GenomeNet

Database: PDB
Entry: 3RR3
LinkDB: 3RR3
Original site: 3RR3 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 28-APR-11   3RR3              
TITLE     STRUCTURE OF (R)-FLURBIPROFEN BOUND TO MCOX-2                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED           
COMPND   5 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-         
COMPND   6 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2    
COMPND   7 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE       
COMPND   8 SYNTHASE 2, TIS10 PROTEIN;                                           
COMPND   9 EC: 1.14.99.1;                                                       
COMPND  10 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    FLURBIPROFEN, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.C.DUGGAN,D.J.HERMANSON,J.MUSEE,J.J.PRUSAKIEWICZ,J.SCHEIB,           
AUTHOR   2 B.D.CARTER,S.BANERJEE,J.A.OATES,L.J.MARNETT                          
REVDAT   2   21-MAR-12 3RR3    1       JRNL                                     
REVDAT   1   09-NOV-11 3RR3    0                                                
JRNL        AUTH   K.C.DUGGAN,D.J.HERMANSON,J.MUSEE,J.J.PRUSAKIEWICZ,           
JRNL        AUTH 2 J.L.SCHEIB,B.D.CARTER,S.BANERJEE,J.A.OATES,L.J.MARNETT       
JRNL        TITL   (R)-PROFENS ARE SUBSTRATE-SELECTIVE INHIBITORS OF            
JRNL        TITL 2 ENDOCANNABINOID OXYGENATION BY COX-2.                        
JRNL        REF    NAT.CHEM.BIOL.                V.   7   803 2011              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   22053353                                                     
JRNL        DOI    10.1038/NCHEMBIO.663                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 62160                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3131                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9266 -  7.9158    0.93     3084   139  0.2373 0.2655        
REMARK   3     2  7.9158 -  6.3023    0.96     3030   161  0.1757 0.2298        
REMARK   3     3  6.3023 -  5.5113    0.95     2977   150  0.1857 0.2490        
REMARK   3     4  5.5113 -  5.0099    0.96     2961   162  0.1701 0.2158        
REMARK   3     5  5.0099 -  4.6522    0.96     2966   161  0.1465 0.1674        
REMARK   3     6  4.6522 -  4.3788    0.96     2939   163  0.1406 0.1980        
REMARK   3     7  4.3788 -  4.1601    0.95     2918   171  0.1461 0.1984        
REMARK   3     8  4.1601 -  3.9795    0.94     2847   162  0.1507 0.1813        
REMARK   3     9  3.9795 -  3.8266    0.92     2807   159  0.1544 0.1848        
REMARK   3    10  3.8266 -  3.6948    0.90     2758   136  0.1675 0.2097        
REMARK   3    11  3.6948 -  3.5795    0.90     2733   147  0.1813 0.2426        
REMARK   3    12  3.5795 -  3.4773    0.89     2706   151  0.2066 0.2769        
REMARK   3    13  3.4773 -  3.3859    0.87     2646   124  0.2190 0.2794        
REMARK   3    14  3.3859 -  3.3034    0.87     2613   140  0.2286 0.2724        
REMARK   3    15  3.3034 -  3.2284    0.85     2590   129  0.2399 0.2909        
REMARK   3    16  3.2284 -  3.1598    0.84     2531   145  0.2512 0.3442        
REMARK   3    17  3.1598 -  3.0966    0.82     2515   132  0.2589 0.3004        
REMARK   3    18  3.0966 -  3.0382    0.79     2393   112  0.2714 0.3174        
REMARK   3    19  3.0382 -  2.9840    0.79     2352   142  0.2615 0.3537        
REMARK   3    20  2.9840 -  2.9335    0.78     2367   107  0.2779 0.2948        
REMARK   3    21  2.9335 -  2.8862    0.76     2299   124  0.2938 0.3930        
REMARK   3    22  2.8862 -  2.8420    0.66     1999   114  0.3093 0.4076        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.24                                          
REMARK   3   B_SOL              : 1.87                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.380           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -22.02690                                            
REMARK   3    B22 (A**2) : 23.19750                                             
REMARK   3    B33 (A**2) : -1.17060                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          19044                                  
REMARK   3   ANGLE     :  1.232          25842                                  
REMARK   3   CHIRALITY :  0.082           2742                                  
REMARK   3   PLANARITY :  0.005           3296                                  
REMARK   3   DIHEDRAL  : 18.525           7070                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 33:583 )                
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 33:583 )                
REMARK   3     ATOM PAIRS NUMBER  : 4474                                        
REMARK   3     RMSD               : 0.041                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 33:583 )                
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 33:583 )                
REMARK   3     ATOM PAIRS NUMBER  : 4474                                        
REMARK   3     RMSD               : 0.034                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 33:583 )                
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 33:583 )                
REMARK   3     ATOM PAIRS NUMBER  : 4474                                        
REMARK   3     RMSD               : 0.040                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065274.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
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          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62162                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.842                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.925                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       90.30750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.27450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.30750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.27450            
