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Database: PDB
Entry: 5VEC
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Original site: 5VEC 
HEADER    ISOMERASE                               04-APR-17   5VEC              
TITLE     CRYSTAL STRUCTURE OF THE R515L 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 5VEC    1       REMARK                                   
REVDAT   3   17-OCT-18 5VEC    1       JRNL                                     
REVDAT   2   05-SEP-18 5VEC    1       JRNL                                     
REVDAT   1   27-JUN-18 5VEC    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.349                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 75165                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.074                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3814                            
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 60.7022 -  6.5973    1.00     2874   155  0.1808 0.2012        
REMARK   3     2  6.5973 -  5.2374    1.00     2752   132  0.1777 0.2159        
REMARK   3     3  5.2374 -  4.5756    1.00     2700   158  0.1327 0.1942        
REMARK   3     4  4.5756 -  4.1574    1.00     2679   138  0.1259 0.1673        
REMARK   3     5  4.1574 -  3.8595    1.00     2687   125  0.1413 0.1945        
REMARK   3     6  3.8595 -  3.6319    1.00     2658   154  0.1477 0.2075        
REMARK   3     7  3.6319 -  3.4501    1.00     2653   140  0.1614 0.2287        
REMARK   3     8  3.4501 -  3.2999    1.00     2636   138  0.1882 0.2508        
REMARK   3     9  3.2999 -  3.1729    1.00     2653   148  0.1946 0.2872        
REMARK   3    10  3.1729 -  3.0634    1.00     2647   125  0.2026 0.2721        
REMARK   3    11  3.0634 -  2.9676    1.00     2642   152  0.2069 0.3065        
REMARK   3    12  2.9676 -  2.8828    1.00     2624   137  0.2289 0.2731        
REMARK   3    13  2.8828 -  2.8069    1.00     2635   138  0.2258 0.3203        
REMARK   3    14  2.8069 -  2.7384    1.00     2639   120  0.2201 0.2936        
REMARK   3    15  2.7384 -  2.6762    1.00     2587   155  0.2215 0.2960        
REMARK   3    16  2.6762 -  2.6192    1.00     2611   163  0.2226 0.3159        
REMARK   3    17  2.6192 -  2.5668    1.00     2598   142  0.2354 0.2957        
REMARK   3    18  2.5668 -  2.5184    1.00     2650   131  0.2339 0.3020        
REMARK   3    19  2.5184 -  2.4734    1.00     2609   121  0.2338 0.3068        
REMARK   3    20  2.4734 -  2.4315    1.00     2582   177  0.2344 0.3120        
REMARK   3    21  2.4315 -  2.3922    1.00     2626   134  0.2452 0.3266        
REMARK   3    22  2.3922 -  2.3554    1.00     2588   126  0.2525 0.3209        
REMARK   3    23  2.3554 -  2.3208    1.00     2643   119  0.2733 0.3546        
REMARK   3    24  2.3208 -  2.2881    1.00     2608   146  0.2754 0.3519        
REMARK   3    25  2.2881 -  2.2572    1.00     2559   153  0.2879 0.3195        
REMARK   3    26  2.2572 -  2.2279    1.00     2619   141  0.2940 0.3982        
REMARK   3    27  2.2279 -  2.2000    1.00     2592   146  0.3074 0.3699        
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)     : 0.295            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.059           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.07                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.17                          
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      :  0.007           8848                                  
REMARK   3   ANGLE     :  0.853          11997                                  
REMARK   3   CHIRALITY :  0.055           1351                                  
REMARK   3   PLANARITY :  0.006           1557                                  
REMARK   3   DIHEDRAL  :  5.220           7219                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 125 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  69.5763  35.4259 -21.5859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1681 T22:   0.3985                                     
REMARK   3      T33:   0.1939 T12:  -0.0292                                     
REMARK   3      T13:   0.0307 T23:  -0.0417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9705 L22:   0.5024                                     
REMARK   3      L33:   0.9575 L12:  -0.1865                                     
REMARK   3      L13:  -0.0909 L23:  -0.4673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0226 S12:  -0.1055 S13:  -0.0306                       
REMARK   3      S21:   0.0364 S22:   0.0193 S23:   0.0034                       
REMARK   3      S31:  -0.2213 S32:   0.5323 S33:   0.0086                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 183 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  74.6701  33.6042 -23.1606              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2270 T22:   0.5399                                     
REMARK   3      T33:   0.2445 T12:  -0.0413                                     
REMARK   3      T13:   0.0471 T23:  -0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6315 L22:   0.2975                                     
REMARK   3      L33:   0.2722 L12:   0.0657                                     
REMARK   3      L13:  -0.1013 L23:   0.1093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1213 S12:  -0.1432 S13:  -0.1007                       
