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Database: PDB
Entry: 2OYU
LinkDB: 2OYU
Original site: 2OYU 
HEADER    OXIDOREDUCTASE                          23-FEB-07   2OYU              
TITLE     INDOMETHACIN-(S)-ALPHA-ETHYL-ETHANOLAMIDE BOUND TO CYCLOOXYGENASE-1   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;                              
COMPND   3 CHAIN: P;                                                            
COMPND   4 SYNONYM: CYCLOOXYGENASE-1, COX-1, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 1, PROSTAGLANDIN H2 SYNTHASE 1, PGH SYNTHASE 1, PGHS-1, PHS 1;       
COMPND   6 EC: 1.14.99.1                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;                                     
SOURCE   3 ORGANISM_COMMON: SHEEP;                                              
SOURCE   4 ORGANISM_TAXID: 9940;                                                
SOURCE   5 OTHER_DETAILS: SHEEP VESICULAR GLAND                                 
KEYWDS    COX, PGHS, INDOMETHACIN, NSAID, HEME, OXIDOREDUCTASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.HARMAN,R.M.GARAVITO                                               
REVDAT   4   13-JUL-11 2OYU    1       VERSN                                    
REVDAT   3   24-FEB-09 2OYU    1       VERSN                                    
REVDAT   2   09-OCT-07 2OYU    1       JRNL                                     
REVDAT   1   24-JUL-07 2OYU    0                                                
JRNL        AUTH   C.A.HARMAN,M.V.TURMAN,K.R.KOZAK,L.J.MARNETT,W.L.SMITH,       
JRNL        AUTH 2 R.M.GARAVITO                                                 
JRNL        TITL   STRUCTURAL BASIS OF ENANTIOSELECTIVE INHIBITION OF           
JRNL        TITL 2 CYCLOOXYGENASE-1 BY S-ALPHA-SUBSTITUTED INDOMETHACIN         
JRNL        TITL 3 ETHANOLAMIDES.                                               
JRNL        REF    J.BIOL.CHEM.                  V. 282 28096 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17656360                                                     
JRNL        DOI    10.1074/JBC.M701335200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 27878                          
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) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1400                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1912                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4408                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 192                                     
REMARK   3   SOLVENT ATOMS            : 52                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.94000                                              
REMARK   3    B22 (A**2) : 0.94000                                              
REMARK   3    B33 (A**2) : -1.41000                                             
REMARK   3    B12 (A**2) : 0.47000                                              
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): 0.510         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.336         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.352         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.204        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4761 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6509 ; 1.520 ; 2.018       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   552 ; 6.412 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   209 ;38.495 ;22.967       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   703 ;20.021 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.336 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   701 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3639 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2534 ; 0.243 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3301 ; 0.324 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   183 ; 0.147 ; 0.200       
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):    64 ; 0.230 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.213 ; 0.200       
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):  2828 ; 0.371 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4472 ; 0.656 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2209 ; 1.005 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2035 ; 1.665 ; 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  : 1                                          
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 :   P    35        P   582                          
REMARK   3    ORIGIN FOR THE GROUP (A): 245.9604  99.6051 -36.3582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2570 T22:  -0.3506                                     
