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Database: PDB
Entry: 5F9C
LinkDB: 5F9C
Original site: 5F9C 
HEADER    ISOMERASE                               09-DEC-15   5F9C              
TITLE     CRYSTAL STRUCTURE OF THE G121R MUTANT OF HUMAN PHOSPHOGLUCOMUTASE 1   
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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    ISOMERASE METABOLISM, ISOMERASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BEAMER                                                            
REVDAT   2   22-NOV-17 5F9C    1       JRNL   REMARK                            
REVDAT   1   27-APR-16 5F9C    0                                                
JRNL        AUTH   K.M.STIERS,B.N.KAIN,A.C.GRAHAM,L.J.BEAMER                    
JRNL        TITL   INDUCED STRUCTURAL DISORDER AS A MOLECULAR MECHANISM FOR     
JRNL        TITL 2 ENZYME DYSFUNCTION IN PHOSPHOGLUCOMUTASE 1 DEFICIENCY.       
JRNL        REF    J.MOL.BIOL.                   V. 428  1493 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   26972339                                                     
JRNL        DOI    10.1016/J.JMB.2016.02.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 71761                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4983                            
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 60.9609 -  7.7630    1.00     3120   172  0.1468 0.1716        
REMARK   3     2  7.7630 -  6.1636    1.00     3135   168  0.1788 0.2046        
REMARK   3     3  6.1636 -  5.3850    1.00     3149   141  0.1833 0.2597        
REMARK   3     4  5.3850 -  4.8929    1.00     3143   173  0.1563 0.1986        
REMARK   3     5  4.8929 -  4.5423    1.00     3103   193  0.1390 0.2262        
REMARK   3     6  4.5423 -  4.2746    1.00     3130   185  0.1354 0.1878        
REMARK   3     7  4.2746 -  4.0605    1.00     3168   122  0.1467 0.1883        
REMARK   3     8  4.0605 -  3.8838    1.00     3160   145  0.1550 0.2023        
REMARK   3     9  3.8838 -  3.7343    1.00     3092   209  0.1569 0.2017        
REMARK   3    10  3.7343 -  3.6055    1.00     3134   155  0.1752 0.2246        
REMARK   3    11  3.6055 -  3.4928    1.00     3136   166  0.1786 0.2308        
REMARK   3    12  3.4928 -  3.3929    1.00     3140   177  0.1872 0.2303        
REMARK   3    13  3.3929 -  3.3036    1.00     3142   148  0.2177 0.2742        
REMARK   3    14  3.3036 -  3.2230    1.00     3112   184  0.2021 0.2356        
REMARK   3    15  3.2230 -  3.1498    1.00     3160   157  0.2223 0.3176        
REMARK   3    16  3.1498 -  3.0827    1.00     3146   148  0.2347 0.3306        
REMARK   3    17  3.0827 -  3.0211    1.00     3108   165  0.2431 0.3069        
REMARK   3    18  3.0211 -  2.9641    1.00     3120   182  0.2412 0.3124        
REMARK   3    19  2.9641 -  2.9111    1.00     3148   175  0.2616 0.2690        
REMARK   3    20  2.9111 -  2.8618    1.00     3116   154  0.2696 0.3442        
REMARK   3    21  2.8618 -  2.8156    1.00     3140   172  0.2705 0.3626        
REMARK   3    22  2.8156 -  2.7723    1.00     3115   139  0.2735 0.3311        
REMARK   3    23  2.7723 -  2.7315    1.00     3170   154  0.2877 0.3708        
REMARK   3    24  2.7315 -  2.6930    1.00     3081   195  0.2965 0.3412        
REMARK   3    25  2.6930 -  2.6567    1.00     3128   173  0.3095 0.3598        
REMARK   3    26  2.6567 -  2.6221    1.00     3095   196  0.3161 0.3615        
REMARK   3    27  2.6221 -  2.5894    1.00     3118   181  0.3225 0.3161        
REMARK   3    28  2.5894 -  2.5582    0.99     3073   162  0.3245 0.3918        
REMARK   3    29  2.5582 -  2.5284    0.99     3134   151  0.3181 0.3445        
REMARK   3    30  2.5284 -  2.5000    0.99     3127   141  0.3367 0.3283        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.008           8249                                  
REMARK   3   ANGLE     :  1.125          11205                                  
REMARK   3   CHIRALITY :  0.046           1294                                  
REMARK   3   PLANARITY :  0.006           1451                                  
REMARK   3   DIHEDRAL  : 13.288           2879                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 202 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9727 -70.9577   1.5094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8044 T22:   0.5431                                     
