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Database: PDB
Entry: 3HS5
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HEADER    OXIDOREDUCTASE                          10-JUN-09   3HS5              
TITLE     X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC 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 3HS5    1       JRNL                                     
REVDAT   2   02-JUN-10 3HS5    1       JRNL                                     
REVDAT   1   12-MAY-10 3HS5    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.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 83526                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4175                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5736                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 314                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8875                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 379                                     
REMARK   3   SOLVENT ATOMS            : 907                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.18000                                             
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): 0.186         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.139         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9610 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13053 ; 1.121 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1117 ; 5.179 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   444 ;36.503 ;23.986       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1510 ;13.465 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;11.777 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1386 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7366 ; 0.005 ; 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):  5546 ; 0.318 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9018 ; 0.638 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4064 ; 1.248 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4028 ; 2.136 ; 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    67                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2244  38.1953  59.8657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1021 T22:    .3160                                     
REMARK   3      T33:    .2521 T12:    .0662                                     
REMARK   3      T13:    .0538 T23:    .0772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0014 L22:   4.6161                                     
REMARK   3      L33:   3.0850 L12:    .7353                                     
REMARK   3      L13:   -.0278 L23:   1.3357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0387 S12:   -.1048 S13:    .0751                       
REMARK   3      S21:   -.0032 S22:    .0772 S23:    .2289                       
REMARK   3      S31:   -.1906 S32:   -.5562 S33:   -.1159                       
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    68        A    94                          
REMARK   3    ORIGIN FOR THE GROUP (A):    .2095  16.7405  67.1545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2283 T22:    .4420                                     
REMARK   3      T33:    .5833 T12:   -.1048                                     
REMARK   3      T13:    .0256 T23:    .1681                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8544 L22:   6.3504                                     
REMARK   3      L33:   2.2144 L12:  -4.0045                                     
REMARK   3      L13:   1.7638 L23:  -3.3690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0919 S12:   -.0715 S13:   -.5024                       
REMARK   3      S21:   -.3743 S22:    .3894 S23:    .7523                       
REMARK   3      S31:    .3708 S32:   -.4514 S33:   -.4814                       
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    95        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6255   2.1907  64.6350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2154 T22:    .2901                                     
REMARK   3      T33:    .4509 T12:   -.1289                                     
REMARK   3      T13:    .0091 T23:    .0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7889 L22:   5.1024                                     
REMARK   3      L33:  13.0009 L12:   1.8961                                     
REMARK   3      L13:  -4.7482 L23:  -2.5327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.4841 S12:    .2346 S13:   -.2735                       
REMARK   3      S21:   -.3581 S22:    .1952 S23:    .5227                       
REMARK   3      S31:    .6969 S32:   -.6672 S33:    .2889                       
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   123        A   187                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2760  36.5234  66.9945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1055 T22:    .0877                                     
REMARK   3      T33:    .1245 T12:    .0466                                     
REMARK   3      T13:    .0184 T23:    .0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9580 L22:    .7658                                     
REMARK   3      L33:   2.7478 L12:   -.2601                                     
REMARK   3      L13:    .0302 L23:   -.3279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0826 S12:   -.1212 S13:    .0881                       
REMARK   3      S21:    .1456 S22:    .1403 S23:    .0152                       
REMARK   3      S31:   -.1607 S32:   -.2157 S33:   -.0577                       
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   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9439  22.1107  70.6682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1933 T22:    .1658                                     
