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Database: PDB
Entry: 3QMO
LinkDB: 3QMO
Original site: 3QMO 
HEADER    OXIDOREDUCTASE                          04-FEB-11   3QMO              
TITLE     X-RAY CRYSTAL STRUCTURE OF NS-398 BOUND TO THE CYCLOOXYGENASE CHANNEL 
TITLE    2 OF CYCLOOXYGENASE-2                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED           
COMPND   5 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-         
COMPND   6 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2    
COMPND   7 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE       
COMPND   8 SYNTHASE 2, TIS10 PROTEIN;                                           
COMPND   9 EC: 1.14.99.1;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    BIOLOGICAL DIMER, OXIDOREDUCTASE, DIMER, N-GLYCOSYLATION, MONOTOPIC   
KEYWDS   2 MEMBRANE PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.VECCHIO,M.G.MALKOWSKI                                             
REVDAT   4   19-OCT-11 3QMO    1       JRNL                                     
REVDAT   3   28-SEP-11 3QMO    1       JRNL                                     
REVDAT   2   24-AUG-11 3QMO    1       JRNL                                     
REVDAT   1   03-AUG-11 3QMO    0                                                
JRNL        AUTH   A.J.VECCHIO,M.G.MALKOWSKI                                    
JRNL        TITL   THE STRUCTURE OF NS-398 BOUND TO CYCLOOXYGENASE-2.           
JRNL        REF    J.STRUCT.BIOL.                V. 176   254 2011              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   21843643                                                     
JRNL        DOI    10.1016/J.JSB.2011.07.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27226                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1452                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1956                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8750                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 346                                     
REMARK   3   SOLVENT ATOMS            : 120                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.06000                                              
REMARK   3    B22 (A**2) : -1.00000                                             
REMARK   3    B33 (A**2) : 0.94000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.400         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.277         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.887        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9413 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12837 ; 1.465 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1106 ; 5.459 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   424 ;38.484 ;23.726       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1421 ;16.511 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;15.206 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1386 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7219 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5518 ; 0.446 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8941 ; 0.905 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3895 ; 1.300 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3891 ; 2.331 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     33       A     583      1                      
REMARK   3           1     B     33       B     583      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   4288 ; 0.030 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   4288 ; 0.060 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QMO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063837.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9777                             
REMARK 200  MONOCHROMATOR                  : HORIZONTAL FOCUSING 5.05           
REMARK 200                                   ASYMMETRIC CUT SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27226                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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   (%): 51.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
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       60.21400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.60650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.78400            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.21400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.60650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.78400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.21400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.60650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.78400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.21400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.60650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.78400            
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: 13040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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     GLU A  46    OE1  OE2                                            
REMARK 470     ASP A  53    CG   OD1  OD2                                       
REMARK 470     GLN A  54    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  56    CD   CE   NZ                                        
REMARK 470     LEU A  75    CG   CD1  CD2                                       
REMARK 470     ILE A  78    CD1                                                 
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     LEU A  81    CG   CD1  CD2                                       
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     LYS A 114    NZ                                                  
