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Database: PDB
Entry: 5VBI
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Original site: 5VBI 
HEADER    ISOMERASE                               29-MAR-17   5VBI              
TITLE     CRYSTAL STRUCTURE OF THE R515W MISSENSE VARIANT OF HUMAN PGM1         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLUCOMUTASE-1;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;                              
COMPND   5 EC: 5.4.2.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PGM1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHOGLUCOMUTASE-1, PGM1, ISOMERASE, PHOSPHORYL TRANSFER            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.STIERS,L.J.BEAMER                                                 
REVDAT   4   27-NOV-19 5VBI    1       REMARK                                   
REVDAT   3   17-OCT-18 5VBI    1       JRNL                                     
REVDAT   2   05-SEP-18 5VBI    1       JRNL                                     
REVDAT   1   20-JUN-18 5VBI    0                                                
JRNL        AUTH   K.M.STIERS,L.J.BEAMER                                        
JRNL        TITL   A HOTSPOT FOR DISEASE-ASSOCIATED VARIANTS OF HUMAN PGM1 IS   
JRNL        TITL 2 ASSOCIATED WITH IMPAIRED LIGAND BINDING AND LOOP DYNAMICS.   
JRNL        REF    STRUCTURE                     V.  26  1337 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   30122451                                                     
JRNL        DOI    10.1016/J.STR.2018.07.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.029                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 149743                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.978                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7454                            
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 54.5219 -  5.4359    0.99     5094   262  0.1774 0.1741        
REMARK   3     2  5.4359 -  4.3152    1.00     4843   280  0.1289 0.1560        
REMARK   3     3  4.3152 -  3.7699    1.00     4868   239  0.1302 0.1412        
REMARK   3     4  3.7699 -  3.4253    1.00     4795   265  0.1369 0.1655        
REMARK   3     5  3.4253 -  3.1798    1.00     4804   254  0.1541 0.1943        
REMARK   3     6  3.1798 -  2.9923    1.00     4747   246  0.1600 0.1973        
REMARK   3     7  2.9923 -  2.8425    1.00     4775   243  0.1658 0.1831        
REMARK   3     8  2.8425 -  2.7187    1.00     4791   250  0.1623 0.1969        
REMARK   3     9  2.7187 -  2.6141    1.00     4689   275  0.1579 0.1839        
REMARK   3    10  2.6141 -  2.5239    1.00     4757   253  0.1586 0.1859        
REMARK   3    11  2.5239 -  2.4450    1.00     4727   268  0.1545 0.1771        
REMARK   3    12  2.4450 -  2.3751    1.00     4706   242  0.1563 0.1801        
REMARK   3    13  2.3751 -  2.3125    1.00     4716   233  0.1578 0.2001        
REMARK   3    14  2.3125 -  2.2561    1.00     4711   273  0.1564 0.1849        
REMARK   3    15  2.2561 -  2.2048    1.00     4722   257  0.1613 0.2094        
REMARK   3    16  2.2048 -  2.1579    1.00     4705   241  0.1683 0.2018        
REMARK   3    17  2.1579 -  2.1147    1.00     4700   248  0.1791 0.2112        
REMARK   3    18  2.1147 -  2.0748    1.00     4681   283  0.1880 0.2209        
REMARK   3    19  2.0748 -  2.0378    1.00     4713   249  0.1931 0.2086        
REMARK   3    20  2.0378 -  2.0032    1.00     4741   214  0.1787 0.1995        
REMARK   3    21  2.0032 -  1.9709    1.00     4690   236  0.1797 0.1939        
REMARK   3    22  1.9709 -  1.9406    1.00     4720   236  0.1884 0.2220        
REMARK   3    23  1.9406 -  1.9121    1.00     4691   243  0.2037 0.2403        
REMARK   3    24  1.9121 -  1.8851    1.00     4697   264  0.2028 0.2453        
REMARK   3    25  1.8851 -  1.8596    1.00     4683   235  0.2154 0.2747        
REMARK   3    26  1.8596 -  1.8355    1.00     4735   218  0.2373 0.2951        
REMARK   3    27  1.8355 -  1.8126    1.00     4686   223  0.2526 0.2973        
REMARK   3    28  1.8126 -  1.7907    1.00     4684   243  0.2902 0.3007        
REMARK   3    29  1.7907 -  1.7699    1.00     4709   248  0.3059 0.3162        
REMARK   3    30  1.7699 -  1.7500    1.00     4709   233  0.3264 0.3578        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.211            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.623           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.22                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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           8890                                  
REMARK   3   ANGLE     :  0.783          12069                                  
REMARK   3   CHIRALITY :  0.055           1350                                  
REMARK   3   PLANARITY :  0.005           1569                                  
REMARK   3   DIHEDRAL  :  4.430           7178                                  
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 0 THROUGH 80 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  72.9921  37.4942 -18.7923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1667 T22:   0.3570                                     
REMARK   3      T33:   0.2052 T12:  -0.0509                                     
REMARK   3      T13:  -0.0063 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6239 L22:   0.7682                                     
REMARK   3      L33:   1.1887 L12:   0.0678                                     
REMARK   3      L13:  -0.1588 L23:   0.0545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0971 S12:  -0.1886 S13:   0.0443                       
