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Database: PDB
Entry: 4O5Q
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Original site: 4O5Q 
HEADER    OXIDOREDUCTASE                          20-DEC-13   4O5Q              
TITLE     CRYSTAL STRUCTURE OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM       
TITLE    2 ESCHERICHIA COLI                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALKYL HYDROPEROXIDE REDUCTASE F52A PROTEIN                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12                                                          
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.V.DIP,N.KAMARIAH,M.S.S.MANIMEKALAI,A.M.BALAKRISHNA,G.GRUBER         
REVDAT   3   25-FEB-15 4O5Q    1       JRNL                                     
REVDAT   2   12-NOV-14 4O5Q    1       JRNL                                     
REVDAT   1   05-NOV-14 4O5Q    0                                                
JRNL        AUTH   P.V.DIP,N.KAMARIAH,M.S.SUBRAMANIAN MANIMEKALAI,W.NARTEY,     
JRNL        AUTH 2 A.M.BALAKRISHNA,F.EISENHABER,B.EISENHABER,G.GRUBER           
JRNL        TITL   STRUCTURE, MECHANISM AND ENSEMBLE FORMATION OF THE           
JRNL        TITL 2 ALKYLHYDROPEROXIDE REDUCTASE SUBUNITS AHPC AND AHPF FROM     
JRNL        TITL 3 ESCHERICHIA COLI                                             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  70  2848 2014              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   25372677                                                     
JRNL        DOI    10.1107/S1399004714019233                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.BIEGER,L.O.ESSEN                                           
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CATALYTIC CORE COMPONENT OF THE     
REMARK   1  TITL 2 ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM ESCHERICHIA COLI      
REMARK   1  REF    J.MOL.BIOL.                   V. 307     1 2010              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Z.A.WOOD,L.B.POOLE,P.A.KARPLUS                               
REMARK   1  TITL   STRUCTURE OF INTACT AHPF REVEALS A MIRRORED THIOREDOXIN-LIKE 
REMARK   1  TITL 2 ACTIVE SITE AND IMPLIES LARGE DOMAIN ROTATIONS DURING        
REMARK   1  TITL 3 CATALYSIS                                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  40  3900 2001              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.62                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 47447                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.144                           
REMARK   3   R VALUE            (WORKING SET) : 0.141                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2399                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 26.6229 -  5.1182    1.00     2758   138  0.1895 0.2333        
REMARK   3     2  5.1182 -  4.0671    0.99     2660   155  0.1292 0.1676        
REMARK   3     3  4.0671 -  3.5544    1.00     2674   127  0.1263 0.1744        
REMARK   3     4  3.5544 -  3.2300    1.00     2663   147  0.1287 0.1506        
REMARK   3     5  3.2300 -  2.9988    1.00     2662   162  0.1300 0.1875        
REMARK   3     6  2.9988 -  2.8222    1.00     2648   150  0.1273 0.1904        
REMARK   3     7  2.8222 -  2.6810    1.00     2668   128  0.1190 0.1848        
REMARK   3     8  2.6810 -  2.5644    1.00     2649   121  0.1248 0.1744        
REMARK   3     9  2.5644 -  2.4658    1.00     2651   155  0.1286 0.1835        
REMARK   3    10  2.4658 -  2.3807    1.00     2644   152  0.1345 0.1882        
REMARK   3    11  2.3807 -  2.3063    1.00     2650   128  0.1324 0.1832        
REMARK   3    12  2.3063 -  2.2405    1.00     2626   132  0.1374 0.2054        
REMARK   3    13  2.2405 -  2.1815    1.00     2660   150  0.1386 0.1839        
REMARK   3    14  2.1815 -  2.1283    1.00     2654   151  0.1516 0.2038        
REMARK   3    15  2.1283 -  2.0799    1.00     2621   131  0.1666 0.2314        
REMARK   3    16  2.0799 -  2.0357    0.99     2618   148  0.1802 0.2209        
REMARK   3    17  2.0357 -  2.0000    0.95     2542   124  0.2029 0.2512        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.090           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.33000                                              
REMARK   3    B22 (A**2) : -0.15000                                             
