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Database: PDB
Entry: 3OLU
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HEADER    OXIDOREDUCTASE                          26-AUG-10   3OLU              
TITLE     X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL BOUND TO THE       
TITLE    2 CYCLOOXYGENASE CHANNEL OF R513H MURINE COX-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: VIRUS;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    MONOTOPIC MEMBRANE PROTEIN, OXIDOREDUCTASE, N-GLYCOSYLATION, MEMBRANE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI                                             
REVDAT   4   29-JUN-11 3OLU    1       JRNL                                     
REVDAT   3   15-JUN-11 3OLU    1       JRNL                                     
REVDAT   2   20-APR-11 3OLU    1       JRNL                                     
REVDAT   1   13-APR-11 3OLU    0                                                
JRNL        AUTH   A.J.VECCHIO,M.G.MALKOWSKI                                    
JRNL        TITL   THE STRUCTURAL BASIS OF ENDOCANNABINOID OXYGENATION BY       
JRNL        TITL 2 CYCLOOXYGENASE-2.                                            
JRNL        REF    J.BIOL.CHEM.                  V. 286 20736 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21489986                                                     
JRNL        DOI    10.1074/JBC.M111.230367                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -6.000                         
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 56810                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3024                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4092                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 213                          
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8864                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 378                                     
REMARK   3   SOLVENT ATOMS            : 666                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.59000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.90000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.214         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.139         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.588        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9577 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13010 ; 1.686 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1116 ; 5.593 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   443 ;36.572 ;23.973       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1500 ;15.022 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;14.231 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1384 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7330 ; 0.006 ; 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):  5534 ; 0.484 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8995 ; 0.947 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4043 ; 1.922 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4004 ; 3.154 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    33        A    68                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3614  37.6811  60.0257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0862 T22:    .2777                                     
REMARK   3      T33:    .1911 T12:    .0357                                     
REMARK   3      T13:    .0424 T23:    .0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7509 L22:   4.7279                                     
REMARK   3      L33:   1.9305 L12:   1.2304                                     
REMARK   3      L13:    .2958 L23:    .6976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0338 S12:   -.2056 S13:    .0818                       
REMARK   3      S21:    .0117 S22:    .0574 S23:    .3388                       
REMARK   3      S31:   -.1328 S32:   -.2671 S33:   -.0236                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    69        A    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1392  18.5827  64.2743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3094 T22:    .4607                                     
REMARK   3      T33:    .5978 T12:   -.1152                                     
REMARK   3      T13:    .0446 T23:    .1921                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5129 L22:   8.8648                                     
REMARK   3      L33:   4.0646 L12:  -1.5016                                     
REMARK   3      L13:   4.3088 L23:  -1.3940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .4999 S12:   -.6573 S13:  -1.5543                       
REMARK   3      S21:    .2194 S22:    .3481 S23:    .2391                       
REMARK   3      S31:    .8190 S32:   -.6551 S33:   -.8480                       
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    88        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5023   3.0380  66.2726              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1395 T22:    .2519                                     
REMARK   3      T33:    .3979 T12:   -.0761                                     
REMARK   3      T13:    .0174 T23:   -.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4499 L22:   7.0282                                     
REMARK   3      L33:   9.6039 L12:   -.7632                                     
REMARK   3      L13:  -2.4837 L23:    .0533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.3104 S12:    .0661 S13:   -.2207                       
REMARK   3      S21:    .0010 S22:   -.0914 S23:    .6362                       
REMARK   3      S31:    .3721 S32:   -.4329 S33:    .4018                       
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   148                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3721  33.7485  53.8737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0199 T22:    .0257                                     
REMARK   3      T33:    .0421 T12:    .0087                                     
REMARK   3      T13:    .0051 T23:    .0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5296 L22:   4.0309                                     
REMARK   3      L33:   4.4712 L12:   -.6903                                     
REMARK   3      L13:   1.0571 L23:  -1.0124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0856 S12:   -.0853 S13:   -.1437                       
REMARK   3      S21:   -.0001 S22:    .0546 S23:    .1835                       
REMARK   3      S31:    .1472 S32:   -.1654 S33:    .0310                       
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   149        A   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4715  29.8675  71.0404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0659 T22:    .0447                                     
REMARK   3      T33:    .0625 T12:    .0001                                     
REMARK   3      T13:   -.0075 T23:   -.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5428 L22:   1.1306                                     