REMARK   3      S21:   0.0143 S22:   0.0459 S23:  -0.0938                       
REMARK   3      S31:  -0.1070 S32:   0.4658 S33:   0.0175                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 319 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1160  30.6706 -28.8240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1366 T22:   0.2373                                     
REMARK   3      T33:   0.2373 T12:   0.0727                                     
REMARK   3      T13:   0.0185 T23:   0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5530 L22:  -0.0172                                     
REMARK   3      L33:   1.0081 L12:   0.3433                                     
REMARK   3      L13:  -0.4600 L23:  -0.1021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0252 S12:   0.2966 S13:   0.1389                       
REMARK   3      S21:  -0.1096 S22:   0.0591 S23:   0.0536                       
REMARK   3      S31:   0.0273 S32:  -0.0654 S33:   0.0177                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 320 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5132  17.2408 -18.1327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1700 T22:   0.1398                                     
REMARK   3      T33:   0.2236 T12:   0.0283                                     
REMARK   3      T13:   0.0070 T23:  -0.0357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8154 L22:   0.5752                                     
REMARK   3      L33:   1.1194 L12:  -0.1166                                     
REMARK   3      L13:  -0.1376 L23:   0.0116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0529 S12:   0.1700 S13:  -0.0537                       
REMARK   3      S21:  -0.0128 S22:  -0.1051 S23:   0.0086                       
REMARK   3      S31:   0.3147 S32:   0.0626 S33:  -0.0259                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 435 THROUGH 483 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.7436  15.4106   5.5915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5121 T22:   0.2661                                     
REMARK   3      T33:   0.3016 T12:   0.0478                                     
REMARK   3      T13:   0.0192 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3657 L22:   0.1643                                     
REMARK   3      L33:   0.7626 L12:  -0.1338                                     
REMARK   3      L13:  -0.1253 L23:   0.2705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2681 S12:  -0.4245 S13:   0.0244                       
REMARK   3      S21:   0.5391 S22:   0.1986 S23:   0.0758                       
REMARK   3      S31:   0.7940 S32:   0.5891 S33:   0.0067                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 484 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.7966  23.4043   0.0439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2060 T22:   0.0592                                     
REMARK   3      T33:   0.2418 T12:  -0.0441                                     
REMARK   3      T13:   0.0379 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1985 L22:   0.3370                                     
REMARK   3      L33:   0.9063 L12:  -0.7373                                     
REMARK   3      L13:  -0.3299 L23:   0.2979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0800 S12:  -0.0003 S13:   0.0933                       
REMARK   3      S21:   0.3377 S22:   0.0728 S23:  -0.0089                       
REMARK   3      S31:   0.3454 S32:   0.0044 S33:  -0.0046                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  22.2495  53.8146 -33.9609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7131 T22:   0.5576                                     
REMARK   3      T33:   0.3571 T12:  -0.2771                                     
REMARK   3      T13:  -0.1898 T23:   0.1178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3211 L22:   0.3955                                     
REMARK   3      L33:   0.3671 L12:   0.1802                                     
REMARK   3      L13:  -0.2732 L23:   0.0312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4894 S12:  -0.4164 S13:  -0.2513                       
REMARK   3      S21:   0.1083 S22:  -0.1515 S23:  -0.0789                       
REMARK   3      S31:   0.6990 S32:  -0.2852 S33:   0.5175                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 405 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6585  68.6068 -39.5932              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3097 T22:   0.1703                                     
REMARK   3      T33:   0.2371 T12:   0.0527                                     
REMARK   3      T13:  -0.0334 T23:  -0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0535 L22:   0.7755                                     
REMARK   3      L33:   2.0012 L12:   0.8413                                     
REMARK   3      L13:   1.1956 L23:   0.4814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2849 S12:   0.1164 S13:  -0.1222                       
REMARK   3      S21:   0.1935 S22:   0.0100 S23:  -0.1780                       