REMARK   3      T33:   0.3743 T12:   0.0716                                     
REMARK   3      T13:  -0.1182 T23:  -0.0984                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3022 L22:   4.2803                                     
REMARK   3      L33:   4.0445 L12:  -1.5523                                     
REMARK   3      L13:   0.0261 L23:   1.0328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1581 S12:  -0.2597 S13:  -0.1301                       
REMARK   3      S21:   0.7818 S22:   0.5066 S23:  -0.4487                       
REMARK   3      S31:   1.3199 S32:   0.4994 S33:  -0.2830                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0374 -42.7519  -5.0522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5876 T22:   0.5634                                     
REMARK   3      T33:   0.5562 T12:  -0.1845                                     
REMARK   3      T13:   0.2147 T23:  -0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6391 L22:   4.3957                                     
REMARK   3      L33:   3.3417 L12:  -0.1106                                     
REMARK   3      L13:  -0.6766 L23:   2.3795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1351 S12:   0.2432 S13:   0.4305                       
REMARK   3      S21:  -0.6226 S22:   0.4060 S23:  -0.9328                       
REMARK   3      S31:  -0.8144 S32:   0.6208 S33:  -0.4324                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 294 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2943 -42.7634  15.5257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2439 T22:   0.4265                                     
REMARK   3      T33:   0.3141 T12:   0.0191                                     
REMARK   3      T13:  -0.0155 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1061 L22:   3.4728                                     
REMARK   3      L33:   4.6660 L12:   1.4201                                     
REMARK   3      L13:   1.3239 L23:   1.3969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1233 S12:  -0.5049 S13:   0.1179                       
REMARK   3      S21:   0.3481 S22:  -0.1709 S23:   0.1178                       
REMARK   3      S31:   0.0052 S32:  -0.6013 S33:   0.0480                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 202 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0407 -62.0075 -11.0556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9480 T22:   1.3452                                     
REMARK   3      T33:   0.4262 T12:  -0.3450                                     
REMARK   3      T13:  -0.1433 T23:   0.0850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0478 L22:   2.9586                                     
REMARK   3      L33:   5.8199 L12:   1.1484                                     
REMARK   3      L13:  -1.0815 L23:  -0.1608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5455 S12:   1.0959 S13:  -0.0805                       
REMARK   3      S21:  -0.7519 S22:   0.6670 S23:   0.3889                       
REMARK   3      S31:   1.3333 S32:  -1.7040 S33:  -0.0818                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 203 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.7833 -34.8097  -4.4960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6832 T22:   0.8611                                     
REMARK   3      T33:   0.6989 T12:   0.2543                                     
REMARK   3      T13:   0.0954 T23:   0.2024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9646 L22:   5.2125                                     
REMARK   3      L33:   4.6044 L12:   1.6936                                     
REMARK   3      L13:  -2.0148 L23:  -2.1433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0519 S12:   0.2676 S13:   0.8419                       
REMARK   3      S21:   0.0157 S22:   0.6642 S23:   1.1825                       
REMARK   3      S31:  -1.0411 S32:  -1.1041 S33:  -0.5990                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 294 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8572 -39.0853 -25.6625              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5981 T22:   1.2141                                     
REMARK   3      T33:   0.4043 T12:  -0.1207                                     
REMARK   3      T13:  -0.0741 T23:   0.1162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0830 L22:   2.4398                                     