REMARK   3      T33:    .1821 T12:    .0092                                     
REMARK   3      T13:   -.0062 T23:   -.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4824 L22:   1.1938                                     
REMARK   3      L33:   1.3784 L12:  -1.2305                                     
REMARK   3      L13:    .6054 L23:   -.9414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0823 S12:   -.0919 S13:    .1066                       
REMARK   3      S21:    .1126 S22:    .0337 S23:   -.0851                       
REMARK   3      S31:   -.1315 S32:    .0276 S33:    .0486                       
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   220        A   271                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0811  21.4136  56.2827              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0571 T22:    .0710                                     
REMARK   3      T33:    .1663 T12:   -.0026                                     
REMARK   3      T13:    .0161 T23:    .0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9006 L22:    .6628                                     
REMARK   3      L33:   1.1954 L12:   -.7840                                     
REMARK   3      L13:    .0442 L23:   -.0231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0772 S12:   -.0081 S13:    .1245                       
REMARK   3      S21:   -.0703 S22:   -.0448 S23:   -.2129                       
REMARK   3      S31:   -.0026 S32:    .2194 S33:   -.0324                       
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   272        A   318                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.8733  19.3653  63.6918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0812 T22:    .1390                                     
REMARK   3      T33:    .2088 T12:   -.0013                                     
REMARK   3      T13:    .0048 T23:    .0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7025 L22:   1.4810                                     
REMARK   3      L33:   2.7499 L12:   -.0953                                     
REMARK   3      L13:    .0356 L23:    .3637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0738 S12:   -.2620 S13:    .2134                       
REMARK   3      S21:    .0600 S22:    .0062 S23:   -.2811                       
REMARK   3      S31:   -.0622 S32:    .1757 S33:   -.0800                       
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   319        A   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1287  13.1005  57.8499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1162 T22:    .0574                                     
REMARK   3      T33:    .1585 T12:   -.0273                                     
REMARK   3      T13:   -.0113 T23:    .0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9920 L22:    .6756                                     
REMARK   3      L33:   1.4536 L12:   -.3746                                     
REMARK   3      L13:   -.4809 L23:   -.3911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0436 S12:   -.0674 S13:   -.1651                       
REMARK   3      S21:   -.0315 S22:    .0625 S23:    .0902                       
REMARK   3      S31:    .2038 S32:   -.0413 S33:   -.0189                       
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   390        A   437                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4243  16.8981  80.0974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1590 T22:    .2321                                     
REMARK   3      T33:    .0824 T12:    .0585                                     
REMARK   3      T13:   -.0288 T23:    .0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2086 L22:    .9593                                     
REMARK   3      L33:   2.2842 L12:   -.4198                                     
REMARK   3      L13:   -.9937 L23:    .2010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1086 S12:   -.4258 S13:    .0257                       
REMARK   3      S21:    .2420 S22:    .1579 S23:   -.1503                       
REMARK   3      S31:    .0033 S32:    .4531 S33:   -.0492                       
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   438        A   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7104  28.6262  77.1465              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1141 T22:    .1800                                     
REMARK   3      T33:    .1037 T12:    .0623                                     
REMARK   3      T13:    .0462 T23:    .0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2606 L22:   1.4934                                     
REMARK   3      L33:   2.0002 L12:   -.6184                                     
REMARK   3      L13:    .0553 L23:   -.2006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1210 S12:   -.2508 S13:   -.0773                       
REMARK   3      S21:    .1860 S22:    .1673 S23:    .0765                       
REMARK   3      S31:   -.0366 S32:   -.1907 S33:   -.0462                       
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   535        A   553                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7102  10.2806  47.7409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2314 T22:    .1348                                     
REMARK   3      T33:    .2278 T12:   -.0253                                     
REMARK   3      T13:   -.0372 T23:    .0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0511 L22:   1.5789                                     
REMARK   3      L33:   1.5874 L12:   -.8010                                     
REMARK   3      L13:   -.9724 L23:   -.0286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0174 S12:    .1125 S13:   -.1666                       
REMARK   3      S21:   -.2106 S22:   -.0292 S23:    .1571                       