REMARK   3      S21:   0.1188 S22:  -0.0466 S23:  -0.1488                       
REMARK   3      S31:  -0.1354 S32:   0.5274 S33:  -0.0405                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 183 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  70.3724  33.0060 -23.9024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1108 T22:   0.2691                                     
REMARK   3      T33:   0.1498 T12:   0.0072                                     
REMARK   3      T13:  -0.0053 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6421 L22:   1.1940                                     
REMARK   3      L33:   1.6720 L12:   0.5054                                     
REMARK   3      L13:  -0.6194 L23:  -0.1251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1072 S12:  -0.1909 S13:  -0.0076                       
REMARK   3      S21:   0.0655 S22:  -0.0524 S23:  -0.1484                       
REMARK   3      S31:  -0.0808 S32:   0.4461 S33:  -0.0530                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 227 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.2290  28.0738 -35.8375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1555 T22:   0.2196                                     
REMARK   3      T33:   0.1464 T12:   0.0342                                     
REMARK   3      T13:  -0.0247 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2219 L22:   0.8266                                     
REMARK   3      L33:   1.3340 L12:   0.3299                                     
REMARK   3      L13:  -0.6518 L23:   0.1636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0014 S12:   0.3126 S13:   0.1077                       
REMARK   3      S21:  -0.0893 S22:   0.0204 S23:   0.0874                       
REMARK   3      S31:   0.0498 S32:  -0.1860 S33:  -0.0126                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 228 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.5319  23.9280 -22.4847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1253 T22:   0.1136                                     
REMARK   3      T33:   0.1669 T12:   0.0140                                     
REMARK   3      T13:  -0.0050 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8477 L22:   0.5410                                     
REMARK   3      L33:   1.6193 L12:   0.0478                                     
REMARK   3      L13:  -0.1541 L23:  -0.1634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0157 S12:   0.1060 S13:   0.0160                       
REMARK   3      S21:  -0.0132 S22:  -0.0037 S23:   0.0438                       
REMARK   3      S31:   0.1198 S32:  -0.0551 S33:  -0.0130                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.3626  22.6208 -12.8449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1133 T22:   0.1282                                     
REMARK   3      T33:   0.2003 T12:  -0.0403                                     
REMARK   3      T13:   0.0173 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0081 L22:   0.8297                                     
REMARK   3      L33:   1.5423 L12:  -0.2898                                     
REMARK   3      L13:  -0.1300 L23:   0.2336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0149 S12:   0.1182 S13:  -0.0916                       
REMARK   3      S21:   0.0205 S22:  -0.0461 S23:   0.1386                       
REMARK   3      S31:   0.1120 S32:  -0.2097 S33:   0.0465                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 435 THROUGH 522 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.1400  18.4013   3.0343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2872 T22:   0.1414                                     
REMARK   3      T33:   0.1623 T12:   0.0181                                     
REMARK   3      T13:  -0.0113 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2541 L22:   1.6555                                     
REMARK   3      L33:   1.6640 L12:  -0.3952                                     
REMARK   3      L13:  -0.1915 L23:   0.3209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0546 S12:  -0.1427 S13:  -0.0482                       
REMARK   3      S21:   0.4049 S22:   0.0305 S23:  -0.0050                       
REMARK   3      S31:   0.3566 S32:   0.1294 S33:   0.0097                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 523 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2859  26.2688   0.6896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1896 T22:   0.1342                                     
REMARK   3      T33:   0.1760 T12:  -0.0371                                     
REMARK   3      T13:   0.0369 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3852 L22:   1.8537                                     
REMARK   3      L33:   1.8516 L12:  -0.2577                                     
REMARK   3      L13:  -0.0359 L23:   0.2292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:  -0.0184 S13:  -0.1407                       
REMARK   3      S21:   0.1376 S22:   0.0081 S23:   0.1228                       
REMARK   3      S31:   0.2561 S32:  -0.2446 S33:   0.0043                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 293 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9283  60.6263 -39.7786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3016 T22:   0.1424                                     
REMARK   3      T33:   0.1441 T12:  -0.0352                                     
REMARK   3      T13:  -0.0715 T23:   0.0547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9146 L22:   1.8563                                     
REMARK   3      L33:   2.1286 L12:   1.4526                                     
