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Database: PDB
Entry: 3QH0
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Original site: 3QH0 
HEADER    OXIDOREDUCTASE                          25-JAN-11   3QH0              
TITLE     X-RAY CRYSTAL STRUCTURE OF PALMITIC ACID BOUND TO THE CYCLOOXYGENASE  
TITLE    2 CHANNEL OF CYCLOOXYGENASE-2                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUE 1-608;                                         
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED           
COMPND   6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-         
COMPND   7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2    
COMPND   8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE       
COMPND   9 SYNTHASE 2, TIS10 PROTEIN;                                           
COMPND  10 EC: 1.14.99.1;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 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: COX-2, COX2, PGHS-B, PTGS2, TIS10;                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    BIOLOGICAL DIMER, OXIDOREDUCTASE, N-GLYCOSYLATION, MONOTOPIC MEMBRANE 
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI                                             
REVDAT   2   08-JUN-11 3QH0    1       JRNL                                     
REVDAT   1   13-APR-11 3QH0    0                                                
JRNL        AUTH   L.DONG,A.J.VECCHIO,N.P.SHARMA,B.J.JURBAN,M.G.MALKOWSKI,      
JRNL        AUTH 2 W.L.SMITH                                                    
JRNL        TITL   HUMAN CYCLOOXYGENASE-2 IS A SEQUENCE HOMODIMER THAT          
JRNL        TITL 2 FUNCTIONS AS A CONFORMATIONAL HETERODIMER.                   
JRNL        REF    J.BIOL.CHEM.                  V. 286 19035 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21467029                                                     
JRNL        DOI    10.1074/JBC.M111.231969                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 77928                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4122                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5576                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 310                          
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8833                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 377                                     
REMARK   3   SOLVENT ATOMS            : 753                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.177         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.901         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9570 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13009 ; 1.329 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1129 ; 5.692 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   446 ;37.361 ;23.924       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1482 ;13.632 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;14.880 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1380 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7344 ; 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):  5565 ; 0.502 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9044 ; 0.970 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4005 ; 1.841 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3952 ; 3.063 ; 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):   1.3394  37.1273  59.8920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0594 T22:    .2753                                     
REMARK   3      T33:    .1489 T12:    .0664                                     
REMARK   3      T13:    .0495 T23:    .0758                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0567 L22:   3.8869                                     
REMARK   3      L33:   1.9850 L12:   -.0687                                     
REMARK   3      L13:    .1704 L23:   1.0562                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0529 S12:   -.2515 S13:    .0305                       
REMARK   3      S21:    .0506 S22:    .1627 S23:    .0524                       
REMARK   3      S31:   -.1368 S32:   -.5552 S33:   -.1097                       
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    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5201  18.1978  63.7919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2147 T22:    .5097                                     
REMARK   3      T33:    .4432 T12:   -.1428                                     
REMARK   3      T13:    .0409 T23:    .1654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9645 L22:   9.9081                                     
REMARK   3      L33:   4.1743 L12:  -3.2354                                     
REMARK   3      L13:   4.1029 L23:  -5.1141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2881 S12:   -.3324 S13:   -.8992                       
REMARK   3      S21:   -.4332 S22:    .5422 S23:    .7747                       
REMARK   3      S31:    .3520 S32:   -.4681 S33:   -.8303                       
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    87        A   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2572   2.3740  66.6624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1581 T22:    .2294                                     
REMARK   3      T33:    .3367 T12:   -.1614                                     
REMARK   3      T13:    .0069 T23:    .0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8541 L22:   4.1887                                     
REMARK   3      L33:   6.7349 L12:   -.2957                                     
REMARK   3      L13:  -1.2977 L23:   -.7335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1090 S12:   -.0229 S13:   -.4238                       
REMARK   3      S21:    .0914 S22:    .0543 S23:    .2639                       
REMARK   3      S31:    .9159 S32:   -.7527 S33:    .0547                       
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   121        A   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3088  35.4625  66.3008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0711 T22:    .1059                                     
REMARK   3      T33:    .0660 T12:    .0664                                     
REMARK   3      T13:    .0060 T23:    .0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .5823 L22:    .6588                                     
REMARK   3      L33:   1.6769 L12:   -.3063                                     
REMARK   3      L13:    .1925 L23:   -.4991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1028 S12:   -.1532 S13:    .0351                       
REMARK   3      S21:    .1144 S22:    .1555 S23:    .0320                       
REMARK   3      S31:   -.1028 S32:   -.1831 S33:   -.0526                       
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   187        A   235                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2293  22.8000  66.6822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0285 T22:    .0418                                     
