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Database: PDB
Entry: 4O5U
LinkDB: 4O5U
Original site: 4O5U 
HEADER    OXIDOREDUCTASE                          20-DEC-13   4O5U              
TITLE     CRYSTAL STRUCTURE OF ALKYLHYDROPEROXIDE REDUCTASE SUBUNIT F FROM E.   
TITLE    2 COLI AT 2.65 ANG RESOLUTION                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALKYL HYDROPEROXIDE REDUCTASE F52A PROTEIN;                 
COMPND   5 EC: 1.8.1.-                                                          
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    N.KAMARIAH,P.V.DIP,M.S.S.MANIMEKALAI,G.GRUBER,F.EISENHABER,           
AUTHOR   2 B.EISENHABER                                                         
REVDAT   3   25-FEB-15 4O5U    1       JRNL                                     
REVDAT   2   12-NOV-14 4O5U    1       JRNL                                     
REVDAT   1   05-NOV-14 4O5U    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.    2.65 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) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 20674                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1055                            
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 28.8205 -  5.2850    0.99     2544   149  0.1739 0.2359        
REMARK   3     2  5.2850 -  4.1990    1.00     2502   137  0.1413 0.1711        
REMARK   3     3  4.1990 -  3.6694    1.00     2510   107  0.1528 0.2037        
REMARK   3     4  3.6694 -  3.3345    1.00     2463   114  0.1669 0.2012        
REMARK   3     5  3.3345 -  3.0958    1.00     2492   140  0.1728 0.2178        
REMARK   3     6  3.0958 -  2.9134    1.00     2433   153  0.2031 0.2787        
REMARK   3     7  2.9134 -  2.7676    0.99     2455   132  0.2141 0.2568        
REMARK   3     8  2.7676 -  2.6472    0.90     2220   123  0.2396 0.2912        
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.67000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.46000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.09000                                             
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      :  0.006           4102                                  
REMARK   3   ANGLE     :  0.908           5562                                  
REMARK   3   CHIRALITY :  0.048            637                                  
REMARK   3   PLANARITY :  0.004            710                                  
REMARK   3   DIHEDRAL  : 15.893           1504                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 1 through 19 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8877  65.2618 -15.7287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6511 T22:   0.7329                                     
REMARK   3      T33:   0.3722 T12:   0.0774                                     
REMARK   3      T13:   0.0515 T23:   0.1562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0153 L22:   0.0047                                     
REMARK   3      L33:   0.0869 L12:   0.0102                                     
REMARK   3      L13:  -0.0116 L23:   0.0123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3513 S12:  -0.1080 S13:   0.0067                       
REMARK   3      S21:   0.0836 S22:  -0.1376 S23:  -0.1961                       
REMARK   3      S31:   0.1160 S32:   0.1460 S33:   0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 20 through 160 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9962  69.4531  -9.5601              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5439 T22:   0.4736                                     
REMARK   3      T33:   0.2363 T12:  -0.0264                                     
REMARK   3      T13:   0.0698 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4690 L22:   0.0074                                     
REMARK   3      L33:   0.6944 L12:  -0.0632                                     
REMARK   3      L13:  -0.3643 L23:   0.1134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0212 S12:  -0.0576 S13:  -0.0754                       
REMARK   3      S21:   0.1516 S22:   0.0469 S23:   0.1389                       
REMARK   3      S31:   0.1218 S32:  -0.1621 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 161 through 186 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5031  84.3159  -2.1695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8051 T22:   0.6616                                     
REMARK   3      T33:   0.4127 T12:  -0.0152                                     
REMARK   3      T13:   0.1454 T23:  -0.0990                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0074 L22:   0.0211                                     
REMARK   3      L33:   0.0158 L12:   0.0131                                     
REMARK   3      L13:   0.0076 L23:  -0.0020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0183 S12:  -0.1567 S13:  -0.0924                       
REMARK   3      S21:   0.4061 S22:  -0.0361 S23:   0.3329                       
REMARK   3      S31:  -0.1390 S32:  -0.0027 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 187 through 206 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4694  68.6411  15.7927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1426 T22:   0.7362                                     
REMARK   3      T33:   0.3915 T12:  -0.0633                                     
REMARK   3      T13:   0.1642 T23:   0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1411 L22:   0.2392                                     
REMARK   3      L33:   0.1134 L12:  -0.0652                                     
REMARK   3      L13:   0.0194 L23:  -0.1485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0588 S12:  -0.1539 S13:  -0.2300                       
REMARK   3      S21:   0.1688 S22:   0.0499 S23:   0.6057                       
REMARK   3      S31:  -0.0930 S32:  -0.0853 S33:   0.0035                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 207 through 280 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1983  62.6158  45.0913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1217 T22:   0.1094                                     
REMARK   3      T33:   0.2056 T12:   0.0038                                     
