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Database: PDB
Entry: 3MDL
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HEADER    OXIDOREDUCTASE                          30-MAR-10   3MDL              
TITLE     X-RAY CRYSTAL STRUCTURE OF 1-ARACHIDONOYL GLYCEROL BOUND TO THE       
TITLE    2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 20 TO 599;                                    
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   6 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,      
COMPND   7 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10 
COMPND   8 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   9 2;                                                                   
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: PTGS2, COX-2, COX2, PGHS-B, TIS10;                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: EXPRESSION;                           
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    COX-2, CYCLOOXYGENASE-2, ENDOCANNABINOID, OXIDOREDUCTASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI                                             
REVDAT   4   29-JUN-11 3MDL    1       JRNL                                     
REVDAT   3   15-JUN-11 3MDL    1       JRNL                                     
REVDAT   2   20-APR-11 3MDL    1       JRNL                                     
REVDAT   1   13-APR-11 3MDL    0                                                
JRNL        AUTH   A.J.VECCHIO,M.G.MALKOWSKI                                    
JRNL        TITL   THE STRUCTURAL BASIS OF ENDOCANNABINOID OXYGENATION BY       
JRNL        TITL 2 CYCLOOXYGENASE-2.                                            
JRNL        REF    J.BIOL.CHEM.                  V. 286 20736 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21489986                                                     
JRNL        DOI    10.1074/JBC.M111.230367                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 67549                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3597                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4546                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 229                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8906                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 354                                     
REMARK   3   SOLVENT ATOMS            : 960                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.08000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
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): 0.233         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.189         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.851        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9605 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13054 ; 1.127 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1113 ; 5.221 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   446 ;36.597 ;23.946       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1528 ;13.612 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;12.710 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1383 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7363 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5553 ; 0.328 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9014 ; 0.668 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4052 ; 1.288 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4036 ; 2.237 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    33        A    67                          
REMARK   3    ORIGIN FOR THE GROUP (A):    .7944  38.0085  59.2429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0502 T22:    .1831                                     
REMARK   3      T33:    .1478 T12:    .0716                                     
REMARK   3      T13:    .0406 T23:    .0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3400 L22:   2.0080                                     
REMARK   3      L33:   2.7309 L12:   1.2029                                     
REMARK   3      L13:   -.0039 L23:    .3589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0756 S12:   -.0313 S13:    .0838                       
REMARK   3      S21:    .0391 S22:    .1919 S23:    .2162                       
REMARK   3      S31:   -.2180 S32:   -.4567 S33:   -.1163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    68        A    92                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0204  17.3088  66.2660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0540 T22:    .2391                                     
REMARK   3      T33:    .3922 T12:   -.0984                                     
REMARK   3      T13:   -.0103 T23:    .1311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4547 L22:   3.9107                                     
REMARK   3      L33:   2.8985 L12:  -3.0199                                     
REMARK   3      L13:   1.8457 L23:  -2.8078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0997 S12:   -.2022 S13:   -.6007                       
REMARK   3      S21:   -.1995 S22:    .4235 S23:    .7528                       
REMARK   3      S31:    .3053 S32:   -.5686 S33:   -.5232                       
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    93        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2919   2.3208  64.7852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0893 T22:    .1335                                     
REMARK   3      T33:    .2360 T12:   -.0988                                     
REMARK   3      T13:    .0175 T23:    .0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9080 L22:   6.4798                                     
REMARK   3      L33:  10.7451 L12:   -.5772                                     
REMARK   3      L13:  -4.0107 L23:  -2.6001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.2947 S12:    .2448 S13:   -.2261                       
REMARK   3      S21:   -.1493 S22:   -.0397 S23:    .2744                       
REMARK   3      S31:    .7390 S32:   -.5137 S33:    .3344                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   123        A   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5687  36.6243  66.1563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0899 T22:    .0835                                     
REMARK   3      T33:    .0946 T12:    .0270                                     
REMARK   3      T13:    .0025 T23:   -.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4753 L22:    .7346                                     
