIX   32  32 SER A  563  ASN A  570  1                                   8    
HELIX   33  33 GLU B   72  LYS B   82  1                                  11    
HELIX   34  34 THR B   84  THR B   93  1                                  10    
HELIX   35  35 PHE B   95  ASN B  103  1                                   9    
HELIX   36  36 ILE B  105  TYR B  122  1                                  18    
HELIX   37  37 SER B  138  ASN B  144  1                                   7    
HELIX   38  38 ASP B  173  LEU B  182  1                                  10    
HELIX   39  39 ASN B  195  HIS B  207  1                                  13    
HELIX   40  40 LEU B  230  GLY B  235  1                                   6    
HELIX   41  41 THR B  237  ARG B  245  1                                   9    
HELIX   42  42 THR B  265  GLN B  270  1                                   6    
HELIX   43  43 VAL B  295  HIS B  320  1                                  26    
HELIX   44  44 GLY B  324  ASP B  347  1                                  24    
HELIX   45  45 ASP B  347  GLY B  354  1                                   8    
HELIX   46  46 ASP B  362  PHE B  367  5                                   6    
HELIX   47  47 ALA B  378  TYR B  385  1                                   8    
HELIX   48  48 HIS B  386  LEU B  391  5                                   6    
HELIX   49  49 SER B  403  LEU B  408  1                                   6    
HELIX   50  50 ASN B  411  GLY B  418  1                                   8    
HELIX   51  51 GLY B  418  GLN B  429  1                                  12    
HELIX   52  52 PRO B  441  ALA B  443  5                                   3    
HELIX   53  53 VAL B  444  MET B  458  1                                  15    
HELIX   54  54 SER B  462  PHE B  470  1                                   9    
HELIX   55  55 SER B  477  GLY B  483  1                                   7    
HELIX   56  56 LYS B  485  TYR B  495  1                                  11    
HELIX   57  57 ASP B  497  MET B  501  5                                   5    
HELIX   58  58 GLU B  502  GLU B  510  1                                   9    
HELIX   59  59 GLY B  519  GLY B  536  1                                  18    
HELIX   60  60 ASN B  537  SER B  541  5                                   5    
HELIX   61  61 LYS B  546  GLY B  551  5                                   6    
HELIX   62  62 GLY B  552  THR B  561  1                                  10    
HELIX   63  63 SER B  563  ASN B  570  1                                   8    
HELIX   64  64 GLU C   72  LYS C   82  1                                  11    
HELIX   65  65 THR C   84  HIS C   94  1                                  11    
HELIX   66  66 PHE C   95  ASN C  103  1                                   9    
HELIX   67  67 ILE C  105  TYR C  122  1                                  18    
HELIX   68  68 SER C  138  ASN C  144  1                                   7    
HELIX   69  69 ASP C  173  LEU C  182  1                                  10    
HELIX   70  70 ASN C  195  HIS C  207  1                                  13    
HELIX   71  71 LEU C  230  GLY C  235  1                                   6    
HELIX   72  72 THR C  237  ARG C  245  1                                   9    
HELIX   73  73 THR C  265  GLN C  270  1                                   6    
HELIX   74  74 VAL C  295  HIS C  320  1                                  26    
HELIX   75  75 GLY C  324  ASP C  347  1                                  24    
HELIX   76  76 ASP C  347  GLY C  354  1                                   8    
HELIX   77  77 ASP C  362  PHE C  367  5                                   6    
HELIX   78  78 ALA C  378  TYR C  385  1                                   8    
HELIX   79  79 HIS C  386  LEU C  391  5                                   6    
HELIX   80  80 SER C  403  LEU C  408  1                                   6    
HELIX   81  81 ASN C  411  GLN C  429  1                                  19    
HELIX   82  82 PRO C  441  ALA C  443  5                                   3    
HELIX   83  83 VAL C  444  MET C  458  1                                  15    
HELIX   84  84 SER C  462  PHE C  470  1                                   9    