REMARK   3      L33:   6.4307 L12:  -0.4708                                     
REMARK   3      L13:  -1.1092 L23:  -0.4107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0139 S12:   1.3113 S13:   0.2966                       
REMARK   3      S21:  -0.6885 S22:   0.2705 S23:  -0.0311                       
REMARK   3      S31:  -0.2691 S32:  -0.2661 S33:  -0.1494                       
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 5F9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216183.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.5                               
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) : 1.00001                            
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          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71761                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.943                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.10                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 3.10100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 5EPC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE WITH 0.15         
REMARK 280  LITHIUM SULFATE AND 0.1 CAPS BUFFER, PH 10.5, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
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       49.95000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       85.99000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       85.99000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.97500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       85.99000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       85.99000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.92500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       85.99000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.99000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.97500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       85.99000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.99000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.92500            
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       49.95000            
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 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     GLY A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     GLY A   506                                                      
REMARK 465     THR A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     ALA A   510                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     SER B   117                                                      
REMARK 465     HIS B   118                                                      
REMARK 465     GLY B   122                                                      
REMARK 465     PRO B   123                                                      
REMARK 465     ASN B   124                                                      
REMARK 465     GLU B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     PHE B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     GLY B   259                                                      
REMARK 465     HIS B   260                                                      
REMARK 465     HIS B   261                                                      
REMARK 465     PRO B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     PRO B   264                                                      
REMARK 465     ASN B   265                                                      
REMARK 465     LEU B   266                                                      
REMARK 465     THR B   267                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     THR B   507                                                      
REMARK 465     GLY B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 465     ALA B   510                                                      
REMARK 465     GLY B   511                                                      
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     MET A   1    CG   SD   CE                                        
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     ARG A  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     ASN A 124    CG   OD1  ND2                                       
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     ASN A 179    CG   OD1  ND2                                       