REMARK   3      S31:   0.2411 S32:   0.0021 S33:   0.0772                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 406 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  49.0402  78.1709 -15.5534              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6254 T22:   0.3504                                     
REMARK   3      T33:   0.3326 T12:  -0.0277                                     
REMARK   3      T13:  -0.0896 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8271 L22:   0.4150                                     
REMARK   3      L33:   1.2047 L12:  -0.4622                                     
REMARK   3      L13:   0.2712 L23:   0.1177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1006 S12:  -0.2124 S13:   0.0697                       
REMARK   3      S21:   0.5924 S22:   0.1890 S23:  -0.0901                       
REMARK   3      S31:   0.0676 S32:   0.1469 S33:   0.0002                       
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 5VEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227174.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-16                          
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               : 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   : 75286                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.90                              
REMARK 200  R MERGE                    (I) : 0.27900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.14100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
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   (%): 58.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M COBALT (II) CHLORIDE              
REMARK 280  HEXAHYDRATE, O.1 M MES MONOHYDRATE PH 6.5, AMMONIUM SULFATE 1.8-    
REMARK 280  1.9M, VAPOR DIFFUSION, HANGING DROP, 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       49.69100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       85.66200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       85.66200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.84550            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       85.66200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       85.66200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.53650            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       85.66200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.66200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.84550            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       85.66200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.66200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.53650            
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       49.69100            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 A1095  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     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 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     SER A  -1    OG                                                  
REMARK 470     ASN A   0    CG   OD1  ND2                                       
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     VAL A   5    CG1  CG2                                            
REMARK 470     VAL A   7    CG1  CG2                                            
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     PRO A 215    CG   CD                                             
REMARK 470     ASN A 216    CG   OD1  ND2                                       
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
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     ASN A 462    CG   OD1  ND2                                       
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     VAL A 525    CG1  CG2                                            
REMARK 470     SER B  -1    OG                                                  
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     GLN B  10    CG   CD   OE1  NE2                                  
REMARK 470     THR B 144    OG1  CG2                                            
REMARK 470     ASP B 145    CG   OD1  OD2                                       
REMARK 470     GLN B 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     PRO B 215    CG   CD                                             
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 325    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
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     ASP B 463    CG   OD1  OD2                                       
REMARK 470     ASP B 524    CG   OD1  OD2                                       
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE B  154   CA   CB   CG1  CG2  CD1                             
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    ALA B   207     O    HOH B   701              1.84            
REMARK 500   OD1  ASN B   179     O    HOH B   702              2.01            
REMARK 500   N    LEU B   211     O    HOH B   701              2.04            
REMARK 500   O    HOH B   833     O    HOH B   844              2.08            
REMARK 500   O    HOH A  1049     O    HOH A  1108              2.08            
REMARK 500   O    HOH B   845     O    HOH B   911              2.12            
REMARK 500   O    HOH A  1000     O    HOH A  1033              2.13            
REMARK 500   O    HOH B   860     O    HOH B   913              2.14            