REMARK   3      T33:    .0629 T12:    .0067                                     
REMARK   3      T13:   -.0110 T23:   -.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8995 L22:   1.0728                                     
REMARK   3      L33:   1.6292 L12:   -.8327                                     
REMARK   3      L13:    .1379 L23:   -.2955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0628 S12:   -.1261 S13:    .0705                       
REMARK   3      S21:    .0834 S22:    .0895 S23:   -.1018                       
REMARK   3      S31:   -.0349 S32:   -.0293 S33:   -.0266                       
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   236        A   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.5671  19.0139  55.7902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0203 T22:    .0472                                     
REMARK   3      T33:    .1319 T12:    .0046                                     
REMARK   3      T13:    .0296 T23:   -.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1833 L22:   1.7125                                     
REMARK   3      L33:   2.2638 L12:   -.0524                                     
REMARK   3      L13:    .8620 L23:   -.3659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1239 S12:    .0527 S13:    .0733                       
REMARK   3      S21:   -.0476 S22:   -.0058 S23:   -.1649                       
REMARK   3      S31:   -.0200 S32:    .2600 S33:   -.1180                       
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   296                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6128  26.8737  65.6095              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0492 T22:    .0532                                     
REMARK   3      T33:    .2295 T12:   -.0116                                     
REMARK   3      T13:    .0262 T23:   -.0636                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3535 L22:   3.4482                                     
REMARK   3      L33:   4.8179 L12:    .5336                                     
REMARK   3      L13:  -1.0888 L23:  -1.2187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0794 S12:   -.3901 S13:    .5118                       
REMARK   3      S21:    .1102 S22:    .0015 S23:   -.2920                       
REMARK   3      S31:   -.3354 S32:    .2622 S33:    .0779                       
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   297        A   375                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8904   9.4197  56.2276              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0659 T22:    .0040                                     
REMARK   3      T33:    .0926 T12:   -.0039                                     
REMARK   3      T13:   -.0282 T23:    .0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3031 L22:    .7833                                     
REMARK   3      L33:   1.1876 L12:   -.3199                                     
REMARK   3      L13:   -.0334 L23:   -.2515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0521 S12:   -.0525 S13:   -.1195                       
REMARK   3      S21:   -.0386 S22:    .0030 S23:    .0837                       
REMARK   3      S31:    .1689 S32:   -.0251 S33:   -.0550                       
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   376        A   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9689  22.1374  73.5913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0760 T22:    .0863                                     
REMARK   3      T33:    .0234 T12:    .0379                                     
REMARK   3      T13:    .0120 T23:   -.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8318 L22:   1.4795                                     
REMARK   3      L33:   4.0377 L12:   -.9555                                     
REMARK   3      L13:   1.5889 L23:  -1.3725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1121 S12:   -.3429 S13:    .0369                       
REMARK   3      S21:    .2293 S22:    .1652 S23:   -.0143                       
REMARK   3      S31:   -.0742 S32:   -.0985 S33:   -.0531                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   445                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.9121  18.0007  79.9808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0967 T22:    .1573                                     
REMARK   3      T33:    .0318 T12:    .0486                                     
REMARK   3      T13:   -.0354 T23:   -.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1558 L22:   1.0357                                     
REMARK   3      L33:   1.6793 L12:   -.9282                                     
REMARK   3      L13:   -.7587 L23:    .2991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0588 S12:   -.3008 S13:    .1569                       
REMARK   3      S21:    .1816 S22:    .1935 S23:   -.1337                       
REMARK   3      S31:   -.0364 S32:    .1790 S33:   -.1347                       
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   446        A   553                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2532  24.7263  71.4308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0567 T22:    .1362                                     
REMARK   3      T33:    .0629 T12:    .0356                                     
REMARK   3      T13:    .0278 T23:    .0442                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6755 L22:    .8506                                     
REMARK   3      L33:   1.0947 L12:   -.5657                                     
REMARK   3      L13:   -.1355 L23:    .3026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0796 S12:   -.2153 S13:   -.0706                       
REMARK   3      S21:    .1379 S22:    .1209 S23:    .1100                       
REMARK   3      S31:   -.0283 S32:   -.1927 S33:   -.0413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   554        A   584                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0055   2.9948  64.4858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1187 T22:    .0350                                     
REMARK   3      T33:    .1546 T12:   -.0034                                     
REMARK   3      T13:   -.0065 T23:    .0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3668 L22:   2.9647                                     
REMARK   3      L33:   3.7331 L12:   -.5151                                     
REMARK   3      L13:    .2208 L23:    .8477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0961 S12:   -.1480 S13:   -.4013                       
REMARK   3      S21:    .0551 S22:    .0502 S23:    .2406                       
REMARK   3      S31:    .3826 S32:   -.2077 S33:    .0458                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    33        B    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4097   1.9099  33.1464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3103 T22:    .0534                                     