REMARK   3      S31:    .1716 S32:   -.1374 S33:    .0118                       
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   584                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.9221   3.7119  65.0785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2309 T22:    .0927                                     
REMARK   3      T33:    .2438 T12:   -.0174                                     
REMARK   3      T13:    .0205 T23:    .0670                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5997 L22:   2.3540                                     
REMARK   3      L33:   3.7588 L12:  -1.0053                                     
REMARK   3      L13:   -.1265 L23:    .6041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1612 S12:   -.1087 S13:   -.3181                       
REMARK   3      S21:   -.0337 S22:    .1017 S23:    .1382                       
REMARK   3      S31:    .5322 S32:   -.1249 S33:    .0595                       
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    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0846   2.2762  33.5872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .5138 T22:    .1150                                     
REMARK   3      T33:    .2995 T12:    .0505                                     
REMARK   3      T13:   -.0311 T23:   -.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2344 L22:    .3876                                     
REMARK   3      L33:   2.2880 L12:   -.6583                                     
REMARK   3      L13:   -.4689 L23:   -.0331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1164 S12:    .0169 S13:   -.1471                       
REMARK   3      S21:   -.3012 S22:   -.0938 S23:    .0354                       
REMARK   3      S31:    .7209 S32:    .0729 S33:   -.0226                       
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    67        B    79                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8160  -3.6732  31.2245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .6664 T22:    .2248                                     
REMARK   3      T33:    .4228 T12:   -.1513                                     
REMARK   3      T13:   -.0901 T23:   -.0420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  46.3665 L22:   9.5197                                     
REMARK   3      L33:   1.5050 L12:  -2.2326                                     
REMARK   3      L13:   1.2987 L23:    .4921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.3644 S12:   -.2241 S13:  -1.7561                       
REMARK   3      S21:   -.3776 S22:    .2493 S23:   1.1143                       
REMARK   3      S31:    .6931 S32:   -.4925 S33:    .1151                       
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    80        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4179  17.0223  25.6309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3463 T22:    .3998                                     
REMARK   3      T33:    .4553 T12:   -.2344                                     
REMARK   3      T13:   -.0821 T23:    .0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8292 L22:   4.2121                                     
REMARK   3      L33:   5.7252 L12:  -1.7101                                     
REMARK   3      L13:   -.4872 L23:   2.5830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1386 S12:    .1346 S13:   -.6382                       
REMARK   3      S21:    .1198 S22:   -.3482 S23:    .5411                       
REMARK   3      S31:    .6135 S32:   -.7223 S33:    .2096                       
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   123        B   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7159  18.8445  28.0477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1861 T22:    .1111                                     
REMARK   3      T33:    .1321 T12:    .0691                                     
REMARK   3      T13:    .0174 T23:    .0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7218 L22:    .7953                                     
REMARK   3      L33:   2.3358 L12:   -.1598                                     
REMARK   3      L13:    .4139 L23:   -.4931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1103 S12:    .1113 S13:   -.0966                       
REMARK   3      S21:   -.1853 S22:   -.1413 S23:   -.0309                       
REMARK   3      S31:    .4060 S32:    .1533 S33:    .0310                       
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   186        B   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.6193  35.3807  20.2063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1141 T22:    .1773                                     
REMARK   3      T33:    .1617 T12:    .0477                                     
REMARK   3      T13:    .0057 T23:    .0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6202 L22:   1.3348                                     
REMARK   3      L33:   1.8212 L12:   -.6969                                     
REMARK   3      L13:   -.1267 L23:   -.3553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1656 S12:    .2141 S13:   -.0288                       
REMARK   3      S21:   -.2393 S22:   -.0461 S23:    .0076                       
REMARK   3      S31:    .0001 S32:   -.1158 S33:   -.1195                       
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   214        B   227                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0400  32.4527  34.7884              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1175 T22:    .1398                                     
REMARK   3      T33:    .1832 T12:    .0245                                     
REMARK   3      T13:    .0029 T23:    .0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.8913 L22:   5.2869                                     