REMARK   3      L13:   1.2659 L23:   0.7483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4863 S12:  -0.3393 S13:  -0.4065                       
REMARK   3      S21:   0.3460 S22:  -0.2153 S23:  -0.2129                       
REMARK   3      S31:   0.5095 S32:  -0.2853 S33:  -0.0935                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 294 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6415  79.6035 -23.7660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2766 T22:   0.1369                                     
REMARK   3      T33:   0.1969 T12:  -0.0266                                     
REMARK   3      T13:  -0.0120 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1302 L22:   0.8698                                     
REMARK   3      L33:   2.4257 L12:  -0.1720                                     
REMARK   3      L13:  -0.1110 L23:  -0.0668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:  -0.1885 S13:   0.0173                       
REMARK   3      S21:   0.2674 S22:  -0.0055 S23:  -0.1083                       
REMARK   3      S31:  -0.1450 S32:   0.1602 S33:  -0.0371                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227004.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00003                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 150294                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 13.60                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.58000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.11.1_2575                                    
REMARK 200 STARTING MODEL: 5EPC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES 7.5, 0.1M SODIUM CHLORIDE,    
REMARK 280  1.5-1.7M AMMONIUM SULFATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 293.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.68500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       86.16500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       86.16500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.84250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       86.16500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       86.16500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.52750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       86.16500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.16500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.84250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       86.16500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.16500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.52750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.68500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 A1179  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1374  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     MET A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     VAL B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     ASN B     0                                                      
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     ASN A   0    CG   OD1  ND2                                       
REMARK 470     MET A   1    CG   SD   CE                                        
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     SER A 460    OG                                                  
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     VAL B   2    CG1  CG2                                            
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     VAL B   5    CG1  CG2                                            
REMARK 470     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     GLN B  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     GLN B 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     GLU B 178    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 179    CG   OD1  ND2                                       
REMARK 470     LYS B 180    CG   CD   CE   NZ                                   
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 325    CG   CD   OE1  NE2                                  
REMARK 470     THR B 348    OG1  CG2                                            
REMARK 470     LYS B 349    CG   CD   CE   NZ                                   
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 443    CG   CD   CE   NZ                                   
REMARK 470     ARG B 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 457    CG   CD   CE   NZ                                   
REMARK 470     SER B 460    OG                                                  
REMARK 470     ASN B 462    CG   OD1  ND2                                       
REMARK 470     ASP B 463    CG   OD1  OD2                                       
REMARK 470     LYS B 464    CG   CD   CE   NZ                                   
REMARK 470     VAL B 465    CG1  CG2                                            
REMARK 470     VAL B 525    CG1  CG2                                            
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1205     O    HOH A  1218              2.00            
REMARK 500   O    HOH A   707     O    HOH A  1226              2.05            
REMARK 500   OE2  GLU B   376     O    HOH B   701              2.06            
REMARK 500   NE2  GLN A   533     O    HOH A   701              2.07            
REMARK 500   OG   SER A   541     O    HOH A   702              2.07            
REMARK 500   O    HOH A   763     O    HOH A   860              2.07            
REMARK 500   O    ARG A   452     O    HOH A   703              2.08            
REMARK 500   O    HOH A  1004     O    HOH A  1095              2.09            
REMARK 500   O    HOH B  1034     O    HOH B  1035              2.10            