REMARK   3      T33:    .1601 T12:    .0630                                     
REMARK   3      T13:   -.0618 T23:   -.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9754 L22:    .3923                                     
REMARK   3      L33:   2.3630 L12:   -.1115                                     
REMARK   3      L13:  -1.1250 L23:   -.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1084 S12:    .0284 S13:   -.0427                       
REMARK   3      S21:   -.2478 S22:   -.0395 S23:    .0117                       
REMARK   3      S31:    .5275 S32:    .0547 S33:   -.0690                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    67        B    81                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7895  -3.7018  30.1323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3346 T22:    .1334                                     
REMARK   3      T33:    .2644 T12:   -.0522                                     
REMARK   3      T13:   -.0700 T23:   -.0527                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.9484 L22:   2.4515                                     
REMARK   3      L33:   2.5035 L12:   2.0424                                     
REMARK   3      L13:   1.5208 L23:   -.3607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.2384 S12:   -.0520 S13:   -.4182                       
REMARK   3      S21:   -.0816 S22:    .1468 S23:    .3555                       
REMARK   3      S31:    .3138 S32:   -.3471 S33:    .0916                       
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    82        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1954  16.6729  25.0434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2704 T22:    .1863                                     
REMARK   3      T33:    .3904 T12:   -.1501                                     
REMARK   3      T13:   -.0543 T23:   -.0860                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3969 L22:   2.1782                                     
REMARK   3      L33:   5.2192 L12:  -1.2917                                     
REMARK   3      L13:   -.6623 L23:   2.3904                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0365 S12:    .1937 S13:   -.4712                       
REMARK   3      S21:    .1566 S22:   -.3866 S23:    .4277                       
REMARK   3      S31:    .6574 S32:   -.7484 S33:    .3501                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   121        B   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.3348  19.3274  26.3919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1308 T22:    .0822                                     
REMARK   3      T33:    .0515 T12:    .1024                                     
REMARK   3      T13:    .0004 T23:   -.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .5947 L22:    .5184                                     
REMARK   3      L33:   1.5008 L12:   -.1048                                     
REMARK   3      L13:    .2798 L23:   -.1524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1399 S12:    .1120 S13:   -.1026                       
REMARK   3      S21:   -.2033 S22:   -.1604 S23:    .0105                       
REMARK   3      S31:    .2096 S32:    .1235 S33:    .0205                       
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   189        B   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2521  34.7795  28.0386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0625 T22:    .0567                                     
REMARK   3      T33:    .0820 T12:    .0269                                     
REMARK   3      T13:    .0048 T23:    .0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7912 L22:   1.0323                                     
REMARK   3      L33:   1.2503 L12:   -.8136                                     
REMARK   3      L13:    .1186 L23:   -.1528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0404 S12:    .0801 S13:    .0558                       
REMARK   3      S21:   -.0845 S22:   -.0641 S23:   -.0629                       
REMARK   3      S31:    .0116 S32:    .1389 S33:    .0237                       
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   235        B   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6925  52.7082  38.8209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0665 T22:    .0141                                     
REMARK   3      T33:    .0990 T12:   -.0110                                     
REMARK   3      T13:   -.0226 T23:    .0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6692 L22:   2.6959                                     
REMARK   3      L33:   2.8517 L12:   -.3781                                     
REMARK   3      L13:    .7073 L23:  -1.0446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1123 S12:   -.0142 S13:    .2588                       
REMARK   3      S21:    .1809 S22:    .0748 S23:   -.1658                       
REMARK   3      S31:   -.3157 S32:    .1079 S33:    .0375                       
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   286                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5920  54.5075  29.0998              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .4071 T22:    .3325                                     
REMARK   3      T33:    .3694 T12:   -.2397                                     
REMARK   3      T13:   -.0260 T23:    .0900                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3472 L22:   7.7115                                     
REMARK   3      L33:   9.1587 L12:    .8824                                     
REMARK   3      L13:    .1328 L23:   5.2232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.4989 S12:    .2613 S13:    .2689                       
REMARK   3      S21:  -1.1470 S22:    .4025 S23:   -.6736                       
REMARK   3      S31:  -1.3388 S32:   1.1241 S33:    .0965                       
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   287        B   376                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9862  37.6197  36.1886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0121 T22:    .0553                                     
REMARK   3      T33:    .0708 T12:    .0128                                     
REMARK   3      T13:   -.0166 T23:    .0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7768 L22:   1.2224                                     
REMARK   3      L33:   1.2314 L12:   -.2174                                     
REMARK   3      L13:    .1436 L23:    .0876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0094 S12:    .0169 S13:   -.0581                       
REMARK   3      S21:   -.0475 S22:    .0145 S23:    .1130                       
REMARK   3      S31:    .0042 S32:   -.0954 S33:   -.0239                       
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   377        B   416                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3669  40.5599  17.9436              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0985 T22:    .1597                                     
