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Database: PDB
Entry: 3HS6
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HEADER    OXIDOREDUCTASE                          10-JUN-09   3HS6              
TITLE     X-RAY CRYSTAL STRUCTURE OF EICOSAPENTAENOIC ACID BOUND TO THE         
TITLE    2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,      
COMPND   6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10 
COMPND   7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   8 2;                                                                   
COMPND   9 EC: 1.14.99.1;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    OXIDOREDUCTASE, DIOXYGENASE, DISULFIDE BOND, ENDOPLASMIC RETICULUM,   
KEYWDS   2 FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, HEME, IRON, LIPID SYNTHESIS,  
KEYWDS   3 MEMBRANE, METAL-BINDING, MICROSOME, PEROXIDASE, PHOSPHOPROTEIN,      
KEYWDS   4 PROSTAGLANDIN BIOSYNTHESIS                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.VECCHIO,D.M.SIMMONS,M.G.MALKOWSKI                                 
REVDAT   3   04-AUG-10 3HS6    1       JRNL                                     
REVDAT   2   02-JUN-10 3HS6    1       JRNL                                     
REVDAT   1   12-MAY-10 3HS6    0                                                
JRNL        AUTH   A.J.VECCHIO,D.M.SIMMONS,M.G.MALKOWSKI                        
JRNL        TITL   STRUCTURAL BASIS OF FATTY ACID SUBSTRATE BINDING TO          
JRNL        TITL 2 CYCLOOXYGENASE-2.                                            
JRNL        REF    J.BIOL.CHEM.                  V. 285 22152 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20463020                                                     
JRNL        DOI    10.1074/JBC.M110.119867                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 56982                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2889                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3877                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 179                          
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8868                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 373                                     
REMARK   3   SOLVENT ATOMS            : 487                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58000                                              
REMARK   3    B22 (A**2) : 0.75000                                              
REMARK   3    B33 (A**2) : -1.32000                                             
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): 0.347         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.231         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.164         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.647        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9565 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13005 ; 1.104 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1112 ; 5.188 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   448 ;36.483 ;23.951       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1490 ;14.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;12.336 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1380 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7372 ; 0.004 ; 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):  5544 ; 0.292 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8999 ; 0.594 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4021 ; 1.082 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4002 ; 1.915 ; 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  : 24                                         
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    68                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5852  37.8555  60.2667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1133 T22:    .2130                                     
REMARK   3      T33:    .1553 T12:    .0339                                     
REMARK   3      T13:    .0212 T23:    .0275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3691 L22:   2.5935                                     
REMARK   3      L33:   1.2348 L12:    .7162                                     
REMARK   3      L13:    .1753 L23:    .3007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0027 S12:   -.1907 S13:    .0855                       
REMARK   3      S21:    .0576 S22:    .0520 S23:    .2021                       
REMARK   3      S31:   -.1092 S32:   -.2392 S33:   -.0547                       
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 :   A    69        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7215  21.3483  61.8891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3456 T22:    .3189                                     
REMARK   3      T33:    .3766 T12:   -.0038                                     
REMARK   3      T13:    .0157 T23:    .0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9561 L22:   6.8934                                     
REMARK   3      L33:    .6366 L12:   1.5597                                     
REMARK   3      L13:   -.0260 L23:   -.0644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0059 S12:   -.0733 S13:   -.3599                       
REMARK   3      S21:    .0131 S22:   -.0175 S23:    .0417                       
REMARK   3      S31:    .2980 S32:   -.0478 S33:    .0234                       
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 :   A    81        A   121                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1490   4.4585  67.3169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1680 T22:    .1761                                     
REMARK   3      T33:    .2824 T12:   -.0572                                     
REMARK   3      T13:    .0102 T23:    .0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8826 L22:   1.9814                                     
REMARK   3      L33:   2.6168 L12:   -.2426                                     
REMARK   3      L13:   -.6726 L23:   -.4353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1155 S12:    .0814 S13:   -.1946                       
REMARK   3      S21:    .0091 S22:   -.0688 S23:    .3792                       
REMARK   3      S31:    .1618 S32:   -.1913 S33:    .1843                       
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 :   A   122        A   187                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8807  36.2124  67.0461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0901 T22:    .0873                                     
REMARK   3      T33:    .1188 T12:    .0194                                     
REMARK   3      T13:    .0032 T23:   -.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7170 L22:    .5451                                     
REMARK   3      L33:   2.4420 L12:   -.1170                                     