REMARK 500   O    HOH A  1218     O    HOH A  1352              2.11            
REMARK 500   O    HOH A  1264     O    HOH A  1268              2.15            
REMARK 500   O    HOH A  1230     O    HOH A  1390              2.16            
REMARK 500   OD2  ASP B   166     O    HOH B   703              2.17            
REMARK 500   O    LYS B   349     O    HOH B   704              2.17            
REMARK 500   O    HOH A  1163     O    HOH A  1348              2.17            
REMARK 500   O    HOH A  1170     O    HOH A  1276              2.18            
REMARK 500   O    HOH A  1254     O    HOH A  1325              2.18            
REMARK 500   O    HOH B   706     O    HOH B   804              2.18            
REMARK 500   O    ALA B   142     O    HOH B   705              2.19            
REMARK 500   O    HOH A   965     O    HOH A  1104              2.19            
REMARK 500   OD1  ASN B   439     O    HOH B   706              2.19            
REMARK 500   O3   GOL A   607     O    HOH A   705              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA B 461   CB  -  CA  -  C   ANGL. DEV. =   9.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  66       -7.79     86.30                                   
REMARK 500    SEP A 117     -115.74     60.56                                   
REMARK 500    SEP A 117     -118.01     56.99                                   
REMARK 500    ILE A 133     -166.28   -106.60                                   
REMARK 500    ALA A 269       40.02   -102.15                                   
REMARK 500    SER A 378       45.54    -82.92                                   
REMARK 500    ALA A 461      122.93    158.61                                   
REMARK 500    TYR B  66      -10.23     85.92                                   
REMARK 500    SEP B 117     -116.69     57.85                                   
REMARK 500    SEP B 117     -114.61     60.65                                   
REMARK 500    ILE B 133     -164.36   -107.56                                   
REMARK 500    ILE B 236      -60.94    -90.55                                   
REMARK 500    SER B 378       45.40    -82.20                                   
REMARK 500    ALA B 461     -157.62    -85.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1400        DISTANCE =  6.09 ANGSTROMS                       
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                              MG A 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP A 117   OG                                                     
REMARK 620 2 SEP A 117   OG    5.9                                              
REMARK 620 3 SEP A 117   O1P  74.4  76.1                                        
REMARK 620 4 ASP A 288   OD1  92.3  86.6  89.8                                  
REMARK 620 5 ASP A 290   OD2  93.2  91.7 167.6  92.0                            
REMARK 620 6 ASP A 292   OD1 171.7 174.1  98.3  91.6  93.9                      
REMARK 620 7 HOH A 762   O    84.5  90.2  88.8 176.7  88.7  91.5                
REMARK 620 8 HOH A 899   O    82.0  83.7   7.6  89.2 175.2  90.7  89.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 603  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP B 117   OG                                                     
REMARK 620 2 SEP B 117   OG    0.5                                              
REMARK 620 3 SEP B 117   O1P  79.1  78.6                                        
REMARK 620 4 ASP B 288   OD2  86.9  87.2 100.7                                  
REMARK 620 5 ASP B 290   OD1  92.5  92.9 167.5  88.0                            
REMARK 620 6 ASP B 292   OD1 173.7 173.4  95.6  90.7  93.3                      
REMARK 620 7 HOH B 761   O    93.1  92.8  80.1 179.2  91.2  89.4                
REMARK 620 8 HOH B 873   O    81.6  81.1  12.0  89.2 173.6  92.6  91.6          
REMARK 620 N                    1     2     3     4     5     6     7           
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 MG A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 610                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE VERSION OF THE ENZYME                                      
DBREF  5VBI A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5VBI B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5VBI MET A  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS A  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS A  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS A  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS A  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS A  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS A  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI SER A  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI SER A  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLY A  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI VAL A  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI ASP A  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI LEU A  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLY A   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI THR A   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLU A   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI ASN A   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI LEU A   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI TYR A   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI PHE A   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLN A   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI TRP A  515  UNP  P36871    ARG   515 ENGINEERED MUTATION            