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: 11830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 11810 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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     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     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     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     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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    THR D   578     O    HOH D   628              1.96            
REMARK 500   O4   NAG B   671     O5   NAG B     9              2.08            
REMARK 500   O    PHE A   142     NH2  ARG A   376              2.15            
REMARK 500   N    GLY C   219     O    HOH C   619              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  34      108.28    -47.78                                   
REMARK 500    ARG A  44        4.91     83.92                                   
REMARK 500    THR A  50       54.58   -119.58                                   
REMARK 500    TYR A 130      132.22     51.84                                   
REMARK 500    SER A 138      142.47     36.44                                   
REMARK 500    LEU A 183      154.53    -49.93                                   
REMARK 500    ARG A 185      -75.93    -89.37                                   
REMARK 500    ASN A 195     -162.75   -103.94                                   
REMARK 500    ALA A 286      -67.63    -96.31                                   
REMARK 500    VAL A 287      -42.31     59.30                                   
REMARK 500    ASP A 347      -53.74   -120.67                                   
REMARK 500    TRP A 387       47.81    -89.42                                   
REMARK 500    GLU A 398      117.03     -1.72                                   
REMARK 500    ASP A 399      -63.45    118.54                                   
REMARK 500    TYR A 409       34.98     38.57                                   
REMARK 500    PHE A 422      -69.10    125.92                                   
REMARK 500    SER A 496      -37.14     82.50                                   
REMARK 500    ASP A 499        2.14    -69.63                                   
REMARK 500    PRO A 514      -95.94    -22.46                                   
REMARK 500    ASP A 515       43.88    -98.75                                   
REMARK 500    ASN B  34      108.51    -48.63                                   
REMARK 500    ARG B  44        4.87     84.00                                   
REMARK 500    ARG B  61       14.81     59.61                                   
REMARK 500    TYR B 130      133.22     49.81                                   
REMARK 500    SER B 138      145.23     36.19                                   
REMARK 500    ARG B 185      -76.18    -88.88                                   
REMARK 500    ASN B 195     -165.00   -104.55                                   
REMARK 500    ALA B 286      -64.92    -95.27                                   
REMARK 500    VAL B 287      -40.90     56.72                                   
REMARK 500    TRP B 387       46.92    -90.76                                   
REMARK 500    GLU B 398      116.29     -4.73                                   
REMARK 500    ASP B 399      -60.94    120.34                                   
REMARK 500    TYR B 409       34.84     38.75                                   
REMARK 500    ASN B 410       76.40   -119.98                                   
REMARK 500    PHE B 422      -67.31    126.29                                   
REMARK 500    SER B 496      -37.29     80.24                                   
REMARK 500    ASP B 499        1.71    -69.08                                   
REMARK 500    PRO B 514      -97.04    -22.73                                   
REMARK 500    ASP B 515       44.61    -99.43                                   
REMARK 500    ASN C  34      109.83    -48.10                                   
REMARK 500    ARG C  44        3.80     83.41                                   
REMARK 500    ARG C  61       13.39     57.73                                   
REMARK 500    TYR C 130      133.75     52.39                                   
REMARK 500    SER C 138      143.05     35.72                                   
REMARK 500    PRO C 172      150.92    -48.80                                   
REMARK 500    ARG C 185      -76.11    -89.15                                   
REMARK 500    ASN C 195     -163.94   -106.16                                   
REMARK 500    ALA C 286      -64.63    -96.28                                   
REMARK 500    VAL C 287      -40.35     54.28                                   
REMARK 500    ASP C 347      -54.74   -121.41                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B 287        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  12        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A 593        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A 609        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH A 623        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A 624        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A 629        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 631        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH A 634        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A 638        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A 640        DISTANCE =  8.20 ANGSTROMS                       
REMARK 525    HOH B  30        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B 596        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH B 597        DISTANCE =  9.90 ANGSTROMS                       
REMARK 525    HOH B 601        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH B 603        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH B 604        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B 605        DISTANCE =  9.09 ANGSTROMS                       
