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Database: PDB
Entry: 3NTB
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Original site: 3NTB 
HEADER    OXIDOREDUCTASE                          03-JUL-10   3NTB              
TITLE     STRUCTURE OF 6-METHYLTHIO NAPROXEN ANALOG BOUND TO MCOX-2.            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2;                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 18-604, CATALYTIC DOMAIN;                     
COMPND   5 EC: 1.14.99.1;                                                       
COMPND   6 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: COX-2 PGHS-B, MCG_5001, PTGS2;                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROSTAGLANDIN H2 SYNTHASE, CYCLOOXYGEANSE-2, NAPROXEN ANALOG,         
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.C.DUGGAN,J.MUSEE,M.J.WALTERS,J.M.HARP,J.R.KIEFER,J.A.OATES,         
AUTHOR   2 L.J.MARNETT                                                          
REVDAT   2   17-NOV-10 3NTB    1       JRNL                                     
REVDAT   1   01-SEP-10 3NTB    0                                                
JRNL        AUTH   K.C.DUGGAN,M.J.WALTERS,J.MUSEE,J.M.HARP,J.R.KIEFER,          
JRNL        AUTH 2 J.A.OATES,L.J.MARNETT                                        
JRNL        TITL   MOLECULAR BASIS FOR CYCLOOXYGENASE INHIBITION BY THE         
JRNL        TITL 2 NON-STEROIDAL ANTI-INFLAMMATORY DRUG NAPROXEN.               
JRNL        REF    J.BIOL.CHEM.                  V. 285 34950 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20810665                                                     
JRNL        DOI    10.1074/JBC.M110.162982                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 121009                         
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 13517                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.27                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8277                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.35                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 903                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17887                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 640                                     
REMARK   3   SOLVENT ATOMS            : 1109                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.04000                                             
REMARK   3    B22 (A**2) : 3.93000                                              
REMARK   3    B33 (A**2) : 3.11000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.372         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.253         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.186         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.946        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19109 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25994 ; 0.923 ; 2.011       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2203 ; 4.350 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   895 ;35.776 ;24.101       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3102 ;12.967 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;12.904 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2765 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14532 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 11029 ; 0.127 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17924 ; 0.251 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8080 ; 0.476 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8070 ; 0.903 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    33        A   583                          
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0870  38.1550  -8.9610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3264 T22:   0.0387                                     
REMARK   3      T33:   0.0198 T12:  -0.0074                                     
REMARK   3      T13:  -0.0163 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4879 L22:   0.9510                                     
REMARK   3      L33:   1.1061 L12:   0.1895                                     
REMARK   3      L13:   0.3877 L23:   0.6038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0242 S12:   0.0091 S13:   0.2332                       
REMARK   3      S21:  -0.0238 S22:  -0.0921 S23:   0.1439                       
REMARK   3      S31:  -0.0117 S32:  -0.1470 S33:   0.1163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    33        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6540  45.8870  -2.4240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3175 T22:   0.1414                                     
REMARK   3      T33:   0.0372 T12:  -0.0237                                     
REMARK   3      T13:  -0.0057 T23:   0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4821 L22:   0.7908                                     
REMARK   3      L33:   1.2981 L12:   0.1648                                     
REMARK   3      L13:   0.0893 L23:   0.5717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:   0.2356 S13:   0.0606                       
REMARK   3      S21:  -0.0744 S22:   0.1062 S23:  -0.1175                       
REMARK   3      S31:  -0.0574 S32:   0.3778 S33:  -0.0647                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    33        C   583                          
REMARK   3    ORIGIN FOR THE GROUP (A): -67.3610  21.8430 -63.3420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3343 T22:   0.0595                                     
REMARK   3      T33:  -0.0034 T12:  -0.0059                                     
REMARK   3      T13:   0.0065 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2574 L22:   0.6018                                     