REMARK   3      L33:   1.2993 L12:   -.9024                                     
REMARK   3      L13:   -.0665 L23:   -.0230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0566 S12:   -.2152 S13:    .1574                       
REMARK   3      S21:    .1477 S22:    .0875 S23:   -.0865                       
REMARK   3      S31:   -.1715 S32:    .0050 S33:   -.0309                       
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   234        A   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6000  18.9340  55.6582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0091 T22:    .0354                                     
REMARK   3      T33:    .1469 T12:   -.0008                                     
REMARK   3      T13:    .0336 T23:   -.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2463 L22:    .7350                                     
REMARK   3      L33:   5.1889 L12:    .1403                                     
REMARK   3      L13:   1.0979 L23:   -.2700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0007 S12:    .0147 S13:    .2473                       
REMARK   3      S21:   -.0579 S22:   -.0060 S23:   -.1701                       
REMARK   3      S31:   -.0093 S32:    .3084 S33:    .0053                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   269        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4741  25.8712  65.9961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0951 T22:    .1726                                     
REMARK   3      T33:    .2843 T12:    .0061                                     
REMARK   3      T13:    .0103 T23:   -.0875                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9029 L22:   1.9913                                     
REMARK   3      L33:   4.8805 L12:   1.0328                                     
REMARK   3      L13:   -.9476 L23:  -2.7585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0349 S12:   -.4222 S13:    .7273                       
REMARK   3      S21:    .0828 S22:   -.1144 S23:   -.2686                       
REMARK   3      S31:   -.2369 S32:    .3877 S33:    .1493                       
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   302        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.3820   9.3251  52.2909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0879 T22:    .0404                                     
REMARK   3      T33:    .1041 T12:    .0458                                     
REMARK   3      T13:    .0163 T23:    .0403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0726 L22:   1.2402                                     
REMARK   3      L33:   3.7371 L12:   -.7634                                     
REMARK   3      L13:    .1344 L23:   -.2964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0523 S12:   -.0332 S13:   -.2003                       
REMARK   3      S21:   -.2426 S22:   -.1077 S23:   -.0189                       
REMARK   3      S31:    .2505 S32:    .2746 S33:    .0554                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   345        A   399                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1736  15.0791  65.3407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0403 T22:    .0661                                     
REMARK   3      T33:    .1018 T12:    .0008                                     
REMARK   3      T13:    .0380 T23:    .0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8467 L22:   1.1479                                     
REMARK   3      L33:   2.2561 L12:   -.5718                                     
REMARK   3      L13:    .1558 L23:   -.4708                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0346 S12:   -.1533 S13:   -.1180                       
REMARK   3      S21:    .0595 S22:    .0732 S23:    .1644                       
REMARK   3      S31:    .2160 S32:   -.1295 S33:   -.0386                       
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   400        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.3081  16.2265  78.4138              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1255 T22:    .2286                                     
REMARK   3      T33:    .0964 T12:    .0442                                     
REMARK   3      T13:   -.0259 T23:    .0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5646 L22:   5.6060                                     
REMARK   3      L33:   3.1686 L12:   2.0761                                     
REMARK   3      L13:    .2477 L23:   2.3191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0246 S12:   -.4605 S13:    .0587                       
REMARK   3      S21:    .4013 S22:    .0660 S23:   -.1657                       
REMARK   3      S31:   -.0360 S32:    .4118 S33:   -.0414                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   430        A   553                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5427  24.8996  72.7338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0802 T22:    .1285                                     
REMARK   3      T33:    .0705 T12:    .0189                                     
REMARK   3      T13:    .0280 T23:    .0362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9894 L22:    .9583                                     
REMARK   3      L33:   1.0838 L12:   -.6586                                     
REMARK   3      L13:   -.3815 L23:    .3450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0668 S12:   -.2483 S13:   -.0645                       
REMARK   3      S21:    .1173 S22:    .0956 S23:    .1097                       
REMARK   3      S31:   -.0113 S32:   -.1357 S33:   -.0288                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   554        A   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9024   3.3220  64.0081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1518 T22:    .0286                                     
REMARK   3      T33:    .1407 T12:   -.0434                                     
REMARK   3      T13:    .0013 T23:    .0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1016 L22:   2.3949                                     
REMARK   3      L33:   4.1812 L12:  -1.5448                                     
REMARK   3      L13:   -.8540 L23:    .1440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0147 S12:   -.1321 S13:   -.2621                       
REMARK   3      S21:    .0511 S22:    .1118 S23:    .1568                       
REMARK   3      S31:    .5691 S32:   -.1922 S33:   -.0971                       
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    67                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.7671   1.6954  33.1921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .4075 T22:    .1384                                     
REMARK   3      T33:    .1827 T12:    .0604                                     
REMARK   3      T13:   -.0447 T23:   -.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5350 L22:    .8695                                     
REMARK   3      L33:   2.5786 L12:    .5646                                     
REMARK   3      L13:  -1.4207 L23:   -.5141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1678 S12:    .0540 S13:   -.2489                       