REMARK 500   O    SER B   547     O    HOH B   703              2.15            
REMARK 500   OE1  GLN A   324     O    HOH A   701              2.16            
REMARK 500   OE1  GLU B   156     O    HOH B   704              2.16            
REMARK 500   O    LYS B   349     O    HOH B   705              2.17            
REMARK 500   O    HOH A   947     O    HOH A   985              2.17            
REMARK 500   NZ   LYS B   389     O3   GOL B   605              2.18            
REMARK 500   O    HOH A   879     O    HOH A  1027              2.19            
REMARK 500   OH   TYR A   420     O    HOH A   702              2.19            
REMARK 500   O    HOH A   961     O    HOH A  1099              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLU B   354     O    HOH B   702     3555     2.13            
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    LEU B 114   CA  -  CB  -  CG  ANGL. DEV. = -17.1 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       -7.41     84.78                                   
REMARK 500    ASN A  91       17.13     57.67                                   
REMARK 500    SER A 117     -120.08     47.96                                   
REMARK 500    CYS A 238      -67.92    -92.03                                   
REMARK 500    ASN A 462     -152.89   -105.59                                   
REMARK 500    ASP A 463      -61.78     70.08                                   
REMARK 500    VAL A 480      -68.70   -109.17                                   
REMARK 500    TYR B  66      -13.66     76.76                                   
REMARK 500    SER B 117     -116.70     60.44                                   
REMARK 500    ILE B 133     -166.18   -104.87                                   
REMARK 500    PRO B 140     -177.28    -69.94                                   
REMARK 500    ASN B 216       34.79    -86.53                                   
REMARK 500    ASN B 216       31.38    -84.01                                   
REMARK 500    CYS B 238      -70.54    -88.54                                   
REMARK 500    ALA B 269       32.11    -94.30                                   
REMARK 500    SER B 378       46.96    -80.97                                   
REMARK 500    GLU B 432       58.51     39.68                                   
REMARK 500    ASN B 462     -147.77   -120.28                                   
REMARK 500    ASP B 463      -50.92     82.21                                   
REMARK 500    THR B 507      147.97     64.70                                   
REMARK 500    SER B 509     -132.58    -70.10                                   
REMARK 500    ALA B 510       82.52     53.51                                   
REMARK 500    LYS B 523      -40.58   -136.51                                   
REMARK 500    GLU B 551       -7.33    -59.91                                   
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 A1113        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A1114        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A1115        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A1116        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A1117        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A1118        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH A1119        DISTANCE =  8.16 ANGSTROMS                       
REMARK 525    HOH B 915        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH B 916        DISTANCE =  7.07 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 605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 117   OG                                                     
REMARK 620 2 ASP A 288   OD2  85.4                                              
REMARK 620 3 ASP A 290   OD1  90.1  83.3                                        
REMARK 620 4 ASP A 292   OD1 167.3  89.4 100.8                                  
REMARK 620 5 HOH A 726   O    92.5 174.8  92.0  93.6                            
REMARK 620 6 HOH A 766   O    76.3  94.8 166.4  92.6  89.3                      
REMARK 620 N                    1     2     3     4     5                       
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 SER B 117   OG                                                     
REMARK 620 2 ASP B 288   OD1  97.6                                              
REMARK 620 3 ASP B 290   OD1  99.7  83.0                                        
REMARK 620 4 ASP B 292   OD1 171.3  90.3  84.9                                  
REMARK 620 5 HOH B 720   O    85.5 170.6  87.8  87.3                            
REMARK 620 6 HOH B 742   O    77.5  97.0 177.2  97.9  92.3                      
REMARK 620 N                    1     2     3     4     5                       
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 SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 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 SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE VERSION OF THE ENZYME                                      