REMARK   3      T33:  -0.2234 T12:  -0.4447                                     
REMARK   3      T13:  -0.0243 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1297 L22:   0.7273                                     
REMARK   3      L33:   1.6470 L12:  -0.5156                                     
REMARK   3      L13:  -0.0687 L23:   0.1519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0243 S12:   0.2693 S13:  -0.0627                       
REMARK   3      S21:  -0.0758 S22:  -0.0737 S23:   0.0003                       
REMARK   3      S31:   0.6082 S32:  -0.3265 S33:   0.0494                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2OYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041754.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28010                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 19.000                             
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DIY (PROTEIN ONLY)                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM CHLORIDE,        
REMARK 280  SODIUM AZIDE, AND BETA-OCTYLGLUCOSIDE, PH 6.5, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 273K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.93200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.46600            
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       51.69900            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.23300            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.16500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.93200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       34.46600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       17.23300            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       51.69900            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       86.16500            
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 14490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P                                     
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 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       68.93200            
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 P     1                                                      
REMARK 465     SER P     2                                                      
REMARK 465     ARG P     3                                                      
REMARK 465     GLN P     4                                                      
REMARK 465     SER P     5                                                      
REMARK 465     ILE P     6                                                      
REMARK 465     SER P     7                                                      
REMARK 465     LEU P     8                                                      
REMARK 465     ARG P     9                                                      
REMARK 465     PHE P    10                                                      
REMARK 465     PRO P    11                                                      
REMARK 465     LEU P    12                                                      
REMARK 465     LEU P    13                                                      
REMARK 465     LEU P    14                                                      
REMARK 465     LEU P    15                                                      
REMARK 465     LEU P    16                                                      
REMARK 465     LEU P    17                                                      
REMARK 465     SER P    18                                                      
REMARK 465     PRO P    19                                                      
REMARK 465     SER P    20                                                      
REMARK 465     PRO P    21                                                      
REMARK 465     VAL P    22                                                      
REMARK 465     PHE P    23                                                      
REMARK 465     SER P    24                                                      
REMARK 465     ALA P    25                                                      
REMARK 465     ASP P    26                                                      
REMARK 465     PRO P    27                                                      
REMARK 465     GLY P    28                                                      
REMARK 465     ALA P    29                                                      
REMARK 465     PRO P    30                                                      
REMARK 465     ALA P    31                                                      