SEQADV 5VBI MET B  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS B  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS B  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS B  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS B  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS B  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI HIS B  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI SER B  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI SER B  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLY B  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI VAL B  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI ASP B  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI LEU B  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLY B   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI THR B   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLU B   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI ASN B   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI LEU B   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI TYR B   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI PHE B   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI GLN B   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VBI TRP B  515  UNP  P36871    ARG   515 ENGINEERED MUTATION            
SEQRES   1 A  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 A  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 A  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 A  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 A  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 A  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 A  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 A  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 A  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 A  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SEP HIS ASN PRO          
SEQRES  12 A  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 A  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 A  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 A  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 A  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 A  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 A  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 A  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 A  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 A  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 A  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP          
SEQRES  23 A  585  PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET          
SEQRES  24 A  585  LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY          
SEQRES  25 A  585  ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE          
SEQRES  26 A  585  PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA          
SEQRES  27 A  585  ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL          
SEQRES  28 A  585  ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU          
SEQRES  29 A  585  ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU          
SEQRES  30 A  585  THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP          
SEQRES  31 A  585  ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY          
SEQRES  32 A  585  THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP          
SEQRES  33 A  585  ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS          
SEQRES  34 A  585  GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS          
SEQRES  35 A  585  TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU          
SEQRES  36 A  585  VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU          
SEQRES  37 A  585  GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN          
SEQRES  38 A  585  PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA          
SEQRES  39 A  585  ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE          
SEQRES  40 A  585  SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY          
SEQRES  41 A  585  SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA          
SEQRES  42 A  585  GLY ALA THR ILE TRP LEU TYR ILE ASP SER TYR GLU LYS          
SEQRES  43 A  585  ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU          
SEQRES  44 A  585  ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU          
SEQRES  45 A  585  GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR          
SEQRES   1 B  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 B  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 B  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 B  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 B  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 B  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 B  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 B  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 B  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 B  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SEP HIS ASN PRO          
SEQRES  12 B  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 B  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 B  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 B  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 B  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 B  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 B  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 B  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 B  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 B  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 B  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP          