DBREF  5VEC A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5VEC B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5VEC MET A  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS A  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS A  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS A  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS A  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS A  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS A  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC SER A  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC SER A  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLY A  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC VAL A  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC ASP A  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC LEU A  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLY A   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC THR A   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLU A   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC ASN A   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC LEU A   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC TYR A   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC PHE A   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLN A   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC LEU A  515  UNP  P36871    ARG   515 ENGINEERED MUTATION            
SEQADV 5VEC MET B  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS B  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS B  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS B  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS B  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS B  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC HIS B  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC SER B  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC SER B  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLY B  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC VAL B  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC ASP B  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC LEU B  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLY B   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC THR B   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLU B   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC ASN B   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC LEU B   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC TYR B   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC PHE B   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC GLN B   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VEC LEU 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 SER 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 LEU 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 SER 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 LEU 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          
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET     MG  A 605       1                                                       
HET    GOL  A 606       6                                                       
HET    GOL  A 607       6                                                       
HET    GOL  A 608       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                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   8  GOL    6(C3 H8 O3)                                                  
FORMUL  17  HOH   *635(H2 O)                                                    
HELIX    1 AA1 VAL A   26  SER A   32  1                                   7    
HELIX    2 AA2 ASN A   34  SER A   45  1                                  12    
HELIX    3 AA3 THR A   46  VAL A   47  5                                   2    
HELIX    4 AA4 GLU A   48  ARG A   52  5                                   5    
HELIX    5 AA5 TYR A   66  ASN A   81  1                                  16    
HELIX    6 AA6 SER A   95  LYS A  107  1                                  13    
HELIX    7 AA7 PRO A  140  ILE A  154  1                                  15    
HELIX    8 AA8 VAL A  192  PHE A  203  1                                  12    
HELIX    9 AA9 ASP A  204  SER A  213  1                                  10    
HELIX   10 AB1 VAL A  228  LEU A  237  1                                  10    
HELIX   11 AB2 PRO A  244  ASN A  246  5                                   3    
HELIX   12 AB3 ASP A  256  HIS A  260  5                                   5    
HELIX   13 AB4 ALA A  269  SER A  278  1                                  10    
HELIX   14 AB5 ASN A  305  ASN A  316  1                                  12    
HELIX   15 AB6 ILE A  317  SER A  319  5                                   3    
HELIX   16 AB7 ILE A  320  GLY A  327  1                                   8    
HELIX   17 AB8 GLY A  339  LYS A  349  1                                  11    
HELIX   18 AB9 GLY A  358  ALA A  368  1                                  11    
HELIX   19 AC1 ASP A  390  LYS A  406  1                                  17    
HELIX   20 AC2 SER A  408  GLY A  421  1                                  14    
HELIX   21 AC3 GLU A  434  ASP A  451  1                                  18    
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  VAL B   47  1                                  14    
HELIX   26 AC8 GLU B   48  ARG B   52  5                                   5    
