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Database: PDB
Entry: 2WWO
LinkDB: 2WWO
Original site: 2WWO 
HEADER    OXIDOREDUCTASE                          26-OCT-09   2WWO              
TITLE     YERSINIA PSEUDOTUBERCULOSIS SUPEROXIDE DISMUTASE C                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE C;                                     
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;                    
SOURCE   3 ORGANISM_TAXID: 633;                                                 
SOURCE   4 STRAIN: IP32953;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P                                   
KEYWDS    OXIDOREDUCTASE, METAL-BINDING                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.BASAK,M.L.DUFFIELD,C.E.NAYLOR,J.HUYET,R.W.TITBALL                 
REVDAT   1   03-NOV-10 2WWO    0                                                
SPRSDE     03-NOV-10 2WWO      2WN0                                             
JRNL        AUTH   J.HUYET,C.E.NAYLOR,R.W.TITBALL,H.BULLIFENT,N.WALKER,         
JRNL        AUTH 2 H.E.JONES,M.L.DUFFIED,A.K.BASAK                              
JRNL        TITL   CRYSTAL STRUCTURE OF THE YERSINIA PSEUDOTUBERCULOSIS         
JRNL        TITL 2 SUPEROXIDE DISMUTASE (SODC)                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.773                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.54                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.91                          
REMARK   3   NUMBER OF REFLECTIONS             : 17944                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1685                          
REMARK   3   R VALUE            (WORKING SET) : 0.1665                          
REMARK   3   FREE R VALUE                     : 0.2054                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 916                             
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 48.7832 -  4.5900    1.00     2562   117  0.1541 0.1810        
REMARK   3     2  4.5900 -  3.6436    1.00     2460   129  0.1335 0.1690        
REMARK   3     3  3.6436 -  3.1831    1.00     2386   153  0.1675 0.1972        
REMARK   3     4  3.1831 -  2.8921    1.00     2434   116  0.1728 0.2417        
REMARK   3     5  2.8921 -  2.6848    1.00     2408   135  0.1712 0.2391        
REMARK   3     6  2.6848 -  2.5265    1.00     2412   128  0.1725 0.2113        
REMARK   3     7  2.5265 -  2.4000    1.00     2366   138  0.1971 0.2547        
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              : 0.356                                         
REMARK   3   B_SOL              : 55.138                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.39             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.31            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.6                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.008                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.7588                                               
REMARK   3    B22 (A**2) : 5.7588                                               
REMARK   3    B33 (A**2) : -11.5176                                             
REMARK   3    B12 (A**2) : -0.0000                                              
REMARK   3    B13 (A**2) : -0.0000                                              
REMARK   3    B23 (A**2) : -0.0000                                              
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           2323                                  
REMARK   3   ANGLE     :  0.992           3160                                  
REMARK   3   CHIRALITY :  0.062            351                                  
REMARK   3   PLANARITY :  0.008            421                                  
REMARK   3   DIHEDRAL  : 16.587            824                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 4:21                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0546  16.9675 -42.5010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6147 T22:   0.4237                                     
REMARK   3      T33:   0.3125 T12:   0.0545                                     
REMARK   3      T13:  -0.0853 T23:  -0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6769 L22:   0.2477                                     
REMARK   3      L33:   0.4480 L12:  -0.1220                                     
REMARK   3      L13:  -0.0481 L23:  -0.7563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1923 S12:   0.3494 S13:  -0.1067                       
REMARK   3      S21:  -0.6004 S22:   0.1276 S23:  -0.6179                       
REMARK   3      S31:  -0.1403 S32:  -0.0426 S33:   0.0007                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 22:75                                
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0986  10.9480 -38.9866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4854 T22:   0.3456                                     
REMARK   3      T33:   0.2604 T12:   0.0956                                     
REMARK   3      T13:  -0.0628 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6227 L22:   0.1281                                     
REMARK   3      L33:   1.7830 L12:   0.2753                                     
REMARK   3      L13:  -0.4722 L23:  -0.8531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0403 S12:   0.3406 S13:   0.0183                       
REMARK   3      S21:  -0.3011 S22:  -0.1939 S23:   0.0347                       
REMARK   3      S31:   0.2395 S32:   0.1215 S33:  -0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 76:155                               
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4409   8.1425 -31.3035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3726 T22:   0.3152                                     
REMARK   3      T33:   0.3004 T12:   0.0539                                     
REMARK   3      T13:   0.0087 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6244 L22:   1.7809                                     
REMARK   3      L33:   1.6379 L12:   0.0022                                     
REMARK   3      L13:   0.2069 L23:   0.2763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0332 S12:   0.0747 S13:  -0.1393                       