REMARK   3      L33:   1.0506 L12:   0.0152                                     
REMARK   3      L13:   0.0754 L23:  -0.4650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0154 S12:   0.1523 S13:  -0.0183                       
REMARK   3      S21:  -0.0366 S22:   0.0468 S23:   0.0667                       
REMARK   3      S31:   0.0111 S32:  -0.2437 S33:  -0.0314                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    33        D   583                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.8050  28.5340 -70.3040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3330 T22:   0.0180                                     
REMARK   3      T33:  -0.0064 T12:  -0.0064                                     
REMARK   3      T13:   0.0067 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3254 L22:   0.8668                                     
REMARK   3      L33:   0.8917 L12:   0.0627                                     
REMARK   3      L13:  -0.1776 L23:  -0.4364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0027 S12:   0.0535 S13:  -0.1311                       
REMARK   3      S21:  -0.0124 S22:  -0.0588 S23:  -0.1049                       
REMARK   3      S31:   0.0051 S32:   0.1291 S33:   0.0615                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3NTB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060253.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : CRYSTAL MONOCHROMATOR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136496                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.50900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MMP550, MGCL2, PH 8, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 291.15K                                   
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       90.59850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.11250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.59850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.11250            
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: 12500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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: 12360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     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     GLN B   583                                                      
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     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     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   ND2  ASN B   410     C2   NAG B   681              2.17            
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    ARG A  61       18.28     58.96                                   
REMARK 500    THR A 129      -89.69   -116.21                                   
REMARK 500    ARG A 185      -70.09    -88.27                                   
REMARK 500    ASP A 249       19.20     59.44                                   
REMARK 500    TRP A 387       52.97    -98.81                                   
REMARK 500    GLU A 398     -119.80     58.58                                   
REMARK 500    SER A 496      -46.75     73.56                                   
REMARK 500    CYS A 575       64.92     38.19                                   
REMARK 500    THR B 129      -87.88   -120.31                                   
REMARK 500    TRP B 387       54.34    -93.03                                   
REMARK 500    GLU B 398     -113.16     59.63                                   
REMARK 500    TYR B 409        6.84     50.27                                   
REMARK 500    ASN B 439       10.04   -142.30                                   
REMARK 500    SER B 496      -50.22     70.97                                   
REMARK 500    THR C 129      -93.90   -117.26                                   
REMARK 500    ARG C 185      -71.23    -97.62                                   
REMARK 500    HIS C 386       71.25    -69.71                                   
REMARK 500    TRP C 387       51.70    -91.06                                   
REMARK 500    GLU C 398     -117.83     56.03                                   
REMARK 500    TYR C 409        9.24     56.12                                   
REMARK 500    ASN C 410       77.02   -105.38                                   
REMARK 500    ASN C 439       11.43   -140.53                                   
REMARK 500    SER C 496      -50.53     71.00                                   
REMARK 500    THR D 129      -88.05   -117.56                                   
REMARK 500    ARG D 185      -76.64    -92.59                                   
REMARK 500    ASP D 347      -51.89   -127.62                                   
REMARK 500    TRP D 387       50.58    -96.93                                   
REMARK 500    GLU D 398     -117.17     57.12                                   
REMARK 500    ASN D 410       77.51   -119.67                                   
REMARK 500    SER D 496      -56.65     72.66                                   
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 C 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 388   NE2                                                    
REMARK 620 2 HEM C 619   NA   90.7                                              
REMARK 620 3 HEM C 619   NB   88.7  89.0                                        
REMARK 620 4 HEM C 619   NC   92.4 176.7  89.9                                  
REMARK 620 5 HEM C 619   ND   90.9  90.5 179.3  90.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 619   NA   90.7                                              
REMARK 620 3 HEM A 619   NB   92.7  89.0                                        
REMARK 620 4 HEM A 619   NC   91.8 177.3  89.9                                  