REMARK   3      L13:    .0127 L23:   -.3494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0270 S12:   -.1275 S13:    .0531                       
REMARK   3      S21:    .0773 S22:    .0489 S23:    .0484                       
REMARK   3      S31:   -.0563 S32:   -.1467 S33:   -.0219                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   188        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1106  23.7507  63.9656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1293 T22:    .1216                                     
REMARK   3      T33:    .1308 T12:    .0066                                     
REMARK   3      T13:   -.0002 T23:   -.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7814 L22:    .6649                                     
REMARK   3      L33:    .5003 L12:   -.4494                                     
REMARK   3      L13:    .1480 L23:    .3511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0188 S12:   -.0380 S13:    .0792                       
REMARK   3      S21:   -.0077 S22:    .0386 S23:   -.0809                       
REMARK   3      S31:   -.0457 S32:    .0154 S33:   -.0198                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   244        A   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.9010  16.8067  57.0945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0878 T22:    .1350                                     
REMARK   3      T33:    .1756 T12:    .0051                                     
REMARK   3      T13:    .0200 T23:    .0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7163 L22:    .5170                                     
REMARK   3      L33:   2.7277 L12:   -.4616                                     
REMARK   3      L13:   1.5216 L23:    .1543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0578 S12:   -.0079 S13:    .0535                       
REMARK   3      S21:   -.0611 S22:    .0115 S23:   -.1710                       
REMARK   3      S31:   -.0339 S32:    .2204 S33:   -.0692                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   269        A   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.5452  25.4621  66.0992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1974 T22:    .2624                                     
REMARK   3      T33:    .3245 T12:   -.0210                                     
REMARK   3      T13:    .0056 T23:   -.0689                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2008 L22:   2.1608                                     
REMARK   3      L33:   1.8837 L12:   1.8090                                     
REMARK   3      L13:   -.4296 L23:  -1.4587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0754 S12:   -.2662 S13:    .4116                       
REMARK   3      S21:    .1303 S22:   -.1161 S23:   -.0671                       
REMARK   3      S31:   -.1719 S32:    .2778 S33:    .0408                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   303        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.6429   9.2390  51.8445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1142 T22:    .0715                                     
REMARK   3      T33:    .1244 T12:    .0230                                     
REMARK   3      T13:   -.0079 T23:    .0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6018 L22:    .5592                                     
REMARK   3      L33:   1.7594 L12:    .1523                                     
REMARK   3      L13:   -.0501 L23:   -.0598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0404 S12:    .0069 S13:   -.1247                       
REMARK   3      S21:   -.0526 S22:   -.0232 S23:   -.0606                       
REMARK   3      S31:    .1909 S32:    .1257 S33:   -.0173                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   345        A   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8419  15.1753  65.9342              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0875 T22:    .0968                                     
REMARK   3      T33:    .1144 T12:    .0052                                     
REMARK   3      T13:    .0194 T23:    .0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4268 L22:    .9221                                     
REMARK   3      L33:   1.4109 L12:   -.3359                                     
REMARK   3      L13:    .0294 L23:   -.2959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0175 S12:   -.1084 S13:   -.1064                       
REMARK   3      S21:    .0781 S22:    .0364 S23:    .0579                       
REMARK   3      S31:    .1508 S32:   -.0628 S33:   -.0189                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.6016  16.6613  78.3825              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1941 T22:    .2523                                     
REMARK   3      T33:    .1378 T12:    .0312                                     
REMARK   3      T13:   -.0162 T23:   -.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1730 L22:   3.5993                                     
REMARK   3      L33:   2.0376 L12:    .2103                                     
REMARK   3      L13:    .6191 L23:   1.0123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0459 S12:   -.3285 S13:    .1202                       
REMARK   3      S21:    .2310 S22:    .1138 S23:   -.1486                       
REMARK   3      S31:   -.0802 S32:    .3532 S33:   -.0679                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   430        A   553                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8092  24.9821  72.9478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1033 T22:    .1244                                     
REMARK   3      T33:    .0934 T12:    .0206                                     
REMARK   3      T13:    .0092 T23:    .0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .5829 L22:    .6643                                     
REMARK   3      L33:    .5544 L12:   -.2324                                     
REMARK   3      L13:   -.1238 L23:    .1861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0254 S12:   -.1745 S13:   -.0364                       
REMARK   3      S21:    .1123 S22:    .0476 S23:    .0923                       
REMARK   3      S31:   -.0067 S32:   -.0685 S33:   -.0222                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   554        A   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2606   3.4434  64.0136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1971 T22:    .1637                                     
REMARK   3      T33:    .2109 T12:   -.0109                                     
REMARK   3      T13:   -.0032 T23:    .0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4011 L22:   1.1783                                     
REMARK   3      L33:   2.9373 L12:   -.5995                                     