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.20000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           4294                                  
REMARK   3   ANGLE     :  1.408           5800                                  
REMARK   3   CHIRALITY :  0.080            649                                  
REMARK   3   PLANARITY :  0.007            732                                  
REMARK   3   DIHEDRAL  : 16.381           1616                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 1 through 150 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7928 -21.5944 -10.5886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4717 T22:   0.2803                                     
REMARK   3      T33:   0.1996 T12:  -0.0412                                     
REMARK   3      T13:   0.0649 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4943 L22:   0.4790                                     
REMARK   3      L33:   0.7340 L12:  -0.4781                                     
REMARK   3      L13:  -0.0809 L23:  -0.0606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1027 S12:   0.1440 S13:  -0.0595                       
REMARK   3      S21:   0.2036 S22:   0.0601 S23:   0.0169                       
REMARK   3      S31:   0.1430 S32:   0.0035 S33:  -0.0005                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 151 through 300 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3459 -22.4208  27.5841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2867 T22:   0.2380                                     
REMARK   3      T33:   0.1945 T12:   0.0028                                     
REMARK   3      T13:  -0.0094 T23:   0.0361                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1830 L22:   0.0583                                     
REMARK   3      L33:   0.3381 L12:  -0.0905                                     
REMARK   3      L13:   0.0298 L23:  -0.2263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:   0.0213 S13:   0.0222                       
REMARK   3      S21:  -0.1385 S22:   0.0158 S23:  -0.0223                       
REMARK   3      S31:  -0.1226 S32:  -0.0739 S33:   0.0134                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 301 through 450 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -49.9456 -34.7220  61.9526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1454 T22:   0.1974                                     
REMARK   3      T33:   0.2457 T12:   0.0069                                     
REMARK   3      T13:  -0.0204 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2511 L22:   0.2334                                     
REMARK   3      L33:   0.3281 L12:   0.0584                                     
REMARK   3      L13:  -0.2428 L23:   0.0135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0330 S12:   0.0228 S13:   0.0216                       
REMARK   3      S21:   0.0302 S22:   0.0123 S23:   0.1396                       
REMARK   3      S31:   0.0639 S32:  -0.0188 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 451 through 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5825 -42.7775  46.8206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:   0.1643                                     
REMARK   3      T33:   0.1781 T12:  -0.0119                                     
REMARK   3      T13:  -0.0042 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1740 L22:   0.4532                                     
REMARK   3      L33:   0.1470 L12:   0.1389                                     
REMARK   3      L13:   0.0877 L23:  -0.1237                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0371 S12:   0.0121 S13:  -0.0137                       
REMARK   3      S21:  -0.0704 S22:   0.0291 S23:  -0.0181                       
REMARK   3      S31:   0.0150 S32:  -0.0127 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 4O5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB084075.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-12                          
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               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
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                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47454                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 1HYU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-HEPES, 2.5%(V/V) PEG400, 2M      