REMARK 525    HOH B 621        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH B 643        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH C 592        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH C 596        DISTANCE =  8.01 ANGSTROMS                       
REMARK 525    HOH C 597        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH C 598        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH C 616        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH C 636        DISTANCE = 10.32 ANGSTROMS                       
REMARK 525    HOH C 638        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH D 602        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH D 605        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH D 606        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH D 636        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH D 643        DISTANCE =  8.60 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  661                                                       
REMARK 610     NAG A  671                                                       
REMARK 610     NAG A  681                                                       
REMARK 610     NAG A    9                                                       
REMARK 610     NAG B  661                                                       
REMARK 610     NAG B  671                                                       
REMARK 610     NAG B  681                                                       
REMARK 610     NAG B    9                                                       
REMARK 610     NAG C  661                                                       
REMARK 610     NAG C  671                                                       
REMARK 610     NAG C  681                                                       
REMARK 610     NAG C    9                                                       
REMARK 610     NAG D  661                                                       
REMARK 610     NAG D  671                                                       
REMARK 610     NAG D  681                                                       
REMARK 610     NAG D    9                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 682   NA   90.7                                              
REMARK 620 3 HEM A 682   NB   96.3  87.5                                        
REMARK 620 4 HEM A 682   NC   98.7 170.3  89.1                                  
REMARK 620 5 HEM A 682   ND   90.7  91.2 172.9  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 388   NE2                                                    
REMARK 620 2 HEM C 682   NA   90.4                                              
REMARK 620 3 HEM C 682   NB   97.2  87.5                                        
REMARK 620 4 HEM C 682   NC   95.5 173.8  89.9                                  
REMARK 620 5 HEM C 682   ND   87.7  92.6 175.1  89.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 388   NE2                                                    
REMARK 620 2 HEM D 682   NA   87.9                                              
REMARK 620 3 HEM D 682   NB   87.7  88.2                                        
REMARK 620 4 HEM D 682   NC   90.9 177.2  89.2                                  
REMARK 620 5 HEM D 682   ND   89.7  91.0 177.4  91.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 HEM B 682   NA   84.8                                              
REMARK 620 3 HEM B 682   NB   86.0  85.8                                        
REMARK 620 4 HEM B 682   NC   89.3 174.0  92.4                                  
REMARK 620 5 HEM B 682   ND   88.3  91.9 174.0  89.2                            
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 NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR C 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR D 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 9                   
DBREF  3RR3 A   33   591  UNP    Q05769   PGH2_MOUSE      18    577             
DBREF  3RR3 B   33   591  UNP    Q05769   PGH2_MOUSE      18    577             
DBREF  3RR3 C   33   591  UNP    Q05769   PGH2_MOUSE      18    577             
DBREF  3RR3 D   33   591  UNP    Q05769   PGH2_MOUSE      18    577             
SEQRES   1 A  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 A  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 A  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 A  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 A  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 A  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 A  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 A  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 A  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 A  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 A  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 A  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 A  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 A  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 A  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 A  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 A  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 A  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 A  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 A  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 A  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 A  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 A  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 A  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 A  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 A  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 A  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 A  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 