REMARK   3      L33:   1.4008 L12:   -.1943                                     
REMARK   3      L13:   -.1822 L23:   -.4155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0412 S12:   -.0669 S13:    .0890                       
REMARK   3      S21:    .1243 S22:    .0996 S23:    .0072                       
REMARK   3      S31:   -.1350 S32:   -.1004 S33:   -.0584                       
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   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4871  23.4280  67.2984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0666 T22:    .0686                                     
REMARK   3      T33:    .1096 T12:    .0085                                     
REMARK   3      T13:   -.0134 T23:    .0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8765 L22:    .9814                                     
REMARK   3      L33:   1.4250 L12:   -.7511                                     
REMARK   3      L13:    .5552 L23:   -.6133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0662 S12:   -.0712 S13:    .0880                       
REMARK   3      S21:    .1178 S22:    .0206 S23:   -.1006                       
REMARK   3      S31:   -.1383 S32:    .0910 S33:    .0457                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   234        A   271                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.0572  19.5714  56.1051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0062 T22:    .0801                                     
REMARK   3      T33:    .1288 T12:    .0062                                     
REMARK   3      T13:    .0143 T23:    .0226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8969 L22:   1.0826                                     
REMARK   3      L33:   2.1309 L12:   -.2838                                     
REMARK   3      L13:    .8569 L23:   -.1573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0160 S12:    .0386 S13:    .0728                       
REMARK   3      S21:   -.0634 S22:   -.0033 S23:   -.0627                       
REMARK   3      S31:   -.0238 S32:    .2122 S33:   -.0127                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   272        A   320                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.2878  18.5955  62.9160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0222 T22:    .1037                                     
REMARK   3      T33:    .1302 T12:    .0149                                     
REMARK   3      T13:    .0062 T23:    .0306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4443 L22:    .7709                                     
REMARK   3      L33:   2.9760 L12:    .1286                                     
REMARK   3      L13:   -.0810 L23:    .3696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0692 S12:   -.2021 S13:    .1149                       
REMARK   3      S21:    .0502 S22:   -.0475 S23:   -.0772                       
REMARK   3      S31:   -.0508 S32:    .1309 S33:   -.0217                       
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   321        A   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.7925  13.9973  61.1420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0792 T22:    .0600                                     
REMARK   3      T33:    .1130 T12:   -.0022                                     
REMARK   3      T13:   -.0046 T23:    .0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4878 L22:    .4647                                     
REMARK   3      L33:   1.0978 L12:   -.2228                                     
REMARK   3      L13:   -.2892 L23:   -.1502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0580 S12:   -.1021 S13:   -.0903                       
REMARK   3      S21:    .0320 S22:    .0621 S23:    .0535                       
REMARK   3      S31:    .1152 S32:    .0213 S33:   -.0041                       
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   401        A   445                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.3672  18.4277  80.0507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0898 T22:    .1250                                     
REMARK   3      T33:    .0266 T12:    .0222                                     
REMARK   3      T13:   -.0260 T23:   -.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2694 L22:   1.2534                                     
REMARK   3      L33:   1.8958 L12:  -1.1034                                     
REMARK   3      L13:  -1.0576 L23:    .6027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0997 S12:   -.4298 S13:    .0955                       
REMARK   3      S21:    .1412 S22:    .1617 S23:   -.1657                       
REMARK   3      S31:   -.0351 S32:    .3632 S33:   -.0620                       
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   446        A   493                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4115  31.5774  76.8399              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1036 T22:    .1043                                     
REMARK   3      T33:    .0521 T12:    .0824                                     
REMARK   3      T13:    .0386 T23:    .0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6548 L22:   1.2491                                     
REMARK   3      L33:   2.2864 L12:    .1235                                     
REMARK   3      L13:    .3674 L23:   -.0355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1204 S12:   -.2340 S13:    .0565                       
REMARK   3      S21:    .2700 S22:    .1708 S23:    .0889                       
REMARK   3      S31:   -.0660 S32:   -.2129 S33:   -.0503                       
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   494        A   553                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4656  20.1759  66.2711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0853 T22:    .0577                                     
REMARK   3      T33:    .0873 T12:    .0177                                     
REMARK   3      T13:    .0041 T23:    .0346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6801 L22:    .7642                                     
REMARK   3      L33:   1.8301 L12:   -.2860                                     
REMARK   3      L13:   -.5181 L23:    .6076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0415 S12:   -.0921 S13:   -.0966                       
REMARK   3      S21:    .0166 S22:   -.0091 S23:    .1555                       