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     PHE A 257    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 280    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 440    CG   CD   CE   NZ                                   
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 453    OG                                                  
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     ASN A 462    CG   OD1  ND2                                       
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     ARG A 486    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 487    CG   OD1  ND2                                       
REMARK 470     LYS A 545    CG   CD   CE   NZ                                   
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     THR B   9    OG1  CG2                                            
REMARK 470     GLN B  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  26    CG1  CG2                                            
REMARK 470     LYS B  27    CG   CD   CE   NZ                                   
REMARK 470     VAL B  28    CG1  CG2                                            
REMARK 470     ASN B  34    CG   OD1  ND2                                       
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  51    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  65    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B  69    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 121    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 126    CG   OD1  OD2                                       
REMARK 470     GLU B 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     ILE B 147    CG1  CG2  CD1                                       
REMARK 470     PHE B 148    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 152    CG   CD   CE   NZ                                   
REMARK 470     ILE B 154    CG1  CG2  CD1                                       
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     LYS B 209    CG   CD   CE   NZ                                   
REMARK 470     PRO B 215    CG   CD                                             
REMARK 470     ASN B 216    CG   OD1  ND2                                       
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     TYR B 268    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 277    CG   CD   CE   NZ                                   
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 418    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 432    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 433    CG1  CG2                                            
REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 440    CG   CD   CE   NZ                                   
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     ASP B 463    CG   OD1  OD2                                       
REMARK 470     LYS B 464    CG   CD   CE   NZ                                   
REMARK 470     VAL B 465    CG1  CG2                                            
REMARK 470     ASN B 487    CG   OD1  ND2                                       
REMARK 470     LEU B 490    CG   CD1  CD2                                       
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     GLN B 530    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 470     ARG B 552    CG   CD   NE   CZ   NH1  NH2                        
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   746     O    HOH A   753              1.90            
REMARK 500   N    ALA A   351     O    HOH A   701              2.03            
REMARK 500   O    HOH A   749     O    HOH A   754              2.04            
REMARK 500   OD1  ASN A    34     OH   TYR A   157              2.08            
REMARK 500   NH1  ARG B   329     OD2  ASP B   384              2.10            
REMARK 500   O1   SO4 A   603     O    HOH A   702              2.12            
REMARK 500   OD1  ASN A   265     O    HOH A   703              2.14            
REMARK 500   NH1  ARG A   329     OD2  ASP A   384              2.17            
REMARK 500   OE1  GLU A   240     O    HOH A   704              2.18            
REMARK 500   O    HOH A   730     O    HOH A   750              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    PRO A 215   C   -  N   -  CA  ANGL. DEV. =  10.1 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    VAL A   2      102.50    -45.98                                   