REMARK   3      S21:   -.2633 S22:   -.1716 S23:    .0210                       
REMARK   3      S31:    .5233 S32:    .1958 S33:    .0038                       
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    68        B    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1809   -.4239  28.2809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .6101 T22:    .3955                                     
REMARK   3      T33:    .5815 T12:   -.1258                                     
REMARK   3      T13:   -.1173 T23:   -.0877                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.6495 L22:   5.3282                                     
REMARK   3      L33:   2.6176 L12:  -4.6137                                     
REMARK   3      L13:   2.3030 L23:  -3.5627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2427 S12:   -.1198 S13:   -.4975                       
REMARK   3      S21:   -.3853 S22:    .4513 S23:   1.1576                       
REMARK   3      S31:    .3170 S32:   -.5582 S33:   -.6940                       
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    88        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1326  18.5317  26.2892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3041 T22:    .2559                                     
REMARK   3      T33:    .4039 T12:   -.1373                                     
REMARK   3      T13:   -.0402 T23:   -.0949                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5950 L22:   5.2728                                     
REMARK   3      L33:   9.1195 L12:  -1.8336                                     
REMARK   3      L13:  -1.5144 L23:   1.6220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1152 S12:    .3482 S13:   -.6173                       
REMARK   3      S21:   -.2314 S22:   -.2444 S23:    .4550                       
REMARK   3      S31:    .3708 S32:   -.3834 S33:    .3596                       
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   151                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8407  19.2922  38.9279              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0785 T22:    .0253                                     
REMARK   3      T33:    .0221 T12:    .0217                                     
REMARK   3      T13:   -.0005 T23:   -.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2020 L22:   2.9709                                     
REMARK   3      L33:   4.9912 L12:  -1.9742                                     
REMARK   3      L13:    .6198 L23:   -.2735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1286 S12:    .0755 S13:   -.1094                       
REMARK   3      S21:   -.1765 S22:   -.1737 S23:    .0703                       
REMARK   3      S31:    .3126 S32:   -.1522 S33:    .0451                       
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   152        B   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9940  27.5285  21.8430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0899 T22:    .1040                                     
REMARK   3      T33:    .0793 T12:    .0274                                     
REMARK   3      T13:    .0128 T23:    .0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0999 L22:   1.3317                                     
REMARK   3      L33:   1.7714 L12:   -.9542                                     
REMARK   3      L13:   -.0769 L23:    .0832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1159 S12:    .1712 S13:    .0567                       
REMARK   3      S21:   -.1999 S22:   -.0758 S23:   -.1256                       
REMARK   3      S31:    .1047 S32:    .2116 S33:   -.0401                       
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   231        B   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5601  51.4507  38.5446              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0674 T22:    .0376                                     
REMARK   3      T33:    .1146 T12:   -.0204                                     
REMARK   3      T13:    .0074 T23:    .0482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3375 L22:   3.7454                                     
REMARK   3      L33:   3.5589 L12:   -.2740                                     
REMARK   3      L13:   1.0351 L23:   -.5012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0361 S12:    .1996 S13:    .3299                       
REMARK   3      S21:    .2852 S22:   -.0596 S23:   -.2143                       
REMARK   3      S31:   -.3951 S32:    .2799 S33:    .0958                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   269        B   308                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2076  50.0868  28.8326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2884 T22:    .2745                                     
REMARK   3      T33:    .2820 T12:   -.2124                                     
REMARK   3      T13:    .1635 T23:   -.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0448 L22:   3.2059                                     
REMARK   3      L33:   1.5565 L12:   1.7365                                     
REMARK   3      L13:   1.1096 L23:   -.4222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1044 S12:    .2237 S13:    .3457                       
REMARK   3      S21:   -.4530 S22:    .0677 S23:   -.4496                       
REMARK   3      S31:   -.3626 S32:    .5490 S33:    .0367                       
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   309        B   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1410  34.0334  36.3893              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0134 T22:    .0508                                     
REMARK   3      T33:    .0805 T12:   -.0042                                     
REMARK   3      T13:   -.0107 T23:    .0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9869 L22:   1.7295                                     
REMARK   3      L33:   1.9375 L12:   -.4252                                     
REMARK   3      L13:    .0566 L23:    .3998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0515 S12:    .1229 S13:   -.0567                       
REMARK   3      S21:   -.0938 S22:   -.0421 S23:    .2341                       
REMARK   3      S31:    .0936 S32:   -.2025 S33:   -.0094                       
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   430                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5702  48.4233  14.6656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1756 T22:    .2979                                     
REMARK   3      T33:    .1648 T12:    .0712                                     
REMARK   3      T13:    .0449 T23:    .1353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4054 L22:   6.7062                                     
REMARK   3      L33:   2.6850 L12:    .2779                                     
REMARK   3      L13:  -1.0794 L23:    .6193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2080 S12:    .4234 S13:    .3809                       
REMARK   3      S21:   -.5078 S22:   -.0699 S23:   -.2502                       