REMARK   3      S31:   -.0327 S32:   -.1495 S33:    .0506                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   554        A   584                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.5765   3.5356  64.7406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1122 T22:    .0424                                     
REMARK   3      T33:    .1470 T12:   -.0121                                     
REMARK   3      T13:    .0219 T23:    .0491                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9657 L22:   2.6977                                     
REMARK   3      L33:   3.1549 L12:   -.6403                                     
REMARK   3      L13:   -.1089 L23:    .3619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0314 S12:   -.0447 S13:   -.2121                       
REMARK   3      S21:    .0883 S22:    .0302 S23:    .0613                       
REMARK   3      S31:    .4086 S32:   -.0600 S33:    .0012                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    33        B    67                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2325   1.7778  33.5452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3001 T22:    .0341                                     
REMARK   3      T33:    .1198 T12:    .0766                                     
REMARK   3      T13:   -.0284 T23:   -.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6239 L22:    .4212                                     
REMARK   3      L33:   3.4491 L12:    .8908                                     
REMARK   3      L13:  -1.4505 L23:   -.2316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0655 S12:   -.1149 S13:   -.3505                       
REMARK   3      S21:   -.1938 S22:   -.0749 S23:    .0162                       
REMARK   3      S31:    .5899 S32:    .2736 S33:    .0094                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    68        B    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2421   1.0290  27.2664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .5001 T22:    .1890                                     
REMARK   3      T33:    .4684 T12:   -.2770                                     
REMARK   3      T13:   -.2410 T23:    .0587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2498 L22:   6.7230                                     
REMARK   3      L33:   5.1094 L12:  -6.7524                                     
REMARK   3      L13:   5.8969 L23:  -5.8608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .4829 S12:   -.3633 S13:  -1.0806                       
REMARK   3      S21:   -.8989 S22:    .5669 S23:   1.2027                       
REMARK   3      S31:    .7744 S32:   -.4925 S33:  -1.0498                       
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    90        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):    .6869  19.0695  25.9556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1695 T22:    .1059                                     
REMARK   3      T33:    .2347 T12:   -.1259                                     
REMARK   3      T13:   -.0247 T23:    .0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5453 L22:   2.5659                                     
REMARK   3      L33:  10.9226 L12:  -2.4241                                     
REMARK   3      L13:  -1.1575 L23:   2.3546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0683 S12:    .1347 S13:   -.6463                       
REMARK   3      S21:    .0681 S22:   -.2108 S23:    .3585                       
REMARK   3      S31:    .7305 S32:   -.6628 S33:    .2791                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   123        B   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1777  19.3525  26.7035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1155 T22:    .0686                                     
REMARK   3      T33:    .0858 T12:    .0316                                     
REMARK   3      T13:    .0124 T23:   -.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6102 L22:    .8508                                     
REMARK   3      L33:   1.7826 L12:   -.2535                                     
REMARK   3      L13:    .1770 L23:   -.3744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0781 S12:    .0709 S13:   -.0410                       
REMARK   3      S21:   -.1489 S22:   -.0737 S23:   -.0455                       
REMARK   3      S31:    .2752 S32:    .1681 S33:   -.0045                       
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   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0789  35.8773  29.6002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0480 T22:    .1055                                     
REMARK   3      T33:    .1549 T12:   -.0133                                     
REMARK   3      T13:    .0124 T23:    .0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8099 L22:    .8505                                     
REMARK   3      L33:   1.2508 L12:   -.6668                                     
REMARK   3      L13:   -.4511 L23:   -.1713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0469 S12:   -.0295 S13:    .1149                       
REMARK   3      S21:   -.0336 S22:    .0218 S23:   -.1111                       
REMARK   3      S31:   -.0409 S32:    .0529 S33:   -.0687                       
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   241        B   269                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3689  54.8537  37.7259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0815 T22:    .0517                                     
REMARK   3      T33:    .1692 T12:   -.0096                                     
REMARK   3      T13:    .0109 T23:    .0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9447 L22:    .7843                                     
REMARK   3      L33:   3.7267 L12:   -.8438                                     
REMARK   3      L13:   1.2778 L23:   -.7502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0562 S12:    .1563 S13:    .2775                       
REMARK   3      S21:    .0899 S22:    .0485 S23:    .0400                       
REMARK   3      S31:   -.4830 S32:    .1929 S33:    .0076                       
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   270        B   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3137  50.2291  27.9276              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0944 T22:    .1161                                     
REMARK   3      T33:    .1459 T12:   -.0643                                     