REMARK   3      L33:   8.0648 L12:  -3.0432                                     
REMARK   3      L13:  -8.3931 L23:    .9914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2984 S12:    .0611 S13:   1.2056                       
REMARK   3      S21:   -.1794 S22:    .0950 S23:   -.7642                       
REMARK   3      S31:   -.2336 S32:    .4267 S33:   -.3934                       
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   228        B   320                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5672  50.6541  34.9537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0873 T22:    .0898                                     
REMARK   3      T33:    .1824 T12:    .0124                                     
REMARK   3      T13:    .0206 T23:    .0623                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3469 L22:   1.8911                                     
REMARK   3      L33:   2.2386 L12:   -.1025                                     
REMARK   3      L13:    .2192 L23:    .1155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0120 S12:    .1175 S13:    .2261                       
REMARK   3      S21:   -.0303 S22:    .0784 S23:   -.1893                       
REMARK   3      S31:   -.2968 S32:    .1352 S33:   -.0665                       
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   321        B   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8367  31.8224  35.4426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0533 T22:    .1381                                     
REMARK   3      T33:    .1358 T12:   -.0201                                     
REMARK   3      T13:   -.0091 T23:    .0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8135 L22:   1.0541                                     
REMARK   3      L33:   1.4876 L12:   -.3381                                     
REMARK   3      L13:    .0360 L23:   -.0484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0628 S12:    .1161 S13:   -.0728                       
REMARK   3      S21:   -.1226 S22:    .0103 S23:    .1521                       
REMARK   3      S31:    .0891 S32:   -.2365 S33:   -.0730                       
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   390        B   424                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2295  49.2742  14.6452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2116 T22:    .2994                                     
REMARK   3      T33:    .1953 T12:    .0822                                     
REMARK   3      T13:    .0713 T23:    .1195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .3993 L22:   3.1957                                     
REMARK   3      L33:   3.4324 L12:    .2768                                     
REMARK   3      L13:   -.3305 L23:    .7116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1374 S12:    .3018 S13:    .1586                       
REMARK   3      S21:   -.4047 S22:    .0247 S23:   -.1486                       
REMARK   3      S31:   -.3321 S32:   -.0398 S33:   -.1622                       
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   425        B   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8156  23.9585  17.1456              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2278 T22:    .1643                                     
REMARK   3      T33:    .0833 T12:    .0541                                     
REMARK   3      T13:   -.0246 T23:   -.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0991 L22:    .8336                                     
REMARK   3      L33:   1.5510 L12:   -.4590                                     
REMARK   3      L13:    .0603 L23:   -.4317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1215 S12:    .2261 S13:   -.0360                       
REMARK   3      S21:   -.2968 S22:   -.0974 S23:    .0043                       
REMARK   3      S31:    .3899 S32:    .0036 S33:   -.0241                       
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   481        B   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9293  18.6127  15.0864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2927 T22:    .1410                                     
REMARK   3      T33:    .1330 T12:    .0278                                     
REMARK   3      T13:   -.0563 T23:   -.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3106 L22:   1.8773                                     
REMARK   3      L33:   2.5233 L12:  -1.0225                                     
REMARK   3      L13:  -1.0369 L23:    .2105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1364 S12:    .2158 S13:   -.2093                       
REMARK   3      S21:   -.3540 S22:   -.1303 S23:    .1551                       
REMARK   3      S31:    .3690 S32:   -.1153 S33:   -.0061                       
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   535        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4190  38.7587  35.8170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0716 T22:    .2284                                     
REMARK   3      T33:    .1891 T12:   -.0012                                     
REMARK   3      T13:   -.0069 T23:    .0691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1473 L22:    .7674                                     
REMARK   3      L33:   2.4837 L12:   -.4232                                     
REMARK   3      L13:    .1727 L23:   -.9996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0530 S12:    .0758 S13:    .0029                       
REMARK   3      S21:   -.0043 S22:    .1111 S23:    .2000                       
REMARK   3      S31:    .0236 S32:   -.4092 S33:   -.1642                       
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 3HS5 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 RCSB053517.                                      
