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Database: PDB
Entry: 4E1G
LinkDB: 4E1G
Original site: 4E1G 
HEADER    OXIDOREDUCTASE                          06-MAR-12   4E1G              
TITLE     X-RAY CRYSTAL STRUCTURE OF ALPHA-LINOLENIC ACID BOUND TO THE          
TITLE    2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-604;                                        
COMPND   5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED           
COMPND   6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-         
COMPND   7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2    
COMPND   8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE       
COMPND   9 SYNTHASE 2, TIS10 PROTEIN;                                           
COMPND  10 EC: 1.14.99.1;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 STRAIN: WILD TYPE;                                                   
SOURCE   6 GENE: COX-2, COX2, PGHS-B, PTGS2, TIS10;                             
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;                               
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    MONOTOPIC MEMBRANE PROTEIN, BIOLOGICAL DIMER, OXIDOREDUCTASE, COX-2,  
KEYWDS   2 N-GLYCOSYLATION, MEMBRANE OF ER                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI                                             
REVDAT   3   01-AUG-12 4E1G    1       JRNL                                     
REVDAT   2   13-JUN-12 4E1G    1       JRNL                                     
REVDAT   1   25-APR-12 4E1G    0                                                
JRNL        AUTH   A.J.VECCHIO,B.J.ORLANDO,R.NANDAGIRI,M.G.MALKOWSKI            
JRNL        TITL   INVESTIGATING SUBSTRATE PROMISCUITY IN CYCLOOXYGENASE-2: THE 
JRNL        TITL 2 ROLE OF ARG-120 AND RESIDUES LINING THE HYDROPHOBIC GROOVE.  
JRNL        REF    J.BIOL.CHEM.                  V. 287 24619 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22637474                                                     
JRNL        DOI    10.1074/JBC.M112.372243                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 79080                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4154                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5579                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 289                          
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8840                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 335                                     
REMARK   3   SOLVENT ATOMS            : 746                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.41000                                              
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -0.56000                                             
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): 0.172         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.101         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.250         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9517 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12954 ; 2.044 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1118 ; 6.327 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   440 ;37.343 ;23.841       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1486 ;14.697 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;14.417 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1381 ; 0.148 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7317 ; 0.012 ; 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):  5541 ; 1.037 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9005 ; 1.757 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3976 ; 3.243 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3939 ; 4.852 ; 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  : 6                                          
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   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7541  45.6869  63.8335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0350 T22:    .1527                                     
REMARK   3      T33:    .1883 T12:   -.0394                                     
REMARK   3      T13:   -.0381 T23:   -.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6320 L22:   1.0370                                     
REMARK   3      L33:    .8200 L12:   -.6482                                     
REMARK   3      L13:    .0323 L23:    .4310                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0526 S12:   -.0470 S13:    .2179                       
REMARK   3      S21:   -.0423 S22:    .1793 S23:   -.2238                       
REMARK   3      S31:   -.1111 S32:    .3047 S33:   -.1268                       
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   115        A   226                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.3441  35.8213  66.9008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0729 T22:    .0686                                     
REMARK   3      T33:    .0695 T12:    .0196                                     
REMARK   3      T13:   -.0083 T23:    .0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6246 L22:    .7472                                     
REMARK   3      L33:    .4718 L12:   -.3485                                     
REMARK   3      L13:   -.0798 L23:    .3139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0673 S12:   -.0913 S13:   -.0387                       
REMARK   3      S21:    .0721 S22:    .0820 S23:    .0048                       
REMARK   3      S31:    .0384 S32:    .0680 S33:   -.0147                       
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   227        A   582                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3961  47.7015  66.4355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0389 T22:    .0351                                     
REMARK   3      T33:    .0532 T12:   -.0048                                     
REMARK   3      T13:   -.0074 T23:   -.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6613 L22:    .5279                                     
REMARK   3      L33:    .6480 L12:   -.4560                                     
REMARK   3      L13:    .0936 L23:    .0625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0271 S12:   -.1330 S13:   -.0008                       