REMARK   3      T13:    .0536 T23:    .0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9598 L22:   2.6772                                     
REMARK   3      L33:   3.3613 L12:   -.6681                                     
REMARK   3      L13:   -.2478 L23:    .7634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1117 S12:   -.0002 S13:    .2110                       
REMARK   3      S21:   -.2620 S22:    .1198 S23:   -.4331                       
REMARK   3      S31:   -.4743 S32:    .5014 S33:   -.2315                       
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   303        B   356                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9765  42.2065  37.5449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0455 T22:    .1059                                     
REMARK   3      T33:    .1281 T12:    .0051                                     
REMARK   3      T13:   -.0061 T23:    .0511                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9119 L22:   1.1399                                     
REMARK   3      L33:   1.2340 L12:   -.4613                                     
REMARK   3      L13:   -.3528 L23:    .1860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0173 S12:    .0594 S13:    .0433                       
REMARK   3      S21:   -.0043 S22:    .0108 S23:    .0892                       
REMARK   3      S31:   -.1071 S32:   -.2186 S33:    .0065                       
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   357        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2266  29.3741  27.4792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0791 T22:    .0553                                     
REMARK   3      T33:    .0994 T12:   -.0156                                     
REMARK   3      T13:   -.0243 T23:   -.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0305 L22:   1.1974                                     
REMARK   3      L33:   1.9369 L12:    .0476                                     
REMARK   3      L13:   -.2169 L23:   -.6741                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0912 S12:    .1227 S13:   -.0536                       
REMARK   3      S21:   -.2037 S22:   -.0183 S23:    .1385                       
REMARK   3      S31:    .1031 S32:   -.0519 S33:   -.0729                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   402        B   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8147  50.1267  15.9849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0699 T22:    .0974                                     
REMARK   3      T33:    .0647 T12:    .0240                                     
REMARK   3      T13:    .0369 T23:    .0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0160 L22:   4.3384                                     
REMARK   3      L33:   2.6874 L12:    .5910                                     
REMARK   3      L13:   -.1458 L23:    .0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1647 S12:    .2772 S13:    .0807                       
REMARK   3      S21:   -.2764 S22:   -.0502 S23:   -.1552                       
REMARK   3      S31:   -.3419 S32:    .0203 S33:   -.1144                       
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   531                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4801  19.6962  15.5314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1354 T22:    .0635                                     
REMARK   3      T33:    .0256 T12:    .0265                                     
REMARK   3      T13:   -.0068 T23:   -.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .8835 L22:    .9511                                     
REMARK   3      L33:   1.4713 L12:   -.3682                                     
REMARK   3      L13:    .3625 L23:   -.4187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0908 S12:    .1966 S13:   -.0656                       
REMARK   3      S21:   -.2084 S22:   -.0604 S23:    .0366                       
REMARK   3      S31:    .2885 S32:    .0154 S33:   -.0304                       
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   532        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9097  37.4845  35.3803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0087 T22:    .1082                                     
REMARK   3      T33:    .1244 T12:   -.0172                                     
REMARK   3      T13:   -.0062 T23:    .0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3650 L22:    .8816                                     
REMARK   3      L33:   2.2849 L12:   -.2126                                     
REMARK   3      L13:   -.2127 L23:   -.8053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0289 S12:    .0541 S13:    .0187                       
REMARK   3      S21:   -.0354 S22:    .0743 S23:    .1227                       
REMARK   3      S31:    .0559 S32:   -.2624 S33:   -.1031                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3MDL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058413.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
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) : 0.9777                             
REMARK 200  MONOCHROMATOR                  : HORIZONTAL FOCUSING 5.05           
REMARK 200                                   ASYMMETRIC CUT 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   : 67549                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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   (%): 52.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID SODIUM SALT,     
REMARK 280  0.1M HEPES PH 7.5, 0.02M MAGNESIUM CHLORIDE, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 296K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       59.47900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.88650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.92900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.47900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.88650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.92900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.47900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.88650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.92900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.47900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.88650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.92900            
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 300 REMARK: ASYMMETRIC UNIT CONTAINS THE COX-2 BIOLOGICAL DIMER.         