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   : 83526                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58200                            
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   (%): 53.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
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       59.99150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.27650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.25800            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.99150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.27650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.25800            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.99150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.27650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.25800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.99150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.27650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.25800            
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: 42430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.8 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     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     GLN A  54    OE1  NE2                                            
REMARK 470     LYS A  83    CE   NZ                                             
REMARK 470     LYS A 114    NZ                                                  
REMARK 470     LYS A 169    CD   CE   NZ                                        
REMARK 470     LYS A 175    NZ                                                  
REMARK 470     LYS A 215    CG   CD   CE   NZ                                   
REMARK 470     ARG A 222    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 272    CD   OE1  OE2                                       
REMARK 470     LYS A 405    CD   CE   NZ                                        
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     LYS A 485    CE   NZ                                             
REMARK 470     LYS A 557    CD   CE   NZ                                        
REMARK 470     GLN A 583    CD   OE1  NE2                                       
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    CE   NZ                                             
REMARK 470     LEU B  81    CD1  CD2                                            
REMARK 470     LYS B  83    CD   CE   NZ                                        
REMARK 470     LYS B  97    CE   NZ                                             
REMARK 470     LYS B 169    CE   NZ                                             
REMARK 470     GLU B 170    CD   OE1  OE2                                       
REMARK 470     GLU B 186    CD   OE1  OE2                                       
REMARK 470     LYS B 215    CD   CE   NZ                                        
REMARK 470     GLU B 281    CD   OE1  OE2                                       
REMARK 470     LYS B 358    CD   CE   NZ                                        
REMARK 470     LYS B 405    CE   NZ                                             
REMARK 470     ARG B 428    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 473    CD   CE   NZ                                        
REMARK 470     LYS B 573    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    46     O    HOH A  1337              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 497   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  61       18.63     56.95                                   
REMARK 500    THR A 129      -94.15   -121.89                                   
REMARK 500    ARG A 185      -66.00    -90.54                                   
REMARK 500    GLU A 398     -118.39     56.17                                   
REMARK 500    ASN A 410       79.11   -116.30                                   
REMARK 500    SER A 496      -47.25     70.74                                   
REMARK 500    THR B 129      -92.48   -120.37                                   
REMARK 500    ARG B 185      -83.61   -101.33                                   
REMARK 500    GLU B 398     -113.53     56.36                                   
REMARK 500    TYR B 409       14.15     57.38                                   
REMARK 500    ASN B 410       77.75   -108.34                                   
REMARK 500    SER B 496      -53.73     70.41                                   
REMARK 500    SER B 579     -178.46   -174.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 755        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH B 910        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A1209        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B1325        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B1358        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B1389        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH B1412        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B1413        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH A1332        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B1427        DISTANCE =  7.73 ANGSTROMS                       
REMARK 525    HOH B1429        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A1351        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A1378        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A1434        DISTANCE =  6.15 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 B 619  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 COH B 619   NA   94.5                                              