REMARK 465     PRO P   585                                                      
REMARK 465     ARG P   586                                                      
REMARK 465     GLN P   587                                                      
REMARK 465     GLU P   588                                                      
REMARK 465     ASP P   589                                                      
REMARK 465     ARG P   590                                                      
REMARK 465     PRO P   591                                                      
REMARK 465     GLY P   592                                                      
REMARK 465     VAL P   593                                                      
REMARK 465     GLU P   594                                                      
REMARK 465     ARG P   595                                                      
REMARK 465     PRO P   596                                                      
REMARK 465     PRO P   597                                                      
REMARK 465     THR P   598                                                      
REMARK 465     GLU P   599                                                      
REMARK 465     LEU P   600                                                      
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     ARG P  79    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG P  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS P 169    CG   CD   CE   NZ                                   
REMARK 470     GLN P 170    CG   CD   OE1  NE2                                  
REMARK 470     ASP P 173    CG   OD1  OD2                                       
REMARK 470     GLU P 175    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 186    CG   CD   CE   NZ                                   
REMARK 470     LYS P 215    CG   CD   CE   NZ                                   
REMARK 470     LYS P 248    CG   CD   CE   NZ                                   
REMARK 470     GLU P 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU P 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 317    CG   CD   CE   NZ                                   
REMARK 470     ARG P 396    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN P 400    CG   CD   OE1  NE2                                  
REMARK 470     GLU P 405    CG   CD   OE1  OE2                                  
REMARK 470     ASP P 416    CG   OD1  OD2                                       
REMARK 470     LYS P 473    CG   CD   CE   NZ                                   
REMARK 470     GLN P 479    CG   CD   OE1  NE2                                  
REMARK 470     LYS P 485    CG   CD   CE   NZ                                   
REMARK 470     GLU P 486    CG   CD   OE1  OE2                                  
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    ASP P  53       22.31   -164.17                                   
REMARK 500    CYS P  69       64.22     69.67                                   
REMARK 500    THR P 129      -80.15   -113.47                                   
REMARK 500    VAL P 145        8.11    -67.77                                   
REMARK 500    PRO P 160      -72.88    -60.13                                   
REMARK 500    PRO P 172      126.01    -39.86                                   
REMARK 500    ASP P 173       99.72    -59.06                                   
REMARK 500    ALA P 174      -63.12    -13.97                                   
REMARK 500    ARG P 185      -90.86    -80.74                                   
REMARK 500    HIS P 204      -72.31    -39.70                                   
REMARK 500    ASP P 249       25.34     48.73                                   
REMARK 500    VAL P 271      137.03   -179.74                                   
REMARK 500    LEU P 272      108.81    -52.38                                   
REMARK 500    ILE P 279       72.29   -119.53                                   
REMARK 500    PRO P 281     -100.82   -103.35                                   
REMARK 500    SER P 283      -42.57     79.12                                   
REMARK 500    GLU P 290       15.44    -66.63                                   
REMARK 500    LEU P 294      -88.28    -62.07                                   
REMARK 500    TYR P 348      -71.07    -55.05                                   
REMARK 500    ASN P 410       98.09    -59.35                                   
REMARK 500    PRO P 430     -150.64    -55.80                                   
REMARK 500    ALA P 431      151.53    178.86                                   
REMARK 500    ASN P 439        7.29   -150.21                                   
REMARK 500    PRO P 583      172.63    -56.68                                   