SEQRES  23 B  585  PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET          
SEQRES  24 B  585  LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY          
SEQRES  25 B  585  ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE          
SEQRES  26 B  585  PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA          
SEQRES  27 B  585  ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL          
SEQRES  28 B  585  ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU          
SEQRES  29 B  585  ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU          
SEQRES  30 B  585  THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP          
SEQRES  31 B  585  ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY          
SEQRES  32 B  585  THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP          
SEQRES  33 B  585  ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS          
SEQRES  34 B  585  GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS          
SEQRES  35 B  585  TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU          
SEQRES  36 B  585  VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU          
SEQRES  37 B  585  GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN          
SEQRES  38 B  585  PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA          
SEQRES  39 B  585  ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE          
SEQRES  40 B  585  SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY          
SEQRES  41 B  585  SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA          
SEQRES  42 B  585  GLY ALA THR ILE TRP LEU TYR ILE ASP SER TYR GLU LYS          
SEQRES  43 B  585  ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU          
SEQRES  44 B  585  ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU          
SEQRES  45 B  585  GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR          
MODRES 5VBI SEP A  117  SER  MODIFIED RESIDUE                                   
MODRES 5VBI SEP B  117  SER  MODIFIED RESIDUE                                   
HET    SEP  A 117      16                                                       
HET    SEP  B 117      16                                                       
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET     MG  A 604       1                                                       
HET    GOL  A 605       6                                                       
HET    GOL  A 606       6                                                       
HET    GOL  A 607       6                                                       
HET    GOL  A 608       6                                                       
HET    GOL  A 609       6                                                       
HET    GOL  A 610       6                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET     MG  B 603       1                                                       
HET    GOL  B 604       6                                                       
HET    GOL  B 605       6                                                       
HET    GOL  B 606       6                                                       
HET    GOL  B 607       6                                                       
HET    GOL  B 608       6                                                       
HET    GOL  B 609       6                                                       
HET    GOL  B 610       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   7  GOL    13(C3 H8 O3)                                                 
FORMUL  23  HOH   *1180(H2 O)                                                   
HELIX    1 AA1 VAL A   26  SER A   32  1                                   7    
HELIX    2 AA2 ASN A   34  THR A   46  1                                  13    
HELIX    3 AA3 GLU A   48  GLN A   53  1                                   6    
HELIX    4 AA4 TYR A   66  ASN A   81  1                                  16    
HELIX    5 AA5 SER A   95  LYS A  107  1                                  13    
HELIX    6 AA6 PRO A  140  ILE A  154  1                                  15    
HELIX    7 AA7 VAL A  192  PHE A  203  1                                  12    
HELIX    8 AA8 ASP A  204  SER A  213  1                                  10    
HELIX    9 AA9 VAL A  229  LEU A  237  1                                   9    
HELIX   10 AB1 PRO A  244  ASN A  246  5                                   3    
HELIX   11 AB2 ASP A  256  HIS A  260  5                                   5    
HELIX   12 AB3 ALA A  269  SER A  278  1                                  10    
HELIX   13 AB4 ASN A  305  ASN A  316  1                                  12    
HELIX   14 AB5 ILE A  317  SER A  319  5                                   3    
HELIX   15 AB6 ILE A  320  GLY A  327  1                                   8    
HELIX   16 AB7 GLY A  339  LYS A  349  1                                  11    
HELIX   17 AB8 GLY A  358  ALA A  368  1                                  11    
HELIX   18 AB9 ASP A  390  LYS A  406  1                                  17    
HELIX   19 AC1 SER A  408  GLY A  421  1                                  14    
HELIX   20 AC2 GLU A  434  ASP A  451  1                                  18    
HELIX   21 AC3 ASP A  524  ASN A  529  1                                   6    
HELIX   22 AC4 ASP A  531  GLN A  548  1                                  18    
HELIX   23 AC5 GLN A  548  GLY A  554  1                                   7    
HELIX   24 AC6 VAL B   26  SER B   32  1                                   7    
HELIX   25 AC7 ASN B   34  THR B   46  1                                  13    
HELIX   26 AC8 VAL B   47  ARG B   52  5                                   6    