REMARK 470     ASP A 157    OD1  OD2                                            
REMARK 470     LYS A 169    CG   CD   CE   NZ                                   
REMARK 470     GLU A 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     GLU A 186    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 215    CD   CE   NZ                                        
REMARK 470     ASP A 239    CG   OD1  OD2                                       
REMARK 470     LYS A 248    CE   NZ                                             
REMARK 470     LYS A 267    CE   NZ                                             
REMARK 470     ASP A 268    OD1  OD2                                            
REMARK 470     GLU A 272    CD   OE1  OE2                                       
REMARK 470     LEU A 294    CG   CD1  CD2                                       
REMARK 470     LYS A 317    NZ                                                  
REMARK 470     LYS A 358    CE   NZ                                             
REMARK 470     LYS A 360    NZ                                                  
REMARK 470     LYS A 405    CD   CE   NZ                                        
REMARK 470     GLU A 416    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 442    CD1                                                 
REMARK 470     LYS A 473    CG   CD   CE   NZ                                   
REMARK 470     GLU A 479    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 485    CG   CD   CE   NZ                                   
REMARK 470     LYS A 492    CD   CE   NZ                                        
REMARK 470     GLU A 553    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 573    CE   NZ                                             
REMARK 470     GLU B  46    OE1  OE2                                            
REMARK 470     ASP B  53    CG   OD1  OD2                                       
REMARK 470     GLN B  54    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  56    CD   CE   NZ                                        
REMARK 470     GLU B  73    OE1  OE2                                            
REMARK 470     LYS B  79    CG   CD   CE   NZ                                   
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     LYS B  97    CD   CE   NZ                                        
REMARK 470     ILE B 102    CG2  CD1                                            
REMARK 470     LYS B 114    CE   NZ                                             
REMARK 470     LYS B 166    NZ                                                  
REMARK 470     LYS B 169    CG   CD   CE   NZ                                   
REMARK 470     GLU B 170    CD   OE1  OE2                                       
REMARK 470     GLU B 186    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 215    CD   CE   NZ                                        
REMARK 470     ASP B 239    OD1  OD2                                            
REMARK 470     LYS B 248    CE   NZ                                             
REMARK 470     ASP B 268    OD1  OD2                                            
REMARK 470     GLU B 281    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 294    CG   CD1  CD2                                       
REMARK 470     LYS B 317    NZ                                                  
REMARK 470     LYS B 360    NZ                                                  
REMARK 470     ASN B 368    CG   OD1  ND2                                       
REMARK 470     LYS B 405    CD   CE   NZ                                        
REMARK 470     GLU B 416    CD   OE1  OE2                                       
REMARK 470     ARG B 428    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 473    CG   CD   CE   NZ                                   
REMARK 470     GLU B 479    OE1  OE2                                            
REMARK 470     LYS B 485    CG   CD   CE   NZ                                   
REMARK 470     LYS B 511    CE   NZ                                             
REMARK 470     GLU B 553    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 557    NZ                                                  
REMARK 470     LYS B 573    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   CG   ASN A   410     C1   NAG A   681              1.62            
REMARK 500   OD1  ASN A   410     C1   NAG A   681              1.71            
REMARK 500   ND2  ASN A   410     C2   NAG A   681              2.09            
REMARK 500   O4   NAG A   672     C1   MAN B   673              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  61       16.62     58.38                                   
REMARK 500    THR A 129      -87.81   -122.36                                   
REMARK 500    ARG A 185      -96.48    -91.64                                   
REMARK 500    HIS A 278        1.87    -65.20                                   
REMARK 500    TRP A 387       51.76    -95.40                                   
REMARK 500    GLU A 398     -119.57     52.10                                   
REMARK 500    TYR A 409      -20.31     86.51                                   
REMARK 500    SER A 496      -57.84     71.83                                   
REMARK 500    ARG B  61       13.57     58.12                                   
REMARK 500    THR B 129      -90.98   -125.03                                   
REMARK 500    ARG B 185      -96.65    -90.92                                   
REMARK 500    TRP B 387       50.28    -91.55                                   
REMARK 500    GLU B 398     -120.27     53.42                                   
REMARK 500    TYR B 409      -18.52     82.13                                   