HELIX   85  85 SER C  477  GLY C  483  1                                   7    
HELIX   86  86 LYS C  485  TYR C  495  1                                  11    
HELIX   87  87 ASP C  497  MET C  501  5                                   5    
HELIX   88  88 GLU C  502  GLU C  510  1                                   9    
HELIX   89  89 GLY C  519  ASN C  537  1                                  19    
HELIX   90  90 PRO C  538  SER C  541  5                                   4    
HELIX   91  91 LYS C  546  GLY C  551  5                                   6    
HELIX   92  92 GLY C  552  THR C  561  1                                  10    
HELIX   93  93 SER C  563  ASN C  570  1                                   8    
HELIX   94  94 GLU D   72  LYS D   82  1                                  11    
HELIX   95  95 THR D   84  HIS D   94  1                                  11    
HELIX   96  96 PHE D   95  ASN D  103  1                                   9    
HELIX   97  97 ILE D  105  TYR D  122  1                                  18    
HELIX   98  98 SER D  138  ASN D  144  1                                   7    
HELIX   99  99 ASP D  173  LEU D  182  1                                  10    
HELIX  100 100 ASN D  195  HIS D  207  1                                  13    
HELIX  101 101 LEU D  230  GLY D  235  1                                   6    
HELIX  102 102 THR D  237  ARG D  245  1                                   9    
HELIX  103 103 THR D  265  GLN D  270  1                                   6    
HELIX  104 104 VAL D  291  LEU D  294  5                                   4    
HELIX  105 105 VAL D  295  HIS D  320  1                                  26    
HELIX  106 106 GLY D  324  ASP D  347  1                                  24    
HELIX  107 107 ASP D  347  GLY D  354  1                                   8    
HELIX  108 108 ASP D  362  PHE D  367  5                                   6    
HELIX  109 109 ALA D  378  TYR D  385  1                                   8    
HELIX  110 110 HIS D  386  LEU D  391  5                                   6    
HELIX  111 111 SER D  403  LEU D  408  1                                   6    
HELIX  112 112 ASN D  411  GLN D  429  1                                  19    
HELIX  113 113 PRO D  441  ALA D  443  5                                   3    
HELIX  114 114 VAL D  444  MET D  458  1                                  15    
HELIX  115 115 SER D  462  PHE D  470  1                                   9    
HELIX  116 116 SER D  477  GLY D  483  1                                   7    
HELIX  117 117 LYS D  485  ALA D  493  1                                   9    
HELIX  118 118 ASP D  497  MET D  501  5                                   5    
HELIX  119 119 GLU D  502  GLU D  510  1                                   9    
HELIX  120 120 GLY D  519  GLY D  536  1                                  18    
HELIX  121 121 ASN D  537  SER D  541  5                                   5    
HELIX  122 122 LYS D  546  GLY D  551  5                                   6    
HELIX  123 123 GLY D  552  THR D  561  1                                  10    
HELIX  124 124 SER D  563  VAL D  572  1                                  10    
SHEET    1   A 2 GLU A  45  SER A  48  0                                        
SHEET    2   A 2 TYR A  54  ASP A  57 -1  O  LYS A  55   N  MET A  47           
SHEET    1   B 2 PHE A  63  TYR A  64  0                                        
SHEET    2   B 2 THR A  70  PRO A  71 -1  O  THR A  70   N  TYR A  64           
SHEET    1   C 2 GLN A 255  ILE A 257  0                                        
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255           
SHEET    1   D 2 GLU B  45  SER B  48  0                                        
SHEET    2   D 2 TYR B  54  ASP B  57 -1  O  ASP B  57   N  GLU B  45           
SHEET    1   E 2 PHE B  63  TYR B  64  0                                        
SHEET    2   E 2 THR B  70  PRO B  71 -1  O  THR B  70   N  TYR B  64           
SHEET    1   F 2 GLN B 255  ILE B 257  0                                        
SHEET    2   F 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   G 2 GLU C  45  SER C  48  0                                        
SHEET    2   G 2 TYR C  54  ASP C  57 -1  O  LYS C  55   N  MET C  47           