REMARK 620 3 COH B 619   NB   91.2  89.4                                        
REMARK 620 4 COH B 619   NC   87.8 177.4  89.3                                  
REMARK 620 5 COH B 619   ND   88.2  88.9 178.1  92.4                            
REMARK 620 N                    1     2     3     4                             
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   88.4                                              
REMARK 620 3 COH A 619   NB   89.7  87.3                                        
REMARK 620 4 COH A 619   NC   87.7 175.4  90.4                                  
REMARK 620 5 COH A 619   ND   84.4  90.3 173.6  91.6                            
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 ACD 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 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 11                  
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: 3HS6   RELATED DB: PDB                                   
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL            
REMARK 900 OF 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  3HS5 A   35   618  UNP    Q05769   PGH2_MOUSE      20    604             
DBREF  3HS5 B   35   618  UNP    Q05769   PGH2_MOUSE      20    604             
SEQADV 3HS5 HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 ALA A  594  UNP  Q05769    ASN   580 ENGINEERED                     
SEQADV 3HS5 HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3HS5 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 3HS5 ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS5 ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS5 ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS5 ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS5 ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3HS5 ASN B  410  ASN  GLYCOSYLATION SITE                                 
HET    ACD  A   1      44                                                       
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  12       4                                                       
HET    ACD  B   1      22                                                       
HET    COH  B 619      43                                                       
HET    NAG  B 661      14                                                       
HET    NAG  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   2       4                                                       
HET    EDO  B   3       4                                                       
HET    EDO  B   6       4                                                       
HET    EDO  B   7       4                                                       
HET    EDO  B   8       4                                                       
HET    EDO  B   9       4                                                       
HET    EDO  B  10       4                                                       
HET    EDO  B  11       4                                                       
HETNAM     ACD ARACHIDONIC 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                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  ACD    2(C20 H32 O2)                                                
FORMUL   4  AKR    2(C3 H4 O2)                                                  
FORMUL   6  COH    2(C34 H32 CO N4 O4)                                          
FORMUL   7  NAG    10(C8 H15 N O6)                                              
FORMUL   8  MAN    C6 H12 O6                                                    
FORMUL  10  BOG    2(C14 H28 O6)                                                
FORMUL  11  EDO    12(C2 H6 O2)                                                 
FORMUL  29  HOH   *907(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  ASN A  105  1                                  10    
HELIX    4   4 ILE A  105A ARG A  120  1                                  16    
HELIX    5   5 SER A  121  ILE A  124  5                                   4    
HELIX    6   6 SER A  138  ASN A  144  1                                   7    
HELIX    7   7 ASP A  173  LEU A  182  1                                  10    
HELIX    8   8 ASN A  195  HIS A  207  1                                  13    
HELIX    9   9 LEU A  230  GLY A  235  1                                   6    
HELIX   10  10 THR A  237  ARG A  245  1                                   9    
HELIX   11  11 THR A  265  GLN A  270  1                                   6    
HELIX   12  12 PRO A  280  GLN A  284  5                                   5    
HELIX   13  13 VAL A  291  LEU A  294  5                                   4    
HELIX   14  14 VAL A  295  HIS A  320  1                                  26    
HELIX   15  15 GLY A  324  ASP A  347  1                                  24    
HELIX   16  16 ASP A  347  GLY A  354  1                                   8    
HELIX   17  17 ASP A  362  PHE A  367  5                                   6    
HELIX   18  18 ALA A  378  TYR A  385  1                                   8    
HELIX   19  19 TRP A  387  LEU A  391  5                                   5    
HELIX   20  20 SER A  403  LEU A  408  1                                   6    