REMARK 500    SER B 471       55.50     71.50                                   
REMARK 500    SER B 496      -54.97     76.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                             HEM B 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 HEM B 619   NA  102.0                                              
REMARK 620 3 HEM B 619   NB   95.6  90.2                                        
REMARK 620 4 HEM B 619   NC   93.6 164.4  87.0                                  
REMARK 620 5 HEM B 619   ND   96.5  91.4 167.2  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 620  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 620   NA   96.9                                              
REMARK 620 3 HEM A 620   NB   89.1  85.6                                        
REMARK 620 4 HEM A 620   NC   87.8 174.4  91.4                                  
REMARK 620 5 HEM A 620   ND   91.8  93.7 178.9  89.2                            
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 GOL A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NS4 A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NS4 B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HS5   RELATED DB: PDB                                   
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF              
REMARK 900 CYCLOOXYGENASE-2                                                     
REMARK 900 RELATED ID: 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: 3LN1   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CELECOXIB BOUND AT THE COX-2 ACTIVE SITE                
REMARK 900 RELATED ID: 6COX   RELATED DB: PDB                                   
REMARK 900 CYCLOOXYGENASE-2 COMPLEXED WITH A SELECTIVE INHIBITOR SC-558         
REMARK 900 RELATED ID: 3NT1   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF NAPROXEN:COX-2 COMPLEX                  
DBREF  3QMO A   10   618  UNP    Q05769   PGH2_MOUSE       1    604             
DBREF  3QMO B   10   618  UNP    Q05769   PGH2_MOUSE       1    604             
SEQADV 3QMO HIS A   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS A   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS A   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS A   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS A   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS A   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO ALA A  594  UNP  Q05769    ASN   580 ENGINEERED MUTATION            
SEQADV 3QMO HIS B   29  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS B   30  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS B   31  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS B   32  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS B   33  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO HIS B   34  UNP  Q05769              EXPRESSION TAG                 
SEQADV 3QMO 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 3QMO ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3QMO ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3QMO ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3QMO ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3QMO ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3QMO ASN A   68  ASN  GLYCOSYLATION SITE                                 
HET    GOL  A   1       6                                                       
HET    GOL  A   6       6                                                       
HET    GOL  A   7       6                                                       
HET    NS4  A 619      21                                                       
HET    HEM  A 620      43                                                       
HET    NAG  A 661      14                                                       
HET    NDG  A 662      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 672      14                                                       
HET    NAG  A 681      14                                                       
HET    BOG  A 703      20                                                       
HET    GOL  B   2       6                                                       
HET    GOL  B   3       6                                                       
HET    GOL  B   4       6                                                       
HET    MAN  B 673      11                                                       
HET    NS4  B   1      21                                                       
HET    HEM  B 619      43                                                       
HET    NAG  B 661      14                                                       
HET    NDG  B 662      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 672      14                                                       
HET    BMA  B 620      11                                                       
HET    NAG  B 681      14                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     NS4 N-[2-(CYCLOHEXYLOXY)-4-NITROPHENYL]METHANESULFONAMIDE            
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     HEM HEME                                                             
FORMUL   3  GOL    6(C3 H8 O3)                                                  
FORMUL   6  NS4    2(C13 H18 N2 O5 S)                                           
FORMUL   7  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   8  NAG    8(C8 H15 N O6)                                               
FORMUL   8  NDG    2(C8 H15 N O6)                                               
FORMUL  11  BOG    C14 H28 O6                                                   
FORMUL  15  MAN    C6 H12 O6                                                    
FORMUL  19  BMA    C6 H12 O6                                                    