REMARK   3      S21:    .0556 S22:    .0654 S23:    .0226                       
REMARK   3      S31:   -.0365 S32:   -.0069 S33:   -.0383                       
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 :   B    33        B   119                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.9869  57.8689  29.1286              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .2051 T22:    .0509                                     
REMARK   3      T33:    .1445 T12:   -.0577                                     
REMARK   3      T13:    .0664 T23:    .0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4679 L22:   1.3492                                     
REMARK   3      L33:   1.1293 L12:  -1.1801                                     
REMARK   3      L13:   -.2180 L23:    .1344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .2193 S12:    .0830 S13:    .2764                       
REMARK   3      S21:   -.2274 S22:   -.1146 S23:   -.3387                       
REMARK   3      S31:   -.4355 S32:    .1588 S33:   -.1047                       
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 :   B   120        B   228                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0893  41.0382  26.7697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0772 T22:    .0918                                     
REMARK   3      T33:    .0462 T12:    .0477                                     
REMARK   3      T13:   -.0160 T23:   -.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .3281 L22:    .6792                                     
REMARK   3      L33:    .7960 L12:   -.2177                                     
REMARK   3      L13:   -.2070 L23:    .3113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0916 S12:    .1063 S13:   -.0175                       
REMARK   3      S21:   -.1366 S22:   -.0954 S23:    .0146                       
REMARK   3      S31:   -.1490 S32:   -.0429 S33:    .0038                       
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 :   B   229        B   582                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3094  29.9826  27.3896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0287 T22:    .0678                                     
REMARK   3      T33:    .0493 T12:    .0130                                     
REMARK   3      T13:    .0044 T23:   -.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4960 L22:    .7349                                     
REMARK   3      L33:    .8355 L12:   -.3199                                     
REMARK   3      L13:    .0696 L23:    .0156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0733 S12:    .1375 S13:   -.0415                       
REMARK   3      S21:   -.1304 S22:   -.0245 S23:   -.0341                       
REMARK   3      S31:   -.0611 S32:    .0110 S33:   -.0488                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4E1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071048.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
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) : 0.9767                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79080                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1CVU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM      
REMARK 280  HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 296K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       60.18900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.06550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.21900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.18900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.06550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.21900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.18900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.06550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.21900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.18900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.06550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.21900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14210 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     GLN A   583                                                      
REMARK 465     ASP A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     THR A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     THR A   592                                                      
REMARK 465     ILE A   593                                                      
REMARK 465     ALA A   594                                                      
REMARK 465     ALA A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     HIS A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ARG A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     ILE A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     VAL A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     MET B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     PHE B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     CYS B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     LEU B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     HIS B    29                                                      
REMARK 465     HIS B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     HIS B    32                                                      
REMARK 465     GLN B   583                                                      
REMARK 465     ASP B   584                                                      
REMARK 465     PRO B   585                                                      
REMARK 465     GLN B   586                                                      
REMARK 465     PRO B   587                                                      
REMARK 465     THR B   588                                                      
REMARK 465     LYS B   589                                                      
REMARK 465     THR B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     THR B   592                                                      
REMARK 465     ILE B   593                                                      
REMARK 465     ALA B   594                                                      
REMARK 465     ALA B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     SER B   598                                                      