REMARK 620 5 HEM A 619   ND   86.8  90.7 179.4  90.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 388   NE2                                                    
REMARK 620 2 HEM D 619   NA   92.0                                              
REMARK 620 3 HEM D 619   NB   94.4  89.3                                        
REMARK 620 4 HEM D 619   NC   90.6 177.4  90.1                                  
REMARK 620 5 HEM D 619   ND   85.4  90.2 179.5  90.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 HEM B 619   NA   91.4                                              
REMARK 620 3 HEM B 619   NB   94.9  89.8                                        
REMARK 620 4 HEM B 619   NC   90.8 177.6  89.2                                  
REMARK 620 5 HEM B 619   ND   84.8  89.5 179.2  91.5                            
REMARK 620 6 HOH B  19   O   167.6  77.6  90.8 100.3  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N C 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N D 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 8                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PGH   RELATED DB: PDB                                   
REMARK 900 COX-2:FLURBIPROFEN                                                   
REMARK 900 RELATED ID: 1PXX   RELATED DB: PDB                                   
REMARK 900 COX-2:DICLOFENAC                                                     
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB                                   
REMARK 900 COX-1:FLURBIPROFEN                                                   
REMARK 900 RELATED ID: 3NT1   RELATED DB: PDB                                   
REMARK 900 COX-2:NAPROXEN                                                       
DBREF  3NTB A   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604             
DBREF  3NTB B   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604             
DBREF  3NTB C   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604             
DBREF  3NTB D   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604             
SEQRES   1 A  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 A  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 A  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 A  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 A  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 A  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 A  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 A  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 A  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 A  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 A  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 A  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 A  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 A  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 A  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 A  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 A  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 A  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 A  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 A  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 A  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 A  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 A  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 A  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 A  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 A  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 A  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 A  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 A  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 A  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 A  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 A  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 A  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 A  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 A  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 A  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 A  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 A  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 A  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 A  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 A  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 A  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 A  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 A  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 A  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 A  587  GLU LEU                                                      
SEQRES   1 B  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 B  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 B  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 B  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 B  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 B  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 B  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 B  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 B  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 B  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 B  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 B  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 B  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 B  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 B  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 B  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 B  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 B  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 B  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 