REMARK 280  AMMONIUM SULFATE, 10MM CADMIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
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       53.24700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.34800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.24700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.34800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 22960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 -1.000000  0.000000  0.000000      -51.57696            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      112.75783            
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   HG   CYS A   129     HG   CYS A   132              1.08            
REMARK 500  HH12  ARG A   401     O    HOH A  1144              1.51            
REMARK 500   HE   ARG A   244     O    HOH A  1057              1.56            
REMARK 500  HH11  ARG A   113     O    HOH A   860              1.60            
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    ASP A  28     -151.54   -110.26                                   
REMARK 500    SER A  47      129.99   -172.43                                   
REMARK 500    LEU A  83     -148.13    -95.91                                   
REMARK 500    PHE A 159       63.84   -102.25                                   
REMARK 500    VAL A 253      -99.24    -99.00                                   
REMARK 500    SER A 260       -8.79     92.69                                   
REMARK 500    ALA A 321       57.28   -142.55                                   
REMARK 500    THR A 339       -4.35     72.46                                   
REMARK 500    LYS A 519       53.14    -90.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 934        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH A 945        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A1052        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A1069        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH A1157        DISTANCE =  7.15 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     PG4 A  617                                                       
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                              CD A 614  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 110   OE2                                                    
REMARK 620 2 HOH A1046   O   106.4                                              
REMARK 620 3 GLU A 110   OE1  54.3 159.7                                        
REMARK 620 4 HIS A 114   NE2  69.1  88.4  78.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 614                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 625                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FL2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O5U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O5R   RELATED DB: PDB                                   
DBREF  4O5Q A    1   521  UNP    P35340   AHPF_ECOLI       1    521             
SEQRES   1 A  521  MET LEU ASP THR ASN MET LYS THR GLN LEU LYS ALA TYR          
SEQRES   2 A  521  LEU GLU LYS LEU THR LYS PRO VAL GLU LEU ILE ALA THR          
SEQRES   3 A  521  LEU ASP ASP SER ALA LYS SER ALA GLU ILE LYS GLU LEU          
SEQRES   4 A  521  LEU ALA GLU ILE ALA GLU LEU SER ASP LYS VAL THR PHE          
SEQRES   5 A  521  LYS GLU ASP ASN SER LEU PRO VAL ARG LYS PRO SER PHE          
SEQRES   6 A  521  LEU ILE THR ASN PRO GLY SER ASN GLN GLY PRO ARG PHE          
SEQRES   7 A  521  ALA GLY SER PRO LEU GLY HIS GLU PHE THR SER LEU VAL          
SEQRES   8 A  521  LEU ALA LEU LEU TRP THR GLY GLY HIS PRO SER LYS GLU          
SEQRES   9 A  521  ALA GLN SER LEU LEU GLU GLN ILE ARG HIS ILE ASP GLY          
SEQRES  10 A  521  ASP PHE GLU PHE GLU THR TYR TYR SER LEU SER CYS HIS          
SEQRES  11 A  521  ASN CYS PRO ASP VAL VAL GLN ALA LEU ASN LEU MET SER          
SEQRES  12 A  521  VAL LEU ASN PRO ARG ILE LYS HIS THR ALA ILE ASP GLY          
SEQRES  13 A  521  GLY THR PHE GLN ASN GLU ILE THR ASP ARG ASN VAL MET          
SEQRES  14 A  521  GLY VAL PRO ALA VAL PHE VAL ASN GLY LYS GLU PHE GLY          
SEQRES  15 A  521  GLN GLY ARG MET THR LEU THR GLU ILE VAL ALA LYS ILE          
SEQRES  16 A  521  ASP THR GLY ALA GLU LYS ARG ALA ALA GLU GLU LEU ASN          