REMARK   3      L13:   -.0520 L23:   -.3987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0170 S12:   -.0340 S13:   -.1804                       
REMARK   3      S21:    .0496 S22:    .0195 S23:    .1452                       
REMARK   3      S31:    .3669 S32:   -.2334 S33:   -.0025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    33        B    64                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2884   2.6013  33.3484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3101 T22:    .1631                                     
REMARK   3      T33:    .2151 T12:    .0568                                     
REMARK   3      T13:   -.0250 T23:   -.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7132 L22:    .4715                                     
REMARK   3      L33:    .5516 L12:   -.2079                                     
REMARK   3      L13:   -.6631 L23:    .3528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0095 S12:    .0296 S13:   -.0966                       
REMARK   3      S21:   -.0861 S22:    .0157 S23:   -.0136                       
REMARK   3      S31:    .1196 S32:    .0926 S33:   -.0252                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    65        B    78                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3536  -4.4258  31.5274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3543 T22:    .2665                                     
REMARK   3      T33:    .3086 T12:   -.0070                                     
REMARK   3      T13:   -.0120 T23:   -.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4613 L22:   2.1893                                     
REMARK   3      L33:   1.7903 L12:    .4807                                     
REMARK   3      L13:   -.3559 L23:   -.3911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0013 S12:    .0710 S13:   -.1678                       
REMARK   3      S21:   -.1184 S22:    .0158 S23:    .3367                       
REMARK   3      S31:    .0911 S32:   -.2668 S33:   -.0144                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    79        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1404  16.5011  25.8038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1733 T22:    .2082                                     
REMARK   3      T33:    .2789 T12:   -.0891                                     
REMARK   3      T13:   -.0491 T23:   -.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8769 L22:   1.7617                                     
REMARK   3      L33:   2.0543 L12:   -.5176                                     
REMARK   3      L13:    .3146 L23:    .2332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0144 S12:    .1374 S13:   -.3470                       
REMARK   3      S21:    .0598 S22:   -.1460 S23:    .2706                       
REMARK   3      S31:    .2392 S32:   -.3295 S33:    .1317                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   121        B   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.3415  18.8888  27.3574              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1394 T22:    .1249                                     
REMARK   3      T33:    .1366 T12:    .0382                                     
REMARK   3      T13:    .0045 T23:   -.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4134 L22:    .8256                                     
REMARK   3      L33:   1.9220 L12:   -.0993                                     
REMARK   3      L13:    .2865 L23:   -.2127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0537 S12:    .1102 S13:   -.0783                       
REMARK   3      S21:   -.1574 S22:   -.0677 S23:   -.0217                       
REMARK   3      S31:    .2791 S32:    .0580 S33:    .0140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   187        B   227                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4737  34.5666  25.3734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1095 T22:    .1196                                     
REMARK   3      T33:    .1168 T12:   -.0010                                     
REMARK   3      T13:    .0199 T23:    .0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7556 L22:   1.0427                                     
REMARK   3      L33:   1.3269 L12:   -.4986                                     
REMARK   3      L13:   -.0783 L23:   -.3210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0215 S12:    .1498 S13:    .0839                       
REMARK   3      S21:   -.0411 S22:   -.0383 S23:   -.0943                       
REMARK   3      S31:   -.0802 S32:    .1235 S33:    .0598                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   228        B   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7745  50.9489  38.6195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0901 T22:    .0924                                     
REMARK   3      T33:    .1441 T12:    .0021                                     
REMARK   3      T13:    .0027 T23:    .0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1780 L22:   2.0690                                     
REMARK   3      L33:   1.8274 L12:    .0454                                     
REMARK   3      L13:    .2068 L23:   -.4529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0598 S12:    .0355 S13:    .2119                       
REMARK   3      S21:    .0996 S22:    .0270 S23:   -.1733                       
REMARK   3      S31:   -.2793 S32:    .1280 S33:    .0327                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   269        B   299                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8846  51.2737  28.7368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1388 T22:    .1762                                     
REMARK   3      T33:    .2333 T12:   -.0378                                     
REMARK   3      T13:    .0233 T23:    .0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2086 L22:   3.9757                                     
REMARK   3      L33:   3.7894 L12:    .6368                                     
REMARK   3      L13:    .3129 L23:   1.1780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0972 S12:    .1504 S13:    .2298                       
REMARK   3      S21:   -.2128 S22:    .1079 S23:   -.4200                       
REMARK   3      S31:   -.3350 S32:    .3650 S33:   -.0107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   300        B   347                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2331  45.3102  40.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0703 T22:    .0722                                     
REMARK   3      T33:    .1099 T12:    .0196                                     
REMARK   3      T13:   -.0006 T23:    .0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8224 L22:    .9235                                     