B  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 B  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 B  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 B  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 B  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 B  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 B  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 B  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 B  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 B  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 B  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 B  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 B  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 B  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 B  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 B  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 B  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 B  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 B  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 B  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 B  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 B  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 B  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 B  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 B  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 B  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 B  587  GLU LEU                                                      
SEQRES   1 C  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 C  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 C  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 C  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 C  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 C  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 C  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 C  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 C  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 C  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 C  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 C  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 C  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 C  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 C  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 C  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 C  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 C  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 C  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 C  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 C  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 C  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 C  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 C  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 C  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 C  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 C  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 C  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 C  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 C  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 C  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 C  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 C  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 C  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 C  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 C  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 C  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 C  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 C  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 C  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 C  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 C  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 C  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 C  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 C  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 C  587  GLU LEU                                                      
SEQRES   1 D  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 D  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 D  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 D  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 D  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 D  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 D  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 D  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 D  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 D  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 D  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 D  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 D  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 D  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 D  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 D  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 D  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 D  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 D  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 D  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 D  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 D  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 D  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 D  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 D  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 D  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 D  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 D  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 D  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 D  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 D  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 D  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 D  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 D  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 D  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 D  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 D  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 D  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 D  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 D  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 D  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 D  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 D  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 D  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 D  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 D  587  GLU LEU                                                      
MODRES 3NTB ASN C  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN D  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN D   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN D  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN C   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3NTB ASN C  144  ASN  GLYCOSYLATION SITE                                 
HET    HEM  A 619      43                                                       
HET    NAG  A 661      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 672      14                                                       
HET    NAG  A 673      14                                                       
HET    NAG  A 681      14                                                       
HET    BOG  A 703      20                                                       
HET    T1N  A   3      17                                                       
HET    BOG  A   7      20                                                       
HET    HEM  B 619      43                                                       
HET    NAG  B 661      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 672      14                                                       
HET    NAG  B 673      14                                                       
HET    NAG  B 681      14                                                       
HET    T1N  B   1      17                                                       
HET    BOG  B   6      20                                                       
HET    HEM  C 619      43                                                       
HET    NAG  C 661      14                                                       
HET    NAG  C 671      14                                                       
HET    NAG  C 672      14                                                       
HET    NAG  C 673      14                                                       
HET    NAG  C 681      14                                                       
HET    T1N  C   2      17                                                       
HET    BOG  C   5      20                                                       
HET    HEM  D 619      43                                                       
HET    NAG  D 661      14                                                       
HET    NAG  D 671      14                                                       
HET    NAG  D 672      14                                                       
HET    NAG  D 673      14                                                       
HET    NAG  D 681      14                                                       
HET    BOG  D 703      20                                                       
HET    T1N  D   4      17                                                       
HET    BOG  D   8      20                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     T1N (2S)-2-[6-(METHYLSULFANYL)NAPHTHALEN-2-YL]PROPANOIC              
HETNAM   2 T1N  ACID                                                            
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  NAG    20(C8 H15 N O6)                                              
FORMUL   9  BOG    6(C14 H28 O6)                                                
FORMUL  10  T1N    4(C14 H14 O2 S)                                              
FORMUL  31  HOH   *1109(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  295  HIS A  320  1                                  26    
HELIX   13  13 GLY A  324  ASP A  347  1                                  24    
HELIX   14  14 ASP A  347  GLY A  354  1                                   8    
HELIX   15  15 ASP A  362  PHE A  367  5                                   6    
HELIX   16  16 ALA A  378  TYR A  385  1                                   8    
HELIX   17  17 TRP A  387  LEU A  391  5                                   5    
HELIX   18  18 SER A  403  LEU A  408  1                                   6    
HELIX   19  19 ASN A  411  GLN A  429  1                                  19    
HELIX   20  20 PRO A  441  ALA A  443  5                                   3    
HELIX   21  21 VAL A  444  MET A  458  1                                  15    
HELIX   22  22 SER A  462  PHE A  470  1                                   9    
HELIX   23  23 SER A  477  GLY A  483  1                                   7    
HELIX   24  24 LYS A  485  SER A  496  1                                  12    
HELIX   25  25 ASP A  497  MET A  501  5                                   5    
HELIX   26  26 GLU A  502  GLU A  510  1                                   9    
HELIX   27  27 GLY A  519  GLY A  536  1                                  18    
HELIX   28  28 ASN A  537  SER A  541  5                                   5    
HELIX   29  29 LYS A  546  GLY A  551  5                                   6    