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: 11490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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     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     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A  75    CG   CD1  CD2                                       
REMARK 470     GLU A 170    OE1  OE2                                            
REMARK 470     LYS A 215    CD   CE   NZ                                        
REMARK 470     ASP A 239    OD1  OD2                                            
REMARK 470     LYS A 358    CE   NZ                                             
REMARK 470     LYS A 405    CD   CE   NZ                                        
REMARK 470     LYS A 557    NZ                                                  
REMARK 470     GLN A 583    CD   OE1  NE2                                       
REMARK 470     LEU B  75    CG   CD1  CD2                                       
REMARK 470     LEU B  81    CD1  CD2                                            
REMARK 470     LYS B  83    CD   CE   NZ                                        
REMARK 470     LYS B  97    CE   NZ                                             
REMARK 470     GLU B 170    OE1  OE2                                            
REMARK 470     LYS B 175    NZ                                                  
REMARK 470     GLU B 186    CD   OE1  OE2                                       
REMARK 470     LYS B 215    NZ                                                  
REMARK 470     LYS B 267    CG   CD   CE   NZ                                   
REMARK 470     ASP B 268    CG   OD1  OD2                                       
REMARK 470     LYS B 358    NZ                                                  
REMARK 470     LYS B 405    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 531   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  61       17.31     57.18                                   
REMARK 500    THR A 129      -92.82   -119.23                                   
REMARK 500    ASP A 249       19.71     58.29                                   
REMARK 500    GLU A 398     -118.64     56.01                                   
REMARK 500    ASN A 439       15.61   -145.74                                   
REMARK 500    SER A 496      -40.35     70.37                                   
REMARK 500    CYS A 575       64.16     39.33                                   
REMARK 500    THR B 129      -91.87   -119.01                                   
REMARK 500    ARG B 185      -92.27    -94.18                                   
REMARK 500    GLU B 398     -120.00     57.12                                   
REMARK 500    SER B 496      -51.06     74.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 830        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 929        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A 952        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A1022        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH A1023        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH A1076        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH B 634        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B 647        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH B 740        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 836        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH B 872        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH B 917        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH B 951        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH B 990        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B 991        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH B 994        DISTANCE =  5.52 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             COH B 615  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 COH B 615   NA   92.2                                              
REMARK 620 3 COH B 615   NB   91.6  87.3                                        
REMARK 620 4 COH B 615   NC   92.2 174.8  89.8                                  
REMARK 620 5 COH B 615   ND   90.2  89.0 175.9  93.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             COH A 614  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 COH A 614   NA   92.4                                              
REMARK 620 3 COH A 614   NB   81.7  86.7                                        
REMARK 620 4 COH A 614   NC   89.3 176.0  89.9                                  
REMARK 620 5 COH A 614   ND   97.6  90.7 177.3  92.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AG B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR B 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
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 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE             
REMARK 900 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                           
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF EICOSAPENTAENOIC ACID BOUND TO            
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                       
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DOCOSAHEXAENOIC ACID BOUND TO             
REMARK 900 THE CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                       
REMARK 900 RELATED ID: 3KRK   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE             
REMARK 900 CYCLOOXYGENASE CHANNEL OF L531F MURINE COX-2                         
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE                   
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF PGHS-1                                 
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE                   
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF COX-2                                  
DBREF  3MDL A   35   613  UNP    Q05769   PGH2_MOUSE      20    599             
DBREF  3MDL B   35   613  UNP    Q05769   PGH2_MOUSE      20    599             
SEQADV 3MDL ASN A   28  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL ALA A  594  UNP  Q05769    ASN   580 ENGINEERED                     
SEQADV 3MDL ASN B   28  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3MDL ALA B  594  UNP  Q05769    ASN   580 ENGINEERED                     
SEQRES   1 A  587  ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO          
SEQRES   2 A  587  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP          
SEQRES   3 A  587  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY          
SEQRES   4 A  587  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS          
SEQRES   5 A  587  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE          
SEQRES   6 A  587  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN          
SEQRES   7 A  587  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU          
SEQRES   8 A  587  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR          