HELIX   27 AC9 TYR B   66  ASN B   81  1                                  16    
HELIX   28 AD1 SER B   95  LYS B  107  1                                  13    
HELIX   29 AD2 PRO B  140  ILE B  154  1                                  15    
HELIX   30 AD3 VAL B  192  PHE B  203  1                                  12    
HELIX   31 AD4 ASP B  204  SER B  213  1                                  10    
HELIX   32 AD5 VAL B  229  LEU B  237  1                                   9    
HELIX   33 AD6 PRO B  244  ASN B  246  5                                   3    
HELIX   34 AD7 ASP B  256  HIS B  260  5                                   5    
HELIX   35 AD8 ALA B  269  LYS B  277  1                                   9    
HELIX   36 AD9 ASN B  305  ASN B  316  1                                  12    
HELIX   37 AE1 ILE B  317  SER B  319  5                                   3    
HELIX   38 AE2 ILE B  320  GLY B  327  1                                   8    
HELIX   39 AE3 GLY B  339  LYS B  349  1                                  11    
HELIX   40 AE4 GLY B  358  ALA B  368  1                                  11    
HELIX   41 AE5 ASP B  390  LYS B  406  1                                  17    
HELIX   42 AE6 SER B  408  GLY B  421  1                                  14    
HELIX   43 AE7 GLU B  434  ASP B  451  1                                  18    
HELIX   44 AE8 ASP B  531  GLN B  548  1                                  18    
HELIX   45 AE9 GLN B  548  GLY B  554  1                                   7    
SHEET    1 AA1 8 MET A   1  VAL A   2  0                                        
SHEET    2 AA1 8 GLY A 171  LEU A 177  1  O  ASP A 176   N  VAL A   2           
SHEET    3 AA1 8 PHE A 184  VAL A 189 -1  O  PHE A 184   N  PHE A 175           
SHEET    4 AA1 8 ARG A  85  ILE A  93  1  N  LEU A  86   O  GLU A 187           
SHEET    5 AA1 8 THR A  56  GLY A  61  1  N  VAL A  59   O  VAL A  87           
SHEET    6 AA1 8 GLY A 110  LEU A 114  1  O  LEU A 114   N  GLY A  60           
SHEET    7 AA1 8 ASP A 126  ILE A 133 -1  O  ASN A 132   N  GLY A 111           
SHEET    8 AA1 8 LEU A  22  ARG A  25 -1  N  LYS A  24   O  PHE A 127           
SHEET    1 AA2 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA2 2 GLU A 156  VAL A 159 -1  O  TYR A 157   N  VAL A   7           
SHEET    1 AA3 5 ALA A 248  VAL A 249  0                                        
SHEET    2 AA3 5 ILE A 220  ASP A 223  1  N  ILE A 222   O  VAL A 249           
SHEET    3 AA3 5 PHE A 283  PHE A 287  1  O  ALA A 285   N  ASP A 223           
SHEET    4 AA3 5 ASN A 294  GLY A 298 -1  O  LEU A 297   N  GLY A 284           
SHEET    5 AA3 5 PHE A 303  VAL A 304 -1  O  VAL A 304   N  ILE A 296           
SHEET    1 AA4 4 LEU A 352  THR A 355  0                                        
SHEET    2 AA4 4 PHE A 331  SER A 334  1  N  PHE A 331   O  TYR A 353           
SHEET    3 AA4 4 LEU A 373  GLU A 376  1  O  LEU A 373   N  ALA A 332           
SHEET    4 AA4 4 GLY A 380  SER A 383 -1  O  GLY A 380   N  GLU A 376           
SHEET    1 AA5 7 GLN A 458  SER A 460  0                                        
SHEET    2 AA5 7 VAL A 465  ASN A 473 -1  O  TYR A 466   N  PHE A 459           
SHEET    3 AA5 7 LEU A 490  PHE A 494 -1  O  ILE A 493   N  GLU A 469           
SHEET    4 AA5 7 ARG A 499  LEU A 504 -1  O  ILE A 500   N  LEU A 492           
SHEET    5 AA5 7 ALA A 512  GLU A 522 -1  O  TRP A 515   N  ARG A 503           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  TYR A 428   O  LEU A 516           
SHEET    7 AA5 7 VAL A 560  THR A 562 -1  O  VAL A 560   N  ASP A 429           
SHEET    1 AA6 2 TYR A 476  SER A 477  0                                        
SHEET    2 AA6 2 ILE A 484  SER A 485 -1  O  SER A 485   N  TYR A 476           
SHEET    1 AA7 2 VAL B   5  LYS B   8  0                                        
SHEET    2 AA7 2 GLU B 156  VAL B 159 -1  O  TYR B 157   N  VAL B   7           
SHEET    1 AA8 7 LEU B  22  ARG B  25  0                                        
SHEET    2 AA8 7 ASP B 126  ASN B 132 -1  O  PHE B 127   N  LYS B  24           
SHEET    3 AA8 7 GLY B 110  LEU B 114 -1  N  GLY B 111   O  ASN B 132           
SHEET    4 AA8 7 THR B  56  GLY B  61  1  N  VAL B  58   O  ILE B 112           
SHEET    5 AA8 7 ARG B  85  ILE B  93  1  O  VAL B  87   N  VAL B  59           
SHEET    6 AA8 7 PHE B 184  VAL B 189  1  O  GLU B 187   N  LEU B  86           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  PHE B 175   O  PHE B 184           
SHEET    1 AA9 5 ALA B 248  VAL B 249  0                                        
SHEET    2 AA9 5 ILE B 220  ASP B 223  1  N  ILE B 222   O  VAL B 249           
SHEET    3 AA9 5 PHE B 283  PHE B 287  1  O  ALA B 285   N  ASP B 223           
SHEET    4 AA9 5 ASN B 294  GLY B 298 -1  O  LEU B 297   N  GLY B 284           
SHEET    5 AA9 5 PHE B 303  VAL B 304 -1  O  VAL B 304   N  ILE B 296           
SHEET    1 AB1 4 LEU B 352  THR B 355  0                                        
SHEET    2 AB1 4 PHE B 331  SER B 334  1  N  PHE B 331   O  TYR B 353           
SHEET    3 AB1 4 LEU B 373  GLU B 376  1  O  LEU B 373   N  ALA B 332           
SHEET    4 AB1 4 GLY B 380  SER B 383 -1  O  GLY B 380   N  GLU B 376           
SHEET    1 AB2 7 GLN B 458  SER B 460  0                                        
SHEET    2 AB2 7 VAL B 465  ASN B 473 -1  O  TYR B 466   N  PHE B 459           
SHEET    3 AB2 7 LEU B 490  PHE B 494 -1  O  ILE B 493   N  GLU B 469           
SHEET    4 AB2 7 ARG B 499  LEU B 504 -1  O  ILE B 500   N  LEU B 492           
SHEET    5 AB2 7 ALA B 512  GLU B 522 -1  O  TRP B 515   N  ARG B 503           
SHEET    6 AB2 7 ARG B 422  VAL B 433 -1  N  TYR B 428   O  LEU B 516           