HELIX   30  30 GLY A  552  THR A  561  1                                  10    
HELIX   31  31 SER A  563  VAL A  572  1                                  10    
HELIX   32  32 GLU B   73  LYS B   83  1                                  11    
HELIX   33  33 THR B   85  THR B   94  1                                  10    
HELIX   34  34 PHE B   96  ASN B  104  1                                   9    
HELIX   35  35 ILE B  105A TYR B  122  1                                  18    
HELIX   36  36 SER B  138  ASN B  144  1                                   7    
HELIX   37  37 ASP B  173  LEU B  182  1                                  10    
HELIX   38  38 ASN B  195  HIS B  207  1                                  13    
HELIX   39  39 LEU B  230  GLY B  235  1                                   6    
HELIX   40  40 THR B  237  ARG B  245  1                                   9    
HELIX   41  41 THR B  265  GLN B  270  1                                   6    
HELIX   42  42 PRO B  280  GLN B  284  5                                   5    
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  SER B  496  1                                  12    
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  VAL B  572  1                                  10    
HELIX   64  64 GLU C   73  LYS C   83  1                                  11    
HELIX   65  65 THR C   85  THR C   94  1                                  10    
HELIX   66  66 PHE C   96  ASN C  105  1                                  10    
HELIX   67  67 ILE C  105A 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 PRO C  280  GLN C  284  5                                   5    
HELIX   75  75 VAL C  291  LEU C  294  5                                   4    
HELIX   76  76 VAL C  295  HIS C  320  1                                  26    
HELIX   77  77 GLY C  324  ASP C  347  1                                  24    
HELIX   78  78 ASP C  347  GLY C  354  1                                   8    
HELIX   79  79 ASP C  362  PHE C  367  5                                   6    
HELIX   80  80 ALA C  378  TYR C  385  1                                   8    
HELIX   81  81 HIS C  386  LEU C  391  5                                   6    
HELIX   82  82 SER C  403  LEU C  408  1                                   6    
HELIX   83  83 ASN C  411  GLY C  418  1                                   8    
HELIX   84  84 GLY C  418  GLN C  429  1                                  12    
HELIX   85  85 PRO C  441  ALA C  443  5                                   3    
HELIX   86  86 VAL C  444  MET C  458  1                                  15    
HELIX   87  87 SER C  462  PHE C  470  1                                   9    
HELIX   88  88 SER C  477  GLY C  483  1                                   7    
HELIX   89  89 LYS C  485  SER C  496  1                                  12    
HELIX   90  90 ASP C  497  MET C  501  5                                   5    
HELIX   91  91 GLU C  502  GLU C  510  1                                   9    
HELIX   92  92 GLY C  519  GLY C  536  1                                  18    
HELIX   93  93 ASN C  537  SER C  541  5                                   5    
HELIX   94  94 LYS C  546  GLY C  551  5                                   6    
HELIX   95  95 GLY C  552  THR C  561  1                                  10    
HELIX   96  96 SER C  563  VAL C  572  1                                  10    
HELIX   97  97 ASN D   34  ASN D   39  5                                   6    
HELIX   98  98 GLU D   73  LYS D   83  1                                  11    
HELIX   99  99 THR D   85  HIS D   95  1                                  11    
HELIX  100 100 PHE D   96  ASN D  105  1                                  10    
HELIX  101 101 ILE D  105A TYR D  122  1                                  18    
HELIX  102 102 SER D  138  ASN D  144  1                                   7    
HELIX  103 103 ASP D  173  LEU D  182  1                                  10    
HELIX  104 104 ASN D  195  HIS D  207  1                                  13    
HELIX  105 105 LEU D  230  GLY D  235  1                                   6    
HELIX  106 106 THR D  237  ARG D  245  1                                   9    
HELIX  107 107 THR D  265  GLN D  270  1                                   6    
HELIX  108 108 PRO D  280  GLN D  284  5                                   5    
HELIX  109 109 VAL D  295  HIS D  320  1                                  26    
HELIX  110 110 GLY D  324  ASP D  347  1                                  24    
HELIX  111 111 ASP D  347  GLY D  354  1                                   8    
HELIX  112 112 ASP D  362  PHE D  367  5                                   6    
HELIX  113 113 ALA D  378  TYR D  385  1                                   8    
HELIX  114 114 TRP D  387  LEU D  391  5                                   5    
HELIX  115 115 SER D  403  LEU D  408  1                                   6    
HELIX  116 116 ASN D  411  GLY D  418  1                                   8    
HELIX  117 117 GLY D  418  GLN D  429  1                                  12    
HELIX  118 118 PRO D  441  ALA D  443  5                                   3    
HELIX  119 119 VAL D  444  MET D  458  1                                  15    
HELIX  120 120 SER D  462  PHE D  470  1                                   9    
HELIX  121 121 SER D  477  GLY D  483  1                                   7    
HELIX  122 122 LYS D  485  SER D  496  1                                  12    
HELIX  123 123 ASP D  497  MET D  501  5                                   5    
HELIX  124 124 GLU D  502  GLU D  510  1                                   9    
HELIX  125 125 GLY D  519  GLY D  536  1                                  18    
HELIX  126 126 ASN D  537  SER D  541  5                                   5    