REMARK 500    GLN A  15       58.24    -99.30                                   
REMARK 500    TYR A  66      -10.65     79.64                                   
REMARK 500    SER A 117     -117.13     57.23                                   
REMARK 500    ILE A 133     -166.26   -106.03                                   
REMARK 500    PHE A 181      -50.35   -122.67                                   
REMARK 500    PRO A 215      -94.01    -26.09                                   
REMARK 500    ASN A 216       52.76    -90.45                                   
REMARK 500    CYS A 238      -65.94    -91.39                                   
REMARK 500    ASP A 256       98.88   -162.42                                   
REMARK 500    ALA A 269       40.95    -95.63                                   
REMARK 500    SER A 378       45.87    -85.35                                   
REMARK 500    SER A 453       36.86    -96.79                                   
REMARK 500    ASN A 462     -147.72    -92.53                                   
REMARK 500    ASP A 463      -72.03     62.10                                   
REMARK 500    VAL A 480      -70.59   -100.11                                   
REMARK 500    GLN B  15       53.27   -100.16                                   
REMARK 500    PRO B  17      -79.98    -45.73                                   
REMARK 500    PHE B  29      -84.35    -68.02                                   
REMARK 500    TYR B  66      -11.35     81.42                                   
REMARK 500    ILE B 133     -166.76   -104.89                                   
REMARK 500    ASN B 216       42.98    -91.91                                   
REMARK 500    ILE B 236      -60.19    -98.42                                   
REMARK 500    CYS B 238      -66.04    -93.10                                   
REMARK 500    ASN B 246        1.36    -69.59                                   
REMARK 500    ALA B 269       56.27    -98.28                                   
REMARK 500    SER B 378       46.74    -84.44                                   
REMARK 500    ALA B 461      114.57   -166.21                                   
REMARK 500    ASN B 462     -135.39     51.55                                   
REMARK 500    LYS B 464      133.82   -173.45                                   
REMARK 500    VAL B 480      -69.63    -98.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 117   OG                                                     
REMARK 620 2 ASP A 288   OD2 109.9                                              
REMARK 620 3 ASP A 290   OD1 106.8  88.6                                        
REMARK 620 4 ASP A 292   OD1 151.7  92.4  90.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 288   OD2                                                    
REMARK 620 2 ASP B 292   OD1  62.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 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 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 SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 607                  
DBREF  5F9C A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5F9C B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5F9C ARG A  121  UNP  P36871    GLY   121 ENGINEERED MUTATION            
SEQADV 5F9C ARG B  121  UNP  P36871    GLY   121 ENGINEERED MUTATION            
SEQRES   1 A  562  MET VAL LYS ILE VAL THR VAL LYS THR GLN ALA TYR GLN          
SEQRES   2 A  562  ASP GLN LYS PRO GLY THR SER GLY LEU ARG LYS ARG VAL          
SEQRES   3 A  562  LYS VAL PHE GLN SER SER ALA ASN TYR ALA GLU ASN PHE          
SEQRES   4 A  562  ILE GLN SER ILE ILE SER THR VAL GLU PRO ALA GLN ARG          
SEQRES   5 A  562  GLN GLU ALA THR LEU VAL VAL GLY GLY ASP GLY ARG PHE          
SEQRES   6 A  562  TYR MET LYS GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA          
SEQRES   7 A  562  ALA ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN          
SEQRES   8 A  562  GLY ILE LEU SER THR PRO ALA VAL SER CYS ILE ILE ARG          
SEQRES   9 A  562  LYS ILE LYS ALA ILE GLY GLY ILE ILE LEU THR ALA SER          
SEQRES  10 A  562  HIS ASN PRO ARG GLY PRO ASN GLY ASP PHE GLY ILE LYS          
SEQRES  11 A  562  PHE ASN ILE SER ASN GLY GLY PRO ALA PRO GLU ALA ILE          
SEQRES  12 A  562  THR ASP LYS ILE PHE GLN ILE SER LYS THR ILE GLU GLU          