SHEET    7 AB2 7 VAL B 560  THR B 562 -1  O  VAL B 560   N  ASP B 429           
SHEET    1 AB3 2 TYR B 476  SER B 477  0                                        
SHEET    2 AB3 2 ILE B 484  SER B 485 -1  O  SER B 485   N  TYR B 476           
LINK         C   ALA A 116                 N  ASEP A 117     1555   1555  1.33  
LINK         C   ALA A 116                 N  BSEP A 117     1555   1555  1.33  
LINK         OG ASEP A 117                MG    MG A 604     1555   1555  2.04  
LINK         OG BSEP A 117                MG    MG A 604     1555   1555  2.11  
LINK         C  ASEP A 117                 N   HIS A 118     1555   1555  1.33  
LINK         C  BSEP A 117                 N   HIS A 118     1555   1555  1.33  
LINK         O1PASEP A 117                MG    MG A 604     1555   1555  2.27  
LINK         OD1 ASP A 288                MG    MG A 604     1555   1555  2.02  
LINK         OD2 ASP A 290                MG    MG A 604     1555   1555  2.19  
LINK         OD1 ASP A 292                MG    MG A 604     1555   1555  2.01  
LINK         C   ALA B 116                 N  ASEP B 117     1555   1555  1.33  
LINK         C   ALA B 116                 N  BSEP B 117     1555   1555  1.33  
LINK         OG ASEP B 117                MG    MG B 603     1555   1555  2.03  
LINK         OG BSEP B 117                MG    MG B 603     1555   1555  2.12  
LINK         C  ASEP B 117                 N   HIS B 118     1555   1555  1.33  
LINK         C  BSEP B 117                 N   HIS B 118     1555   1555  1.33  
LINK         O1PASEP B 117                MG    MG B 603     1555   1555  2.11  
LINK         OD2 ASP B 288                MG    MG B 603     1555   1555  2.02  
LINK         OD1 ASP B 290                MG    MG B 603     1555   1555  2.17  
LINK         OD1 ASP B 292                MG    MG B 603     1555   1555  2.01  
LINK        MG    MG A 604                 O   HOH A 762     1555   1555  2.21  
LINK        MG    MG A 604                 O  BHOH A 899     1555   1555  1.98  
LINK        MG    MG B 603                 O   HOH B 761     1555   1555  2.02  
LINK        MG    MG B 603                 O  BHOH B 873     1555   1555  2.14  
CISPEP   1 ALA A  461    ASN A  462          0       -16.00                     
CISPEP   2 ALA B  461    ASN B  462          0        25.80                     
SITE     1 AC1  6 ASN A 179  LYS A 470  ARG A 491  HOH A 875                    
SITE     2 AC1  6 HOH A1008  HOH A1027                                          
SITE     1 AC2  5 ARG A 217  ARG A 221  PRO A 244  HOH A 906                    
SITE     2 AC2  5 HOH A 927                                                     
SITE     1 AC3  5 SER A 505  GLY A 506  HOH A 706  HOH A 874                    
SITE     2 AC3  5 HOH A1107                                                     
SITE     1 AC4  6 SEP A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     2 AC4  6 HOH A 762  HOH A 899                                          
SITE     1 AC5  5 ARG A 343  ASP A 496  LYS A 523  HOH A 847                    
SITE     2 AC5  5 HOH A 933                                                     
SITE     1 AC6  6 THR A  19  GLY A 358  TRP A 359  HOH A 720                    
SITE     2 AC6  6 HOH A 832  HOH A1119                                          
SITE     1 AC7  5 PRO A 244  ALA A 245  HOH A 705  HOH A 906                    
SITE     2 AC7  5 HOH A1010                                                     
SITE     1 AC8  7 MET A 442  ASN A 473  ASN A 487  GLY A 489                    
SITE     2 AC8  7 LEU A 490  HOH A 707  HOH A 717                               
SITE     1 AC9  9 ASN A 305  PRO A 306  GLU A 377  PHE A 425                    
SITE     2 AC9  9 THR A 426  ARG A 427  THR A 562  HOH A 719                    
SITE     3 AC9  9 HOH A 739                                                     
SITE     1 AD1  8 GLU A 377  ARG A 427  ARG A 503  TRP A 515                    
SITE     2 AD1  8 TYR A 517  HOH A 780  HOH A 874  HOH A1163                    
SITE     1 AD2  5 ARG B 217  ARG B 221  PRO B 244  ASN B 246                    
SITE     2 AD2  5 HOH B 714                                                     
SITE     1 AD3  5 ALA B 314  ALA B 315  PHE B 318  HOH B 737                    
SITE     2 AD3  5 HOH B 902                                                     
SITE     1 AD4  6 SEP B 117  ASP B 288  ASP B 290  ASP B 292                    
SITE     2 AD4  6 HOH B 761  HOH B 873                                          
SITE     1 AD5  7 ILE B 106  VAL B 189  GLU B 193  ALA B 194                    
SITE     2 AD5  7 HOH B 772  HOH B 819  HOH B 835                               
SITE     1 AD6  7 THR B  19  GLY B 358  TRP B 359  HOH B 711                    
SITE     2 AD6  7 HOH B 717  HOH B 756  HOH B 857                               
SITE     1 AD7  4 ARG B 503  LEU B 504  SER B 505  GLY B 506                    
SITE     1 AD8  8 PHE B 303  ASN B 305  ARG B 422  PHE B 424                    
SITE     2 AD8  8 PHE B 425  HOH B 782  HOH B 789  HOH B 871                    
SITE     1 AD9  6 ASN B 179  LYS B 470  ARG B 491  ILE B 493                    
SITE     2 AD9  6 HOH B 716  HOH B 752                                          
SITE     1 AE1  2 ARG B 343  ASP B 496                                          
SITE     1 AE2  6 GLU B 377  ARG B 427  ARG B 503  TRP B 515                    
SITE     2 AE2  6 TYR B 517  HOH B 758                                          
CRYST1  172.330  172.330   99.370  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005803  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005803  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010063        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system