HELIX  127 127 LYS D  546  GLY D  551  5                                   6    
HELIX  128 128 GLY D  552  THR D  561  1                                  10    
HELIX  129 129 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 TYR A 130  ASN A 131  0                                        
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130           
SHEET    1   D 2 GLN A 255  VAL A 256  0                                        
SHEET    2   D 2 VAL A 261  TYR A 262 -1  O  TYR A 262   N  GLN A 255           
SHEET    1   E 2 PHE A 395  ILE A 397  0                                        
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   F 2 GLU B  46  SER B  49  0                                        
SHEET    2   F 2 TYR B  55  ASP B  58 -1  O  LYS B  56   N  MET B  48           
SHEET    1   G 2 PHE B  64  TYR B  65  0                                        
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   H 2 TYR B 130  ASN B 131  0                                        
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130           
SHEET    1   I 2 GLN B 255  ILE B 257  0                                        
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   J 2 PHE B 395  ILE B 397  0                                        
SHEET    2   J 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SHEET    1   K 2 GLU C  46  SER C  49  0                                        
SHEET    2   K 2 TYR C  55  ASP C  58 -1  O  ASP C  58   N  GLU C  46           
SHEET    1   L 2 PHE C  64  TYR C  65  0                                        
SHEET    2   L 2 THR C  71  PRO C  72 -1  O  THR C  71   N  TYR C  65           
SHEET    1   M 2 TYR C 130  ASN C 131  0                                        
SHEET    2   M 2 THR C 149  ARG C 150 -1  O  ARG C 150   N  TYR C 130           
SHEET    1   N 2 GLN C 255  ILE C 257  0                                        
SHEET    2   N 2 GLU C 260  TYR C 262 -1  O  TYR C 262   N  GLN C 255           
SHEET    1   O 2 PHE C 395  ILE C 397  0                                        
SHEET    2   O 2 GLN C 400  TYR C 402 -1  O  TYR C 402   N  PHE C 395           
SHEET    1   P 2 GLU D  46  SER D  49  0                                        
SHEET    2   P 2 TYR D  55  ASP D  58 -1  O  LYS D  56   N  MET D  48           
SHEET    1   Q 2 PHE D  64  TYR D  65  0                                        
SHEET    2   Q 2 THR D  71  PRO D  72 -1  O  THR D  71   N  TYR D  65           
SHEET    1   R 2 GLN D 255  ILE D 257  0                                        
SHEET    2   R 2 GLU D 260  TYR D 262 -1  O  TYR D 262   N  GLN D 255           
SHEET    1   S 2 PHE D 395  ILE D 397  0                                        
SHEET    2   S 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  2.03  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.04  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04  
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  2.04  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03  
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  2.03  
SSBOND  14 CYS C   59    CYS C   69                          1555   1555  2.04  
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.04  
SSBOND  16 CYS D   36    CYS D   47                          1555   1555  2.04  
SSBOND  17 CYS D   37    CYS D  159                          1555   1555  2.04  
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  2.04  
LINK         ND2 ASN C 410                 C1  NAG C 681     1555   1555  1.44  
LINK         ND2 ASN D 410                 C1  NAG D 681     1555   1555  1.44  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         ND2 ASN D  68                 C1  NAG D 661     1555   1555  1.44  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44  
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45  
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.45  
LINK         ND2 ASN D 144                 C1  NAG D 671     1555   1555  1.45  
LINK         ND2 ASN C  68                 C1  NAG C 661     1555   1555  1.45  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.45  
LINK         ND2 ASN C 144                 C1  NAG C 671     1555   1555  1.45  
LINK         O4  NAG C 671                 C1  NAG C 672     1555   1555  1.45  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45  
LINK         O4  NAG D 671                 C1  NAG D 672     1555   1555  1.45  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45  
LINK         O4  NAG B 672                 C1  NAG B 673     1555   1555  1.45  
LINK         O4  NAG C 672                 C1  NAG C 673     1555   1555  1.45  
LINK         O4  NAG D 672                 C1  NAG D 673     1555   1555  1.45  
LINK         O4  NAG A 672                 C1  NAG A 673     1555   1555  1.46  
LINK         NE2 HIS C 388                FE   HEM C 619     1555   1555  2.18  
LINK         NE2 HIS A 388                FE   HEM A 619     1555   1555  2.25  
LINK         NE2 HIS D 388                FE   HEM D 619     1555   1555  2.30  
LINK         NE2 HIS B 388                FE   HEM B 619     1555   1555  2.33  
LINK        FE   HEM B 619                 O   HOH B  19     1555   1555  2.35  
CISPEP   1 SER A  126    PRO A  127          0        -0.70                     
CISPEP   2 SER B  126    PRO B  127          0        -0.12                     
CISPEP   3 SER C  126    PRO C  127          0         0.25                     
CISPEP   4 SER D  126    PRO D  127          0        -0.72                     
SITE     1 AC1 17 HOH A  10  ALA A 199  PHE A 200  ALA A 202                    
SITE     2 AC1 17 GLN A 203  HIS A 207  PHE A 210  LYS A 211                    
SITE     3 AC1 17 THR A 212  HIS A 214  VAL A 295  ASN A 382                    