A  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 A  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 A  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 A  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 A  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 A  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 A  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 A  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 A  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 A  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 A  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 A  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 A  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 A  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 A  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 A  560  ALA                                                          
SEQRES   1 B  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 B  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 B  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 B  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 B  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 B  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 B  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 B  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 B  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 B  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 B  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 B  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 B  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 B  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 B  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 B  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 B  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 B  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 B  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 B  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 B  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 B  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 B  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 B  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 B  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 B  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 B  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 B  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 B  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 B  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 B  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 B  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 B  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 B  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 B  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 B  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 B  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 B  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 B  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 B  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 B  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 B  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 B  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 B  560  ALA                                                          
SEQRES   1 C  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 C  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 C  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 C  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 C  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 C  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 C  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 C  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 C  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 C  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 C  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 C  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 C  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 C  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 C  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 C  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 C  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 C  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 C  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 C  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 C  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 C  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 C  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 C  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 C  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 C  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 C  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 C  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 C  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 C  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 C  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 C  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 C  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 C  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 C  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 C  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 C  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 C  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 C  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 C  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 C  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 C  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 C  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 C  560  ALA                                                          
SEQRES   1 D  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 D  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 D  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 D  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 D  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 D  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 D  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 D  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 D  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 D  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 D  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 D  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 D  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 D  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 D  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 D  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 D  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 D  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 D  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 D  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 D  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 D  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 D  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 D  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 D  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 D  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 D  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 D  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 D  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 D  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 D  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 D  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 D  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 D  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 D  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 D  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 D  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 D  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 D  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 D  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 D  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 D  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 D  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 D  560  ALA                                                          
HET    NAG  A 661      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 681      14                                                       
HET    HEM  A 682      43                                                       
HET    FLR  A 700      18                                                       
HET    BOG  A   3      20                                                       
HET    BOG  A   6      20                                                       
HET    NAG  A   9      14                                                       
HET    NAG  B 661      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 681      14                                                       
HET    HEM  B 682      43                                                       
HET    FLR  B 700      18                                                       
HET    BOG  B   3      20                                                       
HET    NAG  B   9      14                                                       
HET    NAG  C 661      14                                                       
HET    NAG  C 671      14                                                       
HET    NAG  C 681      14                                                       
HET    FLR  C 700      18                                                       
HET    HEM  C 682      43                                                       
HET    BOG  C   3      20                                                       
HET    BOG  C   6      20                                                       
HET    NAG  C   9      14                                                       
HET    NAG  D 661      14                                                       
HET    NAG  D 671      14                                                       
HET    FLR  D 700      18                                                       
HET    NAG  D 681      14                                                       
HET    HEM  D 682      43                                                       
HET    BOG  D   3      20                                                       
HET    NAG  D   9      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     FLR (2R)-2-(3-FLUORO-4-PHENYL-PHENYL)PROPANOIC ACID                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETSYN     HEM HEME                                                             
HETSYN     FLR FLURBIRPROFEN, R-FORM                                            
FORMUL   5  NAG    16(C8 H15 N O6)                                              
FORMUL   8  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   9  FLR    4(C15 H13 F O2)                                              
FORMUL  10  BOG    6(C14 H28 O6)                                                
FORMUL  35  HOH   *241(H2 O)                                                    
HELIX    1   1 GLU A   73  LYS A   83  1                                  11    
HELIX    2   2 THR A   85  HIS A   95  1                                  11    
HELIX    3   3 PHE A   96  ASN A  104  1                                   9    
HELIX    4   4 ILE A  105A 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  GLY A  418  1                                   8    
HELIX   21  21 LEU A  419  GLN A  429  1                                  11    
HELIX   22  22 PRO A  441  ALA A  443  5                                   3    
HELIX   23  23 VAL A  444  MET A  458  1                                  15    