HELIX   21  21 ASN A  410  GLN A  429  1                                  20    
HELIX   22  22 PRO A  441  ALA A  443  5                                   3    
HELIX   23  23 VAL A  444  MET A  458  1                                  15    
HELIX   24  24 SER A  462  PHE A  470  1                                   9    
HELIX   25  25 SER A  477  GLY A  483  1                                   7    
HELIX   26  26 LYS A  485  SER A  496  1                                  12    
HELIX   27  27 ASP A  497  MET A  501  5                                   5    
HELIX   28  28 GLU A  502  GLU A  510  1                                   9    
HELIX   29  29 GLY A  519  GLY A  536  1                                  18    
HELIX   30  30 ASN A  537  SER A  541  5                                   5    
HELIX   31  31 LYS A  546  GLY A  551  5                                   6    
HELIX   32  32 GLY A  552  THR A  561  1                                  10    
HELIX   33  33 SER A  563  VAL A  572  1                                  10    
HELIX   34  34 GLU B   73  LYS B   83  1                                  11    
HELIX   35  35 THR B   85  HIS B   95  1                                  11    
HELIX   36  36 PHE B   96  ASN B  104  1                                   9    
HELIX   37  37 ILE B  105A ARG B  120  1                                  16    
HELIX   38  38 SER B  138  ASN B  144  1                                   7    
HELIX   39  39 ASP B  173  LEU B  182  1                                  10    
HELIX   40  40 ASN B  195  HIS B  207  1                                  13    
HELIX   41  41 LEU B  230  GLY B  235  1                                   6    
HELIX   42  42 THR B  237  ARG B  245  1                                   9    
HELIX   43  43 THR B  265  GLN B  270  1                                   6    
HELIX   44  44 PRO B  280  GLN B  284  5                                   5    
HELIX   45  45 VAL B  291  LEU B  294  5                                   4    
HELIX   46  46 VAL B  295  HIS B  320  1                                  26    
HELIX   47  47 GLY B  324  ASP B  347  1                                  24    
HELIX   48  48 ASP B  347  GLY B  354  1                                   8    
HELIX   49  49 ASP B  362  PHE B  367  5                                   6    
HELIX   50  50 ALA B  378  TYR B  385  1                                   8    
HELIX   51  51 HIS B  386  LEU B  391  5                                   6    
HELIX   52  52 SER B  403  LEU B  408  1                                   6    
HELIX   53  53 ASN B  411  GLY B  418  1                                   8    
HELIX   54  54 GLY B  418  GLN B  429  1                                  12    
HELIX   55  55 PRO B  441  ALA B  443  5                                   3    
HELIX   56  56 VAL B  444  MET B  458  1                                  15    
HELIX   57  57 SER B  462  PHE B  470  1                                   9    
HELIX   58  58 SER B  477  GLY B  483  1                                   7    
HELIX   59  59 LYS B  485  SER B  496  1                                  12    
HELIX   60  60 ASP B  497  MET B  501  5                                   5    
HELIX   61  61 GLU B  502  GLU B  510  1                                   9    
HELIX   62  62 GLY B  519  GLY B  536  1                                  18    
HELIX   63  63 ASN B  537  SER B  541  5                                   5    
HELIX   64  64 LYS B  546  GLY B  551  5                                   6    
HELIX   65  65 GLY B  552  THR B  561  1                                  10    
HELIX   66  66 SER B  563  VAL B  572  1                                  10    
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 GLN A 255  ILE A 257  0                                        
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255           
SHEET    1   D 2 PHE A 395  ILE A 397  0                                        
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   E 2 GLU B  46  SER B  49  0                                        
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46           
SHEET    1   F 2 PHE B  64  TYR B  65  0                                        
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   G 2 TYR B 130  ASN B 131  0                                        
SHEET    2   G 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130           
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  2.03  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.06  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.04  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.02  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.05  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.04  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.42  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.43  
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  1.44  
LINK         NE2AHIS B 388                CO   COH B 619     1555   1555  2.28  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.45  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44  
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.45  
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.43  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45  
LINK         NE2AHIS A 388                CO   COH A 619     1555   1555  2.71  