SITE     4 AC1 17 TYR A 385  HIS A 386  HIS A 388  LEU A 391                    
SITE     5 AC1 17 VAL A 447                                                     
SITE     1 AC2  5 TYR A  55  GLU A  67  ASN A  68  HOH A4050                    
SITE     2 AC2  5 HOH A4063                                                     
SITE     1 AC3  8 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC3  8 NAG A 672  HOH A4017  HOH A4298  HOH A4799                    
SITE     1 AC4  3 ARG A 216  NAG A 671  NAG A 673                               
SITE     1 AC5  2 NAG A 672  HOH A4059                                          
SITE     1 AC6  4 GLN A 406  ASN A 410  SER A 412  ILE A 413                    
SITE     1 AC7 10 GLU A 179  ARG A 184  ARG A 185  ILE A 442                    
SITE     2 AC7 10 GLN A 445  ARG B 184  ARG B 185  ARG B 438                    
SITE     3 AC7 10 GLU B 486  GLU B 490                                          
SITE     1 AC8  9 ARG A 120  VAL A 349  LEU A 352  TYR A 355                    
SITE     2 AC8  9 TYR A 385  TRP A 387  VAL A 523  ALA A 527                    
SITE     3 AC8  9 LEU A 531                                                     
SITE     1 AC9  5 LYS A  83  PRO A  84  VAL A  89  SER A 119                    
SITE     2 AC9  5 ARG A 120                                                     
SITE     1 BC1 16 HOH B  19  ALA B 199  ALA B 202  GLN B 203                    
SITE     2 BC1 16 HIS B 207  PHE B 210  THR B 212  HIS B 214                    
SITE     3 BC1 16 VAL B 295  ASN B 382  TYR B 385  HIS B 386                    
SITE     4 BC1 16 HIS B 388  LEU B 391  LEU B 408  VAL B 447                    
SITE     1 BC2  5 TYR B  55  GLU B  67  ASN B  68  HOH B4018                    
SITE     2 BC2  5 HOH B4422                                                     
SITE     1 BC3  7 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 BC3  7 NAG B 672  HOH B4045  HOH B4370                               
SITE     1 BC4  4 ASP A 239  ARG B 216  NAG B 671  NAG B 673                    
SITE     1 BC5  1 NAG B 672                                                     
SITE     1 BC6  6 TYR B 402  GLN B 406  TYR B 409  ASN B 410                    
SITE     2 BC6  6 ILE B 413  HOH B4700                                          
SITE     1 BC7  9 ARG B 120  VAL B 349  TYR B 355  TYR B 385                    
SITE     2 BC7  9 TRP B 387  VAL B 523  GLY B 526  ALA B 527                    
SITE     3 BC7  9 LEU B 531                                                     
SITE     1 BC8  7 LYS B  83  PRO B  84  PRO B  86  TYR B 115                    
SITE     2 BC8  7 SER B 119  ARG B 120  LEU B 123                               
SITE     1 BC9 17 ALA C 199  PHE C 200  ALA C 202  GLN C 203                    
SITE     2 BC9 17 HIS C 207  PHE C 210  THR C 212  HIS C 214                    
SITE     3 BC9 17 VAL C 295  ASN C 382  TYR C 385  HIS C 386                    
SITE     4 BC9 17 HIS C 388  LEU C 391  LEU C 408  ALA C 450                    
SITE     5 BC9 17 HOH C4061                                                     
SITE     1 CC1  4 TYR C  55  GLU C  67  ASN C  68  HOH C4349                    
SITE     1 CC2  7 ASN C 144  TYR C 147  ARG C 216  NAG C 672                    
SITE     2 CC2  7 HOH C4085  HOH C4331  HOH C4974                               
SITE     1 CC3  3 ARG C 216  NAG C 671  NAG C 673                               
SITE     1 CC4  1 NAG C 672                                                     
SITE     1 CC5  6 TYR C 402  GLN C 406  ASN C 410  SER C 412                    
SITE     2 CC5  6 ILE C 413  HOH C4055                                          
SITE     1 CC6  8 VAL C 116  ARG C 120  VAL C 349  TYR C 355                    
SITE     2 CC6  8 TYR C 385  TRP C 387  VAL C 523  ALA C 527                    
SITE     1 CC7  4 LYS C  83  PRO C  84  SER C 119  ARG C 120                    
SITE     1 CC8 16 ALA D 199  PHE D 200  ALA D 202  GLN D 203                    
SITE     2 CC8 16 HIS D 207  PHE D 210  LYS D 211  THR D 212                    
SITE     3 CC8 16 HIS D 214  VAL D 295  ASN D 382  TYR D 385                    
SITE     4 CC8 16 HIS D 386  HIS D 388  LEU D 391  LEU D 408                    
SITE     1 CC9  5 TYR D  55  GLU D  67  ASN D  68  HOH D 654                    
SITE     2 CC9  5 HOH D 689                                                     
SITE     1 DC1  9 LEU C 238  GLU D 140  ASN D 144  TYR D 147                    
SITE     2 DC1  9 ARG D 216  HOH D 640  NAG D 672  HOH D4013                    
SITE     3 DC1  9 HOH D4295                                                     
SITE     1 DC2  3 ARG D 216  NAG D 671  NAG D 673                               
SITE     1 DC3  1 NAG D 672                                                     
SITE     1 DC4  8 GLN D 406  ASN D 410  SER D 412  ILE D 413                    
SITE     2 DC4  8 GLU D 416  HOH D 670  HOH D 688  HOH D4821                    
SITE     1 DC5 11 GLU C 179  LYS C 180  ARG C 184  ARG C 185                    
SITE     2 DC5 11 ARG C 438  GLU C 486  GLU C 490  GLU D 179                    
SITE     3 DC5 11 ARG D 185  ILE D 442  GLN D 445                               
SITE     1 DC6  7 ARG D 120  VAL D 349  TYR D 355  TYR D 385                    
SITE     2 DC6  7 TRP D 387  ALA D 527  LEU D 531                               
SITE     1 DC7  7 LYS D  83  PRO D  84  PRO D  86  SER D 119                    
SITE     2 DC7  7 ARG D 120  LEU D 123  GLU D 524                               
CRYST1  181.197  134.225  121.990  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      0.005519  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007450  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008197        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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