REMARK   3      T13:  -0.0418 T23:   0.0620                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3901 L22:   0.6555                                     
REMARK   3      L33:   0.1389 L12:   0.2336                                     
REMARK   3      L13:   0.1653 L23:  -0.1473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0048 S12:   0.2506 S13:   0.3646                       
REMARK   3      S21:  -0.0417 S22:   0.0934 S23:  -0.0397                       
REMARK   3      S31:  -0.0657 S32:  -0.1516 S33:   0.0515                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 281 through 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7567  50.7097  34.4207              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1611 T22:   0.2268                                     
REMARK   3      T33:   0.0964 T12:  -0.0157                                     
REMARK   3      T13:  -0.0257 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2076 L22:   0.2842                                     
REMARK   3      L33:   0.3197 L12:  -0.0446                                     
REMARK   3      L13:  -0.1353 L23:   0.0195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0136 S12:   0.3550 S13:   0.0951                       
REMARK   3      S21:  -0.2338 S22:  -0.0203 S23:   0.2523                       
REMARK   3      S31:  -0.0705 S32:   0.0186 S33:  -0.0063                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 326 through 437 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5259  54.9354  66.8438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1216 T22:   0.1404                                     
REMARK   3      T33:   0.2165 T12:  -0.0061                                     
REMARK   3      T13:   0.0097 T23:  -0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4695 L22:   1.0581                                     
REMARK   3      L33:   0.6636 L12:   0.0107                                     
REMARK   3      L13:  -0.0636 L23:  -0.1295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0383 S12:  -0.0428 S13:   0.0187                       
REMARK   3      S21:   0.0527 S22:  -0.0638 S23:  -0.0614                       
REMARK   3      S31:   0.0203 S32:  -0.0688 S33:  -0.0014                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 438 through 514 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7153  48.5396  51.5162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0785 T22:   0.0594                                     
REMARK   3      T33:   0.1553 T12:  -0.0019                                     
REMARK   3      T13:  -0.0168 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3153 L22:   0.1348                                     
REMARK   3      L33:   0.3539 L12:  -0.0040                                     
REMARK   3      L13:   0.0700 L23:   0.1366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0935 S12:  -0.0387 S13:  -0.1191                       
REMARK   3      S21:   0.0148 S22:   0.0379 S23:   0.0094                       
REMARK   3      S31:   0.0211 S32:   0.0543 S33:  -0.1094                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'A' and (resid 515 through 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4301  44.4758  36.2343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1860 T22:   0.3902                                     
REMARK   3      T33:   0.3567 T12:  -0.0670                                     
REMARK   3      T13:   0.0570 T23:  -0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0114 L22:   0.0029                                     
REMARK   3      L33:   0.0057 L12:  -0.0071                                     
REMARK   3      L13:  -0.0105 L23:   0.0064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0927 S12:  -0.0438 S13:  -0.1606                       
REMARK   3      S21:  -0.0329 S22:   0.0975 S23:  -0.0562                       
REMARK   3      S31:  -0.0997 S32:  -0.0266 S33:   0.0002                       
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 4O5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB084079.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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, 1.55072, 1.58994, 1.59048     
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   : 21022                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
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     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.5, 2 M AMMONIUM      
REMARK 280  SULFATE, 10 MM CADMIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 296K                                                    
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       53.34900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.79900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.34900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.79900            
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: 10730 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -248.0 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       57.01058            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      113.29855            
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     -161.08   -107.99                                   
REMARK 500    ASP A 116      -71.46    -71.44                                   
REMARK 500    PHE A 159       65.79   -102.14                                   
REMARK 500    ASP A 165      -74.65    -79.12                                   
REMARK 500    ASN A 177       40.34     39.90                                   
REMARK 500    THR A 197       76.21   -115.74                                   
REMARK 500    ALA A 199      -80.70   -131.07                                   
REMARK 500    ARG A 244       96.70   -162.03                                   
REMARK 500    VAL A 253      -93.20   -110.01                                   
REMARK 500    SER A 260        0.47     82.99                                   
REMARK 500    LYS A 340       31.10   -145.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 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 FAD 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 CD A 610                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FL2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O5R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O5Q   RELATED DB: PDB                                   