SEQRES  13 A  562  TYR ALA VAL CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL          
SEQRES  14 A  562  LEU GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS          
SEQRES  15 A  562  PRO PHE THR VAL GLU ILE VAL ASP SER VAL GLU ALA TYR          
SEQRES  16 A  562  ALA THR MET LEU ARG SER ILE PHE ASP PHE SER ALA LEU          
SEQRES  17 A  562  LYS GLU LEU LEU SER GLY PRO ASN ARG LEU LYS ILE ARG          
SEQRES  18 A  562  ILE ASP ALA MET HIS GLY VAL VAL GLY PRO TYR VAL LYS          
SEQRES  19 A  562  LYS ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA ASN SER          
SEQRES  20 A  562  ALA VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS          
SEQRES  21 A  562  HIS PRO ASP PRO ASN LEU THR TYR ALA ALA ASP LEU VAL          
SEQRES  22 A  562  GLU THR MET LYS SER GLY GLU HIS ASP PHE GLY ALA ALA          
SEQRES  23 A  562  PHE ASP GLY ASP GLY ASP ARG ASN MET ILE LEU GLY LYS          
SEQRES  24 A  562  HIS GLY PHE PHE VAL ASN PRO SER ASP SER VAL ALA VAL          
SEQRES  25 A  562  ILE ALA ALA ASN ILE PHE SER ILE PRO TYR PHE GLN GLN          
SEQRES  26 A  562  THR GLY VAL ARG GLY PHE ALA ARG SER MET PRO THR SER          
SEQRES  27 A  562  GLY ALA LEU ASP ARG VAL ALA SER ALA THR LYS ILE ALA          
SEQRES  28 A  562  LEU TYR GLU THR PRO THR GLY TRP LYS PHE PHE GLY ASN          
SEQRES  29 A  562  LEU MET ASP ALA SER LYS LEU SER LEU CYS GLY GLU GLU          
SEQRES  30 A  562  SER PHE GLY THR GLY SER ASP HIS ILE ARG GLU LYS ASP          
SEQRES  31 A  562  GLY LEU TRP ALA VAL LEU ALA TRP LEU SER ILE LEU ALA          
SEQRES  32 A  562  THR ARG LYS GLN SER VAL GLU ASP ILE LEU LYS ASP HIS          
SEQRES  33 A  562  TRP GLN LYS TYR GLY ARG ASN PHE PHE THR ARG TYR ASP          
SEQRES  34 A  562  TYR GLU GLU VAL GLU ALA GLU GLY ALA ASN LYS MET MET          
SEQRES  35 A  562  LYS ASP LEU GLU ALA LEU MET PHE ASP ARG SER PHE VAL          
SEQRES  36 A  562  GLY LYS GLN PHE SER ALA ASN ASP LYS VAL TYR THR VAL          
SEQRES  37 A  562  GLU LYS ALA ASP ASN PHE GLU TYR SER ASP PRO VAL ASP          
SEQRES  38 A  562  GLY SER ILE SER ARG ASN GLN GLY LEU ARG LEU ILE PHE          
SEQRES  39 A  562  THR ASP GLY SER ARG ILE VAL PHE ARG LEU SER GLY THR          
SEQRES  40 A  562  GLY SER ALA GLY ALA THR ILE ARG LEU TYR ILE ASP SER          
SEQRES  41 A  562  TYR GLU LYS ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN          
SEQRES  42 A  562  VAL MET LEU ALA PRO LEU ILE SER ILE ALA LEU LYS VAL          
SEQRES  43 A  562  SER GLN LEU GLN GLU ARG THR GLY ARG THR ALA PRO THR          
SEQRES  44 A  562  VAL ILE THR                                                  
SEQRES   1 B  562  MET VAL LYS ILE VAL THR VAL LYS THR GLN ALA TYR GLN          
SEQRES   2 B  562  ASP GLN LYS PRO GLY THR SER GLY LEU ARG LYS ARG VAL          
SEQRES   3 B  562  LYS VAL PHE GLN SER SER ALA ASN TYR ALA GLU ASN PHE          
SEQRES   4 B  562  ILE GLN SER ILE ILE SER THR VAL GLU PRO ALA GLN ARG          
SEQRES   5 B  562  GLN GLU ALA THR LEU VAL VAL GLY GLY ASP GLY ARG PHE          
SEQRES   6 B  562  TYR MET LYS GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA          
SEQRES   7 B  562  ALA ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN          
SEQRES   8 B  562  GLY ILE LEU SER THR PRO ALA VAL SER CYS ILE ILE ARG          
SEQRES   9 B  562  LYS ILE LYS ALA ILE GLY GLY ILE ILE LEU THR ALA SER          
SEQRES  10 B  562  HIS ASN PRO ARG GLY PRO ASN GLY ASP PHE GLY ILE LYS          
SEQRES  11 B  562  PHE ASN ILE SER ASN GLY GLY PRO ALA PRO GLU ALA ILE          
SEQRES  12 B  562  THR ASP LYS ILE PHE GLN ILE SER LYS THR ILE GLU GLU          
SEQRES  13 B  562  TYR ALA VAL CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL          
SEQRES  14 B  562  LEU GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS          
SEQRES  15 B  562  PRO PHE THR VAL GLU ILE VAL ASP SER VAL GLU ALA TYR          
SEQRES  16 B  562  ALA THR MET LEU ARG SER ILE PHE ASP PHE SER ALA LEU          
SEQRES  17 B  562  LYS GLU LEU LEU SER GLY PRO ASN ARG LEU LYS ILE ARG          
SEQRES  18 B  562  ILE ASP ALA MET HIS GLY VAL VAL GLY PRO TYR VAL LYS          
SEQRES  19 B  562  LYS ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA ASN SER          
SEQRES  20 B  562  ALA VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS          
SEQRES  21 B  562  HIS PRO ASP PRO ASN LEU THR TYR ALA ALA ASP LEU VAL          
SEQRES  22 B  562  GLU THR MET LYS SER GLY GLU HIS ASP PHE GLY ALA ALA          