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    ASP P 584        22.3      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 P 802        DISTANCE =  5.96 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BOG P  750                                                       
REMARK 610     BOG P  751                                                       
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 P 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P 388   NE2                                                    
REMARK 620 2 HEM P 601   NA   77.7                                              
REMARK 620 3 HEM P 601   NB  106.2  91.2                                        
REMARK 620 4 HEM P 601   NC  117.5 163.7  89.9                                  
REMARK 620 5 HEM P 601   ND   83.8  82.3 166.7  93.2                            
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 NAG P 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA P 673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG P 750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG P 751                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMS P 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PGG   RELATED DB: PDB                                   
REMARK 900 INDOMETHACIN BOUND TO COX-1 (TRANS MODEL)                            
REMARK 900 RELATED ID: 1PGF   RELATED DB: PDB                                   
REMARK 900 INDOMETHACIN BOUND TO COX-1                                          
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB                                   
REMARK 900 FLURIBPROFEN BOUND TO COX-1                                          
REMARK 900 RELATED ID: 1EQE   RELATED DB: PDB                                   
REMARK 900 FLURBIPROFEN BOUND TO COX-1 (HIGHER RESOLUTION)                      
REMARK 900 RELATED ID: 2OYE   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 THERE IS A SEQUENCE CONFLICT IN UNP DATABASE AT RESIDUE 92           
REMARK 999 (MET -> LEU).                                                        
DBREF  2OYU P    1   600  UNP    P05979   PGH1_SHEEP       1    600             
SEQADV 2OYU LEU P   92  UNP  P05979    MET    92 SEE REMARK 999                 
SEQRES   1 P  600  MET SER ARG GLN SER ILE SER LEU ARG PHE PRO LEU LEU          
SEQRES   2 P  600  LEU LEU LEU LEU SER PRO SER PRO VAL PHE SER ALA ASP          
SEQRES   3 P  600  PRO GLY ALA PRO ALA PRO VAL ASN PRO CYS CYS TYR TYR          
SEQRES   4 P  600  PRO CYS GLN HIS GLN GLY ILE CYS VAL ARG PHE GLY LEU          
SEQRES   5 P  600  ASP ARG TYR GLN CYS ASP CYS THR ARG THR GLY TYR SER          
SEQRES   6 P  600  GLY PRO ASN CYS THR ILE PRO GLU ILE TRP THR TRP LEU          
SEQRES   7 P  600  ARG THR THR LEU ARG PRO SER PRO SER PHE ILE HIS PHE          
SEQRES   8 P  600  LEU LEU THR HIS GLY ARG TRP LEU TRP ASP PHE VAL ASN          
SEQRES   9 P  600  ALA THR PHE ILE ARG ASP THR LEU MET ARG LEU VAL LEU          
SEQRES  10 P  600  THR VAL ARG SER ASN LEU ILE PRO SER PRO PRO THR TYR          
SEQRES  11 P  600  ASN ILE ALA HIS ASP TYR ILE SER TRP GLU SER PHE SER          
SEQRES  12 P  600  ASN VAL SER TYR TYR THR ARG ILE LEU PRO SER VAL PRO          
SEQRES  13 P  600  ARG ASP CYS PRO THR PRO MET GLY THR LYS GLY LYS LYS          
SEQRES  14 P  600  GLN LEU PRO ASP ALA GLU PHE LEU SER ARG ARG PHE LEU          
SEQRES  15 P  600  LEU ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY THR ASN          
SEQRES  16 P  600  LEU MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN          
SEQRES  17 P  600  PHE PHE LYS THR SER GLY LYS MET GLY PRO GLY PHE THR          
SEQRES  18 P  600  LYS ALA LEU GLY HIS GLY VAL ASP LEU GLY HIS ILE TYR          
SEQRES  19 P  600  GLY ASP ASN LEU GLU ARG GLN TYR GLN LEU ARG LEU PHE          
SEQRES  20 P  600  LYS ASP GLY LYS LEU LYS TYR GLN MET LEU ASN GLY GLU          
SEQRES  21 P  600  VAL TYR PRO PRO SER VAL GLU GLU ALA PRO VAL LEU MET          
SEQRES  22 P  600  HIS TYR PRO ARG GLY ILE PRO PRO GLN SER GLN MET ALA          
SEQRES  23 P  600  VAL GLY GLN GLU VAL PHE GLY LEU LEU PRO GLY LEU MET          
SEQRES  24 P  600  LEU TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL          
SEQRES  25 P  600  CYS ASP LEU LEU LYS ALA GLU HIS PRO THR TRP GLY ASP          
SEQRES  26 P  600  GLU GLN LEU PHE GLN THR ALA ARG LEU ILE LEU ILE GLY          
SEQRES  27 P  600  GLU THR ILE LYS ILE VAL ILE GLU GLU TYR VAL GLN GLN          
SEQRES  28 P  600  LEU SER GLY TYR PHE LEU GLN LEU LYS PHE ASP PRO GLU          
SEQRES  29 P  600  LEU LEU PHE GLY ALA GLN PHE GLN TYR ARG ASN ARG ILE          
SEQRES  30 P  600  ALA MET GLU PHE ASN GLN LEU TYR HIS TRP HIS PRO LEU          