REMARK 465     HIS B   599                                                      
REMARK 465     SER B   600                                                      
REMARK 465     ARG B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     ASP B   603                                                      
REMARK 465     ASP B   604                                                      
REMARK 465     ILE B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     VAL B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     SER B   615                                                      
REMARK 465     THR B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     LEU B   618                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  53    CG   OD1  OD2                                       
REMARK 470     GLN A  54    CD   OE1  NE2                                       
REMARK 470     LYS A  56    CE   NZ                                             
REMARK 470     LEU A  75    CD1  CD2                                            
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     LEU A  81    CD1  CD2                                            
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     LYS A  97    CD   CE   NZ                                        
REMARK 470     LYS A 169    CD   CE   NZ                                        
REMARK 470     GLU A 170    CD   OE1  OE2                                       
REMARK 470     LYS A 175    NZ                                                  
REMARK 470     LYS A 215    CD   CE   NZ                                        
REMARK 470     ASP A 239    OD1  OD2                                            
REMARK 470     LYS A 248    CE   NZ                                             
REMARK 470     LYS A 267    CD   CE   NZ                                        
REMARK 470     GLU A 272    CD   OE1  OE2                                       
REMARK 470     LYS A 358    CE   NZ                                             
REMARK 470     LYS A 405    CD   CE   NZ                                        
REMARK 470     GLU A 416    OE1  OE2                                            
REMARK 470     LYS A 473    CG   CD   CE   NZ                                   
REMARK 470     LYS A 485    CE   NZ                                             
REMARK 470     LYS A 511    CE   NZ                                             
REMARK 470     LYS A 557    CG   CD   CE   NZ                                   
REMARK 470     GLN B  54    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  56    CE   NZ                                             
REMARK 470     LEU B  75    CD1  CD2                                            
REMARK 470     LYS B  79    CE   NZ                                             
REMARK 470     LYS B  83    CD   CE   NZ                                        
REMARK 470     LYS B  97    CE   NZ                                             
REMARK 470     LYS B 169    CD   CE   NZ                                        
REMARK 470     LYS B 215    CD   CE   NZ                                        
REMARK 470     ASP B 239    OD1  OD2                                            
REMARK 470     LYS B 267    NZ                                                  
REMARK 470     GLU B 281    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 358    CE   NZ                                             
REMARK 470     ASP B 399    OD1  OD2                                            
REMARK 470     LYS B 405    CE   NZ                                             
REMARK 470     GLU B 416    CD   OE1  OE2                                       
REMARK 470     LYS B 473    CD   CE   NZ                                        
REMARK 470     LYS B 492    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN B    68     O5   NAG B   703              1.55            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 275   CE2   TYR A 275   CD2     0.093                       
REMARK 500    CYS A 575   CB    CYS A 575   SG      0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 230   CB  -  CG  -  CD1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    LEU A 294   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    MET A 299   CG  -  SD  -  CE  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG B  44   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP B 173   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LEU B 294   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    MET B 458   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG B 467   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG B 467   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  60      119.36    -36.49                                   
REMARK 500    SER A 126      111.10   -160.33                                   
REMARK 500    THR A 129      -96.79   -125.37                                   
REMARK 500    TRP A 387       45.98    -90.16                                   
REMARK 500    GLU A 398     -123.60     60.84                                   
REMARK 500    ASN A 410       74.02   -111.28                                   
REMARK 500    SER A 496      -47.90     62.93                                   
REMARK 500    THR B 129      -92.34   -124.86                                   
REMARK 500    ARG B 185      -89.00    -88.14                                   
REMARK 500    TRP B 387       46.25    -88.86                                   
REMARK 500    GLU B 398     -117.63     59.49                                   
REMARK 500    TYR B 409       -1.61     73.48                                   
REMARK 500    ASN B 439       20.50   -140.83                                   
REMARK 500    SER B 496      -54.77     66.69                                   
REMARK 500    SER B 579     -169.57   -169.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A  581     VAL A  582                  145.05                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A 207        24.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 582        16.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 209        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1135        DISTANCE =  5.07 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 702  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 COH B 702   NA   88.8                                              