REMARK   3      L33:   2.1631 L12:   -.1076                                     
REMARK   3      L13:    .0463 L23:    .1975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0289 S12:   -.0032 S13:    .0963                       
REMARK   3      S21:    .0715 S22:   -.0213 S23:    .0974                       
REMARK   3      S31:   -.1438 S32:   -.1520 S33:   -.0075                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   348        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2857  29.4761  27.0768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0844 T22:    .0892                                     
REMARK   3      T33:    .0984 T12:   -.0018                                     
REMARK   3      T13:   -.0207 T23:   -.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7204 L22:    .5299                                     
REMARK   3      L33:   1.5687 L12:   -.2706                                     
REMARK   3      L13:    .0513 L23:    .0014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0273 S12:    .1592 S13:   -.0322                       
REMARK   3      S21:   -.1055 S22:    .0076 S23:    .0925                       
REMARK   3      S31:    .0560 S32:   -.1138 S33:   -.0349                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   402        B   434                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4054  48.4315  15.5702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1479 T22:    .1708                                     
REMARK   3      T33:    .0958 T12:    .0291                                     
REMARK   3      T13:    .0226 T23:    .0704                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9615 L22:   3.5097                                     
REMARK   3      L33:   1.5908 L12:   -.2203                                     
REMARK   3      L13:   -.2162 L23:   1.0320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1360 S12:    .2055 S13:    .1499                       
REMARK   3      S21:   -.2612 S22:   -.0834 S23:   -.0795                       
REMARK   3      S31:   -.2474 S32:    .0569 S33:   -.0526                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   435        B   530                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0339  19.1541  15.7776              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1788 T22:    .1429                                     
REMARK   3      T33:    .0761 T12:    .0388                                     
REMARK   3      T13:   -.0111 T23:   -.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1498 L22:    .8900                                     
REMARK   3      L33:    .3820 L12:    .0445                                     
REMARK   3      L13:    .0842 L23:   -.1277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0545 S12:    .2003 S13:   -.1361                       
REMARK   3      S21:   -.1923 S22:   -.0356 S23:    .0112                       
REMARK   3      S31:    .1738 S32:    .0425 S33:   -.0189                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   531        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4514  37.5928  35.9941              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0678 T22:    .1139                                     
REMARK   3      T33:    .1326 T12:   -.0064                                     
REMARK   3      T13:   -.0070 T23:    .0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7669 L22:   1.0718                                     
REMARK   3      L33:   1.6672 L12:   -.3039                                     
REMARK   3      L13:   -.1957 L23:   -.4786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0099 S12:    .0362 S13:   -.0260                       
REMARK   3      S21:   -.0401 S22:    .0426 S23:    .1288                       
REMARK   3      S31:    .0602 S32:   -.1776 S33:   -.0525                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3HS6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053518.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56982                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1CVU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM      
REMARK 280  HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 296K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       60.92550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.16800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.14500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.92550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.16800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.14500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.92550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.16800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.14500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.92550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.16800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.14500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 5020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.7 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 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     HIS A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     GLN A   583                                                      
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     ALA 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     HIS B    29                                                      
REMARK 465     HIS B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     HIS B    32                                                      
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     ALA 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  56    CE   NZ                                             
REMARK 470     LYS A  79    CE   NZ                                             
REMARK 470     LYS A  83    CD   CE   NZ                                        
REMARK 470     LYS A 169    CE   NZ                                             
REMARK 470     LYS A 215    CG   CD   CE   NZ                                   
REMARK 470     LYS A 248    CE   NZ                                             
REMARK 470     LYS A 358    CE   NZ                                             
REMARK 470     LYS A 405    CG   CD   CE   NZ                                   
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     LYS A 511    CE   NZ                                             
REMARK 470     LYS A 557    CD   CE   NZ                                        
REMARK 470     ASP B  53    OD1  OD2                                            
REMARK 470     GLN B  54    CD   OE1  NE2                                       
REMARK 470     LEU B  75    CG   CD1  CD2                                       
REMARK 470     LYS B  79    CD   CE   NZ                                        