REMARK   3      S31:   -.2758 S32:    .0680 S33:   -.1381                       
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   431        B   457                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7593  29.8030  13.6802              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2057 T22:    .2171                                     
REMARK   3      T33:    .0505 T12:    .1109                                     
REMARK   3      T13:    .0192 T23:   -.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3548 L22:   1.4357                                     
REMARK   3      L33:   1.2734 L12:   -.8588                                     
REMARK   3      L13:   1.1587 L23:  -1.2760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0987 S12:    .1876 S13:    .0762                       
REMARK   3      S21:   -.1773 S22:   -.1354 S23:   -.0391                       
REMARK   3      S31:    .1451 S32:    .2109 S33:    .0367                       
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   458        B   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3925  16.5373  16.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2530 T22:    .1277                                     
REMARK   3      T33:    .0916 T12:    .0490                                     
REMARK   3      T13:   -.0403 T23:   -.0420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8198 L22:   2.2117                                     
REMARK   3      L33:   3.0570 L12:   -.6704                                     
REMARK   3      L13:    .2042 L23:   -.0586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1255 S12:    .2739 S13:   -.2188                       
REMARK   3      S21:   -.3241 S22:   -.1260 S23:    .1387                       
REMARK   3      S31:    .3377 S32:   -.0552 S33:    .0005                       
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):   6.6738  38.1478  35.8958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0106 T22:    .0550                                     
REMARK   3      T33:    .1035 T12:    .0025                                     
REMARK   3      T13:   -.0004 T23:    .0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2300 L22:   1.6681                                     
REMARK   3      L33:   3.5260 L12:    .0023                                     
REMARK   3      L13:    .0947 L23:  -1.1794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0753 S12:    .1345 S13:   -.0480                       
REMARK   3      S21:   -.0589 S22:    .0796 S23:    .2236                       
REMARK   3      S31:    .0874 S32:   -.3002 S33:   -.1548                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3OLU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061278.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-09                          
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) : 0.9780                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
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   : 59835                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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   (%): 53.47                                     
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       60.65600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.87700            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.01100            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.65600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.87700            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.01100            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.65600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.87700            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.01100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.65600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.87700            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.01100            
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: 14160 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     GLN A   583                                                      
REMARK 465     ASP A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     THR A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     THR A   592                                                      
REMARK 465     ILE A   593                                                      
REMARK 465     ASN A   594                                                      
REMARK 465     ALA A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     HIS A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ARG A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     ILE A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     VAL A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     ALA B    28                                                      
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     ASN B   594                                                      
REMARK 465     ALA B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     SER B   598                                                      
REMARK 465     HIS B   599                                                      
REMARK 465     SER B   600                                                      
REMARK 465     ARG B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     ASP B   603                                                      
REMARK 465     ASP B   604                                                      
REMARK 465     ILE B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     VAL B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     SER B   615                                                      
REMARK 465     THR B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     LEU B   618                                                      
REMARK 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     LEU A  75    CG   CD1  CD2                                       
REMARK 470     LYS A  79    CD   CE   NZ                                        
REMARK 470     LYS A  83    CE   NZ                                             
REMARK 470     GLU A 170    OE1  OE2                                            
REMARK 470     LYS A 215    CD   CE   NZ                                        
REMARK 470     ASP A 239    OD1  OD2                                            
REMARK 470     LYS A 358    CE   NZ                                             
REMARK 470     LYS A 405    CD   CE   NZ                                        
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     LYS A 485    CD   CE   NZ                                        
REMARK 470     LYS A 557    NZ                                                  
REMARK 470     GLN B  54    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  75    CG   CD1  CD2                                       
REMARK 470     ILE B  78    CD1                                                 
REMARK 470     LYS B  79    CD   CE   NZ                                        