REMARK 620 3 COH B 702   NB   92.3  89.6                                        
REMARK 620 4 COH B 702   NC   86.9 175.1  92.9                                  
REMARK 620 5 COH B 702   ND   80.0  88.7 172.1  88.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             COH A 702  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 COH A 702   NA   80.8                                              
REMARK 620 3 COH A 702   NB   90.4  81.2                                        
REMARK 620 4 COH A 702   NC   89.8 169.8  95.2                                  
REMARK 620 5 COH A 702   ND   77.2  93.2 167.1  88.4                            
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 LNL A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNL B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 712                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TZI   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF              
REMARK 900 G533V MURINE COX-2                                                   
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF              
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 3HS6   RELATED DB: PDB                                   
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL            
REMARK 900 OF CYCLOOXYGENASE-2                                                  
REMARK 900 RELATED ID: 3HS7   RELATED DB: PDB                                   
REMARK 900 DOCOSAHEXAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF          
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 3QH0   RELATED DB: PDB                                   
REMARK 900 PALMITIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF                 
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1                                      
DBREF  4E1G A   10   618  UNP    Q05769   PGH2_MOUSE       1    604             
DBREF  4E1G B   10   618  UNP    Q05769   PGH2_MOUSE       1    604             
SEQADV 4E1G HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G ALA A  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION            
SEQADV 4E1G HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 4E1G ALA B  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION            
SEQRES   1 A  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 A  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO          
SEQRES   3 A  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET          
SEQRES   4 A  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG          
SEQRES   5 A  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE          
SEQRES   6 A  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN          
SEQRES   7 A  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP          
SEQRES   8 A  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE          
SEQRES   9 A  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP          
SEQRES  10 A  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER          
SEQRES  11 A  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA          
SEQRES  12 A  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY          
SEQRES  13 A  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL          
SEQRES  14 A  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP          
SEQRES  15 A  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN          
SEQRES  16 A  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG          
SEQRES  17 A  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP          
SEQRES  18 A  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS          
SEQRES  19 A  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN          
SEQRES  20 A  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP          
SEQRES  21 A  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU          
SEQRES  22 A  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU          
SEQRES  23 A  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG          
SEQRES  24 A  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS          
SEQRES  25 A  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG          
SEQRES  26 A  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU          
SEQRES  27 A  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU          
SEQRES  28 A  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN          
SEQRES  29 A  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR          
SEQRES  30 A  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU          
SEQRES  31 A  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN          
SEQRES  32 A  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU          
SEQRES  33 A  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY          
SEQRES  34 A  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA          
SEQRES  35 A  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU          
SEQRES  36 A  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR          
SEQRES  37 A  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA          
SEQRES  38 A  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU          
SEQRES  39 A  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP          
SEQRES  40 A  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO          
SEQRES  41 A  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER          
SEQRES  42 A  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL          
SEQRES  43 A  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU          
SEQRES  44 A  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE          
SEQRES  45 A  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE          
SEQRES  46 A  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN          
SEQRES  47 A  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU              
SEQRES   1 B  610  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY          
SEQRES   2 B  610  LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO          
SEQRES   3 B  610  CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET          
SEQRES   4 B  610  SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG          
SEQRES   5 B  610  THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE          