REMARK   3      T33:    .0482 T12:    .0466                                     
REMARK   3      T13:    .0298 T23:    .0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6783 L22:   3.0221                                     
REMARK   3      L33:   2.1355 L12:   -.7495                                     
REMARK   3      L13:    .3859 L23:  -1.5934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2083 S12:    .2358 S13:    .0589                       
REMARK   3      S21:   -.3966 S22:   -.2078 S23:   -.0524                       
REMARK   3      S31:    .0470 S32:    .3079 S33:   -.0005                       
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   417        B   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8664  49.7504  16.7382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1074 T22:    .1285                                     
REMARK   3      T33:    .0908 T12:    .0439                                     
REMARK   3      T13:   -.0014 T23:    .0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8639 L22:  11.7041                                     
REMARK   3      L33:   4.4600 L12:   1.8539                                     
REMARK   3      L13:    .6332 L23:   2.2756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0690 S12:    .2082 S13:    .0596                       
REMARK   3      S21:   -.1694 S22:    .0581 S23:   -.0235                       
REMARK   3      S31:   -.1169 S32:    .0316 S33:   -.1272                       
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   430        B   468                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5570  25.4508  16.8981              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1753 T22:    .1387                                     
REMARK   3      T33:    .0098 T12:    .1200                                     
REMARK   3      T13:    .0108 T23:   -.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1690 L22:   1.4340                                     
REMARK   3      L33:    .9758 L12:   -.3295                                     
REMARK   3      L13:    .8164 L23:   -.3672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2036 S12:    .2538 S13:   -.0309                       
REMARK   3      S21:   -.2803 S22:   -.1890 S23:    .0289                       
REMARK   3      S31:    .1901 S32:    .2156 S33:   -.0147                       
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   469        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0330  25.5901  23.7865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1051 T22:    .0607                                     
REMARK   3      T33:    .0762 T12:    .0169                                     
REMARK   3      T13:   -.0635 T23:   -.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8854 L22:    .7145                                     
REMARK   3      L33:    .6536 L12:   -.4827                                     
REMARK   3      L13:    .0145 L23:   -.2688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1177 S12:    .1463 S13:   -.1451                       
REMARK   3      S21:   -.1968 S22:   -.0787 S23:    .1283                       
REMARK   3      S31:    .2014 S32:   -.0269 S33:   -.0390                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QH0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063633.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-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) : 0.9769                             
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   : 77928                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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   (%): 52.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
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       60.95300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.44400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.98400            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.95300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.44400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.98400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.95300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.44400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.98400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.95300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.44400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.98400            
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: 16450 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 46.0 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     MET A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     ASP A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     THR A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     THR A   592                                                      
REMARK 465     ILE A   593                                                      
REMARK 465     ALA A   594                                                      
REMARK 465     ALA A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     HIS A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ARG A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     ILE A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     VAL A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     MET B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     PHE B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     CYS B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     LEU B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     ASN 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     ALA B   594                                                      
REMARK 465     ALA B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     SER B   598                                                      
REMARK 465     HIS B   599                                                      
REMARK 465     SER B   600                                                      
REMARK 465     ARG B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     ASP B   603                                                      
REMARK 465     ASP B   604                                                      
REMARK 465     ILE B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     VAL B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     SER B   615                                                      
REMARK 465     THR B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     LEU B   618                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  54    CD   OE1  NE2                                       
REMARK 470     LYS A  56    CE   NZ                                             
REMARK 470     LEU A  75    CD1  CD2                                            
REMARK 470     ILE A  78    CD1                                                 