REMARK   3      S21:  -0.2277 S22:  -0.1139 S23:  -0.0241                       
REMARK   3      S31:   0.4001 S32:   0.1285 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 156:161                              
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9900  15.2563 -43.0827              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5666 T22:   0.4112                                     
REMARK   3      T33:   0.3041 T12:   0.0820                                     
REMARK   3      T13:  -0.0208 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0094 L22:  -0.0415                                     
REMARK   3      L33:  -0.0035 L12:   0.1413                                     
REMARK   3      L13:   0.0377 L23:   0.0680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2511 S12:   0.6632 S13:   0.2352                       
REMARK   3      S21:  -0.5787 S22:  -0.1956 S23:  -0.4564                       
REMARK   3      S31:  -0.5972 S32:  -0.0658 S33:  -0.0010                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 7:21                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8167   8.9190  -6.2853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4844 T22:   0.3144                                     
REMARK   3      T33:   0.4242 T12:  -0.0151                                     
REMARK   3      T13:   0.1024 T23:  -0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0266 L22:  -0.0104                                     
REMARK   3      L33:   0.2741 L12:  -0.3494                                     
REMARK   3      L13:   0.0324 L23:   0.1595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3099 S12:  -0.6799 S13:   0.1413                       
REMARK   3      S21:   0.7097 S22:  -0.3049 S23:   0.1371                       
REMARK   3      S31:   0.1214 S32:  -0.0574 S33:  -0.0022                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 22:75                                
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4848  13.7762 -10.9156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2787 T22:   0.2440                                     
REMARK   3      T33:   0.3803 T12:   0.0543                                     
REMARK   3      T13:   0.0789 T23:  -0.0628                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6411 L22:   1.0977                                     
REMARK   3      L33:   1.5778 L12:   0.5961                                     
REMARK   3      L13:  -0.5073 L23:  -0.6168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1282 S12:  -0.0606 S13:   0.0912                       
REMARK   3      S21:   0.2946 S22:  -0.0690 S23:   0.3857                       
REMARK   3      S31:  -0.1227 S32:  -0.1166 S33:  -0.0004                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 76:143                               
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1935  19.4975 -14.9175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3273 T22:   0.2821                                     
REMARK   3      T33:   0.3141 T12:   0.0080                                     
REMARK   3      T13:   0.0163 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6052 L22:   1.5601                                     
REMARK   3      L33:   0.4877 L12:  -0.1319                                     
REMARK   3      L13:  -0.1070 L23:  -0.2887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0254 S12:   0.0222 S13:   0.0025                       
REMARK   3      S21:   0.0933 S22:  -0.0727 S23:   0.2424                       
REMARK   3      S31:  -0.2324 S32:  -0.1072 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 156:161                              
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4991  12.5458  -4.0566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4692 T22:   0.3168                                     
REMARK   3      T33:   0.3609 T12:  -0.0424                                     
REMARK   3      T13:   0.0788 T23:   0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0541 L22:  -0.0535                                     
REMARK   3      L33:  -0.0381 L12:   0.0027                                     
REMARK   3      L13:  -0.1472 L23:  -0.0725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2323 S12:  -1.0518 S13:   0.1102                       
REMARK   3      S21:   0.8988 S22:  -0.3499 S23:  -0.0861                       
REMARK   3      S31:  -0.0633 S32:  -0.0800 S33:   0.0007                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:18 OR RESSEQ  20:56   
REMARK   3                          OR RESSEQ 58:64 OR RESSEQ 70:143 OR         
REMARK   3                           RESSEQ 145:145 OR RESSEQ 147:160)          
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 7:18 OR RESSEQ 20:56    
REMARK   3                           OR RESSEQ 58:64 OR RESSEQ 70:143           
REMARK   3                           OR RESSEQ 145:145 OR RESSEQ 147:160)       
REMARK   3     ATOM PAIRS NUMBER  : 1021                                        
REMARK   3     RMSD               : 0.078                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2WWO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41226.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : SILICON (311)                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17976                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 84.50                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.5                               
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.8                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ESO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES-NAOH, PH 6.5, 0.2M              
REMARK 280  ZNSO4, 25% PEG-MME 550                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.27000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.54000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       54.54000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       27.27000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2035   LIES ON A SPECIAL POSITION.                         