SEQRES  17 A  521  LYS ARG ASP ALA TYR ASP VAL LEU ILE VAL GLY SER GLY          
SEQRES  18 A  521  PRO ALA GLY ALA ALA ALA ALA ILE TYR SER ALA ARG LYS          
SEQRES  19 A  521  GLY ILE ARG THR GLY LEU MET GLY GLU ARG PHE GLY GLY          
SEQRES  20 A  521  GLN ILE LEU ASP THR VAL ASP ILE GLU ASN TYR ILE SER          
SEQRES  21 A  521  VAL PRO LYS THR GLU GLY GLN LYS LEU ALA GLY ALA LEU          
SEQRES  22 A  521  LYS VAL HIS VAL ASP GLU TYR ASP VAL ASP VAL ILE ASP          
SEQRES  23 A  521  SER GLN SER ALA SER LYS LEU ILE PRO ALA ALA VAL GLU          
SEQRES  24 A  521  GLY GLY LEU HIS GLN ILE GLU THR ALA SER GLY ALA VAL          
SEQRES  25 A  521  LEU LYS ALA ARG SER ILE ILE VAL ALA THR GLY ALA LYS          
SEQRES  26 A  521  TRP ARG ASN MET ASN VAL PRO GLY GLU ASP GLN TYR ARG          
SEQRES  27 A  521  THR LYS GLY VAL THR TYR CYS PRO HIS CYS ASP GLY PRO          
SEQRES  28 A  521  LEU PHE LYS GLY LYS ARG VAL ALA VAL ILE GLY GLY GLY          
SEQRES  29 A  521  ASN SER GLY VAL GLU ALA ALA ILE ASP LEU ALA GLY ILE          
SEQRES  30 A  521  VAL GLU HIS VAL THR LEU LEU GLU PHE ALA PRO GLU MET          
SEQRES  31 A  521  LYS ALA ASP GLN VAL LEU GLN ASP LYS LEU ARG SER LEU          
SEQRES  32 A  521  LYS ASN VAL ASP ILE ILE LEU ASN ALA GLN THR THR GLU          
SEQRES  33 A  521  VAL LYS GLY ASP GLY SER LYS VAL VAL GLY LEU GLU TYR          
SEQRES  34 A  521  ARG ASP ARG VAL SER GLY ASP ILE HIS ASN ILE GLU LEU          
SEQRES  35 A  521  ALA GLY ILE PHE VAL GLN ILE GLY LEU LEU PRO ASN THR          
SEQRES  36 A  521  ASN TRP LEU GLU GLY ALA VAL GLU ARG ASN ARG MET GLY          
SEQRES  37 A  521  GLU ILE ILE ILE ASP ALA LYS CYS GLU THR ASN VAL LYS          
SEQRES  38 A  521  GLY VAL PHE ALA ALA GLY ASP CYS THR THR VAL PRO TYR          
SEQRES  39 A  521  LYS GLN ILE ILE ILE ALA THR GLY GLU GLY ALA LYS ALA          
SEQRES  40 A  521  SER LEU SER ALA PHE ASP TYR LEU ILE ARG THR LYS THR          
SEQRES  41 A  521  ALA                                                          
HET    FAD  A 601      53                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    PGE  A 610      24                                                       
HET    PGE  A 611      24                                                       
HET    PGE  A 612      24                                                       
HET    GOL  A 613      14                                                       
HET     CD  A 614       1                                                       
HET    GOL  A 615      14                                                       
HET    PGE  A 616      24                                                       
HET    PG4  A 617       8                                                       
HET    PGE  A 618      24                                                       
HET    GOL  A 619      14                                                       
HET    TRS  A 620      20                                                       
HET    PGE  A 621      24                                                       
HET    GOL  A 622      14                                                       
HET    GOL  A 623      14                                                       
HET    GOL  A 624      14                                                       
HET    GOL  A 625      14                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM      CD CADMIUM ION                                                      
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  SO4    8(O4 S 2-)                                                   
FORMUL  11  PGE    6(C6 H14 O4)                                                 
FORMUL  14  GOL    7(C3 H8 O3)                                                  
FORMUL  15   CD    CD 2+                                                        
FORMUL  18  PG4    C8 H18 O5                                                    
FORMUL  21  TRS    C4 H12 N O3 1+                                               
FORMUL  27  HOH   *503(H2 O)                                                    
HELIX    1   1 ASP A    3  LYS A   16  1                                  14    
HELIX    2   2 SER A   30  GLU A   45  1                                  16    
HELIX    3   3 LEU A   83  HIS A   85  5                                   3    
HELIX    4   4 GLU A   86  GLY A   98  1                                  13    