REMARK 470     LEU B  81    CG   CD1  CD2                                       
REMARK 470     LEU B  82    CD1  CD2                                            
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     LYS B  97    CG   CD   CE   NZ                                   
REMARK 470     LYS B 169    CD   CE   NZ                                        
REMARK 470     GLU B 170    OE1  OE2                                            
REMARK 470     LYS B 215    CD   CE   NZ                                        
REMARK 470     ASP B 239    OD1  OD2                                            
REMARK 470     LYS B 358    CE   NZ                                             
REMARK 470     LYS B 405    CE   NZ                                             
REMARK 470     LYS B 459    NZ                                                  
REMARK 470     LYS B 473    CG   CD   CE   NZ                                   
REMARK 470     LYS B 485    CD   CE   NZ                                        
REMARK 470     LYS B 511    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 129      -84.52   -119.56                                   
REMARK 500    VAL A 165      -30.46   -137.22                                   
REMARK 500    ARG A 185      -72.01    -94.73                                   
REMARK 500    TRP A 387       46.64    -89.75                                   
REMARK 500    GLU A 398     -113.08     56.46                                   
REMARK 500    TYR A 409        3.07     55.71                                   
REMARK 500    SER A 496      -46.43     73.37                                   
REMARK 500    CYS A 575       67.42     39.86                                   
REMARK 500    ARG B  61       14.64     57.80                                   
REMARK 500    THR B 129      -96.34   -117.66                                   
REMARK 500    ARG B 185      -89.24    -94.93                                   
REMARK 500    GLN B 284       78.11   -101.95                                   
REMARK 500    GLU B 398     -119.16     58.88                                   
REMARK 500    SER B 496      -46.97     73.04                                   
REMARK 500    CYS B 575       70.01     47.78                                   
REMARK 500    SER B 579     -172.35   -171.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 806        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH B 807        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH B 820        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH A 836        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A 837        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B 836        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B 838        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A 842        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A 861        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH A 867        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A 873        DISTANCE =  6.71 ANGSTROMS                       
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                             COH A 619  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 COH A 619   NA   94.1                                              
REMARK 620 3 COH A 619   NB   96.6  88.3                                        
REMARK 620 4 COH A 619   NC   90.7 175.0  89.8                                  
REMARK 620 5 COH A 619   ND   84.7  91.6 178.7  90.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             COH B 619  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 COH B 619   NA   96.8                                              
REMARK 620 3 COH B 619   NB   91.9  89.0                                        
REMARK 620 4 COH B 619   NC   81.5 177.9  89.8                                  
REMARK 620 5 COH B 619   ND   82.8  91.8 174.7  89.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPA A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPA B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO COX-2                                      
REMARK 900 RELATED ID: 1DDX   RELATED DB: PDB                                   
REMARK 900 PGG2 BOUND TO COX-2                                                  
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1                                      
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB                                   
REMARK 900 UNINHIBITED COX-2                                                    
REMARK 900 RELATED ID: 1IGX   RELATED DB: PDB                                   
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO COX-1                                 
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF              
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB                                   
REMARK 900 DOCOSAHEXAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF          
REMARK 900 CYCLOOXYGENASE-2                                                     
DBREF  3HS6 A   35   618  UNP    Q05769   PGH2_MOUSE      20    604             
DBREF  3HS6 B   35   618  UNP    Q05769   PGH2_MOUSE      20    604             
SEQADV 3HS6 HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 ALA A  594  UNP  Q05769    ASN   580 ENGINEERED                     
SEQADV 3HS6 HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS6 ALA B  594  UNP  Q05769    ASN   580 ENGINEERED                     
SEQRES   1 A  591  HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO CYS          
SEQRES   2 A  591  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN          
SEQRES   3 A  591  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU          
SEQRES   4 A  591  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU          
SEQRES   5 A  591  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU          
SEQRES   6 A  591  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE          
SEQRES   7 A  591  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR          
SEQRES   8 A  591  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN          
SEQRES   9 A  591  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN          
SEQRES  10 A  591  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP          
SEQRES  11 A  591  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU          
SEQRES  12 A  591  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU          
SEQRES  13 A  591  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET          
SEQRES  14 A  591  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE          
SEQRES  15 A  591  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG          
SEQRES  16 A  591  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY          
SEQRES  17 A  591  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS          