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A    -7                                                      
REMARK 465     MET A    -6                                                      
REMARK 465     ALA A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     MET A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     LYS A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     ASN B    -7                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     ALA B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     MET B    -3                                                      
REMARK 465     ASN B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     LYS B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     MET B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   6    CG   CD   CE   NZ                                   
REMARK 470     LYS A  12    CE   NZ                                             
REMARK 470     LYS A  23    CE   NZ                                             
REMARK 470     LYS A  66    CD   CE   NZ                                        
REMARK 470     LYS A  69    CE   NZ                                             
REMARK 470     LYS A  84    CD   CE   NZ                                        
REMARK 470     LYS B  66    CE   NZ                                             
REMARK 470     LYS B  69    CD   CE   NZ                                        
REMARK 470     LYS B  84    CE   NZ                                             
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    PRO A  59       44.40    -72.73                                   
REMARK 500    ALA A  73       14.74     56.30                                   
REMARK 500    ALA B  73       15.21     59.95                                   
REMARK 500    ASP B  81       65.97   -155.97                                   
REMARK 500    ASP B 139      110.28   -161.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     HOH B 2035                                                       
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                              ZN A1162  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  79   ND1                                                    
REMARK 620 2 HIS A  88   ND1 101.6                                              
REMARK 620 3 ASP A 100   OD1 113.5  98.6                                        
REMARK 620 4 HIS A  97   ND1 101.7 122.2 118.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1163  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 130   NE2                                                    
REMARK 620 2 HOH A2090   O    85.2                                              
REMARK 620 3 HOH A2091   O    86.0 170.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1164  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2093   O                                                      
REMARK 620 2 ASP A   5   OD1  78.1                                              
REMARK 620 3 HIS B 130   NE2 106.5 144.2                                        
REMARK 620 4 HOH A2094   O    98.7 112.0 102.5                                  
REMARK 620 5 ASP A   5   OD2  94.3  61.1  83.1 163.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1165  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 135   NE2                                                    
REMARK 620 2 HIS A  56   NE2 106.9                                              
REMARK 620 3 HIS A  54   ND1  90.5 129.5                                        
REMARK 620 4 HIS A  79   NE2 150.1  98.0  86.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1162  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  88   ND1                                                    
REMARK 620 2 HIS B  79   ND1 104.8                                              
REMARK 620 3 HIS B  97   ND1 126.6 103.4                                        