HELIX    5   5 ALA A  105  HIS A  114  1                                  10    
HELIX    6   6 ASN A  131  ASN A  146  1                                  16    
HELIX    7   7 PHE A  159  ARG A  166  1                                   8    
HELIX    8   8 THR A  187  ASP A  196  1                                  10    
HELIX    9   9 ARG A  202  LYS A  209  1                                   8    
HELIX   10  10 GLY A  221  LYS A  234  1                                  14    
HELIX   11  11 GLY A  246  THR A  252  5                                   7    
HELIX   12  12 GLY A  266  GLU A  279  1                                  14    
HELIX   13  13 GLY A  333  ARG A  338  1                                   6    
HELIX   14  14 CYS A  345  GLY A  350  1                                   6    
HELIX   15  15 PRO A  351  LYS A  354  5                                   4    
HELIX   16  16 GLY A  364  GLY A  376  1                                  13    
HELIX   17  17 ASP A  393  SER A  402  1                                  10    
HELIX   18  18 THR A  455  GLU A  459  5                                   5    
HELIX   19  19 GLN A  496  THR A  518  1                                  23    
SHEET    1   A 8 VAL A  50  GLU A  54  0                                        
SHEET    2   A 8 VAL A  21  THR A  26  1  N  LEU A  23   O  THR A  51           
SHEET    3   A 8 SER A  64  THR A  68 -1  O  THR A  68   N  GLU A  22           
SHEET    4   A 8 ARG A  77  ALA A  79 -1  O  PHE A  78   N  PHE A  65           
SHEET    5   A 8 ILE A 149  ASP A 155  1  O  ASP A 155   N  ALA A  79           
SHEET    6   A 8 PHE A 119  TYR A 125  1  N  THR A 123   O  ILE A 154           
SHEET    7   A 8 ALA A 173  VAL A 176 -1  O  PHE A 175   N  GLU A 122           
SHEET    8   A 8 LYS A 179  GLN A 183 -1  O  GLY A 182   N  VAL A 174           
SHEET    1   B 5 ASP A 283  ASP A 286  0                                        
SHEET    2   B 5 THR A 238  GLY A 242  1  N  LEU A 240   O  ILE A 285           
SHEET    3   B 5 VAL A 215  VAL A 218  1  N  ILE A 217   O  MET A 241           
SHEET    4   B 5 ILE A 318  VAL A 320  1  O  ILE A 319   N  VAL A 218           
SHEET    5   B 5 VAL A 483  ALA A 485  1  O  PHE A 484   N  VAL A 320           
SHEET    1   C 2 ASP A 254  ILE A 255  0                                        
SHEET    2   C 2 THR A 264  GLU A 265 -1  O  THR A 264   N  ILE A 255           
SHEET    1   D 3 ALA A 290  ILE A 294  0                                        
SHEET    2   D 3 HIS A 303  THR A 307 -1  O  GLN A 304   N  ILE A 294           
SHEET    3   D 3 VAL A 312  ALA A 315 -1  O  ALA A 315   N  HIS A 303           
SHEET    1   E 2 ALA A 324  TRP A 326  0                                        
SHEET    2   E 2 LEU A 451  PRO A 453 -1  O  LEU A 452   N  LYS A 325           
SHEET    1   F 5 VAL A 342  THR A 343  0                                        
SHEET    2   F 5 GLY A 444  VAL A 447  1  O  VAL A 447   N  THR A 343           
SHEET    3   F 5 ARG A 357  ILE A 361  1  N  ALA A 359   O  PHE A 446           
SHEET    4   F 5 HIS A 380  LEU A 384  1  O  LEU A 384   N  VAL A 360           
SHEET    5   F 5 VAL A 406  ILE A 409  1  O  ILE A 409   N  LEU A 383           
SHEET    1   G 3 ALA A 412  GLY A 419  0                                        
SHEET    2   G 3 VAL A 424  ASP A 431 -1  O  GLU A 428   N  THR A 415           
SHEET    3   G 3 ILE A 437  GLU A 441 -1  O  HIS A 438   N  TYR A 429           
SSBOND   1 CYS A  345    CYS A  348                          1555   1555  2.07  
LINK         OE2 GLU A 110                CD    CD A 614     1555   1555  2.33  
LINK        CD    CD A 614                 O   HOH A1046     1555   1555  2.37  
LINK         OE1 GLU A 110                CD    CD A 614     1555   1555  2.49  
LINK         NE2 HIS A 114                CD    CD A 614     1555   1555  2.63  
CISPEP   1 LYS A   62    PRO A   63          0        -1.50                     
CISPEP   2 VAL A  171    PRO A  172          0        -2.59                     
SITE     1 AC1 37 GLY A 219  GLY A 221  PRO A 222  ALA A 223                    
SITE     2 AC1 37 GLY A 242  GLU A 243  ARG A 244  GLY A 247                    
SITE     3 AC1 37 GLN A 248  THR A 252  ASN A 257  GLN A 288                    
SITE     4 AC1 37 SER A 289  ALA A 290  ALA A 321  THR A 322                    