SEQRES   9 A  587  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER          
SEQRES  10 A  587  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA          
SEQRES  11 A  587  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS          
SEQRES  12 A  587  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU          
SEQRES  13 A  587  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN          
SEQRES  14 A  587  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN          
SEQRES  15 A  587  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR          
SEQRES  16 A  587  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR          
SEQRES  17 A  587  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE          
SEQRES  18 A  587  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU          
SEQRES  19 A  587  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET          
SEQRES  20 A  587  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA          
SEQRES  21 A  587  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET          
SEQRES  22 A  587  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL          
SEQRES  23 A  587  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP          
SEQRES  24 A  587  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY          
SEQRES  25 A  587  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS          
SEQRES  26 A  587  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU          
SEQRES  27 A  587  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE          
SEQRES  28 A  587  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU          
SEQRES  29 A  587  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER          
SEQRES  30 A  587  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU          
SEQRES  31 A  587  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN          
SEQRES  32 A  587  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE          
SEQRES  33 A  587  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER          
SEQRES  34 A  587  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS          
SEQRES  35 A  587  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU          
SEQRES  36 A  587  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU          
SEQRES  37 A  587  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU          
SEQRES  38 A  587  LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU          
SEQRES  39 A  587  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY          
SEQRES  40 A  587  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS          
SEQRES  41 A  587  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE          
SEQRES  42 A  587  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL          
SEQRES  43 A  587  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO          
SEQRES  44 A  587  GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER          
SEQRES  45 A  587  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE          
SEQRES  46 A  587  LYS ARG                                                      
SEQRES   1 B  587  ASN HIS HIS HIS HIS HIS HIS PRO CYS CYS SER ASN PRO          
SEQRES   2 B  587  CYS GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP          
SEQRES   3 B  587  GLN TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY          
SEQRES   4 B  587  GLU ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS          
SEQRES   5 B  587  LEU LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE          
SEQRES   6 B  587  LEU THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN          
SEQRES   7 B  587  ILE PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU          
SEQRES   8 B  587  THR SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR          
SEQRES   9 B  587  ASN VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER          
SEQRES  10 B  587  ASN LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA          
SEQRES  11 B  587  ASP ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS          
SEQRES  12 B  587  GLU LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU          
SEQRES  13 B  587  LEU ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN          
SEQRES  14 B  587  MET MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN          
SEQRES  15 B  587  PHE PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR          
SEQRES  16 B  587  ARG GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR          
SEQRES  17 B  587  GLY GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE          
SEQRES  18 B  587  LYS ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU          
SEQRES  19 B  587  VAL TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET          
SEQRES  20 B  587  ILE TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA          
SEQRES  21 B  587  VAL GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET          
SEQRES  22 B  587  MET TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL          
SEQRES  23 B  587  CYS ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP          
SEQRES  24 B  587  GLU GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY          
SEQRES  25 B  587  GLU THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS          
SEQRES  26 B  587  LEU SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU          
SEQRES  27 B  587  LEU LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE          
SEQRES  28 B  587  ALA SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU          
SEQRES  29 B  587  LEU PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER          
SEQRES  30 B  587  PHE LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU          
SEQRES  31 B  587  HIS GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN          
SEQRES  32 B  587  ILE ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE          
SEQRES  33 B  587  ALA VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER          
SEQRES  34 B  587  ARG GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS          
SEQRES  35 B  587  ARG PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU          
SEQRES  36 B  587  THR GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU          
SEQRES  37 B  587  TYR SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU          
SEQRES  38 B  587  LEU VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU          
SEQRES  39 B  587  THR MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY          
SEQRES  40 B  587  LEU MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS          
SEQRES  41 B  587  PRO SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE          
SEQRES  42 B  587  ASN THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL          
SEQRES  43 B  587  LYS GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO          
SEQRES  44 B  587  GLN PRO THR LYS THR ALA THR ILE ALA ALA SER ALA SER          
SEQRES  45 B  587  HIS SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE          