DBREF  4O5U 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    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    FAD  A 604      53                                                       
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     CD  A 610       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM      CD CADMIUM ION                                                      
FORMUL   2  SO4    8(O4 S 2-)                                                   
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL  11   CD    CD 2+                                                        
FORMUL  12  HOH   *162(H2 O)                                                    
HELIX    1   1 ASP A    3  LEU A   14  1                                  12    
HELIX    2   2 GLU A   15  LEU A   17  5                                   3    
HELIX    3   3 SER A   30  LEU A   46  1                                  17    
HELIX    4   4 LEU A   83  HIS A   85  5                                   3    
HELIX    5   5 GLU A   86  GLY A   98  1                                  13    
HELIX    6   6 ALA A  105  HIS A  114  1                                  10    
HELIX    7   7 ASN A  131  ASN A  146  1                                  16    
HELIX    8   8 PHE A  159  ARG A  166  1                                   8    
HELIX    9   9 THR A  187  ASP A  196  1                                  10    
HELIX   10  10 ARG A  202  LYS A  209  1                                   8    
HELIX   11  11 GLY A  221  ARG A  233  1                                  13    
HELIX   12  12 GLY A  246  THR A  252  5                                   7    
HELIX   13  13 GLY A  266  GLU A  279  1                                  14    
HELIX   14  14 GLU A  334  ARG A  338  5                                   5    
HELIX   15  15 CYS A  345  GLY A  350  1                                   6    
HELIX   16  16 PRO A  351  LYS A  354  5                                   4    
HELIX   17  17 GLY A  364  ALA A  375  1                                  12    
HELIX   18  18 ASP A  393  SER A  402  1                                  10    
HELIX   19  19 THR A  455  GLU A  459  5                                   5    
HELIX   20  20 GLN A  496  THR A  520  1                                  25    
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  PHE A 121   O  LYS A 150           
SHEET    7   A 8 ALA A 173  VAL A 176 -1  O  ALA A 173   N  TYR A 124           
SHEET    8   A 8 LYS A 179  GLN A 183 -1  O  LYS A 179   N  VAL A 176           
SHEET    1   B 6 VAL A 282  ILE A 285  0                                        
SHEET    2   B 6 THR A 238  MET A 241  1  N  LEU A 240   O  ILE A 285           
SHEET    3   B 6 TYR A 213  VAL A 218  1  N  ILE A 217   O  GLY A 239           
SHEET    4   B 6 VAL A 312  VAL A 320  1  O  ILE A 319   N  VAL A 218           
SHEET    5   B 6 HIS A 303  THR A 307 -1  N  ILE A 305   O  LEU A 313           
SHEET    6   B 6 ALA A 290  ILE A 294 -1  N  SER A 291   O  GLU A 306           
SHEET    1   C 5 VAL A 282  ILE A 285  0                                        
SHEET    2   C 5 THR A 238  MET A 241  1  N  LEU A 240   O  ILE A 285           
SHEET    3   C 5 TYR A 213  VAL A 218  1  N  ILE A 217   O  GLY A 239           
SHEET    4   C 5 VAL A 312  VAL A 320  1  O  ILE A 319   N  VAL A 218           
SHEET    5   C 5 VAL A 483  ALA A 485  1  O  PHE A 484   N  VAL A 320           
SHEET    1   D 2 ASP A 254  ILE A 255  0                                        
SHEET    2   D 2 THR A 264  GLU A 265 -1  O  THR A 264   N  ILE A 255           
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  THR A 382   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  ARG A 430   N  GLN A 413           
SHEET    3   G 3 ILE A 437  GLU A 441 -1  O  ILE A 440   N  LEU A 427           
SSBOND   1 CYS A  129    CYS A  132                          1555   1555  2.04  
SSBOND   2 CYS A  345    CYS A  348                          1555   1555  2.04  
CISPEP   1 LYS A   62    PRO A   63          0        -1.62                     
CISPEP   2 VAL A  171    PRO A  172          0         0.69                     
SITE     1 AC1  6 PRO A 453  ASN A 454  THR A 455  ASN A 456                    
SITE     2 AC1  6 TRP A 457  HOH A 767                                          
SITE     1 AC2  4 GLY A 333  GLU A 334  ASP A 335  GLN A 336                    
SITE     1 AC3  2 ASP A 473  ALA A 474                                          
SITE     1 AC4 36 GLY A 219  GLY A 221  PRO A 222  ALA A 223                    
SITE     2 AC4 36 TYR A 230  GLY A 242  GLU A 243  ARG A 244                    
SITE     3 AC4 36 GLY A 247  GLN A 248  THR A 252  ASN A 257                    
SITE     4 AC4 36 GLN A 288  SER A 289  ALA A 290  ALA A 321                    
SITE     5 AC4 36 THR A 322  GLY A 323  ALA A 324  TRP A 326                    
SITE     6 AC4 36 CYS A 348  TRP A 457  GLY A 487  ASP A 488                    
SITE     7 AC4 36 LYS A 495  GLN A 496  ILE A 497  ALA A 500                    
SITE     8 AC4 36 HOH A 706  HOH A 717  HOH A 727  HOH A 728                    
SITE     9 AC4 36 HOH A 792  HOH A 794  HOH A 814  HOH A 815                    
SITE     1 AC5  2 HIS A 438  ASN A 439                                          
SITE     1 AC6  5 GLY A 364  ASN A 365  SER A 366  HOH A 751                    
SITE     2 AC6  5 HOH A 795                                                     
SITE     1 AC7  3 ARG A 357  HIS A 380  HOH A 777                               
SITE     1 AC8  3 ASP A 393  GLN A 394  HOH A 718                               
SITE     1 AC9  6 TRP A 326  TYR A 344  VAL A 447  GLN A 448                    
SITE     2 AC9  6 GLY A 450  LEU A 451                                          
SITE     1 BC1  2 HIS A  85  HIS A 130                                          
CRYST1  106.698   59.598  123.715  90.00 113.68  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      0.009372  0.000000  0.004110        0.00000                         
SCALE2      0.000000  0.016779  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008826        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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