SEQRES  18 A  591  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL          
SEQRES  19 A  591  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE          
SEQRES  20 A  591  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL          
SEQRES  21 A  591  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET          
SEQRES  22 A  591  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS          
SEQRES  23 A  591  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU          
SEQRES  24 A  591  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU          
SEQRES  25 A  591  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU          
SEQRES  26 A  591  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU          
SEQRES  27 A  591  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA          
SEQRES  28 A  591  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU          
SEQRES  29 A  591  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE          
SEQRES  30 A  591  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS          
SEQRES  31 A  591  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE          
SEQRES  32 A  591  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA          
SEQRES  33 A  591  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG          
SEQRES  34 A  591  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG          
SEQRES  35 A  591  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR          
SEQRES  36 A  591  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR          
SEQRES  37 A  591  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU          
SEQRES  38 A  591  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR          
SEQRES  39 A  591  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU          
SEQRES  40 A  591  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO          
SEQRES  41 A  591  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN          
SEQRES  42 A  591  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS          
SEQRES  43 A  591  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN          
SEQRES  44 A  591  PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER HIS          
SEQRES  45 A  591  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS          
SEQRES  46 A  591  ARG ARG SER THR GLU LEU                                      
SEQRES   1 B  591  HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO CYS          
SEQRES   2 B  591  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN          
SEQRES   3 B  591  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU          
SEQRES   4 B  591  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU          
SEQRES   5 B  591  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU          
SEQRES   6 B  591  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE          
SEQRES   7 B  591  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR          
SEQRES   8 B  591  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN          
SEQRES   9 B  591  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN          
SEQRES  10 B  591  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP          
SEQRES  11 B  591  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU          
SEQRES  12 B  591  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU          
SEQRES  13 B  591  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET          
SEQRES  14 B  591  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE          
SEQRES  15 B  591  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG          
SEQRES  16 B  591  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY          
SEQRES  17 B  591  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS          
SEQRES  18 B  591  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL          
SEQRES  19 B  591  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE          
SEQRES  20 B  591  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL          
SEQRES  21 B  591  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET          
SEQRES  22 B  591  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS          
SEQRES  23 B  591  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU          
SEQRES  24 B  591  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU          
SEQRES  25 B  591  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU          
SEQRES  26 B  591  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU          
SEQRES  27 B  591  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA          
SEQRES  28 B  591  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU          
SEQRES  29 B  591  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE          
SEQRES  30 B  591  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS          
SEQRES  31 B  591  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE          
SEQRES  32 B  591  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA          
SEQRES  33 B  591  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG          
SEQRES  34 B  591  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG          
SEQRES  35 B  591  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR          
SEQRES  36 B  591  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR          
SEQRES  37 B  591  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU          
SEQRES  38 B  591  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR          
SEQRES  39 B  591  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU          
SEQRES  40 B  591  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO          
SEQRES  41 B  591  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN          
SEQRES  42 B  591  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS          
SEQRES  43 B  591  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN          
SEQRES  44 B  591  PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER HIS          
SEQRES  45 B  591  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS          
SEQRES  46 B  591  ARG ARG SER THR GLU LEU                                      
MODRES 3HS6 ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS6 ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS6 ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS6 ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS6 ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS6 ASN B  410  ASN  GLYCOSYLATION SITE                                 
HET    EPA  A   1      22                                                       
HET    AKR  A   2       5                                                       
HET    AKR  A   3       5                                                       
HET    COH  A 619      43                                                       