SEQRES  46 B  587  LYS ARG                                                      
MODRES 3MDL ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDL ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDL ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDL ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDL ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDL ASN B  410  ASN  GLYCOSYLATION SITE                                 
HET    1AG  A   1      27                                                       
HET    AKR  A   2       5                                                       
HET    AKR  A   3       5                                                       
HET    GOL  A   4       6                                                       
HET    COH  A 614      43                                                       
HET    NAG  A 661      14                                                       
HET    NAG  A 662      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 672      14                                                       
HET    MAN  A 673      11                                                       
HET    NAG  A 681      14                                                       
HET    BOG  A 703      20                                                       
HET    GOL  B   7       6                                                       
HET    1AG  B   1      27                                                       
HET    AKR  B   3       5                                                       
HET    AKR  B   4       5                                                       
HET    AKR  B   5       5                                                       
HET    GOL  B   6       6                                                       
HET    COH  B 615      43                                                       
HET    NAG  B 661      14                                                       
HET    NAG  B 662      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 672      14                                                       
HET    NAG  B 681      14                                                       
HETNAM     1AG (2S)-2,3-DIHYDROXYPROPYL (5Z,8Z,11Z,14Z)-ICOSA-5,8,11,           
HETNAM   2 1AG  14-TETRAENOATE                                                  
HETNAM     AKR ACRYLIC ACID                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  1AG    2(C23 H38 O4)                                                
FORMUL   4  AKR    5(C3 H4 O2)                                                  
FORMUL   6  GOL    3(C3 H8 O3)                                                  
FORMUL   7  COH    2(C34 H32 CO N4 O4)                                          
FORMUL   8  NAG    10(C8 H15 N O6)                                              
FORMUL   9  MAN    C6 H12 O6                                                    
FORMUL  11  BOG    C14 H28 O6                                                   
FORMUL  22  HOH   *960(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  295  HIS A  320  1                                  26    
HELIX   13  13 GLY A  324  ASP A  347  1                                  24    
HELIX   14  14 ASP A  347  GLY A  354  1                                   8    
HELIX   15  15 ASP A  362  PHE A  367  5                                   6    
HELIX   16  16 ALA A  378  TYR A  385  1                                   8    
HELIX   17  17 TRP A  387  LEU A  391  5                                   5    
HELIX   18  18 SER A  403  LEU A  408  1                                   6    
HELIX   19  19 ASN A  410  GLN A  429  1                                  20    
HELIX   20  20 PRO A  441  ALA A  443  5                                   3    
HELIX   21  21 VAL A  444  MET A  458  1                                  15    
HELIX   22  22 SER A  462  PHE A  470  1                                   9    
HELIX   23  23 SER A  477  GLY A  483  1                                   7    
HELIX   24  24 LYS A  485  SER A  496  1                                  12    
HELIX   25  25 ASP A  497  MET A  501  5                                   5    
HELIX   26  26 GLU A  502  GLU A  510  1                                   9    
HELIX   27  27 GLY A  519  GLY A  536  1                                  18    
HELIX   28  28 ASN A  537  SER A  541  5                                   5    
HELIX   29  29 LYS A  546  GLY A  551  5                                   6    
HELIX   30  30 GLY A  552  THR A  561  1                                  10    
HELIX   31  31 SER A  563  VAL A  572  1                                  10    
HELIX   32  32 GLU B   73  LYS B   83  1                                  11    
HELIX   33  33 THR B   85  HIS B   95  1                                  11    
HELIX   34  34 PHE B   96  ASN B  104  1                                   9    
HELIX   35  35 ILE B  105A TYR B  122  1                                  18    
HELIX   36  36 SER B  138  ASN B  144  1                                   7    
HELIX   37  37 ASP B  173  LEU B  182  1                                  10    
HELIX   38  38 ASN B  195  HIS B  207  1                                  13    
HELIX   39  39 LEU B  230  GLY B  235  1                                   6    
HELIX   40  40 THR B  237  ARG B  245  1                                   9    
HELIX   41  41 THR B  265  GLN B  270  1                                   6    
HELIX   42  42 PRO B  280  GLN B  284  5                                   5    
HELIX   43  43 VAL B  291  LEU B  294  5                                   4    
HELIX   44  44 VAL B  295  HIS B  320  1                                  26    
HELIX   45  45 GLY B  324  ASP B  347  1                                  24    
HELIX   46  46 ASP B  347  GLY B  354  1                                   8    
HELIX   47  47 ASP B  362  PHE B  367  5                                   6    
HELIX   48  48 ALA B  378  TYR B  385  1                                   8    
HELIX   49  49 HIS B  386  LEU B  391  5                                   6    
HELIX   50  50 SER B  403  LEU B  408  1                                   6    
HELIX   51  51 ASN B  411  GLN B  429  1                                  19    
HELIX   52  52 PRO B  441  ALA B  443  5                                   3    
HELIX   53  53 VAL B  444  MET B  458  1                                  15    
HELIX   54  54 SER B  462  PHE B  470  1                                   9    
HELIX   55  55 SER B  477  GLY B  483  1                                   7    
HELIX   56  56 LYS B  485  SER B  496  1                                  12    
HELIX   57  57 ASP B  497  MET B  501  5                                   5    
HELIX   58  58 GLU B  502  GLU B  510  1                                   9    
HELIX   59  59 GLY B  519  GLY B  536  1                                  18    
HELIX   60  60 ASN B  537  SER B  541  5                                   5    
HELIX   61  61 LYS B  546  GLY B  551  5                                   6    