SEQRES  23 B  562  PHE ASP GLY ASP GLY ASP ARG ASN MET ILE LEU GLY LYS          
SEQRES  24 B  562  HIS GLY PHE PHE VAL ASN PRO SER ASP SER VAL ALA VAL          
SEQRES  25 B  562  ILE ALA ALA ASN ILE PHE SER ILE PRO TYR PHE GLN GLN          
SEQRES  26 B  562  THR GLY VAL ARG GLY PHE ALA ARG SER MET PRO THR SER          
SEQRES  27 B  562  GLY ALA LEU ASP ARG VAL ALA SER ALA THR LYS ILE ALA          
SEQRES  28 B  562  LEU TYR GLU THR PRO THR GLY TRP LYS PHE PHE GLY ASN          
SEQRES  29 B  562  LEU MET ASP ALA SER LYS LEU SER LEU CYS GLY GLU GLU          
SEQRES  30 B  562  SER PHE GLY THR GLY SER ASP HIS ILE ARG GLU LYS ASP          
SEQRES  31 B  562  GLY LEU TRP ALA VAL LEU ALA TRP LEU SER ILE LEU ALA          
SEQRES  32 B  562  THR ARG LYS GLN SER VAL GLU ASP ILE LEU LYS ASP HIS          
SEQRES  33 B  562  TRP GLN LYS TYR GLY ARG ASN PHE PHE THR ARG TYR ASP          
SEQRES  34 B  562  TYR GLU GLU VAL GLU ALA GLU GLY ALA ASN LYS MET MET          
SEQRES  35 B  562  LYS ASP LEU GLU ALA LEU MET PHE ASP ARG SER PHE VAL          
SEQRES  36 B  562  GLY LYS GLN PHE SER ALA ASN ASP LYS VAL TYR THR VAL          
SEQRES  37 B  562  GLU LYS ALA ASP ASN PHE GLU TYR SER ASP PRO VAL ASP          
SEQRES  38 B  562  GLY SER ILE SER ARG ASN GLN GLY LEU ARG LEU ILE PHE          
SEQRES  39 B  562  THR ASP GLY SER ARG ILE VAL PHE ARG LEU SER GLY THR          
SEQRES  40 B  562  GLY SER ALA GLY ALA THR ILE ARG LEU TYR ILE ASP SER          
SEQRES  41 B  562  TYR GLU LYS ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN          
SEQRES  42 B  562  VAL MET LEU ALA PRO LEU ILE SER ILE ALA LEU LYS VAL          
SEQRES  43 B  562  SER GLN LEU GLN GLU ARG THR GLY ARG THR ALA PRO THR          
SEQRES  44 B  562  VAL ILE THR                                                  
HET     MG  A 601       1                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    GOL  A 605       6                                                       
HET    GOL  A 606       6                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET    SO4  B 604       5                                                       
HET    SO4  B 605       5                                                       
HET    SO4  B 606       5                                                       
HET     MG  B 607       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  SO4    9(O4 S 2-)                                                   
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL  16  HOH   *80(H2 O)                                                     
HELIX    1 AA1 LYS A   27  SER A   32  1                                   6    
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  GLY A   82  1                                  17    
HELIX    6 AA6 SER A   95  ILE A  106  1                                  12    
HELIX    7 AA7 PRO A  140  THR A  153  1                                  14    
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  229  LEU A  237  1                                   9    
HELIX   11 AB2 PRO A  244  ASN A  246  5                                   3    
HELIX   12 AB3 ALA A  269  LYS A  277  1                                   9    
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  ALA A  347  1                                   9    
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  531  LEU A  536  1                                   6    
HELIX   22 AC4 LEU A  536  GLN A  548  1                                  13    
HELIX   23 AC5 GLN A  548  GLY A  554  1                                   7    
HELIX   24 AC6 VAL B   26  GLN B   30  1                                   5    
HELIX   25 AC7 ASN B   34  SER B   45  1                                  12    
HELIX   26 AC8 THR B   46  VAL B   47  5                                   2    
HELIX   27 AC9 GLU B   48  ARG B   52  5                                   5    
HELIX   28 AD1 TYR B   66  GLY B   82  1                                  17    
HELIX   29 AD2 SER B   95  ILE B  106  1                                  12    
HELIX   30 AD3 PRO B  140  LYS B  152  1                                  13    
HELIX   31 AD4 VAL B  192  PHE B  203  1                                  12    
HELIX   32 AD5 ASP B  204  LEU B  212  1                                   9    
HELIX   33 AD6 VAL B  229  LEU B  237  1                                   9    
HELIX   34 AD7 PRO B  244  ASN B  246  5                                   3    