SEQRES   6 B  610  LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN          
SEQRES   7 B  610  THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP          
SEQRES   8 B  610  ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE          
SEQRES   9 B  610  MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP          
SEQRES  10 B  610  SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER          
SEQRES  11 B  610  TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA          
SEQRES  12 B  610  LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY          
SEQRES  13 B  610  VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL          
SEQRES  14 B  610  LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP          
SEQRES  15 B  610  PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN          
SEQRES  16 B  610  HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG          
SEQRES  17 B  610  GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP          
SEQRES  18 B  610  LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS          
SEQRES  19 B  610  LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN          
SEQRES  20 B  610  VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP          
SEQRES  21 B  610  THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU          
SEQRES  22 B  610  ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU          
SEQRES  23 B  610  VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG          
SEQRES  24 B  610  GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS          
SEQRES  25 B  610  PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG          
SEQRES  26 B  610  LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU          
SEQRES  27 B  610  ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU          
SEQRES  28 B  610  LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN          
SEQRES  29 B  610  TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR          
SEQRES  30 B  610  HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU          
SEQRES  31 B  610  ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN          
SEQRES  32 B  610  SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU          
SEQRES  33 B  610  SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY          
SEQRES  34 B  610  ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA          
SEQRES  35 B  610  SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU          
SEQRES  36 B  610  ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR          
SEQRES  37 B  610  SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA          
SEQRES  38 B  610  GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU          
SEQRES  39 B  610  LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP          
SEQRES  40 B  610  ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO          
SEQRES  41 B  610  PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER          
SEQRES  42 B  610  PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL          
SEQRES  43 B  610  GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU          
SEQRES  44 B  610  ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE          
SEQRES  45 B  610  ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE          
SEQRES  46 B  610  ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN          
SEQRES  47 B  610  PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU              
MODRES 4E1G ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4E1G ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4E1G ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4E1G ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4E1G ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 4E1G ASN A  410  ASN  GLYCOSYLATION SITE                                 
HET    LNL  A 701      20                                                       
HET    COH  A 702      43                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    NAG  A 705      14                                                       
HET    NAG  A 706      14                                                       
HET    MAN  A 707      11                                                       
HET    NAG  A 708      14                                                       
HET    BOG  A 709      20                                                       
HET    EDO  A 710       4                                                       
HET    EDO  A 711       4                                                       
HET    AKR  A 712       5                                                       
HET    AKR  A 713       5                                                       
HET    LNL  B 701      20                                                       
HET    COH  B 702      43                                                       
HET    NAG  B 703      14                                                       
HET    NAG  B 704      14                                                       
HET    NAG  B 705      14                                                       
HET    NAG  B 706      14                                                       
HET    NAG  B 707      14                                                       
HET    EDO  B 708       4                                                       
HET    EDO  B 709       4                                                       
HET    EDO  B 710       4                                                       
HET    EDO  B 711       4                                                       
HET    EDO  B 712       4                                                       
HETNAM     LNL ALPHA-LINOLENIC ACID                                             
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     AKR ACRYLIC ACID                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  LNL    2(C18 H30 O2)                                                
FORMUL   4  COH    2(C34 H32 CO N4 O4)                                          
FORMUL   5  NAG    10(C8 H15 N O6)                                              
FORMUL   6  MAN    C6 H12 O6                                                    
FORMUL   8  BOG    C14 H28 O6                                                   