HET    NAG  A 661      14                                                       
HET    NAG  A 662      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 672      14                                                       
HET    MAN  A 673      11                                                       
HET    NAG  A 681      14                                                       
HET    BOG  A 703      20                                                       
HET    EDO  A 620       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   5       4                                                       
HET    EDO  A   6       4                                                       
HET    EDO  A   8       4                                                       
HET    EPA  B   1      22                                                       
HET    AKR  B   2       5                                                       
HET    AKR  B   3       5                                                       
HET    COH  B 619      43                                                       
HET    NAG  B 661      14                                                       
HET    NDG  B 662      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 672      14                                                       
HET    NAG  B 681      14                                                       
HET    BOG  B 703      20                                                       
HET    EDO  B 620       4                                                       
HET    EDO  B 621       4                                                       
HET    EDO  B   7       4                                                       
HETNAM     EPA 5,8,11,14,17-EICOSAPENTAENOIC ACID                               
HETNAM     AKR ACRYLIC ACID                                                     
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EPA    2(C20 H30 O2)                                                
FORMUL   4  AKR    4(C3 H4 O2)                                                  
FORMUL   6  COH    2(C34 H32 CO N4 O4)                                          
FORMUL   7  NAG    9(C8 H15 N O6)                                               
FORMUL   8  MAN    C6 H12 O6                                                    
FORMUL  10  BOG    2(C14 H28 O6)                                                
FORMUL  11  EDO    8(C2 H6 O2)                                                  
FORMUL  20  NDG    C8 H15 N O6                                                  
FORMUL  27  HOH   *487(H2 O)                                                    
HELIX    1   1 GLU A   73  LYS A   83  1                                  11    
HELIX    2   2 THR A   85  THR A   94  1                                  10    
HELIX    3   3 PHE A   96  ILE A  105A 1                                  11    
HELIX    4   4 ILE A  105A ARG A  120  1                                  16    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  ARG A  245  1                                   9    
HELIX   10  10 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 PRO A  280  GLN A  284  5                                   5    
HELIX   12  12 VAL A  291  LEU A  294  5                                   4    
HELIX   13  13 VAL A  295  HIS A  320  1                                  26    
HELIX   14  14 GLY A  324  ASP A  347  1                                  24    
HELIX   15  15 ASP A  347  GLY A  354  1                                   8    
HELIX   16  16 ASP A  362  PHE A  367  5                                   6    
HELIX   17  17 ALA A  378  TYR A  385  1                                   8    
HELIX   18  18 TRP A  387  LEU A  391  5                                   5    
HELIX   19  19 SER A  403  LEU A  408  1                                   6    
HELIX   20  20 ASN A  411  GLN A  429  1                                  19    
HELIX   21  21 PRO A  441  ALA A  443  5                                   3    
HELIX   22  22 VAL A  444  MET A  458  1                                  15    
HELIX   23  23 SER A  462  PHE A  470  1                                   9    
HELIX   24  24 SER A  477  GLY A  483  1                                   7    
HELIX   25  25 LYS A  485  SER A  496  1                                  12    
HELIX   26  26 ASP A  497  MET A  501  5                                   5    
HELIX   27  27 GLU A  502  GLU A  510  1                                   9    
HELIX   28  28 GLY A  519  GLY A  536  1                                  18    
HELIX   29  29 ASN A  537  SER A  541  5                                   5    
HELIX   30  30 LYS A  546  GLY A  551  5                                   6    
HELIX   31  31 GLY A  552  ASN A  560  1                                   9    
HELIX   32  32 SER A  563  VAL A  572  1                                  10    
HELIX   33  33 GLU B   73  LYS B   83  1                                  11    
HELIX   34  34 THR B   85  THR B   94  1                                  10    
HELIX   35  35 PHE B   96  ASN B  104  1                                   9    
HELIX   36  36 ILE B  105A SER B  119  1                                  15    
HELIX   37  37 SER B  138  ASN B  144  1                                   7    
HELIX   38  38 ASP B  173  LEU B  182  1                                  10    
HELIX   39  39 ASN B  195  HIS B  207  1                                  13    
HELIX   40  40 LEU B  230  GLY B  235  1                                   6    
HELIX   41  41 THR B  237  ARG B  245  1                                   9    
HELIX   42  42 THR B  265  GLN B  270  1                                   6    
HELIX   43  43 PRO B  280  GLN B  284  5                                   5    
HELIX   44  44 VAL B  295  HIS B  320  1                                  26    
HELIX   45  45 GLY B  324  ASP B  347  1                                  24    
HELIX   46  46 ASP B  347  GLY B  354  1                                   8    
HELIX   47  47 ASP B  362  PHE B  367  5                                   6    
HELIX   48  48 ALA B  378  TYR B  385  1                                   8    
HELIX   49  49 HIS B  386  LEU B  391  5                                   6    
HELIX   50  50 SER B  403  LEU B  408  1                                   6    
HELIX   51  51 ASN B  411  GLY B  418  1                                   8    
HELIX   52  52 GLY B  418  GLN B  429  1                                  12    
HELIX   53  53 PRO B  441  ALA B  443  5                                   3    
HELIX   54  54 VAL B  444  MET B  458  1                                  15    
HELIX   55  55 SER B  462  PHE B  470  1                                   9    
HELIX   56  56 SER B  477  GLY B  483  1                                   7    
HELIX   57  57 LYS B  485  SER B  496  1                                  12    