FORMUL  21  HOH   *120(H2 O)                                                    
HELIX    1   1 HIS A   34  ASN A   39  5                                   6    
HELIX    2   2 GLU A   73  LYS A   83  1                                  11    
HELIX    3   3 THR A   85  HIS A   95  1                                  11    
HELIX    4   4 PHE A   96  ILE A  105A 1                                  11    
HELIX    5   5 ILE A  105A TYR A  122  1                                  18    
HELIX    6   6 SER A  138  ASN A  144  1                                   7    
HELIX    7   7 ASP A  173  LEU A  182  1                                  10    
HELIX    8   8 ASN A  195  HIS A  207  1                                  13    
HELIX    9   9 LEU A  230  GLY A  235  1                                   6    
HELIX   10  10 THR A  237  ARG A  245  1                                   9    
HELIX   11  11 THR A  265  GLN A  270  1                                   6    
HELIX   12  12 VAL A  295  HIS A  320  1                                  26    
HELIX   13  13 GLY A  324  ASP A  347  1                                  24    
HELIX   14  14 ASP A  347  GLY A  354  1                                   8    
HELIX   15  15 ASP A  362  PHE A  367  5                                   6    
HELIX   16  16 ALA A  378  TYR A  385  1                                   8    
HELIX   17  17 HIS A  386  LEU A  391  5                                   6    
HELIX   18  18 SER A  403  LEU A  408  1                                   6    
HELIX   19  19 ASN A  410  GLN A  429  1                                  20    
HELIX   20  20 PRO A  441  ALA A  443  5                                   3    
HELIX   21  21 VAL A  444  MET A  458  1                                  15    
HELIX   22  22 SER A  462  PHE A  470  1                                   9    
HELIX   23  23 SER A  477  GLY A  483  1                                   7    
HELIX   24  24 LYS A  485  SER A  496  1                                  12    
HELIX   25  25 ASP A  497  MET A  501  5                                   5    
HELIX   26  26 GLU A  502  GLU A  510  1                                   9    
HELIX   27  27 GLY A  519  GLY A  536  1                                  18    
HELIX   28  28 ASN A  537  SER A  541  5                                   5    
HELIX   29  29 LYS A  546  GLY A  551  5                                   6    
HELIX   30  30 GLY A  552  THR A  561  1                                  10    
HELIX   31  31 SER A  563  VAL A  572  1                                  10    
HELIX   32  32 HIS B   34  ASN B   39  5                                   6    
HELIX   33  33 GLU B   73  LYS B   83  1                                  11    
HELIX   34  34 THR B   85  HIS B   95  1                                  11    
HELIX   35  35 PHE B   96  ILE B  105A 1                                  11    
HELIX   36  36 ILE B  105A TYR B  122  1                                  18    
HELIX   37  37 SER B  138  ASN B  144  1                                   7    
HELIX   38  38 ASP B  173  LEU B  182  1                                  10    
HELIX   39  39 ASN B  195  HIS B  207  1                                  13    
HELIX   40  40 LEU B  230  GLY B  235  1                                   6    
HELIX   41  41 THR B  237  ARG B  245  1                                   9    
HELIX   42  42 THR B  265  GLN B  270  1                                   6    
HELIX   43  43 PRO B  280  GLN B  284  5                                   5    
HELIX   44  44 VAL B  295  HIS B  320  1                                  26    
HELIX   45  45 GLY B  324  ASP B  347  1                                  24    
HELIX   46  46 ASP B  347  GLY B  354  1                                   8    
HELIX   47  47 ASP B  362  PHE B  367  5                                   6    
HELIX   48  48 ALA B  378  TYR B  385  1                                   8    
HELIX   49  49 HIS B  386  LEU B  391  5                                   6    
HELIX   50  50 SER B  403  LEU B  408  1                                   6    
HELIX   51  51 ASN B  410  GLN B  429  1                                  20    
HELIX   52  52 PRO B  441  ALA B  443  5                                   3    
HELIX   53  53 VAL B  444  MET B  458  1                                  15    
HELIX   54  54 SER B  462  PHE B  470  1                                   9    
HELIX   55  55 SER B  477  GLY B  483  1                                   7    
HELIX   56  56 LYS B  485  SER B  496  1                                  12    
HELIX   57  57 ASP B  497  MET B  501  5                                   5    
HELIX   58  58 GLU B  502  GLU B  510  1                                   9    
HELIX   59  59 GLY B  519  GLY B  536  1                                  18    
HELIX   60  60 ASN B  537  SER B  541  5                                   5    
HELIX   61  61 LYS B  546  GLY B  551  5                                   6    
HELIX   62  62 GLY B  552  THR B  561  1                                  10    
HELIX   63  63 SER B  563  VAL B  572  1                                  10    
SHEET    1   A 2 GLU A  46  SER A  49  0                                        
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  LYS A  56   N  MET A  48           
SHEET    1   B 2 PHE A  64  TYR A  65  0                                        
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65           
SHEET    1   C 2 TYR A 130  ASN A 131  0                                        
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130           
SHEET    1   D 2 GLN A 255  ILE A 257  0                                        
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255           
SHEET    1   E 2 PHE A 395  ILE A 397  0                                        