REMARK 620 4 ASP B 100   OD1  90.6 108.0 121.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1163  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 144   NE2                                                    
REMARK 620 2 HOH B2119   O    89.3                                              
REMARK 620 3 HIS A 144   NE2  87.8  82.0                                        
REMARK 620 4 HOH B2118   O    92.4 172.6 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1164  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 135   NE2                                                    
REMARK 620 2 HIS B  54   ND1  96.3                                              
REMARK 620 3 HIS B  56   NE2 104.9 129.1                                        
REMARK 620 4 HIS B  79   NE2 152.6  79.0  98.7                                  
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  ZN A1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1164                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1165                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1164                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B1165                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1166                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1167                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WWN   RELATED DB: PDB                                   
REMARK 900  YERSINIA PSEUDOTUBERCULOSIS SUPEROXIDE DISMUTASE                    
REMARK 900  C WITH BOUND AZIDE                                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE CONTAINS SIGNAL PEPTIDE NOT PRESENT IN MATURE               
REMARK 999 PROTEIN                                                              
DBREF  2WWO A   -7   161  UNP    Q66ED7   Q66ED7_YERPS    21    189             
DBREF  2WWO B   -7   161  UNP    Q66ED7   Q66ED7_YERPS    21    189             
SEQRES   1 A  169  ASN MET ALA GLY MET ASN ASP LYS ALA SER MET ASN ASP          
SEQRES   2 A  169  LYS ALA SER MET THR VAL LYS ILE ASN GLU SER LEU PRO          
SEQRES   3 A  169  GLN GLY ASN GLY LYS ALA LEU GLY THR VAL THR VAL THR          
SEQRES   4 A  169  GLU THR ALA TYR GLY LEU LEU PHE THR PRO HIS LEU THR          
SEQRES   5 A  169  GLY LEU ALA PRO GLY ILE HIS GLY PHE HIS LEU HIS GLU          
SEQRES   6 A  169  LYS PRO SER CYS ALA PRO GLY MET LYS ASP GLY LYS ALA          
SEQRES   7 A  169  VAL PRO ALA LEU ALA ALA GLY GLY HIS LEU ASP PRO ASN          
SEQRES   8 A  169  LYS THR GLY VAL HIS LEU GLY PRO TYR ASN ASP LYS GLY          
SEQRES   9 A  169  HIS LEU GLY ASP LEU PRO GLY LEU VAL VAL ASN ALA ASP          
SEQRES  10 A  169  GLY THR ALA THR TYR PRO VAL LEU ALA PRO ARG LEU LYS          
SEQRES  11 A  169  SER LEU SER GLU VAL LYS GLN HIS ALA LEU MET ILE HIS          
SEQRES  12 A  169  ALA GLY GLY ASP ASN TYR SER ASP HIS PRO MET PRO LEU          
SEQRES  13 A  169  GLY GLY GLY GLY ALA ARG MET ALA CYS GLY VAL ILE GLU          
SEQRES   1 B  169  ASN MET ALA GLY MET ASN ASP LYS ALA SER MET ASN ASP          
SEQRES   2 B  169  LYS ALA SER MET THR VAL LYS ILE ASN GLU SER LEU PRO          
SEQRES   3 B  169  GLN GLY ASN GLY LYS ALA LEU GLY THR VAL THR VAL THR          
SEQRES   4 B  169  GLU THR ALA TYR GLY LEU LEU PHE THR PRO HIS LEU THR          
SEQRES   5 B  169  GLY LEU ALA PRO GLY ILE HIS GLY PHE HIS LEU HIS GLU          
SEQRES   6 B  169  LYS PRO SER CYS ALA PRO GLY MET LYS ASP GLY LYS ALA          
SEQRES   7 B  169  VAL PRO ALA LEU ALA ALA GLY GLY HIS LEU ASP PRO ASN          
SEQRES   8 B  169  LYS THR GLY VAL HIS LEU GLY PRO TYR ASN ASP LYS GLY          
SEQRES   9 B  169  HIS LEU GLY ASP LEU PRO GLY LEU VAL VAL ASN ALA ASP          
SEQRES  10 B  169  GLY THR ALA THR TYR PRO VAL LEU ALA PRO ARG LEU LYS          
SEQRES  11 B  169  SER LEU SER GLU VAL LYS GLN HIS ALA LEU MET ILE HIS          