HELIX   62  62 GLY B  552  THR B  561  1                                  10    
HELIX   63  63 SER B  563  VAL B  572  1                                  10    
SHEET    1   A 2 GLU A  46  SER A  49  0                                        
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46           
SHEET    1   B 2 PHE A  64  TYR A  65  0                                        
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65           
SHEET    1   C 2 TYR A 130  ASN A 131  0                                        
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130           
SHEET    1   D 2 GLN A 255  ILE A 257  0                                        
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255           
SHEET    1   E 2 PHE A 395  ILE A 397  0                                        
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   F 2 GLU B  46  SER B  49  0                                        
SHEET    2   F 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46           
SHEET    1   G 2 PHE B  64  TYR B  65  0                                        
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   H 2 TYR B 130  ASN B 131  0                                        
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130           
SHEET    1   I 2 GLN B 255  ILE B 257  0                                        
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   J 2 PHE B 395  ILE B 397  0                                        
SHEET    2   J 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.05  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.02  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.05  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05  
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.44  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44  
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.44  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.44  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45  
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.45  
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.46  
LINK         NE2AHIS B 388                CO   COH B 615     1555   1555  2.27  
LINK         NE2AHIS A 388                CO   COH A 614     1555   1555  2.27  
CISPEP   1 SER A  126    PRO A  127          0         1.86                     
CISPEP   2 SER B  126    PRO B  127          0         1.00                     
SITE     1 AC1 20 VAL A 116  ARG A 120  PHE A 205  TYR A 348                    
SITE     2 AC1 20 VAL A 349  LEU A 352  SER A 353  TYR A 355                    
SITE     3 AC1 20 PHE A 381  TYR A 385  TRP A 387  PHE A 518                    
SITE     4 AC1 20 MET A 522  VAL A 523  GLY A 526  ALA A 527                    
SITE     5 AC1 20 SER A 530  LEU A 531  LEU A 534  HOH A1034                    
SITE     1 AC2  3 SER A 477  PHE A 478  GLU A 479                               
SITE     1 AC3  5 ARG A 240  LYS A 243  VAL A 271  GLU A 272                    
SITE     2 AC3  5 HOH A 846                                                     
SITE     1 AC4 10 HIS A  34  CYS A  36  CYS A  37  PRO A 154                    
SITE     2 AC4 10 VAL A 155  ALA A 156  CYS A 159  HOH A 676                    
SITE     3 AC4 10 HOH A 687  HOH A 968                                          
SITE     1 AC5 17 ALA A 199  PHE A 200  ALA A 202  GLN A 203                    
SITE     2 AC5 17 HIS A 207  PHE A 210  LYS A 211  THR A 212                    
SITE     3 AC5 17 HIS A 214  VAL A 295  ASN A 382  TYR A 385                    
SITE     4 AC5 17 HIS A 386  HIS A 388  LEU A 391  HOH A 853                    
SITE     5 AC5 17 HOH A1090                                                     
SITE     1 AC6  5 TYR A  55  GLU A  67  ASN A  68  NAG A 662                    
SITE     2 AC6  5 HOH A 792                                                     
SITE     1 AC7  1 NAG A 661                                                     
SITE     1 AC8  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC8  9 PHE A 220  HOH A 666  NAG A 672  HOH A 994                    
SITE     3 AC8  9 HOH A 998                                                     
SITE     1 AC9  3 ARG A 216  NAG A 671  MAN A 673                               
SITE     1 BC1  4 NAG A 672  HOH A 930  HOH A1027  HOH A1065                    
SITE     1 BC2  6 GLN A 406  ASN A 410  SER A 412  ILE A 413                    
SITE     2 BC2  6 GLU A 416  HOH A 932                                          
SITE     1 BC3 12 LYS A 180  ARG A 184  ARG A 185  ARG A 438                    
SITE     2 BC3 12 ILE A 442  GLU A 486  GLU A 490  GLU B 179                    
SITE     3 BC3 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445                    
SITE     1 BC4  5 GLN A 543  ARG B  44  ARG B  61  HOH B 683                    
SITE     2 BC4  5 HOH B1141                                                     
SITE     1 BC5 15 VAL B 116  PHE B 205  PHE B 209  VAL B 349                    
SITE     2 BC5 15 TYR B 355  ILE B 377  PHE B 381  TYR B 385                    
SITE     3 BC5 15 VAL B 523  ALA B 527  SER B 530  LEU B 531                    
SITE     4 BC5 15 GLY B 533  LEU B 534  HOH B 630                               
SITE     1 BC6  4 SER B 477  PHE B 478  GLU B 479  LYS B 492                    
SITE     1 BC7  4 ASP B 239  ARG B 240  LYS B 243  GLU B 272                    
SITE     1 BC8  1 ASN B  87                                                     
SITE     1 BC9  9 HIS B  34  CYS B  36  CYS B  37  PRO B 154                    
SITE     2 BC9  9 ALA B 156  HOH B 762  HOH B 964  HOH B 995                    
SITE     3 BC9  9 HOH B1106                                                     
SITE     1 CC1 16 ALA B 199  PHE B 200  ALA B 202  GLN B 203                    
SITE     2 CC1 16 HIS B 207  PHE B 210  LYS B 211  THR B 212                    
SITE     3 CC1 16 VAL B 295  ASN B 382  TYR B 385  HIS B 386                    
SITE     4 CC1 16 HIS B 388  LEU B 391  GLN B 454  HOH B 743                    
SITE     1 CC2  5 TYR B  55  GLU B  67  ASN B  68  NAG B 662                    
SITE     2 CC2  5 HOH B 803                                                     
SITE     1 CC3  1 NAG B 661                                                     
SITE     1 CC4  8 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 CC4  8 HOH B 625  NAG B 672  HOH B 697  HOH B 922                    
SITE     1 CC5  4 ARG B 216  NAG B 671  HOH B 906  HOH B1020                    
SITE     1 CC6  5 GLN B 406  ASN B 410  ILE B 413  HOH B 676                    
SITE     2 CC6  5 HOH B1096                                                     
CRYST1  118.958  131.773  179.858  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      0.008406  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007589  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005560        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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