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  ALA B  347  1                                   9    
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  LEU B  536  1                                   6    
HELIX   45 AE9 LEU B  536  GLN B  548  1                                  13    
HELIX   46 AF1 GLN B  548  GLY B  554  1                                   7    
SHEET    1 AA1 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA1 2 GLU A 156  VAL A 159 -1  O  TYR A 157   N  VAL A   7           
SHEET    1 AA2 7 LEU A  22  ARG A  25  0                                        
SHEET    2 AA2 7 ASP A 126  ASN A 132 -1  O  PHE A 127   N  LYS A  24           
SHEET    3 AA2 7 GLY A 110  LEU A 114 -1  N  ILE A 113   O  LYS A 130           
SHEET    4 AA2 7 THR A  56  GLY A  61  1  N  GLY A  60   O  LEU A 114           
SHEET    5 AA2 7 ARG A  85  ILE A  93  1  O  VAL A  87   N  VAL A  59           
SHEET    6 AA2 7 PHE A 184  VAL A 189  1  O  GLU A 187   N  LEU A  86           
SHEET    7 AA2 7 GLY A 171  PHE A 175 -1  N  GLN A 173   O  VAL A 186           
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  ARG A 333   O  THR A 355           
SHEET    3 AA4 4 LEU A 373  GLU A 376  1  O  GLY A 375   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  ARG A 515   N  ARG A 503           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  ARG A 422   O  GLU A 522           
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  THR B   6  0                                        
SHEET    2 AA7 2 ALA B 158  VAL B 159 -1  O  VAL B 159   N  VAL B   5           
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  ILE B 113   O  LYS B 130           
SHEET    4 AA8 7 THR B  56  GLY B  61  1  N  GLY B  60   O  LEU B 114           
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  ILE B  88           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  GLN B 173   O  VAL B 186           
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  GLY B 375   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  LEU B 504 -1  O  ILE B 500   N  LEU B 492           
SHEET    5 AB2 7 THR B 513  GLU B 522 -1  O  TYR B 517   N  VAL B 501           
SHEET    6 AB2 7 ARG B 422  GLU B 431 -1  N  ARG B 422   O  GLU B 522           
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 601     1555   1555  2.80  
LINK         OD2 ASP A 288                MG    MG A 601     1555   1555  1.90  
LINK         OD1 ASP A 290                MG    MG A 601     1555   1555  2.28  
LINK         OD1 ASP A 292                MG    MG A 601     1555   1555  1.95  
LINK         OD2 ASP B 288                MG    MG B 607     1555   1555  2.72  
LINK         OD1 ASP B 292                MG    MG B 607     1555   1555  2.94  
CISPEP   1 ALA A  461    ASN A  462          0         6.91                     
SITE     1 AC1  4 SER A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     1 AC2  3 ARG A 503  SER A 505  ARG A 515                               
SITE     1 AC3  2 TRP A 359  HOH A 702                                          
SITE     1 AC4  6 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     2 AC4  6 SER A 247  HOH A 724                                          
SITE     1 AC5  7 PHE A 303  ASN A 305  ARG A 422  PHE A 424                    
SITE     2 AC5  7 PHE A 425  PRO A 532  HOH A 718                               
SITE     1 AC6  7 TYR A 428  GLN A 533  LEU A 544  THR A 556                    
SITE     2 AC6  7 ALA A 557  PRO A 558  ILE A 561                               
SITE     1 AC7  3 ARG B 503  SER B 505  ARG B 515                               
SITE     1 AC8  2 ARG B  85  ILE B 106                                          
SITE     1 AC9  3 ASN B 316  PHE B 318  SER B 319                               
SITE     1 AD1  4 VAL B 165  ASP B 166  LEU B 167  GLY B 168                    
SITE     1 AD2  2 SER B 378  ARG B 427                                          
SITE     1 AD3  2 GLY B 358  TRP B 359                                          
SITE     1 AD4  4 ASP B 288  ASP B 290  ASP B 292  ARG B 293                    
CRYST1  171.980  171.980   99.900  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      0.005815  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005815  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010010        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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