SEQRES  12 B  169  ALA GLY GLY ASP ASN TYR SER ASP HIS PRO MET PRO LEU          
SEQRES  13 B  169  GLY GLY GLY GLY ALA ARG MET ALA CYS GLY VAL ILE GLU          
HET     ZN  A1162       1                                                       
HET     ZN  B1162       1                                                       
HET     ZN  A1163       1                                                       
HET     ZN  B1163       1                                                       
HET     ZN  A1164       1                                                       
HET     ZN  A1165       1                                                       
HET     ZN  B1164       1                                                       
HET    MES  B1165      12                                                       
HET    GOL  B1166       6                                                       
HET    GOL  B1167       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN                                                         
FORMUL   3   ZN    7(ZN 2+)                                                     
FORMUL   4  MES    C6 H13 N O4 S                                                
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6  HOH   *217(H2 O)                                                    
HELIX    1   1 ALA A   73  GLY A   77  5                                   5    
HELIX    2   2 SER A  123  VAL A  127  5                                   5    
HELIX    3   3 MET A  146  GLY A  151  5                                   6    
HELIX    4   4 ALA B   73  GLY B   77  5                                   5    
HELIX    5   5 SER B  123  VAL B  127  5                                   5    
HELIX    6   6 MET B  146  GLY B  151  5                                   6    
SHEET    1  AA 7 PHE A  53  HIS A  56  0                                        
SHEET    2  AA 7 ALA A 131  HIS A 135 -1  O  ALA A 131   N  HIS A  56           
SHEET    3  AA 7 ARG A 154  VAL A 159 -1  N  MET A 155   O  ILE A 134           
SHEET    4  AA 7 SER A   8  SER A  16 -1  O  ASN A  14   N  CYS A 157           
SHEET    5  AA 7 ASN A  21  THR A  33 -1  N  GLY A  22   O  GLU A  15           
SHEET    6  AA 7 GLY A  36  LEU A  43 -1  O  GLY A  36   N  THR A  33           
SHEET    7  AA 7 VAL A 116  ALA A 118 -1  O  VAL A 116   N  PHE A  39           
SHEET    1  AB 2 GLY A  49  HIS A  51  0                                        
SHEET    2  AB 2 LEU A 104  VAL A 106 -1  O  LEU A 104   N  HIS A  51           
SHEET    1  AC 2 GLY A  64  LYS A  66  0                                        
SHEET    2  AC 2 LYS A  69  VAL A  71 -1  O  LYS A  69   N  LYS A  66           
SHEET    1  BA 7 PHE B  53  HIS B  56  0                                        
SHEET    2  BA 7 ALA B 131  HIS B 135 -1  O  ALA B 131   N  HIS B  56           
SHEET    3  BA 7 ARG B 154  VAL B 159 -1  N  MET B 155   O  ILE B 134           
SHEET    4  BA 7 SER B   8  SER B  16 -1  O  ASN B  14   N  CYS B 157           
SHEET    5  BA 7 ASN B  21  THR B  33 -1  N  GLY B  22   O  GLU B  15           
SHEET    6  BA 7 GLY B  36  LEU B  43 -1  O  GLY B  36   N  THR B  33           
SHEET    7  BA 7 VAL B 116  ALA B 118 -1  O  VAL B 116   N  PHE B  39           
SHEET    1  BB 2 GLY B  49  HIS B  51  0                                        
SHEET    2  BB 2 LEU B 104  VAL B 106 -1  O  LEU B 104   N  HIS B  51           
SHEET    1  BC 2 GLY B  64  LYS B  66  0                                        
SHEET    2  BC 2 LYS B  69  VAL B  71 -1  O  LYS B  69   N  LYS B  66           
SSBOND   1 CYS A   61    CYS A  157                          1555   1555  2.04  
SSBOND   2 CYS B   61    CYS B  157                          1555   1555  2.04  
LINK        ZN    ZN A1162                 ND1 HIS A  79     1555   1555  2.19  
LINK        ZN    ZN A1162                 ND1 HIS A  88     1555   1555  2.16  
LINK        ZN    ZN A1162                 OD1 ASP A 100     1555   1555  2.06  