SEQRES  31 P  600  MET PRO ASP SER PHE ARG VAL GLY PRO GLN ASP TYR SER          
SEQRES  32 P  600  TYR GLU GLN PHE LEU PHE ASN THR SER MET LEU VAL ASP          
SEQRES  33 P  600  TYR GLY VAL GLU ALA LEU VAL ASP ALA PHE SER ARG GLN          
SEQRES  34 P  600  PRO ALA GLY ARG ILE GLY GLY GLY ARG ASN ILE ASP HIS          
SEQRES  35 P  600  HIS ILE LEU HIS VAL ALA VAL ASP VAL ILE LYS GLU SER          
SEQRES  36 P  600  ARG VAL LEU ARG LEU GLN PRO PHE ASN GLU TYR ARG LYS          
SEQRES  37 P  600  ARG PHE GLY MET LYS PRO TYR THR SER PHE GLN GLU LEU          
SEQRES  38 P  600  THR GLY GLU LYS GLU MET ALA ALA GLU LEU GLU GLU LEU          
SEQRES  39 P  600  TYR GLY ASP ILE ASP ALA LEU GLU PHE TYR PRO GLY LEU          
SEQRES  40 P  600  LEU LEU GLU LYS CYS HIS PRO ASN SER ILE PHE GLY GLU          
SEQRES  41 P  600  SER MET ILE GLU MET GLY ALA PRO PHE SER LEU LYS GLY          
SEQRES  42 P  600  LEU LEU GLY ASN PRO ILE CYS SER PRO GLU TYR TRP LYS          
SEQRES  43 P  600  ALA SER THR PHE GLY GLY GLU VAL GLY PHE ASN LEU VAL          
SEQRES  44 P  600  LYS THR ALA THR LEU LYS LYS LEU VAL CYS LEU ASN THR          
SEQRES  45 P  600  LYS THR CYS PRO TYR VAL SER PHE HIS VAL PRO ASP PRO          
SEQRES  46 P  600  ARG GLN GLU ASP ARG PRO GLY VAL GLU ARG PRO PRO THR          
SEQRES  47 P  600  GLU LEU                                                      
MODRES 2OYU ASN P   68  ASN  GLYCOSYLATION SITE                                 
MODRES 2OYU ASN P  144  ASN  GLYCOSYLATION SITE                                 
MODRES 2OYU ASN P  410  ASN  GLYCOSYLATION SITE                                 
HET    NAG  P 661      14                                                       
HET    NAG  P 662      14                                                       
HET    NAG  P 671      14                                                       
HET    NAG  P 672      14                                                       
HET    BMA  P 673      11                                                       
HET    NAG  P 681      14                                                       
HET    NAG  P 682      14                                                       
HET    BOG  P 750      12                                                       
HET    BOG  P 751      12                                                       
HET    IMS  P 700      30                                                       
HET    HEM  P 601      43                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     IMS 2-[1-(4-CHLOROBENZOYL)-5-METHOXY-2-METHYL-1H-INDOL-3-            
HETNAM   2 IMS  YL]-N-[(1S)-1-(HYDROXYMETHYL)PROPYL]ACETAMIDE                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   2  NAG    6(C8 H15 N O6)                                               
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   5  BOG    2(C14 H28 O6)                                                
FORMUL   7  IMS    C23 H25 CL N2 O4                                             
FORMUL   8  HEM    C34 H32 FE N4 O4                                             
FORMUL   9  HOH   *52(H2 O)                                                     
HELIX    1   1 ASN P   34  TYR P   39  5                                   6    
HELIX    2   2 GLU P   73  ARG P   83  1                                  11    
HELIX    3   3 SER P   85  THR P   94  1                                  10    
HELIX    4   4 GLY P   96  THR P  106  1                                  11    
HELIX    5   5 PHE P  107  ASN P  122  1                                  16    
HELIX    6   6 SER P  138  ASN P  144  1                                   7    
HELIX    7   7 ASP P  173  LEU P  182  1                                  10    
HELIX    8   8 ASN P  195  HIS P  207  1                                  13    
HELIX    9   9 ASN P  237  ARG P  245  1                                   9    
HELIX   10  10 LEU P  295  HIS P  320  1                                  26    
HELIX   11  11 GLY P  324  GLU P  347  1                                  24    
HELIX   12  12 GLU P  347  GLY P  354  1                                   8    
HELIX   13  13 ASP P  362  LEU P  366  5                                   5    
HELIX   14  14 ALA P  378  TYR P  385  1                                   8    
HELIX   15  15 HIS P  386  MET P  391  5                                   6    
HELIX   16  16 SER P  403  LEU P  408  1                                   6    
HELIX   17  17 SER P  412  GLY P  418  1                                   7    
HELIX   18  18 GLY P  418  GLN P  429  1                                  12    
HELIX   19  19 ILE P  444  LEU P  458  1                                  15    
HELIX   20  20 PRO P  462  PHE P  470  1                                   9    