SHEET    1   H 2 PHE C  63  TYR C  64  0                                        
SHEET    2   H 2 THR C  70  PRO C  71 -1  O  THR C  70   N  TYR C  64           
SHEET    1   I 2 GLN C 255  ILE C 257  0                                        
SHEET    2   I 2 GLU C 260  TYR C 262 -1  O  GLU C 260   N  ILE C 257           
SHEET    1   J 2 GLU D  45  SER D  48  0                                        
SHEET    2   J 2 TYR D  54  ASP D  57 -1  O  LYS D  55   N  MET D  47           
SHEET    1   K 2 PHE D  63  TYR D  64  0                                        
SHEET    2   K 2 THR D  70  PRO D  71 -1  O  THR D  70   N  TYR D  64           
SHEET    1   L 2 GLN D 255  ILE D 257  0                                        
SHEET    2   L 2 GLU D 260  TYR D 262 -1  O  TYR D 262   N  GLN D 255           
SSBOND   1 CYS A   35    CYS A   46                          1555   1555  2.06  
SSBOND   2 CYS A   36    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A   40    CYS A   56                          1555   1555  2.03  
SSBOND   4 CYS A   58    CYS A   68                          1555   1555  2.05  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05  
SSBOND   6 CYS B   35    CYS B   46                          1555   1555  2.05  
SSBOND   7 CYS B   36    CYS B  159                          1555   1555  2.05  
SSBOND   8 CYS B   40    CYS B   56                          1555   1555  2.04  
SSBOND   9 CYS B   58    CYS B   68                          1555   1555  2.05  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.02  
SSBOND  11 CYS C   35    CYS C   46                          1555   1555  2.11  
SSBOND  12 CYS C   36    CYS C  159                          1555   1555  2.06  
SSBOND  13 CYS C   40    CYS C   56                          1555   1555  2.03  
SSBOND  14 CYS C   58    CYS C   68                          1555   1555  2.09  
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.05  
SSBOND  16 CYS D   35    CYS D   46                          1555   1555  2.07  
SSBOND  17 CYS D   36    CYS D  159                          1555   1555  2.04  
SSBOND  18 CYS D   40    CYS D   56                          1555   1555  2.04  
SSBOND  19 CYS D   58    CYS D   68                          1555   1555  2.07  
SSBOND  20 CYS D  569    CYS D  575                          1555   1555  2.05  
LINK         ND2 ASN B 144                 C1  NAG B 703     1555   1555  1.43  
LINK         ND2 ASN D 144                 C1  NAG D 703     1555   1555  1.45  
LINK         ND2 ASN A 144                 C1  NAG A 704     1555   1555  1.46  
LINK         ND2 ASN C 144                 C1  NAG C 704     1555   1555  1.76  
LINK         NE2 HIS B 388                FE   HEM B 704     1555   1555  1.97  
LINK         NE2 HIS D 388                FE   HEM D 704     1555   1555  2.00  
LINK         NE2 HIS C 388                FE   HEM C 705     1555   1555  2.03  
LINK         NE2 HIS A 388                FE   HEM A 705     1555   1555  2.16  
LINK         C1  NAG A 703                 O4  NAG A 704     1555   1555  1.20  
LINK         C1  NAG B 702                 O4  NAG B 703     1555   1555  1.46  
LINK         C1  NAG C 703                 O4  NAG C 704     1555   1555  1.47  
LINK         O4  NAG D 703                 C1  NAG D 702     1555   1555  1.43  
CISPEP   1 SER A  126    PRO A  127          0         2.31                     
CISPEP   2 SER B  126    PRO B  127          0         1.38                     
CISPEP   3 SER C  126    PRO C  127          0         4.10                     
CISPEP   4 SER D  126    PRO D  127          0         4.90                     
SITE     1 AC1 11 GLU A 179  ARG A 185  ARG A 438  GLU A 486                    
SITE     2 AC1 11 GLU A 490  HOH A 831  GLU B 179  ARG B 184                    
SITE     3 AC1 11 ARG B 185  ILE B 442  GLN B 445                               
SITE     1 AC2  5 PRO A  83  SER A 119  ARG A 120  LEU A 123                    
SITE     2 AC2  5 GLU A 524                                                     
SITE     1 AC3  3 ARG A 216  NAG A 704  LEU B 238                               
SITE     1 AC4  4 ASN A 144  TYR A 147  ARG A 216  NAG A 703                    
SITE     1 AC5 17 TYR A 148  ALA A 199  ALA A 202  GLN A 203                    