FORMUL   9  EDO    7(C2 H6 O2)                                                  
FORMUL  11  AKR    2(C3 H4 O2)                                                  
FORMUL  23  HOH   *746(H2 O)                                                    
HELIX    1   1 GLU A   73  LYS A   83  1                                  11    
HELIX    2   2 THR A   85  THR A   94  1                                  10    
HELIX    3   3 PHE A   96  ASN A  105  1                                  10    
HELIX    4   4 ILE A  105A TYR A  122  1                                  18    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  ARG A  245  1                                   9    
HELIX   10  10 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 PRO A  280  GLN A  284  5                                   5    
HELIX   12  12 VAL A  291  LEU A  294  5                                   4    
HELIX   13  13 VAL A  295  HIS A  320  1                                  26    
HELIX   14  14 GLY A  324  ASP A  347  1                                  24    
HELIX   15  15 ASP A  347  GLY A  354  1                                   8    
HELIX   16  16 ASP A  362  PHE A  367  5                                   6    
HELIX   17  17 ALA A  378  TYR A  385  1                                   8    
HELIX   18  18 HIS A  386  LEU A  391  5                                   6    
HELIX   19  19 SER A  403  LEU A  408  1                                   6    
HELIX   20  20 ASN A  410  GLN A  429  1                                  20    
HELIX   21  21 PRO A  441  ALA A  443  5                                   3    
HELIX   22  22 VAL A  444  MET A  458  1                                  15    
HELIX   23  23 SER A  462  PHE A  470  1                                   9    
HELIX   24  24 SER A  477  GLY A  483  1                                   7    
HELIX   25  25 LYS A  485  SER A  496  1                                  12    
HELIX   26  26 ASP A  497  MET A  501  5                                   5    
HELIX   27  27 GLU A  502  GLU A  510  1                                   9    
HELIX   28  28 GLY A  519  GLY A  536  1                                  18    
HELIX   29  29 ASN A  537  SER A  541  5                                   5    
HELIX   30  30 LYS A  546  GLY A  551  5                                   6    
HELIX   31  31 GLY A  552  THR A  561  1                                  10    
HELIX   32  32 SER A  563  VAL A  572  1                                  10    
HELIX   33  33 GLU B   73  LYS B   83  1                                  11    
HELIX   34  34 THR B   85  THR B   94  1                                  10    
HELIX   35  35 PHE B   96  ASN B  105  1                                  10    
HELIX   36  36 ILE B  105A LEU B  123  1                                  19    
HELIX   37  37 SER B  138  ASN B  144  1                                   7    
HELIX   38  38 ASP B  173  LEU B  182  1                                  10    
HELIX   39  39 ASN B  195  HIS B  207  1                                  13    
HELIX   40  40 LEU B  230  GLY B  235  1                                   6    
HELIX   41  41 THR B  237  ARG B  245  1                                   9    
HELIX   42  42 THR B  265  GLN B  270  1                                   6    
HELIX   43  43 PRO B  280  GLN B  284  5                                   5    
HELIX   44  44 VAL B  291  LEU B  294  5                                   4    
HELIX   45  45 VAL B  295  HIS B  320  1                                  26    
HELIX   46  46 GLY B  324  ASP B  347  1                                  24    
HELIX   47  47 ASP B  347  GLY B  354  1                                   8    
HELIX   48  48 ASP B  362  PHE B  367  5                                   6    
HELIX   49  49 ALA B  378  TYR B  385  1                                   8    
HELIX   50  50 HIS B  386  LEU B  391  5                                   6    
HELIX   51  51 SER B  403  LEU B  408  1                                   6    
HELIX   52  52 ASN B  411  GLY B  418  1                                   8    
HELIX   53  53 GLY B  418  GLN B  429  1                                  12    
HELIX   54  54 PRO B  441  ALA B  443  5                                   3    
HELIX   55  55 VAL B  444  MET B  458  1                                  15    
HELIX   56  56 SER B  462  PHE B  470  1                                   9    
HELIX   57  57 SER B  477  GLY B  483  1                                   7    
HELIX   58  58 LYS B  485  SER B  496  1                                  12    
HELIX   59  59 ASP B  497  MET B  501  5                                   5    
HELIX   60  60 GLU B  502  GLU B  510  1                                   9    
HELIX   61  61 GLY B  519  GLY B  536  1                                  18    
HELIX   62  62 ASN B  537  SER B  541  5                                   5    
HELIX   63  63 LYS B  546  GLY B  551  5                                   6    
HELIX   64  64 GLY B  552  THR B  561  1                                  10    
HELIX   65  65 SER B  563  VAL B  572  1                                  10    
SHEET    1   A 2 GLU A  46  GLY A  51  0                                        
SHEET    2   A 2 GLN A  54  ASP A  58 -1  O  GLN A  54   N  THR A  50           
SHEET    1   B 2 PHE A  64  TYR A  65  0                                        
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65           
SHEET    1   C 2 GLN A 255  ILE A 257  0                                        
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257           
SHEET    1   D 2 PHE A 395  ILE A 397  0                                        
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   E 2 GLU B  46  SER B  49  0                                        
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46           
SHEET    1   F 2 PHE B  64  TYR B  65  0                                        
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   G 2 THR B 212  ASP B 213  0                                        
SHEET    2   G 2 GLY B 217  THR B 221 -1  O  GLY B 217   N  ASP B 213           
SHEET    1   H 2 GLN B 255  ILE B 257  0                                        
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   I 2 PHE B 395  ILE B 397  0                                        