HELIX   24  24 SER A  462  PHE A  470  1                                   9    
HELIX   25  25 SER A  477  GLY A  483  1                                   7    
HELIX   26  26 LYS A  485  TYR A  495  1                                  11    
HELIX   27  27 ASP A  497  MET A  501  5                                   5    
HELIX   28  28 GLU A  502  GLU A  510  1                                   9    
HELIX   29  29 GLY A  519  GLY A  536  1                                  18    
HELIX   30  30 ASN A  537  SER A  541  5                                   5    
HELIX   31  31 LYS A  546  GLY A  551  5                                   6    
HELIX   32  32 GLY A  552  THR A  561  1                                  10    
HELIX   33  33 SER A  563  VAL A  572  1                                  10    
HELIX   34  34 GLU B   73  LYS B   83  1                                  11    
HELIX   35  35 THR B   85  HIS B   95  1                                  11    
HELIX   36  36 PHE B   96  ASN B  104  1                                   9    
HELIX   37  37 ILE B  105A TYR B  122  1                                  18    
HELIX   38  38 SER B  138  ASN B  144  1                                   7    
HELIX   39  39 ASP B  173  LEU B  182  1                                  10    
HELIX   40  40 ASN B  195  HIS B  207  1                                  13    
HELIX   41  41 LEU B  230  GLY B  235  1                                   6    
HELIX   42  42 THR B  237  ARG B  245  1                                   9    
HELIX   43  43 THR B  265  GLN B  270  1                                   6    
HELIX   44  44 PRO B  280  GLN B  284  5                                   5    
HELIX   45  45 VAL B  291  LEU B  294  5                                   4    
HELIX   46  46 VAL B  295  HIS B  320  1                                  26    
HELIX   47  47 GLY B  324  ASP B  347  1                                  24    
HELIX   48  48 ASP B  347  GLY B  354  1                                   8    
HELIX   49  49 ASP B  362  PHE B  367  5                                   6    
HELIX   50  50 ALA B  378  TYR B  385  1                                   8    
HELIX   51  51 HIS B  386  LEU B  391  5                                   6    
HELIX   52  52 SER B  403  LEU B  408  1                                   6    
HELIX   53  53 ASN B  411  GLY B  418  1                                   8    
HELIX   54  54 LEU B  419  GLN B  429  1                                  11    
HELIX   55  55 PRO B  441  ALA B  443  5                                   3    
HELIX   56  56 VAL B  444  MET B  458  1                                  15    
HELIX   57  57 SER B  462  PHE B  470  1                                   9    
HELIX   58  58 SER B  477  GLY B  483  1                                   7    
HELIX   59  59 LYS B  485  TYR B  495  1                                  11    
HELIX   60  60 ASP B  497  MET B  501  5                                   5    
HELIX   61  61 GLU B  502  GLU B  510  1                                   9    
HELIX   62  62 GLY B  519  GLY B  536  1                                  18    
HELIX   63  63 ASN B  537  SER B  541  5                                   5    
HELIX   64  64 LYS B  546  GLY B  551  5                                   6    
HELIX   65  65 GLY B  552  THR B  561  1                                  10    
HELIX   66  66 SER B  563  VAL B  572  1                                  10    
HELIX   67  67 GLU C   73  LYS C   83  1                                  11    
HELIX   68  68 THR C   85  HIS C   95  1                                  11    
HELIX   69  69 PHE C   96  ASN C  104  1                                   9    
HELIX   70  70 ILE C  105A TYR C  122  1                                  18    
HELIX   71  71 SER C  138  ASN C  144  1                                   7    
HELIX   72  72 ASP C  173  LEU C  182  1                                  10    
HELIX   73  73 ASN C  195  HIS C  207  1                                  13    
HELIX   74  74 LEU C  230  GLY C  235  1                                   6    
HELIX   75  75 THR C  237  ARG C  245  1                                   9    
HELIX   76  76 THR C  265  GLN C  270  1                                   6    
HELIX   77  77 PRO C  280  GLN C  284  5                                   5    
HELIX   78  78 VAL C  291  LEU C  294  5                                   4    
HELIX   79  79 VAL C  295  HIS C  320  1                                  26    
HELIX   80  80 GLY C  324  ASP C  347  1                                  24    
HELIX   81  81 ASP C  347  GLY C  354  1                                   8    
HELIX   82  82 ASP C  362  PHE C  367  5                                   6    
HELIX   83  83 ALA C  378  TYR C  385  1                                   8    
HELIX   84  84 HIS C  386  LEU C  391  5                                   6    
HELIX   85  85 SER C  403  LEU C  408  1                                   6    
HELIX   86  86 ASN C  410  GLY C  418  1                                   9    
HELIX   87  87 LEU C  419  GLN C  429  1                                  11    
HELIX   88  88 PRO C  441  ALA C  443  5                                   3    
HELIX   89  89 VAL C  444  MET C  458  1                                  15    
HELIX   90  90 SER C  462  PHE C  470  1                                   9    
HELIX   91  91 SER C  477  GLY C  483  1                                   7    
HELIX   92  92 LYS C  485  TYR C  495  1                                  11    
HELIX   93  93 ASP C  497  MET C  501  5                                   5    
HELIX   94  94 GLU C  502  GLU C  510  1                                   9    
HELIX   95  95 GLY C  519  GLY C  536  1                                  18    
HELIX   96  96 ASN C  537  SER C  541  5                                   5    
HELIX   97  97 LYS C  546  GLY C  551  5                                   6    
HELIX   98  98 GLY C  552  THR C  561  1                                  10    