REMARK 470     LYS A  79    NZ                                                  
REMARK 470     LEU A  80    CD1                                                 
REMARK 470     LEU A  81    CG   CD1  CD2                                       
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     LYS A  97    CD   CE   NZ                                        
REMARK 470     ILE A 105A   CD1                                                 
REMARK 470     LYS A 169    CD   CE   NZ                                        
REMARK 470     LYS A 175    NZ                                                  
REMARK 470     LYS A 215    CG   CD   CE   NZ                                   
REMARK 470     LYS A 267    NZ                                                  
REMARK 470     GLU A 272    CD   OE1  OE2                                       
REMARK 470     LYS A 317    NZ                                                  
REMARK 470     LYS A 358    CD   CE   NZ                                        
REMARK 470     LYS A 405    CG   CD   CE   NZ                                   
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     LYS A 511    NZ                                                  
REMARK 470     LYS A 557    CD   CE   NZ                                        
REMARK 470     GLN A 583    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  54    CD   OE1  NE2                                       
REMARK 470     LYS B  56    CE   NZ                                             
REMARK 470     LEU B  75    CG   CD1  CD2                                       
REMARK 470     LYS B  79    CD   CE   NZ                                        
REMARK 470     LEU B  81    CD1  CD2                                            
REMARK 470     LEU B  82    CD1  CD2                                            
REMARK 470     LYS B  83    CD   CE   NZ                                        
REMARK 470     LYS B  97    CD   CE   NZ                                        
REMARK 470     ASN B 101    OD1                                                 
REMARK 470     ILE B 102    CG1  CD1                                            
REMARK 470     LYS B 169    CD   CE   NZ                                        
REMARK 470     GLU B 170    OE1  OE2                                            
REMARK 470     GLU B 186    CD   OE1  OE2                                       
REMARK 470     LYS B 215    CD   CE   NZ                                        
REMARK 470     LYS B 248    CE   NZ                                             
REMARK 470     LYS B 267    CD   CE   NZ                                        
REMARK 470     ASP B 268    CG   OD1  OD2                                       
REMARK 470     GLU B 281    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 282    CG   OD1                                            
REMARK 470     LYS B 358    CE   NZ                                             
REMARK 470     ASP B 399    OD1  OD2                                            
REMARK 470     LYS B 405    CE   NZ                                             
REMARK 470     ARG B 428    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 473    CD   CE   NZ                                        
REMARK 470     LYS B 485    CE   NZ                                             
REMARK 470     LYS B 492    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN B    68     O5   NAG B   661              1.50            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 456   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 456   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    THR A 129      -89.62   -118.65                                   
REMARK 500    ARG A 185      -65.94    -91.61                                   
REMARK 500    TRP A 387       52.54    -91.63                                   
REMARK 500    GLU A 398     -123.37     53.12                                   
REMARK 500    ASN A 410       73.65   -110.58                                   
REMARK 500    ASN A 439       14.41   -141.69                                   
REMARK 500    SER A 496      -44.76     63.80                                   
REMARK 500    ARG B  61       15.51     58.25                                   
REMARK 500    THR B 129      -89.10   -124.12                                   
REMARK 500    ARG B 185      -91.10    -94.25                                   
REMARK 500    TRP B 387       49.88    -82.66                                   
REMARK 500    GLU B 398     -118.44     55.29                                   
REMARK 500    ASN B 410       76.96   -103.88                                   
REMARK 500    ASN B 439       19.41   -142.72                                   
REMARK 500    SER B 496      -47.30     69.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN B  581     VAL B  582                  145.45                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B 582        22.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1023        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH B 858        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH B 859        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH B 973        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH B1040        DISTANCE =  5.53 ANGSTROMS                       
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 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HSQ A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
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: 3HS5   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF              
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1                                      
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB                                   
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL            
REMARK 900 OF CYCLOOXYGENASE-2                                                  
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB                                   
REMARK 900 DOCOSAHEXAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF          
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB                                   
REMARK 900 UNINHIBITED COX-2                                                    
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO COX-2                                      
DBREF  3QH0 A   10   618  UNP    Q05769   PGH2_MOUSE       1    604             
DBREF  3QH0 B   10   618  UNP    Q05769   PGH2_MOUSE       1    604             
SEQADV 3QH0 HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 ALA A  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION            
SEQADV 3QH0 HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QH0 ALA B  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION            
SEQRES   1 A  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 A  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO          
SEQRES   3 A  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET          