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.08  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.01  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.10  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.09  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.14  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.07  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.02  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.06  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.07  
LINK         ND2 ASN B  68                 C1  NAG B 703     1555   1555  1.34  
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.43  
LINK         O4  NAG A 703                 C1  NAG A 704     1555   1555  1.43  
LINK         ND2 ASN B 144                 C1  NAG B 705     1555   1555  1.43  
LINK         ND2 ASN A  68                 C1  NAG A 703     1555   1555  1.44  
LINK         ND2 ASN A 144                 C1  NAG A 705     1555   1555  1.44  
LINK         O4  NAG A 705                 C1  NAG A 706     1555   1555  1.45  
LINK         ND2 ASN B 410                 C1  NAG B 707     1555   1555  1.45  
LINK         O4  NAG B 705                 C1  NAG B 706     1555   1555  1.45  
LINK         O4  NAG A 706                 C1  MAN A 707     1555   1555  1.45  
LINK         ND2 ASN A 410                 C1  NAG A 708     1555   1555  1.46  
LINK         NE2AHIS B 388                CO   COH B 702     1555   1555  2.38  
LINK         NE2BHIS A 388                CO   COH A 702     1555   1555  2.72  
CISPEP   1 SER A  126    PRO A  127          0        -0.92                     
CISPEP   2 SER B  126    PRO B  127          0         1.15                     
SITE     1 AC1 13 ARG A 120  PHE A 205  PHE A 209  TYR A 348                    
SITE     2 AC1 13 VAL A 349  TYR A 355  ILE A 377  PHE A 381                    
SITE     3 AC1 13 TYR A 385  ALA A 527  SER A 530  GLY A 533                    
SITE     4 AC1 13 LEU A 534                                                     
SITE     1 AC2 15 ALA A 199  GLN A 203  HIS A 207  PHE A 210                    
SITE     2 AC2 15 THR A 212  HIS A 214  VAL A 295  ASN A 382                    
SITE     3 AC2 15 TYR A 385  HIS A 386  HIS A 388  LEU A 391                    
SITE     4 AC2 15 LEU A 408  VAL A 447  HOH A1080                               
SITE     1 AC3  7 TYR A  55  GLU A  67  ASN A  68  NAG A 704                    
SITE     2 AC3  7 HOH A 882  HOH A1078  HOH A1162                               
SITE     1 AC4  3 NAG A 703  HOH A1078  HOH A1153                               
SITE     1 AC5  9 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC5  9 NAG A 706  HOH A 847  HOH A 904  HOH A 914                    
SITE     3 AC5  9 HOH A1077                                                     
SITE     1 AC6  3 ARG A 216  NAG A 705  MAN A 707                               
SITE     1 AC7  2 NAG A 706  HOH A1180                                          
SITE     1 AC8  3 ASN A 410  SER A 412  ILE A 413                               
SITE     1 AC9 11 GLU A 179  LYS A 180  ARG A 184  ARG A 185                    
SITE     2 AC9 11 ARG A 438  GLU A 486  GLU A 490  GLU B 179                    
SITE     3 AC9 11 ARG B 185  ILE B 442  GLN B 445                               
SITE     1 BC1  6 PRO A 162  SER A 455  ARG A 456  LYS A 459                    
SITE     2 BC1  6 TYR A 460  HOH A 942                                          
SITE     1 BC2  8 GLU A 308  ARG A 311  GLU A 339  SER A 566                    
SITE     2 BC2  8 LEU A 567  ASN A 570  ASN A 571  HOH A 845                    
SITE     1 BC3  5 SER A 477  PHE A 478  GLU A 479  LYS A 492                    
SITE     2 BC3  5 HOH A1076                                                     
SITE     1 BC4  6 ASP A 239  ARG A 240  LYS A 243  VAL A 271                    
SITE     2 BC4  6 GLU A 272  HOH A1114                                          
SITE     1 BC5 14 ARG B 120  PHE B 205  PHE B 209  TYR B 348                    
SITE     2 BC5 14 VAL B 349  LEU B 352  TYR B 355  ILE B 377                    
SITE     3 BC5 14 PHE B 381  TYR B 385  ALA B 527  SER B 530                    
SITE     4 BC5 14 GLY B 533  LEU B 534                                          
SITE     1 BC6 17 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 BC6 17 LYS B 211  THR B 212  HIS B 214  VAL B 295                    
SITE     3 BC6 17 ASN B 382  TYR B 385  HIS B 386  TRP B 387                    
SITE     4 BC6 17 HIS B 388  LEU B 391  LEU B 408  VAL B 447                    
SITE     5 BC6 17 HOH B1119                                                     
SITE     1 BC7  5 TYR B  55  GLU B  67  ASN B  68  NAG B 704                    
SITE     2 BC7  5 HOH B1004                                                     
SITE     1 BC8  1 NAG B 703                                                     
SITE     1 BC9  9 LEU A 238  GLU B 140  ASN B 144  ARG B 216                    
SITE     2 BC9  9 NAG B 706  HOH B 802  HOH B 916  HOH B1019                    
SITE     3 BC9  9 HOH B1117                                                     
SITE     1 CC1  3 ARG B 216  NAG B 705  HOH B1091                               
SITE     1 CC2  6 GLN B 406  ASN B 410  ILE B 413  HOH B 937                    
SITE     2 CC2  6 HOH B 938  HOH B1125                                          
SITE     1 CC3  5 PRO B 162  ARG B 456  LYS B 459  TYR B 460                    
SITE     2 CC3  5 HOH B 914                                                     
SITE     1 CC4  5 ARG B 240  LYS B 243  GLN B 270  VAL B 271                    
SITE     2 CC4  5 GLU B 272                                                     
SITE     1 CC5  6 LYS B 251  TYR B 254  VAL B 261  ASN B 310                    
SITE     2 CC5  6 HOH B 857  HOH B1007                                          
SITE     1 CC6  6 LEU A 224  SER B 143  HOH B 867  HOH B 911                    
SITE     2 CC6  6 HOH B 954  HOH B1093                                          
SITE     1 CC7  7 GLU B 308  ARG B 311  GLU B 339  SER B 566                    
SITE     2 CC7  7 LEU B 567  ASN B 570  HOH B 854                               
CRYST1  120.378  132.131  180.438  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      0.008307  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007568  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005542        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system