HELIX   58  58 ASP B  497  MET B  501  5                                   5    
HELIX   59  59 GLU B  502  GLU B  510  1                                   9    
HELIX   60  60 GLY B  519  GLY B  536  1                                  18    
HELIX   61  61 ASN B  537  SER B  541  5                                   5    
HELIX   62  62 LYS B  546  GLY B  551  5                                   6    
HELIX   63  63 GLY B  552  THR B  561  1                                  10    
HELIX   64  64 SER B  563  VAL B  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  LYS A  56   N  MET A  48           
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  ILE A 257  0                                        
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257           
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 GLN B 255  ILE B 257  0                                        
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   I 2 PHE B 395  ILE B 397  0                                        
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.05  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.04  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.05  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.67  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.05  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.04  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.05  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.43  
LINK         NE2AHIS A 388                CO   COH A 619     1555   1555  2.54  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44  
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.44  
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.43  
LINK         NE2AHIS B 388                CO   COH B 619     1555   1555  2.48  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.46  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44  
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.46  
LINK         O4  NAG B 661                 C1  NDG B 662     1555   1555  1.43  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44  
CISPEP   1 SER A  126    PRO A  127          0         3.42                     
CISPEP   2 SER B  126    PRO B  127          0        -0.78                     
SITE     1 AC1  9 PHE A 205  TYR A 348  TYR A 355  TYR A 385                    
SITE     2 AC1  9 TRP A 387  GLY A 526  ALA A 527  SER A 530                    
SITE     3 AC1  9 HOH A 736                                                     
SITE     1 AC2  4 SER A 477  PHE A 478  GLU A 479  LYS A 492                    
SITE     1 AC3  5 THR A 237  ARG A 240  LYS A 243  VAL A 271                    
SITE     2 AC3  5 GLU A 272                                                     
SITE     1 AC4 13 ALA A 199  GLN A 203  HIS A 207  PHE A 210                    
SITE     2 AC4 13 THR A 212  HIS A 214  VAL A 295  ASN A 382                    
SITE     3 AC4 13 TYR A 385  HIS A 386  HIS A 388  VAL A 447                    
SITE     4 AC4 13 HOH A 878                                                     
SITE     1 AC5  4 TYR A  55  GLU A  67  ASN A  68  NAG A 662                    
SITE     1 AC6  1 NAG A 661                                                     
SITE     1 AC7  8 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC7  8 HOH A 649  NAG A 672  HOH A 682  HOH A 720                    
SITE     1 AC8  5 ARG A 216  NAG A 671  MAN A 673  HOH A 851                    
SITE     2 AC8  5 ASP B 239                                                     
SITE     1 AC9  1 NAG A 672                                                     
SITE     1 BC1  5 GLN A 406  ASN A 410  SER A 412  ILE A 413                    
SITE     2 BC1  5 GLU A 416                                                     
SITE     1 BC2 11 LYS A 180  ARG A 184  ARG A 185  ARG A 438                    
SITE     2 BC2 11 GLU A 486  GLU A 490  GLU B 179  ARG B 185                    
SITE     3 BC2 11 ILE B 442  GLN B 445  BOG B 703                               
SITE     1 BC3  8 HIS A  90  GLN A 192  LEU A 352  ARG A 513                    
SITE     2 BC3  8 ALA A 516  ILE A 517  PHE A 518  VAL A 523                    
SITE     1 BC4  7 EDO A   5  PRO A 162  SER A 455  ARG A 456                    
SITE     2 BC4  7 LYS A 459  TYR A 460  HOH A 877                               
SITE     1 BC5  7 EDO A   4  ALA A 156  ASP A 157  CYS A 159                    
SITE     2 BC5  7 THR A 161  PRO A 162  LYS A 459                               
SITE     1 BC6  2 ASP A  58  CYS A  59                                          
SITE     1 BC7  4 HOH A 855  LEU B 178  GLN B 445  LYS B 449                    
SITE     1 BC8 13 PHE B 205  PHE B 209  TYR B 348  TYR B 355                    
SITE     2 BC8 13 ILE B 377  PHE B 381  TYR B 385  VAL B 523                    
SITE     3 BC8 13 GLY B 526  ALA B 527  SER B 530  GLY B 533                    
SITE     4 BC8 13 LEU B 534                                                     
SITE     1 BC9  4 SER B 477  PHE B 478  GLU B 479  LYS B 492                    
SITE     1 CC1  4 ARG B 240  LYS B 243  GLN B 270  GLU B 272                    
SITE     1 CC2 11 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 CC2 11 THR B 212  VAL B 295  ASN B 382  TYR B 385                    
SITE     3 CC2 11 HIS B 386  HIS B 388  LEU B 391                               
SITE     1 CC3  4 TYR B  55  GLU B  67  ASN B  68  NDG B 662                    
SITE     1 CC4  1 NAG B 661                                                     
SITE     1 CC5  8 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 CC5  8 PHE B 220  HOH B 627  NAG B 672  HOH B 815                    
SITE     1 CC6  5 ASP A 239  ARG B 216  NAG B 671  HOH B 804                    
SITE     2 CC6  5 HOH B 834                                                     
SITE     1 CC7  4 HOH B  20  ASN B 410  ILE B 413  GLU B 416                    
SITE     1 CC8 12 GLU A 179  ARG A 185  ARG A 438  GLU A 486                    
SITE     2 CC8 12 GLU A 490  BOG A 703  LYS B 175  GLU B 179                    
SITE     3 CC8 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445                    
SITE     1 CC9  8 HIS B  90  GLN B 192  LEU B 352  ARG B 513                    
SITE     2 CC9  8 ALA B 516  ILE B 517  PHE B 518  VAL B 523                    
SITE     1 DC1  4 LYS B 251  TYR B 254  VAL B 261  ASN B 310                    
SITE     1 DC2  5 PRO B 162  ARG B 456  LYS B 459  TYR B 460                    
SITE     2 DC2  5 HOH B 729                                                     
CRYST1  121.851  132.336  180.290  90.00  90.00  90.00 I 2 2 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      0.008207  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007557  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005547        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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