SEQRES   4 A  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG          
SEQRES   5 A  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE          
SEQRES   6 A  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN          
SEQRES   7 A  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP          
SEQRES   8 A  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE          
SEQRES   9 A  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP          
SEQRES  10 A  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER          
SEQRES  11 A  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA          
SEQRES  12 A  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY          
SEQRES  13 A  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL          
SEQRES  14 A  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP          
SEQRES  15 A  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN          
SEQRES  16 A  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG          
SEQRES  17 A  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP          
SEQRES  18 A  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS          
SEQRES  19 A  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN          
SEQRES  20 A  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP          
SEQRES  21 A  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU          
SEQRES  22 A  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU          
SEQRES  23 A  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG          
SEQRES  24 A  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS          
SEQRES  25 A  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG          
SEQRES  26 A  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU          
SEQRES  27 A  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU          
SEQRES  28 A  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN          
SEQRES  29 A  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR          
SEQRES  30 A  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU          
SEQRES  31 A  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN          
SEQRES  32 A  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU          
SEQRES  33 A  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY          
SEQRES  34 A  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA          
SEQRES  35 A  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU          
SEQRES  36 A  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR          
SEQRES  37 A  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA          
SEQRES  38 A  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU          
SEQRES  39 A  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP          
SEQRES  40 A  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO          
SEQRES  41 A  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER          
SEQRES  42 A  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL          
SEQRES  43 A  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU          
SEQRES  44 A  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE          
SEQRES  45 A  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE          
SEQRES  46 A  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN          
SEQRES  47 A  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU              
SEQRES   1 B  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 B  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO          
SEQRES   3 B  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET          
SEQRES   4 B  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG          
SEQRES   5 B  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE          
SEQRES   6 B  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN          
SEQRES   7 B  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP          
SEQRES   8 B  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE          
SEQRES   9 B  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP          
SEQRES  10 B  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER          
SEQRES  11 B  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA          
SEQRES  12 B  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY          
SEQRES  13 B  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL          
SEQRES  14 B  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP          
SEQRES  15 B  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN          
SEQRES  16 B  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG          
SEQRES  17 B  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP          
SEQRES  18 B  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS          
SEQRES  19 B  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN          
SEQRES  20 B  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP          
SEQRES  21 B  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU          
SEQRES  22 B  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU          
SEQRES  23 B  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG          
SEQRES  24 B  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS          
SEQRES  25 B  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG          
SEQRES  26 B  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU          
SEQRES  27 B  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU          
SEQRES  28 B  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN          
SEQRES  29 B  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR          
SEQRES  30 B  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU          
SEQRES  31 B  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN          
SEQRES  32 B  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU          
SEQRES  33 B  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY          
SEQRES  34 B  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA          
SEQRES  35 B  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU          
SEQRES  36 B  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR          
SEQRES  37 B  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA          
SEQRES  38 B  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU          
SEQRES  39 B  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP          
SEQRES  40 B  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO          
SEQRES  41 B  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER          
SEQRES  42 B  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL          
SEQRES  43 B  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU          
SEQRES  44 B  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE          
SEQRES  45 B  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE          
SEQRES  46 B  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN          
SEQRES  47 B  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU              