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  GLN A 400   N  ILE A 397           
SHEET    1   F 2 GLU B  46  SER B  49  0                                        
SHEET    2   F 2 TYR B  55  ASP B  58 -1  O  LYS B  56   N  MET B  48           
SHEET    1   G 2 PHE B  64  TYR B  65  0                                        
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   H 2 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  GLN B 400   N  ILE B 397           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.06  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.06  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.05  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.06  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.06  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.06  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.04  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.05  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.05  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.07  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.29  
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.37  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.42  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.45  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45  
LINK         O4  NAG A 661                 C1  NDG A 662     1555   1555  1.46  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.46  
LINK         O4  NAG B 661                 C1  NDG B 662     1555   1555  1.46  
LINK         O4  NAG B 672                 C1  BMA B 620     1555   1555  1.46  
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.47  
LINK         NE2 HIS B 388                FE   HEM B 619     1555   1555  2.07  
LINK         NE2 HIS A 388                FE   HEM A 620     1555   1555  2.25  
LINK         O4  NAG A 672                 O5  MAN B 673     1555   1555  1.11  
LINK         ND2 ASN A 410                 O5  NAG A 681     1555   1555  1.52  
LINK         ND2 ASN B 144                 O5  NAG B 671     1555   1555  1.58  
CISPEP   1 SER A  126    PRO A  127          0        -3.16                     
CISPEP   2 SER B  126    PRO B  127          0        -3.15                     
SITE     1 AC1  7 CYS A  36  CYS A  37  ASN A  39  PRO A 154                    
SITE     2 AC1  7 VAL A 155  ALA A 156  HOH A 640                               
SITE     1 AC2  3 GLN A 203  HIS A 207  HEM A 620                               
SITE     1 AC3  3 SER A 143  LEU A 145  LEU B 224                               
SITE     1 AC4 12 HIS A  90  ARG A 120  LEU A 352  SER A 353                    
SITE     2 AC4 12 TYR A 355  TYR A 385  TRP A 387  PHE A 518                    
SITE     3 AC4 12 VAL A 523  ALA A 527  LEU A 531  HOH A 644                    
SITE     1 AC5 14 GOL A   6  TYR A 148  GLN A 203  HIS A 207                    
SITE     2 AC5 14 PHE A 210  LYS A 211  THR A 212  VAL A 295                    
SITE     3 AC5 14 ASN A 382  TYR A 385  HIS A 386  HIS A 388                    
SITE     4 AC5 14 LEU A 391  PHE A 404                                          
SITE     1 AC6  4 TYR A  55  GLU A  67  ASN A  68  NDG A 662                    
SITE     1 AC7  1 NAG A 661                                                     
SITE     1 AC8  6 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC8  6 HOH A 637  NAG A 672                                          
SITE     1 AC9  4 ARG A 216  NAG A 671  ASP B 239  MAN B 673                    
SITE     1 BC1  4 ASN A 410  SER A 412  ILE A 413  HOH A 670                    
SITE     1 BC2 11 GLU A 179  LYS A 180  ARG A 184  ARG A 185                    
SITE     2 BC2 11 ARG A 438  GLU A 486  GLU A 490  GLU B 179                    
SITE     3 BC2 11 ARG B 184  ILE B 442  GLN B 445                               
SITE     1 BC3  3 LEU A 224  SER B 143  HOH B 623                               
SITE     1 BC4  6 CYS B  36  CYS B  37  ASN B  39  PRO B 154                    
SITE     2 BC4  6 VAL B 155  ALA B 156                                          
SITE     1 BC5  4 HIS B 207  VAL B 291  LEU B 294  HEM B 619                    
SITE     1 BC6  3 NAG A 672  HIS B 242  HOH B 676                               
SITE     1 BC7 13 ARG B 120  VAL B 349  LEU B 352  SER B 353                    
SITE     2 BC7 13 TYR B 355  TRP B 387  PHE B 518  MET B 522                    
SITE     3 BC7 13 VAL B 523  GLY B 526  ALA B 527  LEU B 531                    
SITE     4 BC7 13 HOH B 626                                                     
SITE     1 BC8 13 GOL B   4  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 BC8 13 LYS B 211  THR B 212  HIS B 214  VAL B 295                    
SITE     3 BC8 13 ASN B 382  TYR B 385  HIS B 386  HIS B 388                    
SITE     4 BC8 13 LEU B 391                                                     
SITE     1 BC9  4 TYR B  55  GLU B  67  ASN B  68  NDG B 662                    
SITE     1 CC1  1 NAG B 661                                                     
SITE     1 CC2  7 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 CC2  7 PHE B 220  HOH B 659  NAG B 672                               
SITE     1 CC3  3 ARG B 216  BMA B 620  NAG B 671                               
SITE     1 CC4  3 HOH B 635  HOH B 668  NAG B 672                               
SITE     1 CC5  3 GLN B 406  ASN B 410  HOH B 643                               
CRYST1  120.428  131.213  179.568  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      0.008304  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007621  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005569        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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