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  LYS B  152  1                                  13    
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  228  LEU B  237  1                                  10    
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  SER B  278  1                                  10    
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  524  ASN B  529  1                                   6    
HELIX   45 AE9 ASP B  531  GLN B  548  1                                  18    
HELIX   46 AF1 LEU B  549  GLY B  554  1                                   6    
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  VAL A 186   N  GLN A 173           
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  ILE A 112   N  VAL A  58           
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 382   N  CYS A 374           
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  LEU 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 8 MET B   1  VAL B   2  0                                        
SHEET    2 AA7 8 GLY B 171  LEU B 177  1  O  ASP B 176   N  VAL B   2           
SHEET    3 AA7 8 PHE B 184  VAL B 189 -1  O  ILE B 188   N  GLY B 171           
SHEET    4 AA7 8 ARG B  85  ILE B  93  1  N  LEU B  86   O  GLU B 187           
SHEET    5 AA7 8 THR B  56  GLY B  61  1  N  VAL B  59   O  VAL B  87           
SHEET    6 AA7 8 GLY B 110  LEU B 114  1  O  ILE B 112   N  VAL B  58           
SHEET    7 AA7 8 ASP B 126  ILE B 133 -1  O  LYS B 130   N  ILE B 113           
SHEET    8 AA7 8 LEU B  22  ARG B  25 -1  N  LEU B  22   O  ILE B 129           
SHEET    1 AA8 2 VAL B   5  LYS B   8  0                                        
SHEET    2 AA8 2 GLU B 156  VAL B 159 -1  O  TYR B 157   N  VAL B   7           
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 382   N  CYS B 374           
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  SER B 505 -1  O  ILE B 500   N  LEU B 492           
SHEET    5 AB2 7 ALA B 512  GLU B 522 -1  O  LEU B 515   N  ARG B 503           
SHEET    6 AB2 7 ARG B 422  VAL B 433 -1  N  PHE B 424   O  SER B 520           
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         OG  SER A 117                MG    MG A 605     1555   1555  2.08  
LINK         OD2 ASP A 288                MG    MG A 605     1555   1555  2.11  
LINK         OD1 ASP A 290                MG    MG A 605     1555   1555  2.20  
LINK         OD1 ASP A 292                MG    MG A 605     1555   1555  1.97  
LINK         OG  SER B 117                MG    MG B 603     1555   1555  2.18  
LINK         OD1 ASP B 288                MG    MG B 603     1555   1555  1.99  
LINK         OD1 ASP B 290                MG    MG B 603     1555   1555  2.40  
LINK         OD1 ASP B 292                MG    MG B 603     1555   1555  2.11  
LINK        MG    MG A 605                 O   HOH A 726     1555   1555  2.22  
LINK        MG    MG A 605                 O   HOH A 766     1555   1555  2.10  
LINK        MG    MG B 603                 O   HOH B 720     1555   1555  2.07  
LINK        MG    MG B 603                 O   HOH B 742     1555   1555  1.93  
CISPEP   1 ALA A  461    ASN A  462          0         4.96                     
CISPEP   2 ALA B  461    ASN B  462          0         0.05                     
CISPEP   3 THR B  507    GLY B  508          0         7.98                     
SITE     1 AC1  3 ARG A 503  SER A 505  GLY A 506                               
SITE     1 AC2  4 ASN A 179  LYS A 470  ARG A 491  HOH A 862                    
SITE     1 AC3  5 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     2 AC3  5 HOH A 724                                                     
SITE     1 AC4  2 ARG A  23  HOH A 704                                          
SITE     1 AC5  6 SER A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     2 AC5  6 HOH A 726  HOH A 766                                          
SITE     1 AC6  3 PRO A 244  ALA A 245  HOH A 714                               
SITE     1 AC7  8 PHE A  65  TYR A  66  MET A  67  LYS A  68                    
SITE     2 AC7  8 GLU A  69  GLU A 255  HOH A 723  HOH A 819                    
SITE     1 AC8  5 GLU A 432  VAL A 433  GLU A 434  THR A 553                    
SITE     2 AC8  5 ARG A 555                                                     
SITE     1 AC9  3 ARG B 503  SER B 505  GLY B 506                               
SITE     1 AD1  3 ARG B 293  ARG B 427  HOH B 809                               
SITE     1 AD2  6 SER B 117  ASP B 288  ASP B 290  ASP B 292                    
SITE     2 AD2  6 HOH B 720  HOH B 742                                          
SITE     1 AD3  6 THR B  19  SER B  20  GLY B 358  TRP B 359                    
SITE     2 AD3  6 GLU B 376  GOL B 605                                          
SITE     1 AD4  8 THR B  19  LYS B 130  PRO B 138  ASP B 292                    
SITE     2 AD4  8 TRP B 359  LYS B 389  GOL B 604  HOH B 870                    
SITE     1 AD5  4 GLN B  41  SER B  45  ARG B  52  ASN B  81                    
CRYST1  171.324  171.324   99.382  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      0.005837  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005837  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010062        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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