REMARK 470     LEU B  80    CD1  CD2                                            
REMARK 470     LEU B  82    CD1  CD2                                            
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     LYS B  97    CE   NZ                                             
REMARK 470     LYS B 169    CD   CE   NZ                                        
REMARK 470     GLU B 170    CD   OE1  OE2                                       
REMARK 470     LYS B 175    NZ                                                  
REMARK 470     GLU B 186    CD   OE1  OE2                                       
REMARK 470     LYS B 215    CG   CD   CE   NZ                                   
REMARK 470     LYS B 267    CG   CD   CE   NZ                                   
REMARK 470     GLU B 272    OE1  OE2                                            
REMARK 470     GLU B 281    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 358    CE   NZ                                             
REMARK 470     LYS B 405    CD   CE   NZ                                        
REMARK 470     LYS B 492    NZ                                                  
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    LEU B 531   CA  -  CB  -  CG  ANGL. DEV. =  15.7 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    LYS A  83      120.52    -37.40                                   
REMARK 500    TYR A 122       -8.56    -53.22                                   
REMARK 500    THR A 129      -94.17   -121.59                                   
REMARK 500    TRP A 387       40.16    -95.10                                   
REMARK 500    GLU A 398     -114.02     60.30                                   
REMARK 500    TYR A 409       13.38     59.58                                   
REMARK 500    ASN A 410       79.81   -100.22                                   
REMARK 500    ASN A 439       15.36   -142.52                                   
REMARK 500    SER A 471       32.32     70.84                                   
REMARK 500    SER A 496      -50.86     68.72                                   
REMARK 500    CYS A 575       66.03     39.73                                   
REMARK 500    ARG B  61       11.39     59.89                                   
REMARK 500    THR B 129      -91.08   -122.84                                   
REMARK 500    ARG B 185      -98.41    -89.61                                   
REMARK 500    ASP B 249       16.94     57.37                                   
REMARK 500    TRP B 387       45.74    -87.30                                   
REMARK 500    GLU B 398     -123.45     60.60                                   
REMARK 500    TYR B 409       10.86     57.81                                   
REMARK 500    SER B 496      -45.26     67.78                                   
REMARK 500    SER B 579     -174.89   -174.85                                   
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 750        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 916        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH B 917        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH B 935        DISTANCE =  5.88 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   86.8                                              
REMARK 620 3 COH B 619   NB   91.0  90.5                                        
REMARK 620 4 COH B 619   NC   98.4 174.1  86.7                                  
REMARK 620 5 COH B 619   ND   91.3  92.0 176.7  90.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             COH A 620  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 COH A 620   NA   96.1                                              
REMARK 620 3 COH A 620   NB   98.4  83.6                                        
REMARK 620 4 COH A 620   NC   92.2 169.7  89.2                                  
REMARK 620 5 COH A 620   ND   84.4  94.8 176.9  91.9                            
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 EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 14                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MDL   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL BOUND TO          
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                       
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE             
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                           
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF EICOSAPENTAENOIC ACID BOUND TO            
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                       
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DOCOSAHEXAENOIC ACID BOUND TO             
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                       
REMARK 900 RELATED ID: 3KRK   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE             
REMARK 900 CYCLOOXYGENASE CHANNEL OF L531F MURINE COX-2                         
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE                   
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF PGHS-1                                 
REMARK 900 RELATED ID: 3OLT   RELATED DB: PDB                                   
DBREF  3OLU A   35   618  UNP    Q05769   PGH2_MOUSE      20    604             
DBREF  3OLU B   35   618  UNP    Q05769   PGH2_MOUSE      20    604             
SEQADV 3OLU ALA A   28  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS A  513  UNP  Q05769    ARG   499 ENGINEERED MUTATION            
SEQADV 3OLU ALA B   28  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3OLU HIS B  513  UNP  Q05769    ARG   499 ENGINEERED MUTATION            
SEQRES   1 A  592  ALA HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO          
SEQRES   2 A  592  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP          
SEQRES   3 A  592  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY          
SEQRES   4 A  592  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS          
SEQRES   5 A  592  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE          
SEQRES   6 A  592  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN          
SEQRES   7 A  592  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU          
SEQRES   8 A  592  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR          
SEQRES   9 A  592  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER          
SEQRES  10 A  592  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA          
SEQRES  11 A  592  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS          
SEQRES  12 A  592  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU          
SEQRES  13 A  592  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN          
SEQRES  14 A  592  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN          
SEQRES  15 A  592  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR          
SEQRES  16 A  592  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR          
SEQRES  17 A  592  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE          
SEQRES  18 A  592  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU          