CISPEP   1 SER A  126    PRO A  127          0        -0.38                     
CISPEP   2 SER B  126    PRO B  127          0         1.67                     
SITE     1 AC1 14 VAL A 116  ARG A 120  PHE A 205  TYR A 348                    
SITE     2 AC1 14 VAL A 349  SER A 353  TYR A 355  TYR A 385                    
SITE     3 AC1 14 TRP A 387  VAL A 523  GLY A 526  SER A 530                    
SITE     4 AC1 14 LEU A 531  HOH A 806                                          
SITE     1 AC2  4 SER A 477  PHE A 478  GLU A 479  LYS A 492                    
SITE     1 AC3  5 ASP A 239  ARG A 240  GLN A 270  VAL A 271                    
SITE     2 AC3  5 GLU A 272                                                     
SITE     1 AC4 15 ALA A 202  GLN A 203  HIS A 207  PHE A 210                    
SITE     2 AC4 15 THR A 212  HIS A 214  VAL A 295  ASN A 382                    
SITE     3 AC4 15 TYR A 385  HIS A 386  HIS A 388  LEU A 391                    
SITE     4 AC4 15 HOH A 670  HOH A1058  HOH A1345                               
SITE     1 AC5  6 TYR A  55  GLU A  67  ASN A  68  NAG A 662                    
SITE     2 AC5  6 HOH A 689  HOH A 754                                          
SITE     1 AC6  2 NAG A 661  HOH A 689                                          
SITE     1 AC7  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC7  9 HOH A 626  NAG A 672  HOH A 684  HOH A 796                    
SITE     3 AC7  9 HOH A 845                                                     
SITE     1 AC8  4 ARG A 216  NAG A 671  MAN A 673  ASP B 239                    
SITE     1 AC9  1 NAG A 672                                                     
SITE     1 BC1  6 GLN A 406  ASN A 410  SER A 412  ILE A 413                    
SITE     2 BC1  6 GLU A 416  HOH A 844                                          
SITE     1 BC2 14 LYS A 180  ARG A 184  ARG A 185  ARG A 438                    
SITE     2 BC2 14 ILE A 442  GLU A 486  GLU A 490  LYS B 175                    
SITE     3 BC2 14 GLU B 179  ILE B 442  GLN B 445  BOG B 703                    
SITE     4 BC2 14 HOH B 921  HOH B1425                                          
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 PRO A 162  LEU A 171  SER A 455  ARG A 456                    
SITE     2 BC4  7 LYS A 459  TYR A 460  HOH A 642                               
SITE     1 BC5  4 CYS A  57  ASP A  58  CYS A  59  GLU B 553                    
SITE     1 BC6  7 GLU A 308  ARG A 311  GLU A 339  SER A 566                    
SITE     2 BC6  7 LEU A 567  ASN A 570  HOH A 697                               
SITE     1 BC7 14 PHE B 205  PHE B 209  TYR B 348  VAL B 349                    
SITE     2 BC7 14 TYR B 355  ILE B 377  PHE B 381  TYR B 385                    
SITE     3 BC7 14 ALA B 527  SER B 530  LEU B 531  GLY B 533                    
SITE     4 BC7 14 LEU B 534  HOH B 778                                          
SITE     1 BC8 14 TYR B 148  ALA B 199  GLN B 203  HIS B 207                    
SITE     2 BC8 14 PHE B 210  LYS B 211  THR B 212  VAL B 295                    
SITE     3 BC8 14 ASN B 382  TYR B 385  HIS B 386  HIS B 388                    
SITE     4 BC8 14 LEU B 391  GLN B 454                                          
SITE     1 BC9  4 TYR B  55  GLU B  67  ASN B  68  NAG B 662                    
SITE     1 CC1  2 NAG B 661  HOH B 916                                          
SITE     1 CC2  9 HOH B  15  GLU B 140  ASN B 144  TYR B 147                    
SITE     2 CC2  9 ARG B 216  NAG B 672  HOH B 793  HOH B 872                    
SITE     3 CC2  9 HOH B 915                                                     
SITE     1 CC3  4 ARG B 216  HOH B 620  NAG B 671  HOH B 772                    
SITE     1 CC4  4 GLN B 406  ASN B 410  ILE B 413  GLU B 416                    
SITE     1 CC5 12 LYS A 180  ARG A 185  ARG A 438  GLU A 486                    
SITE     2 CC5 12 GLU A 490  BOG A 703  GLU B 179  ARG B 184                    
SITE     3 CC5 12 ARG B 185  ILE B 442  GLN B 445  HOH B 921                    
SITE     1 CC6  9 HIS B  90  GLN B 192  LEU B 352  ARG B 513                    
SITE     2 CC6  9 ALA B 516  ILE B 517  PHE B 518  VAL B 523                    
SITE     3 CC6  9 HOH B 774                                                     
SITE     1 CC7  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310                    
SITE     2 CC7  6 HOH B 834  HOH B 847                                          
SITE     1 CC8  6 PRO B 162  LEU B 171  ARG B 456  LYS B 459                    
SITE     2 CC8  6 TYR B 460  HOH B 641                                          
SITE     1 CC9  4 SER A 548  MET B  48  LYS B  56  HOH B 889                    
SITE     1 DC1  7 GLU B 308  ARG B 311  GLU B 339  SER B 566                    
SITE     2 DC1  7 LEU B 567  ASN B 570  HOH B 792                               
SITE     1 DC2  6 LEU A 224  SER B 143  HOH B 810  HOH B 859                    
SITE     2 DC2  6 HOH B 879  HOH B1428                                          
SITE     1 DC3  4 ASP B 325  GLU B 326  HOH B 737  HOH B 891                    
SITE     1 DC4  5 ARG B 240  LYS B 243  GLN B 270  VAL B 271                    
SITE     2 DC4  5 GLU B 272                                                     
CRYST1  119.983  132.553  180.516  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      0.008335  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007544  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system