SITE     2 AC5 17 HIS A 207  PHE A 210  LYS A 211  THR A 212                    
SITE     3 AC5 17 HIS A 214  VAL A 295  ASN A 382  TYR A 385                    
SITE     4 AC5 17 HIS A 386  HIS A 388  LEU A 391  VAL A 447                    
SITE     5 AC5 17 ALA A 450                                                     
SITE     1 AC6  8 ARG A 120  VAL A 349  LEU A 352  TYR A 355                    
SITE     2 AC6  8 TYR A 385  TRP A 387  GLY A 526  ALA A 527                    
SITE     1 AC7  8 LYS B  82  PRO B  83  VAL B  88  LEU B  92                    
SITE     2 AC7  8 TYR B 115  SER B 119  ARG B 120  LEU B 123                    
SITE     1 AC8  5 LEU A 238  ASP A 239  ARG B 216  NAG B 703                    
SITE     2 AC8  5 HOH B 817                                                     
SITE     1 AC9  6 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 AC9  6 NAG B 702  HOH B 815                                          
SITE     1 BC1 15 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 BC1 15 LYS B 211  THR B 212  HIS B 214  VAL B 295                    
SITE     3 BC1 15 ASN B 382  TYR B 385  HIS B 386  HIS B 388                    
SITE     4 BC1 15 LEU B 391  LEU B 408  HOH B 832                               
SITE     1 BC2  9 ARG B 120  VAL B 349  LEU B 352  TYR B 355                    
SITE     2 BC2  9 TYR B 385  TRP B 387  GLY B 526  ALA B 527                    
SITE     3 BC2  9 SER B 530                                                     
SITE     1 BC3  9 GLU C 179  ARG C 185  ARG C 438  GLU C 486                    
SITE     2 BC3  9 GLU C 490  GLU D 179  ARG D 185  ILE D 442                    
SITE     3 BC3  9 GLN D 445                                                     
SITE     1 BC4  7 LYS C  82  PRO C  83  VAL C  88  ILE C 112                    
SITE     2 BC4  7 TYR C 115  SER C 119  HOH C 816                               
SITE     1 BC5  3 ARG C 216  PHE C 220  NAG C 704                               
SITE     1 BC6  6 ASN C 144  TYR C 147  ARG C 216  PHE C 220                    
SITE     2 BC6  6 NAG C 703  HOH C 815                                          
SITE     1 BC7 15 ALA C 199  ALA C 202  GLN C 203  PHE C 210                    
SITE     2 BC7 15 LYS C 211  THR C 212  VAL C 295  ASN C 382                    
SITE     3 BC7 15 TYR C 385  HIS C 386  HIS C 388  LEU C 391                    
SITE     4 BC7 15 LEU C 408  VAL C 447  GLN C 454                               
SITE     1 BC8  9 ARG C 120  VAL C 349  LEU C 352  TYR C 355                    
SITE     2 BC8  9 TYR C 385  TRP C 387  GLY C 526  ALA C 527                    
SITE     3 BC8  9 SER C 530                                                     
SITE     1 BC9  7 LYS D  82  PRO D  83  PRO D  85  VAL D  88                    
SITE     2 BC9  7 SER D 119  ARG D 120  LEU D 123                               
SITE     1 CC1  4 LEU C 238  ARG D 216  PHE D 220  NAG D 703                    
SITE     1 CC2  7 GLU D 140  ASN D 144  TYR D 147  ARG D 216                    
SITE     2 CC2  7 PHE D 220  NAG D 702  HOH D 815                               
SITE     1 CC3 14 GLN D 203  HIS D 207  PHE D 210  LYS D 211                    
SITE     2 CC3 14 THR D 212  HIS D 214  ASN D 382  TYR D 385                    
SITE     3 CC3 14 HIS D 386  HIS D 388  LEU D 391  PHE D 395                    
SITE     4 CC3 14 LEU D 408  HOH D 814                                          
SITE     1 CC4  9 ARG D 120  VAL D 349  LEU D 352  TYR D 355                    
SITE     2 CC4  9 TYR D 385  TRP D 387  GLY D 526  ALA D 527                    
SITE     3 CC4  9 SER D 530                                                     
CRYST1  181.632  135.696  125.150  90.00  90.00  90.00 P 21 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      0.005506  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007369  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007990        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.999611 -0.020025 -0.019422       82.99772    1                    
MTRIX2   2 -0.020518  0.056091  0.998215       33.57566    1                    
MTRIX3   2 -0.018900  0.998225 -0.056480      -33.75602    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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