SEQRES  19 A  592  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET          
SEQRES  20 A  592  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA          
SEQRES  21 A  592  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET          
SEQRES  22 A  592  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL          
SEQRES  23 A  592  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP          
SEQRES  24 A  592  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY          
SEQRES  25 A  592  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS          
SEQRES  26 A  592  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU          
SEQRES  27 A  592  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE          
SEQRES  28 A  592  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU          
SEQRES  29 A  592  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER          
SEQRES  30 A  592  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU          
SEQRES  31 A  592  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN          
SEQRES  32 A  592  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE          
SEQRES  33 A  592  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER          
SEQRES  34 A  592  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS          
SEQRES  35 A  592  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU          
SEQRES  36 A  592  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU          
SEQRES  37 A  592  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU          
SEQRES  38 A  592  LEU VAL GLU LYS PRO HIS PRO ASP ALA ILE PHE GLY GLU          
SEQRES  39 A  592  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY          
SEQRES  40 A  592  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS          
SEQRES  41 A  592  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE          
SEQRES  42 A  592  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL          
SEQRES  43 A  592  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO          
SEQRES  44 A  592  GLN PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER          
SEQRES  45 A  592  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE          
SEQRES  46 A  592  LYS ARG ARG SER THR GLU LEU                                  
SEQRES   1 B  592  ALA HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO          
SEQRES   2 B  592  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP          
SEQRES   3 B  592  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY          
SEQRES   4 B  592  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS          
SEQRES   5 B  592  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE          
SEQRES   6 B  592  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN          
SEQRES   7 B  592  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU          
SEQRES   8 B  592  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR          
SEQRES   9 B  592  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER          
SEQRES  10 B  592  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA          
SEQRES  11 B  592  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS          
SEQRES  12 B  592  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU          
SEQRES  13 B  592  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN          
SEQRES  14 B  592  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN          
SEQRES  15 B  592  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR          
SEQRES  16 B  592  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR          
SEQRES  17 B  592  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE          
SEQRES  18 B  592  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU          
SEQRES  19 B  592  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET          
SEQRES  20 B  592  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA          
SEQRES  21 B  592  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET          
SEQRES  22 B  592  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL          
SEQRES  23 B  592  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP          
SEQRES  24 B  592  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY          
SEQRES  25 B  592  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS          
SEQRES  26 B  592  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU          
SEQRES  27 B  592  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE          
SEQRES  28 B  592  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU          
SEQRES  29 B  592  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER          
SEQRES  30 B  592  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU          
SEQRES  31 B  592  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN          
SEQRES  32 B  592  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE          
SEQRES  33 B  592  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER          
SEQRES  34 B  592  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS          
SEQRES  35 B  592  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU          
SEQRES  36 B  592  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU          
SEQRES  37 B  592  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU          
SEQRES  38 B  592  LEU VAL GLU LYS PRO HIS PRO ASP ALA ILE PHE GLY GLU          
SEQRES  39 B  592  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY          
SEQRES  40 B  592  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS          
SEQRES  41 B  592  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE          
SEQRES  42 B  592  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL          
SEQRES  43 B  592  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO          
SEQRES  44 B  592  GLN PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER          
SEQRES  45 B  592  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE          
SEQRES  46 B  592  LYS ARG ARG SER THR GLU LEU                                  
MODRES 3OLU ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3OLU ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3OLU ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3OLU ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3OLU ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3OLU ASN B  144  ASN  GLYCOSYLATION SITE                                 
HET    EDO  A   1       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   5       4                                                       
HET    EDO  A  12       4                                                       
HET    EDO  A  13       4                                                       
HET    EDO  A  14       4                                                       
HET    EDO  A  15       4                                                       
HET    1AG  A 619      27                                                       
HET    COH  A 620      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  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  11       4                                                       