SITE     5 AC1 37 GLY A 323  CYS A 348  ASN A 454  TRP A 457                    
SITE     6 AC1 37 GLY A 487  ASP A 488  LYS A 495  GLN A 496                    
SITE     7 AC1 37 ILE A 497  ALA A 500  GOL A 619  HOH A 701                    
SITE     8 AC1 37 HOH A 702  HOH A 736  HOH A 738  HOH A 739                    
SITE     9 AC1 37 HOH A 747  HOH A 748  HOH A 753  HOH A 814                    
SITE    10 AC1 37 HOH A 834                                                     
SITE     1 AC2  8 ALA A 105  GLN A 106  SER A 107  SER A 126                    
SITE     2 AC2  8 SER A 128  HOH A 930  HOH A1084  HOH A1085                    
SITE     1 AC3  5 GLY A 364  ASN A 365  SER A 366  PGE A 621                    
SITE     2 AC3  5 HOH A 785                                                     
SITE     1 AC4  9 PRO A 453  ASN A 454  THR A 455  ASN A 456                    
SITE     2 AC4  9 TRP A 457  HOH A 774  HOH A 834  HOH A 918                    
SITE     3 AC4  9 HOH A1117                                                     
SITE     1 AC5  8 PRO A 332  GLY A 333  GLU A 334  ASP A 335                    
SITE     2 AC5  8 GLN A 336  HOH A 865  HOH A 902  HOH A 903                    
SITE     1 AC6  4 ARG A 357  HIS A 380  HOH A 789  HOH A1141                    
SITE     1 AC7  5 HIS A 438  ASN A 439  HOH A 802  HOH A 842                    
SITE     2 AC7  5 HOH A1022                                                     
SITE     1 AC8  5 SER A  30  ALA A  31  HOH A 812  HOH A 958                    
SITE     2 AC8  5 HOH A1178                                                     
SITE     1 AC9  4 ASP A 473  ALA A 474  HOH A1064  HOH A1105                    
SITE     1 BC1  8 ASN A 439  GLU A 459  GLY A 460  ALA A 461                    
SITE     2 BC1  8 GLU A 463  ASN A 479  HOH A 915  HOH A1022                    
SITE     1 BC2  7 ILE A 471  GLU A 477  THR A 478  ASN A 479                    
SITE     2 BC2  7 HOH A 922  HOH A1131  HOH A1138                               
SITE     1 BC3  4 ILE A 236  ILE A 372  LYS A 519  HOH A1101                    
SITE     1 BC4  8 HIS A 100  PRO A 101  SER A 102  GLN A 106                    
SITE     2 BC4  8 ASN A 131  LEU A 145  HOH A1100  HOH A1114                    
SITE     1 BC5  5 HIS A  85  GLU A 110  HIS A 114  HIS A 130                    
SITE     2 BC5  5 HOH A1046                                                     
SITE     1 BC6  4 ARG A 233  GLY A 235  LYS A 354  HOH A1191                    
SITE     1 BC7  6 GLU A 477  THR A 478  ASN A 479  LYS A 481                    
SITE     2 BC7  6 GOL A 625  HOH A 921                                          
SITE     1 BC8  4 PHE A 245  LYS A 274  HOH A 813  HOH A1017                    
SITE     1 BC9  6 GLU A 104  GLY A 156  GLN A 160  MET A 169                    
SITE     2 BC9  6 HOH A 930  HOH A1086                                          
SITE     1 CC1 10 THR A 252  VAL A 253  ASP A 254  THR A 339                    
SITE     2 CC1 10 ASP A 349  FAD A 601  HOH A 702  HOH A 703                    
SITE     3 CC1 10 HOH A 815  HOH A1183                                          
SITE     1 CC2  6 GLU A 416  ASN A 465  ARG A 466  HOH A 714                    
SITE     2 CC2  6 HOH A 923  HOH A1147                                          
SITE     1 CC3  8 ARG A 327  SER A 366  VAL A 447  GLN A 448                    
SITE     2 CC3  8 ILE A 449  GLY A 450  LEU A 451  SO4 A 603                    
SITE     1 CC4  4 GLY A 341  PHE A 353  HOH A 706  HOH A1182                    
SITE     1 CC5  6 ASP A 335  GLN A 336  ARG A 338  LYS A 340                    
SITE     2 CC5  6 LYS A 391  HOH A1119                                          
SITE     1 CC6  8 ASP A  28  ALA A  34  LYS A  37  GLU A  54                    
SITE     2 CC6  8 GLY A 300  ARG A 316  THR A 518  ALA A 521                    
SITE     1 CC7  7 GLU A 299  LYS A 481  ARG A 517  THR A 518                    
SITE     2 CC7  7 PGE A 616  HOH A 837  HOH A1129                               
CRYST1  106.494   58.696  123.994  90.00 114.58  90.00 C 1 2 1       4          
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      0.009390  0.000000  0.004295        0.00000                         
SCALE2      0.000000  0.017037  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008869        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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