HELIX   99  99 SER C  563  VAL C  572  1                                  10    
HELIX  100 100 GLU D   73  LYS D   83  1                                  11    
HELIX  101 101 THR D   85  HIS D   95  1                                  11    
HELIX  102 102 PHE D   96  ASN D  104  1                                   9    
HELIX  103 103 ILE D  105A TYR D  122  1                                  18    
HELIX  104 104 SER D  138  ASN D  144  1                                   7    
HELIX  105 105 ASP D  173  LEU D  182  1                                  10    
HELIX  106 106 ASN D  195  HIS D  207  1                                  13    
HELIX  107 107 LEU D  230  GLY D  235  1                                   6    
HELIX  108 108 THR D  237  ARG D  245  1                                   9    
HELIX  109 109 THR D  265  GLN D  270  1                                   6    
HELIX  110 110 PRO D  280  GLN D  284  5                                   5    
HELIX  111 111 VAL D  291  LEU D  294  5                                   4    
HELIX  112 112 VAL D  295  HIS D  320  1                                  26    
HELIX  113 113 GLY D  324  ASP D  347  1                                  24    
HELIX  114 114 ASP D  347  GLY D  354  1                                   8    
HELIX  115 115 ASP D  362  PHE D  367  5                                   6    
HELIX  116 116 ALA D  378  TYR D  385  1                                   8    
HELIX  117 117 HIS D  386  LEU D  391  5                                   6    
HELIX  118 118 SER D  403  LEU D  408  1                                   6    
HELIX  119 119 ASN D  410  GLY D  418  1                                   9    
HELIX  120 120 LEU D  419  GLN D  429  1                                  11    
HELIX  121 121 PRO D  441  ALA D  443  5                                   3    
HELIX  122 122 VAL D  444  MET D  458  1                                  15    
HELIX  123 123 SER D  462  PHE D  470  1                                   9    
HELIX  124 124 SER D  477  GLY D  483  1                                   7    
HELIX  125 125 LYS D  485  TYR D  495  1                                  11    
HELIX  126 126 ASP D  497  MET D  501  5                                   5    
HELIX  127 127 GLU D  502  GLU D  510  1                                   9    
HELIX  128 128 GLY D  519  GLY D  536  1                                  18    
HELIX  129 129 ASN D  537  SER D  541  5                                   5    
HELIX  130 130 LYS D  546  GLY D  551  5                                   6    
HELIX  131 131 GLY D  552  THR D  561  1                                  10    
HELIX  132 132 SER D  563  VAL D  572  1                                  10    
SHEET    1   A 2 GLU A  46  SER A  49  0                                        
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46           
SHEET    1   B 2 PHE A  64  TYR A  65  0                                        
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65           
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 PHE A 395  ILE A 397  0                                        
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   E 2 GLU B  46  SER B  49  0                                        
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46           
SHEET    1   F 2 PHE B  64  TYR B  65  0                                        
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   G 2 GLN B 255  ILE B 257  0                                        
SHEET    2   G 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   H 2 PHE B 395  ILE B 397  0                                        
SHEET    2   H 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SHEET    1   I 2 GLU C  46  SER C  49  0                                        
SHEET    2   I 2 TYR C  55  ASP C  58 -1  O  ASP C  58   N  GLU C  46           
SHEET    1   J 2 PHE C  64  TYR C  65  0                                        
SHEET    2   J 2 THR C  71  PRO C  72 -1  O  THR C  71   N  TYR C  65           
SHEET    1   K 2 GLN C 255  ILE C 257  0                                        
SHEET    2   K 2 GLU C 260  TYR C 262 -1  O  TYR C 262   N  GLN C 255           
SHEET    1   L 2 PHE C 395  ILE C 397  0                                        
SHEET    2   L 2 GLN C 400  TYR C 402 -1  O  TYR C 402   N  PHE C 395           
SHEET    1   M 2 GLU D  46  SER D  49  0                                        
SHEET    2   M 2 TYR D  55  ASP D  58 -1  O  ASP D  58   N  GLU D  46           
SHEET    1   N 2 PHE D  64  TYR D  65  0                                        
SHEET    2   N 2 THR D  71  PRO D  72 -1  O  THR D  71   N  TYR D  65           
SHEET    1   O 2 GLN D 255  ILE D 257  0                                        
SHEET    2   O 2 GLU D 260  TYR D 262 -1  O  TYR D 262   N  GLN D 255           
SHEET    1   P 2 PHE D 395  ILE D 397  0                                        
SHEET    2   P 2 GLN D 400  TYR D 402 -1  O  TYR D 402   N  PHE D 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.04  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.06  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.06  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05  
SSBOND  11 CYS C   36    CYS C   47                          1555   1555  2.04  
SSBOND  12 CYS C   37    CYS C  159                          1555   1555  2.03  
SSBOND  13 CYS C   41    CYS C   57                          1555   1555  2.04  
SSBOND  14 CYS C   59    CYS C   69                          1555   1555  2.05  
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.05  
SSBOND  16 CYS D   36    CYS D   47                          1555   1555  2.04  
SSBOND  17 CYS D   37    CYS D  159                          1555   1555  2.03  
SSBOND  18 CYS D   41    CYS D   57                          1555   1555  2.03  
SSBOND  19 CYS D   59    CYS D   69                          1555   1555  2.04  