HET    1AG  B   1      27                                                       
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    MAN  B 673      11                                                       
HET    NAG  B 681      14                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     1AG (2S)-2,3-DIHYDROXYPROPYL (5Z,8Z,11Z,14Z)-ICOSA-5,8,11,           
HETNAM   2 1AG  14-TETRAENOATE                                                  
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    14(C2 H6 O2)                                                 
FORMUL  10  1AG    2(C23 H38 O4)                                                
FORMUL  11  COH    2(C34 H32 CO N4 O4)                                          
FORMUL  12  NAG    10(C8 H15 N O6)                                              
FORMUL  13  MAN    2(C6 H12 O6)                                                 
FORMUL  15  BOG    C14 H28 O6                                                   
FORMUL  28  HOH   *666(H2 O)                                                    
HELIX    1   1 GLU A   73  LYS A   83  1                                  11    
HELIX    2   2 THR A   85  THR A   94  1                                  10    
HELIX    3   3 PHE A   96  ILE A  105A 1                                  11    
HELIX    4   4 ILE A  105A ARG A  120  1                                  16    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  ARG A  245  1                                   9    
HELIX   10  10 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 PRO A  280  GLN A  284  5                                   5    
HELIX   12  12 VAL A  291  LEU A  294  5                                   4    
HELIX   13  13 VAL A  295  HIS A  320  1                                  26    
HELIX   14  14 GLY A  324  ASP A  347  1                                  24    
HELIX   15  15 ASP A  347  GLY A  354  1                                   8    
HELIX   16  16 ASP A  362  PHE A  367  5                                   6    
HELIX   17  17 ALA A  378  TYR A  385  1                                   8    
HELIX   18  18 HIS A  386  LEU A  391  5                                   6    
HELIX   19  19 SER A  403  LEU A  408  1                                   6    
HELIX   20  20 ASN A  410  GLN A  429  1                                  20    
HELIX   21  21 PRO A  441  ALA A  443  5                                   3    
HELIX   22  22 VAL A  444  MET A  458  1                                  15    
HELIX   23  23 SER A  462  PHE A  470  1                                   9    
HELIX   24  24 SER A  477  GLY A  483  1                                   7    
HELIX   25  25 LYS A  485  SER A  496  1                                  12    
HELIX   26  26 ASP A  497  MET A  501  5                                   5    
HELIX   27  27 GLU A  502  GLU A  510  1                                   9    
HELIX   28  28 GLY A  519  GLY A  536  1                                  18    
HELIX   29  29 ASN A  537  SER A  541  5                                   5    
HELIX   30  30 LYS A  546  GLY A  551  5                                   6    
HELIX   31  31 GLY A  552  THR A  561  1                                  10    
HELIX   32  32 SER A  563  VAL A  572  1                                  10    
HELIX   33  33 GLU B   73  LYS B   83  1                                  11    
HELIX   34  34 THR B   85  THR B   94  1                                  10    
HELIX   35  35 PHE B   96  ASN B  104  1                                   9    
HELIX   36  36 ILE B  105A TYR B  122  1                                  18    
HELIX   37  37 SER B  138  ASN B  144  1                                   7    
HELIX   38  38 ASP B  173  LEU B  182  1                                  10    
HELIX   39  39 ASN B  195  HIS B  207  1                                  13    
HELIX   40  40 LEU B  230  GLY B  235  1                                   6    
HELIX   41  41 THR B  237  ARG B  245  1                                   9    
HELIX   42  42 THR B  265  GLN B  270  1                                   6    
HELIX   43  43 PRO B  280  GLN B  284  5                                   5    
HELIX   44  44 VAL B  295  HIS B  320  1                                  26    
HELIX   45  45 GLY B  324  ASP B  347  1                                  24    
HELIX   46  46 ASP B  347  GLY B  354  1                                   8    
HELIX   47  47 ASP B  362  PHE B  367  5                                   6    
HELIX   48  48 ALA B  378  TYR B  385  1                                   8    
HELIX   49  49 HIS B  386  LEU B  391  5                                   6    
HELIX   50  50 SER B  403  LEU B  408  1                                   6    
HELIX   51  51 ASN B  411  GLN B  429  1                                  19    
HELIX   52  52 PRO B  441  ALA B  443  5                                   3    
HELIX   53  53 VAL B  444  MET B  458  1                                  15    
HELIX   54  54 SER B  462  PHE B  470  1                                   9    
HELIX   55  55 SER B  477  GLY B  483  1                                   7    
HELIX   56  56 LYS B  485  SER B  496  1                                  12    
HELIX   57  57 ASP B  497  MET B  501  5                                   5    
HELIX   58  58 GLU B  502  GLU B  510  1                                   9    
HELIX   59  59 GLY B  519  GLY B  536  1                                  18    
HELIX   60  60 ASN B  537  SER B  541  5                                   5    
HELIX   61  61 LYS B  546  GLY B  551  5                                   6    
HELIX   62  62 GLY B  552  THR B  561  1                                  10    
HELIX   63  63 SER B  563  VAL B  572  1                                  10    
SHEET    1   A 2 GLU A  46  SER A  49  0                                        
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46           
SHEET    1   B 2 PHE A  64  TYR A  65  0                                        
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65           
SHEET    1   C 2 GLN A 255  ILE A 257  0                                        
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257           
SHEET    1   D 2 PHE A 395  ILE A 397  0                                        
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  GLN A 400   N  ILE A 397           
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 THR B 212  ASP B 213  0                                        
SHEET    2   G 2 GLY B 217  THR B 221 -1  O  GLY B 217   N  ASP B 213           
SHEET    1   H 2 GLN B 255  ILE B 257  0                                        
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  GLU B 260   N  ILE B 257           
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  2.07  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.05  