MODRES 3QH0 ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3QH0 ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3QH0 ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3QH0 ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3QH0 ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3QH0 ASN A   68  ASN  GLYCOSYLATION SITE                                 
HET    EDO  A   1       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   5       4                                                       
HET    EDO  A 619       4                                                       
HET    EDO  A 620       4                                                       
HET    EDO  A 621       4                                                       
HET    EDO  A 622       4                                                       
HET    EDO  A 623       4                                                       
HET    EDO  A 624       4                                                       
HET    PLM  A 625      18                                                       
HET    AKR  A   2       5                                                       
HET    AKR  A   3       5                                                       
HET    COH  A 626      43                                                       
HET    HSQ  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 619       4                                                       
HET    EDO  B 620       4                                                       
HET    EDO  B 621       4                                                       
HET    EDO  B 622       4                                                       
HET    EDO  B 623       4                                                       
HET    EDO  B 624       4                                                       
HET    EDO  B 625       4                                                       
HET    EDO  B 626       4                                                       
HET    COH  B 627      43                                                       
HET    NAG  B 661      14                                                       
HET    NDG  B 662      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 672      14                                                       
HET    NAG  B 681      14                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     AKR ACRYLIC ACID                                                     
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO                                  
HETNAM     HSQ 2-(ACETYLAMINO)-2-DEOXY-ALPHA-L-IDOPYRANOSE                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    23(C2 H6 O2)                                                 
FORMUL  12  PLM    C16 H32 O2                                                   
FORMUL  13  AKR    2(C3 H4 O2)                                                  
FORMUL  15  COH    2(C34 H32 CO N4 O4)                                          
FORMUL  16  HSQ    C8 H15 N O6                                                  
FORMUL  16  NAG    8(C8 H15 N O6)                                               
FORMUL  17  MAN    C6 H12 O6                                                    
FORMUL  19  BOG    C14 H28 O6                                                   
FORMUL  35  NDG    C8 H15 N O6                                                  
FORMUL  38  HOH   *753(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 TYR A  122  1                                  18    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  ARG A  245  1                                   9    
HELIX   10  10 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 PRO A  280  GLN A  284  5                                   5    
HELIX   12  12 VAL A  291  LEU A  294  5                                   4    
HELIX   13  13 VAL A  295  HIS A  320  1                                  26    
HELIX   14  14 GLY A  324  ASP A  347  1                                  24    
HELIX   15  15 ASP A  347  GLY A  354  1                                   8    
HELIX   16  16 ASP A  362  PHE A  367  5                                   6    
HELIX   17  17 ALA A  378  TYR A  385  1                                   8    
HELIX   18  18 HIS A  386  LEU A  391  5                                   6    
HELIX   19  19 SER A  403  LEU A  408  1                                   6    
HELIX   20  20 ASN A  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  LEU B   82  1                                  10    
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  291  LEU B  294  5                                   4    
HELIX   45  45 VAL B  295  HIS B  320  1                                  26    
HELIX   46  46 GLY B  324  ASP B  347  1                                  24    
HELIX   47  47 ASP B  347  GLY B  354  1                                   8    
HELIX   48  48 ASP B  362  PHE B  367  5                                   6    
HELIX   49  49 ALA B  378  TYR B  385  1                                   8    
HELIX   50  50 HIS B  386  LEU B  391  5                                   6    
HELIX   51  51 SER B  403  LEU B  408  1                                   6    
HELIX   52  52 ASN B  410  GLY B  418  1                                   9    
HELIX   53  53 GLY B  418  GLN B  429  1                                  12    
HELIX   54  54 PRO B  441  ALA B  443  5                                   3    
HELIX   55  55 VAL B  444  MET B  458  1                                  15    
HELIX   56  56 SER B  462  PHE B  470  1                                   9    
HELIX   57  57 SER B  477  GLY B  483  1                                   7    
HELIX   58  58 LYS B  485  SER B  496  1                                  12    
HELIX   59  59 ASP B  497  MET B  501  5                                   5    
HELIX   60  60 GLU B  502  GLU B  510  1                                   9    
HELIX   61  61 GLY B  519  GLY B  536  1                                  18    
HELIX   62  62 ASN B  537  SER B  541  5                                   5    
HELIX   63  63 LYS B  546  GLY B  551  5                                   6    
HELIX   64  64 GLY B  552  THR B  561  1                                  10    
HELIX   65  65 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  TYR A 262   N  GLN A 255           
SHEET    1   D 2 PHE A 395  ILE A 397  0                                        
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   E 2 GLU B  46  SER B  49  0                                        
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46           
SHEET    1   F 2 PHE B  64  TYR B  65  0                                        
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   G 2 GLN B 255  ILE B 257  0                                        
SHEET    2   G 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   H 2 PHE B 395  ILE B 397  0                                        