SSBOND  20 CYS D  569    CYS D  575                          1555   1555  2.02  
LINK         NE2 HIS A 388                FE   HEM A 682     1555   1555  2.41  
LINK         NE2 HIS C 388                FE   HEM C 682     1555   1555  2.50  
LINK         NE2 HIS D 388                FE   HEM D 682     1555   1555  2.53  
LINK         NE2 HIS B 388                FE   HEM B 682     1555   1555  2.58  
CISPEP   1 SER A  126    PRO A  127          0         5.82                     
CISPEP   2 SER B  126    PRO B  127          0         7.00                     
CISPEP   3 SER C  126    PRO C  127          0         7.02                     
CISPEP   4 SER D  126    PRO D  127          0         6.37                     
SITE     1 AC1  5 HOH A   4  TYR A  55  GLU A  67  ASN A  68                    
SITE     2 AC1  5 HOH A 592                                                     
SITE     1 AC2  5 NAG A   9  GLU A 140  ASN A 144  TYR A 147                    
SITE     2 AC2  5 ARG A 216                                                     
SITE     1 AC3  3 GLN A 406  ASN A 410  SER A 412                               
SITE     1 AC4 14 TYR A 148  ALA A 199  GLN A 203  HIS A 207                    
SITE     2 AC4 14 PHE A 210  LYS A 211  THR A 212  HIS A 214                    
SITE     3 AC4 14 VAL A 295  ASN A 382  TYR A 385  HIS A 386                    
SITE     4 AC4 14 HIS A 388  LEU A 391                                          
SITE     1 AC5 11 ARG A 120  VAL A 349  LEU A 352  TYR A 355                    
SITE     2 AC5 11 LEU A 359  TYR A 385  TRP A 387  VAL A 523                    
SITE     3 AC5 11 GLY A 526  ALA A 527  SER A 530                               
SITE     1 AC6 12 GLU A 179  ARG A 184  ARG A 185  ARG A 438                    
SITE     2 AC6 12 GLU A 486  GLU A 490  GLU B 179  LEU B 183                    
SITE     3 AC6 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445                    
SITE     1 AC7  6 PRO A  84  TYR A 115  SER A 119  ARG A 120                    
SITE     2 AC7  6 HOH A 619  HOH A 620                                          
SITE     1 AC8  2 ARG A 216  NAG A 671                                          
SITE     1 AC9  4 TYR B  55  GLU B  67  ASN B  68  HOH B 599                    
SITE     1 BC1  6 NAG B   9  GLU B 140  ASN B 144  TYR B 147                    
SITE     2 BC1  6 ARG B 216  HOH B 593                                          
SITE     1 BC2  3 ASN B 410  SER B 412  HOH B 634                               
SITE     1 BC3 12 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 BC3 12 THR B 212  HIS B 214  ASN B 382  TYR B 385                    
SITE     3 BC3 12 HIS B 386  HIS B 388  LEU B 391  VAL B 447                    
SITE     1 BC4 11 ARG B 120  VAL B 349  LEU B 352  TYR B 355                    
SITE     2 BC4 11 LEU B 359  TYR B 385  TRP B 387  VAL B 523                    
SITE     3 BC4 11 GLY B 526  ALA B 527  SER B 530                               
SITE     1 BC5  6 LYS B  83  PRO B  84  TYR B 115  SER B 119                    
SITE     2 BC5  6 ARG B 120  GLU B 524                                          
SITE     1 BC6  3 ARG B 216  HOH B 649  NAG B 671                               
SITE     1 BC7  8 SER C  38  PRO C  40  TYR C  55  GLU C  67                    
SITE     2 BC7  8 ASN C  68  HOH C 593  HOH C 594  HOH C 595                    
SITE     1 BC8  5 NAG C   9  GLU C 140  ASN C 144  TYR C 147                    
SITE     2 BC8  5 ARG C 216                                                     
SITE     1 BC9  4 GLN C 406  ASN C 410  SER C 412  HOH C 633                    
SITE     1 CC1 11 ARG C 120  VAL C 349  LEU C 352  TYR C 355                    
SITE     2 CC1 11 LEU C 359  TYR C 385  TRP C 387  VAL C 523                    
SITE     3 CC1 11 GLY C 526  ALA C 527  SER C 530                               
SITE     1 CC2 11 ALA C 199  ALA C 202  GLN C 203  HIS C 207                    
SITE     2 CC2 11 THR C 212  HIS C 214  VAL C 295  ASN C 382                    
SITE     3 CC2 11 HIS C 386  HIS C 388  LEU C 391                               
SITE     1 CC3 12 LYS C 180  LEU C 183  ARG C 184  ARG C 185                    
SITE     2 CC3 12 ARG C 438  ILE C 442  GLU C 486  GLU C 490                    
SITE     3 CC3 12 GLU D 179  ARG D 184  ARG D 185  ILE D 442                    
SITE     1 CC4  4 PRO C  84  TYR C 115  SER C 119  GLU C 524                    
SITE     1 CC5  3 ARG C 216  HOH C 637  NAG C 671                               
SITE     1 CC6  6 SER D  38  TYR D  55  GLU D  67  ASN D  68                    
SITE     2 CC6  6 HOH D 603  HOH D 640                                          
SITE     1 CC7  5 NAG D   9  GLU D 140  ASN D 144  TYR D 147                    
SITE     2 CC7  5 ARG D 216                                                     
SITE     1 CC8 11 VAL D 116  ARG D 120  VAL D 349  LEU D 352                    
SITE     2 CC8 11 TYR D 355  TYR D 385  TRP D 387  VAL D 523                    
SITE     3 CC8 11 GLY D 526  ALA D 527  SER D 530                               
SITE     1 CC9  3 ASN D 410  SER D 412  ILE D 413                               
SITE     1 DC1 13 ALA D 199  GLN D 203  HIS D 207  THR D 212                    
SITE     2 DC1 13 HIS D 214  ASN D 382  TYR D 385  HIS D 386                    
SITE     3 DC1 13 TRP D 387  HIS D 388  LEU D 391  VAL D 447                    
SITE     4 DC1 13 HOH D 642                                                     
SITE     1 DC2  7 LYS D  83  PRO D  84  TYR D 115  SER D 119                    
SITE     2 DC2  7 ARG D 120  LEU D 123  GLU D 524                               
SITE     1 DC3  2 ARG D 216  NAG D 671                                          
CRYST1  180.615  134.549  122.775  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      0.005537  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007432  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008145        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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