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  2.05  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.07  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.04  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.04  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.06  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.07  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.36  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.36  
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.37  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.37  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.39  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.43  
LINK         ND2 ASN B 144                 C1  NAG B 671     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  1.45  
LINK         O4  NAG B 672                 C1  MAN B 673     1555   1555  1.46  
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.47  
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.47  
LINK         NE2AHIS B 388                CO   COH B 619     1555   1555  2.17  
LINK         NE2 HIS A 388                CO   COH A 620     1555   1555  2.46  
LINK         ND2 ASN A  68                 O5  NAG A 661     1555   1555  1.43  
LINK         ND2 ASN B  68                 O5  NAG B 661     1555   1555  1.49  
LINK         ND2 ASN A 410                 O5  NAG A 681     1555   1555  1.50  
LINK         ND2 ASN B 410                 O5  NAG B 681     1555   1555  1.49  
LINK         ND2 ASN A 144                 O5  NAG A 671     1555   1555  1.53  
CISPEP   1 SER A  126    PRO A  127          0        -0.86                     
CISPEP   2 SER B  126    PRO B  127          0        -1.91                     
SITE     1 AC1  3 ASP A 157  CYS A 159  LYS A 459                               
SITE     1 AC2  6 PRO A 162  SER A 455  ARG A 456  LYS A 459                    
SITE     2 AC2  6 TYR A 460  HOH A 768                                          
SITE     1 AC3  2 HOH A 905  MAN B 673                                          
SITE     1 AC4  7 GLU A 308  ARG A 311  GLU A 339  SER A 566                    
SITE     2 AC4  7 LEU A 567  ASN A 570  HOH A 645                               
SITE     1 AC5  5 LYS A 251  TYR A 254  ASN A 310  HOH A 831                    
SITE     2 AC5  5 HOH A 858                                                     
SITE     1 AC6  4 ASP A 239  ARG A 240  LYS A 243  GLU A 272                    
SITE     1 AC7 10 HIS A  90  GLN A 192  LEU A 352  SER A 353                    
SITE     2 AC7 10 HIS A 513  ALA A 516  ILE A 517  PHE A 518                    
SITE     3 AC7 10 VAL A 523  HOH A 844                                          
SITE     1 AC8 18 ARG A 120  PHE A 205  PHE A 209  TYR A 348                    
SITE     2 AC8 18 VAL A 349  SER A 353  TYR A 355  ILE A 377                    
SITE     3 AC8 18 PHE A 381  TYR A 385  TRP A 387  MET A 522                    
SITE     4 AC8 18 GLY A 526  ALA A 527  SER A 530  LEU A 531                    
SITE     5 AC8 18 GLY A 533  LEU A 534                                          
SITE     1 AC9 15 ALA A 199  GLN A 203  HIS A 207  PHE A 210                    
SITE     2 AC9 15 LYS A 211  THR A 212  VAL A 295  ASN A 382                    
SITE     3 AC9 15 TYR A 385  HIS A 386  HIS A 388  LEU A 391                    
SITE     4 AC9 15 VAL A 447  HOH A 724  HOH A 909                               
SITE     1 BC1  5 TYR A  55  GLU A  67  ASN A  68  NAG A 662                    
SITE     2 BC1  5 HOH A 811                                                     
SITE     1 BC2  2 NAG A 661  HOH A 667                                          
SITE     1 BC3 10 HOH A  27  GLU A 140  ASN A 144  TYR A 147                    
SITE     2 BC3 10 ARG A 216  PHE A 220  HOH A 639  HOH A 670                    
SITE     3 BC3 10 NAG A 672  LEU B 238                                          
SITE     1 BC4  3 ARG A 216  NAG A 671  MAN A 673                               
SITE     1 BC5  1 NAG A 672                                                     
SITE     1 BC6  7 GLN A 406  ASN A 410  SER A 412  ILE A 413                    
SITE     2 BC6  7 GLU A 416  HOH A 813  HOH A 878                               
SITE     1 BC7 12 GLU A 179  LYS A 180  ARG A 184  ARG A 185                    
SITE     2 BC7 12 ARG A 438  GLU A 486  GLU A 490  GLU B 179                    
SITE     3 BC7 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445                    
SITE     1 BC8  8 HIS B  90  GLN B 192  LEU B 352  SER B 353                    
SITE     2 BC8  8 ALA B 516  ILE B 517  PHE B 518  HOH B 659                    
SITE     1 BC9  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310                    
SITE     2 BC9  6 HOH B 760  HOH B 862                                          
SITE     1 CC1  5 PRO B 162  ARG B 456  LYS B 459  TYR B 460                    
SITE     2 CC1  5 HOH B 649                                                     
SITE     1 CC2  7 PRO A 547  SER A 548  GLU A 553  MET B  48                    
SITE     2 CC2  7 LYS B  56  ASP B  58  HOH B 838                               
SITE     1 CC3  7 GLU B 308  ARG B 311  GLU B 339  SER B 566                    
SITE     2 CC3  7 LEU B 567  ASN B 570  HOH B 677                               
SITE     1 CC4  3 LEU A 145  SER B 143  HOH B 652                               
SITE     1 CC5  5 ASP B 239  ARG B 240  LYS B 243  VAL B 271                    
SITE     2 CC5  5 GLU B 272                                                     
SITE     1 CC6 16 ARG B 120  PHE B 205  PHE B 209  VAL B 349                    
SITE     2 CC6 16 TYR B 355  ASN B 375  ILE B 377  PHE B 381                    
SITE     3 CC6 16 TYR B 385  GLY B 526  ALA B 527  SER B 530                    
SITE     4 CC6 16 LEU B 531  GLY B 533  LEU B 534  HOH B 789                    
SITE     1 CC7 14 ALA B 199  PHE B 200  GLN B 203  HIS B 207                    
SITE     2 CC7 14 PHE B 210  LYS B 211  THR B 212  HIS B 214                    
SITE     3 CC7 14 VAL B 295  ASN B 382  TYR B 385  HIS B 386                    
SITE     4 CC7 14 HIS B 388  LEU B 391                                          
SITE     1 CC8  5 TYR B  55  GLU B  67  ASN B  68  NAG B 662                    
SITE     2 CC8  5 HOH B 730                                                     
SITE     1 CC9  3 NAG B 661  HOH B 732  HOH B 922                               
SITE     1 DC1  9 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 DC1  9 PHE B 220  HOH B 627  NAG B 672  HOH B 701                    
SITE     3 DC1  9 HOH B 703                                                     
SITE     1 DC2  5 HOH A 679  ARG B 216  NAG B 671  MAN B 673                    
SITE     2 DC2  5 HOH B 674                                                     
SITE     1 DC3  7 EDO A   5  HOH A 905  HOH B 644  HOH B 651                    
SITE     2 DC3  7 HOH B 657  NAG B 672  HOH B 674                               
SITE     1 DC4  5 ASN B 410  SER B 412  ILE B 413  GLU B 416                    
SITE     2 DC4  5 HOH B 914                                                     
CRYST1  121.312  131.754  180.022  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      0.008243  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007590  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005555        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system