SHEET    2   H 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.02  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.07  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.05  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.07  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05  
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.37  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.42  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44  
LINK         O4  HSQ A 661                 C1  NAG A 662     1555   1555  1.44  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44  
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44  
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.46  
LINK         O4  NAG B 661                 C1  NDG B 662     1555   1555  1.46  
LINK         ND2 ASN A  68                 C1  HSQ A 661     1555   1555  1.44  
CISPEP   1 SER A  126    PRO A  127          0         5.62                     
CISPEP   2 SER B  126    PRO B  127          0        -0.62                     
SITE     1 AC1  8 HIS A  90  GLN A 192  LEU A 352  ARG A 513                    
SITE     2 AC1  8 ALA A 516  ILE A 517  PHE A 518  VAL A 523                    
SITE     1 AC2  8 PRO A 162  MET A 163  SER A 455  ARG A 456                    
SITE     2 AC2  8 LYS A 459  TYR A 460  EDO A 623  HOH A 743                    
SITE     1 AC3  2 CYS A  59  HOH A 892                                          
SITE     1 AC4  8 GLU A 308  ARG A 311  GLU A 339  SER A 566                    
SITE     2 AC4  8 LEU A 567  ASN A 570  ASN A 571  HOH A 737                    
SITE     1 AC5  5 LYS A 251  TYR A 254  ASN A 310  HOH A 688                    
SITE     2 AC5  5 HOH A 744                                                     
SITE     1 AC6  4 LEU A 246  LYS A 253  TYR A 254  HOH A 959                    
SITE     1 AC7  5 SER A 143  EDO A 624  HOH A 793  LEU B 145                    
SITE     2 AC7  5 LEU B 224                                                     
SITE     1 AC8  8 EDO A   4  VAL A 155  ALA A 156  ASP A 157                    
SITE     2 AC8  8 CYS A 159  THR A 161  PRO A 162  LYS A 459                    
SITE     1 AC9  3 EDO A 622  HOH B 899  HOH B 926                               
SITE     1 BC1 12 VAL A 116  ARG A 120  PHE A 205  TYR A 348                    
SITE     2 BC1 12 VAL A 349  SER A 353  TYR A 355  TYR A 385                    
SITE     3 BC1 12 ALA A 527  SER A 530  LEU A 531  HOH A1048                    
SITE     1 BC2  4 SER A 477  PHE A 478  GLU A 479  LYS A 492                    
SITE     1 BC3  5 THR A 237  ASP A 239  ARG A 240  LYS A 243                    
SITE     2 BC3  5 GLU A 272                                                     
SITE     1 BC4 13 GLN A 203  HIS A 207  PHE A 210  LYS A 211                    
SITE     2 BC4 13 THR A 212  HIS A 214  ASN A 382  TYR A 385                    
SITE     3 BC4 13 HIS A 386  TRP A 387  HIS A 388  LEU A 391                    
SITE     4 BC4 13 VAL A 447                                                     
SITE     1 BC5  4 TYR A  55  GLU A  67  ASN A  68  NAG A 662                    
SITE     1 BC6  1 HSQ A 661                                                     
SITE     1 BC7  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 BC7  9 NAG A 672  HOH A 706  HOH A 790  HOH A 906                    
SITE     3 BC7  9 HOH A 943                                                     
SITE     1 BC8  3 ARG A 216  NAG A 671  MAN A 673                               
SITE     1 BC9  3 NAG A 672  HOH A 685  HOH A 853                               
SITE     1 CC1  4 ASN A 410  SER A 412  ILE A 413  GLU A 416                    
SITE     1 CC2 12 GLU A 179  LYS A 180  ARG A 184  ARG A 185                    
SITE     2 CC2 12 ARG A 438  GLU A 486  GLU A 490  GLU B 179                    
SITE     3 CC2 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445                    
SITE     1 CC3  8 HIS B  90  GLN B 192  LEU B 352  ARG B 513                    
SITE     2 CC3  8 ALA B 516  ILE B 517  PHE B 518  VAL B 523                    
SITE     1 CC4  5 LYS B 251  TYR B 254  ASN B 310  HOH B 872                    
SITE     2 CC4  5 HOH B1076                                                     
SITE     1 CC5  6 PRO B 162  LEU B 171  ARG B 456  LYS B 459                    
SITE     2 CC5  6 TYR B 460  HOH B 783                                          
SITE     1 CC6  2 SER A 548  MET B  48                                          
SITE     1 CC7  7 GLU B 308  ARG B 311  GLU B 339  SER B 566                    
SITE     2 CC7  7 LEU B 567  ASN B 570  HOH B 746                               
SITE     1 CC8  5 LEU A 145  HOH A 891  SER B 143  HOH B 631                    
SITE     2 CC8  5 HOH B 683                                                     
SITE     1 CC9  6 ASP B 239  ARG B 240  LYS B 243  GLN B 270                    
SITE     2 CC9  6 VAL B 271  GLU B 272                                          
SITE     1 DC1  3 ARG B 428  VAL B 582  HOH B 753                               
SITE     1 DC2  7 LYS B 175  GLN B 445  ALA B 446  LYS B 449                    
SITE     2 DC2  7 HOH B 654  HOH B 764  HOH B 880                               
SITE     1 DC3  3 VAL B 349  TYR B 355  HOH B1078                               
SITE     1 DC4  2 SER B 530  HOH B1078                                          
SITE     1 DC5  5 VAL A 554  LEU B 246  LYS B 253  TYR B 254                    
SITE     2 DC5  5 HOH B 635                                                     
SITE     1 DC6  8 PHE A 142  GLY B 225  HIS B 226  ASN B 375                    
SITE     2 DC6  8 GLY B 536  PRO B 538  HOH B 684  HOH B 926                    
SITE     1 DC7  2 CYS B 569  ASN B 570                                          
SITE     1 DC8 14 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 DC8 14 THR B 212  HIS B 214  VAL B 295  ASN B 382                    
SITE     3 DC8 14 TYR B 385  HIS B 386  HIS B 388  LEU B 391                    
SITE     4 DC8 14 VAL B 447  HOH B 864                                          
SITE     1 DC9  5 TYR B  55  GLU B  67  ASN B  68  NDG B 662                    
SITE     2 DC9  5 HOH B 933                                                     
SITE     1 EC1  2 NAG B 661  HOH B 906                                          
SITE     1 EC2  9 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 EC2  9 HOH B 670  NAG B 672  HOH B 775  HOH B 825                    
SITE     3 EC2  9 HOH B 833                                                     
SITE     1 EC3  5 ASP A 239  ARG B 216  NAG B 671  HOH B 919                    
SITE     2 EC3  5 HOH B1055                                                     
SITE     1 EC4  6 ASN B 410  ILE B 413  GLU B 416  HOH B 765                    
SITE     2 EC4  6 HOH B 866  HOH B1007                                          
CRYST1  121.906  130.888  179.968  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      0.008203  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007640  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005557        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system