LINK        ZN    ZN A1162                 ND1 HIS A  97     1555   1555  2.22  
LINK        ZN    ZN A1163                 NE2 HIS A 130     1555   1555  2.24  
LINK        ZN    ZN A1163                 O   HOH A2090     1555   1555  2.37  
LINK        ZN    ZN A1163                 O   HOH A2091     1555   1555  2.40  
LINK        ZN    ZN A1164                 O   HOH A2093     1555   1555  2.35  
LINK        ZN    ZN A1164                 OD1 ASP A   5     1555   1555  2.30  
LINK        ZN    ZN A1164                 NE2 HIS B 130     1555   3664  2.03  
LINK        ZN    ZN A1164                 O   HOH A2094     1555   1555  2.28  
LINK        ZN    ZN A1164                 OD2 ASP A   5     1555   1555  2.02  
LINK        ZN    ZN A1165                 NE2 HIS A 135     1555   1555  2.15  
LINK        ZN    ZN A1165                 NE2 HIS A  56     1555   1555  2.28  
LINK        ZN    ZN A1165                 ND1 HIS A  54     1555   1555  2.28  
LINK        ZN    ZN A1165                 NE2 HIS A  79     1555   1555  2.14  
LINK        ZN    ZN B1162                 ND1 HIS B  79     1555   1555  2.07  
LINK        ZN    ZN B1162                 ND1 HIS B  97     1555   1555  2.26  
LINK        ZN    ZN B1162                 OD1 ASP B 100     1555   1555  2.02  
LINK        ZN    ZN B1162                 ND1 HIS B  88     1555   1555  2.19  
LINK        ZN    ZN B1163                 O   HOH B2119     1555   1555  2.11  
LINK        ZN    ZN B1163                 NE2 HIS A 144     1555   6664  2.15  
LINK        ZN    ZN B1163                 O   HOH B2118     1555   1555  2.49  
LINK        ZN    ZN B1163                 NE2 HIS B 144     1555   1555  2.24  
LINK        ZN    ZN B1164                 ND1 HIS B  54     1555   1555  2.22  
LINK        ZN    ZN B1164                 NE2 HIS B  56     1555   1555  2.14  
LINK        ZN    ZN B1164                 NE2 HIS B  79     1555   1555  2.28  
LINK        ZN    ZN B1164                 NE2 HIS B 135     1555   1555  2.19  
CISPEP   1 HIS A  144    PRO A  145          0         0.28                     
CISPEP   2 HIS B  144    PRO B  145          0         7.24                     
SITE     1 AC1  4 HIS A  79  HIS A  88  HIS A  97  ASP A 100                    
SITE     1 AC2  4 HIS B  79  HIS B  88  HIS B  97  ASP B 100                    
SITE     1 AC3  4 HIS A 130  HOH A2090  HOH A2091  HOH A2092                    
SITE     1 AC4  4 HIS A 144  HIS B 144  HOH B2118  HOH B2119                    
SITE     1 AC5  5 ASN A   4  ASP A   5  HOH A2093  HOH A2094                    
SITE     2 AC5  5 HIS B 130                                                     
SITE     1 AC6  4 HIS A  54  HIS A  56  HIS A  79  HIS A 135                    
SITE     1 AC7  4 HIS B  54  HIS B  56  HIS B  79  HIS B 135                    
SITE     1 AC8  9 ASN A 140  THR B  29  HIS B  42  THR B 113                    
SITE     2 AC8  9 PRO B 115  GOL B1167  HOH B2120  HOH B2121                    
SITE     3 AC8  9 HOH B2122                                                     
SITE     1 AC9  4 LEU B  46  PRO B  48  ALA B 108  HOH B2123                    
SITE     1 BC1  5 LYS B   6  THR B  31  LEU B  38  MES B1165                    
SITE     2 BC1  5 HOH B2122                                                     
CRYST1   97.546   97.546   81.810  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010252  0.005919  0.000000        0.00000                         
SCALE2      0.000000  0.011837  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012223        0.00000                         
MTRIX1   1  0.400810  0.680640  0.613260       30.46413    1                    
MTRIX2   1  0.696470 -0.661250  0.278700       -0.22247    1                    
MTRIX3   1  0.595210  0.315410 -0.739080      -70.51259    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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