HELIX   21  21 SER P  477  THR P  482  1                                   6    
HELIX   22  22 GLU P  484  GLY P  496  1                                  13    
HELIX   23  23 ASP P  497  LEU P  501  5                                   5    
HELIX   24  24 GLU P  502  GLU P  510  1                                   9    
HELIX   25  25 GLY P  519  GLY P  536  1                                  18    
HELIX   26  26 ASN P  537  SER P  541  5                                   5    
HELIX   27  27 ALA P  547  GLY P  551  5                                   5    
HELIX   28  28 GLY P  552  THR P  561  1                                  10    
HELIX   29  29 THR P  563  LEU P  570  1                                   8    
SHEET    1   A 2 ILE P  46  PHE P  50  0                                        
SHEET    2   A 2 ARG P  54  ASP P  58 -1  O  ARG P  54   N  PHE P  50           
SHEET    1   B 2 TYR P  64  SER P  65  0                                        
SHEET    2   B 2 ILE P  71  PRO P  72 -1  O  ILE P  71   N  SER P  65           
SHEET    1   C 2 GLN P 255  LEU P 257  0                                        
SHEET    2   C 2 GLU P 260  TYR P 262 -1  O  TYR P 262   N  GLN P 255           
SHEET    1   D 2 PHE P 395  VAL P 397  0                                        
SHEET    2   D 2 GLN P 400  TYR P 402 -1  O  TYR P 402   N  PHE P 395           
SSBOND   1 CYS P   36    CYS P   47                          1555   1555  2.10  
SSBOND   2 CYS P   37    CYS P  159                          1555   1555  2.05  
SSBOND   3 CYS P   41    CYS P   57                          1555   1555  2.03  
SSBOND   4 CYS P   59    CYS P   69                          1555   1555  2.05  
SSBOND   5 CYS P  569    CYS P  575                          1555   1555  2.06  
LINK         ND2 ASN P  68                 C1  NAG P 661     1555   1555  1.45  
LINK         ND2 ASN P 144                 C1  NAG P 671     1555   1555  1.46  
LINK         ND2 ASN P 410                 C1  NAG P 681     1555   1555  1.45  
LINK         O4  NAG P 661                 C1  NAG P 662     1555   1555  1.45  
LINK         O4  NAG P 671                 C1  NAG P 672     1555   1555  1.46  
LINK         O4  NAG P 672                 C1  BMA P 673     1555   1555  1.48  
LINK         O4  NAG P 681                 C1  NAG P 682     1555   1555  1.46  
LINK         NE2 HIS P 388                FE   HEM P 601     1555   1555  2.47  
CISPEP   1 SER P  126    PRO P  127          0        -2.74                     
SITE     1 AC1  3 TYR P  55  ASN P  68  NAG P 662                               
SITE     1 AC2  2 TYR P  38  NAG P 661                                          
SITE     1 AC3  6 GLU P 140  ASN P 144  TYR P 147  LEU P 238                    
SITE     2 AC3  6 NAG P 672  HOH P 759                                          
SITE     1 AC4  5 MET P 216  GLU P 239  NAG P 671  BMA P 673                    
SITE     2 AC4  5 HOH P 789                                                     
SITE     1 AC5  1 NAG P 672                                                     
SITE     1 AC6  6 GLY P 278  PRO P 280  TYR P 402  GLN P 406                    
SITE     2 AC6  6 ASN P 410  NAG P 682                                          
SITE     1 AC7  3 TYR P 402  GLN P 406  NAG P 681                               
SITE     1 AC8  2 SER P  87  PHE P  88                                          
SITE     1 AC9  6 PRO P  86  ILE P  89  VAL P 119  ARG P 120                    
SITE     2 AC9  6 LEU P 123  GLU P 524                                          
SITE     1 BC1 18 HIS P  90  MET P 113  VAL P 116  ARG P 120                    
SITE     2 BC1 18 GLN P 192  VAL P 349  LEU P 352  SER P 353                    
SITE     3 BC1 18 TYR P 355  LEU P 359  TRP P 387  SER P 516                    
SITE     4 BC1 18 PHE P 518  ILE P 523  GLY P 526  ALA P 527                    
SITE     5 BC1 18 SER P 530  LEU P 531                                          
SITE     1 BC2 17 ALA P 199  ALA P 202  GLN P 203  THR P 206                    
SITE     2 BC2 17 HIS P 207  PHE P 210  LYS P 211  THR P 212                    
SITE     3 BC2 17 LEU P 295  ASN P 382  HIS P 386  TRP P 387                    
SITE     4 BC2 17 HIS P 388  MET P 391  VAL P 447  ASP P 450                    
SITE     5 BC2 17 HOH P 763                                                     
CRYST1  181.410  181.410  103.398  90.00  90.00 120.00 P 65 2 2     12          
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      0.005512  0.003183  0.000000        0.00000                         
SCALE2      0.000000  0.006365  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009671        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system