GenomeNet

Database: PDB
Entry: 5VG7
LinkDB: 5VG7
Original site: 5VG7 
HEADER    ISOMERASE                               10-APR-17   5VG7              
TITLE     CRYSTAL STRUCTURE OF THE R503Q MISSENSE VARIANT OF HUMAN PGM1         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLUCOMUTASE-1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;                              
COMPND   5 EC: 5.4.2.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PHOSPHOGLUCOMUTASE-1;                                      
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;                              
COMPND  12 EC: 5.4.2.2;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 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;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PGM1;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 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 5VG7    1       REMARK                                   
REVDAT   3   17-OCT-18 5VG7    1       JRNL                                     
REVDAT   2   05-SEP-18 5VG7    1       JRNL                                     
REVDAT   1   20-JUN-18 5VG7    0                                                
JRNL        AUTH   K.M.STIERS,L.J.BEAMER                                        
JRNL        TITL   A HOTSPOT FOR DISEASE-ASSOCIATED VARIANTS OF HUMAN PGM1 IS   
JRNL        TITL 2 ASSOCIATED WITH IMPAIRED LIGAND BINDING AND LOOP DYNAMICS.   
JRNL        REF    STRUCTURE                     V.  26  1337 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   30122451                                                     
JRNL        DOI    10.1016/J.STR.2018.07.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.348                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 108895                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.037                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5485                            
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 60.8871 -  6.0572    1.00     3734   202  0.1746 0.1929        
REMARK   3     2  6.0572 -  4.8084    1.00     3577   180  0.1523 0.1835        
REMARK   3     3  4.8084 -  4.2007    1.00     3504   197  0.1255 0.1738        
REMARK   3     4  4.2007 -  3.8167    1.00     3506   173  0.1319 0.1856        
REMARK   3     5  3.8167 -  3.5432    1.00     3507   185  0.1341 0.1679        
REMARK   3     6  3.5432 -  3.3343    1.00     3451   192  0.1525 0.1973        
REMARK   3     7  3.3343 -  3.1673    1.00     3462   184  0.1608 0.2085        
REMARK   3     8  3.1673 -  3.0295    1.00     3462   169  0.1666 0.2167        
REMARK   3     9  3.0295 -  2.9128    1.00     3458   197  0.1792 0.2219        
REMARK   3    10  2.9128 -  2.8123    1.00     3451   177  0.1876 0.2322        
REMARK   3    11  2.8123 -  2.7244    1.00     3446   173  0.1808 0.2316        
REMARK   3    12  2.7244 -  2.6465    1.00     3412   209  0.1806 0.2469        
REMARK   3    13  2.6465 -  2.5768    1.00     3409   189  0.1819 0.2274        
REMARK   3    14  2.5768 -  2.5140    1.00     3458   174  0.1766 0.2218        
REMARK   3    15  2.5140 -  2.4568    1.00     3411   187  0.1687 0.2083        
REMARK   3    16  2.4568 -  2.4045    1.00     3423   197  0.1696 0.2288        
REMARK   3    17  2.4045 -  2.3564    1.00     3442   153  0.1803 0.2257        
REMARK   3    18  2.3564 -  2.3120    1.00     3392   178  0.1869 0.2417        
REMARK   3    19  2.3120 -  2.2707    1.00     3411   204  0.1842 0.2439        
REMARK   3    20  2.2707 -  2.2322    1.00     3416   177  0.1895 0.2506        
REMARK   3    21  2.2322 -  2.1962    1.00     3398   197  0.1905 0.2514        
REMARK   3    22  2.1962 -  2.1624    1.00     3414   173  0.1994 0.2372        
REMARK   3    23  2.1624 -  2.1306    1.00     3430   179  0.2126 0.2639        
REMARK   3    24  2.1306 -  2.1006    1.00     3410   177  0.2253 0.2535        
REMARK   3    25  2.1006 -  2.0722    1.00     3348   216  0.2307 0.2909        
REMARK   3    26  2.0722 -  2.0453    1.00     3414   175  0.2412 0.2726        
REMARK   3    27  2.0453 -  2.0197    1.00     3448   159  0.2406 0.2524        
REMARK   3    28  2.0197 -  1.9954    1.00     3393   175  0.2322 0.2770        
REMARK   3    29  1.9954 -  1.9722    1.00     3433   169  0.2556 0.2758        
REMARK   3    30  1.9722 -  1.9500    1.00     3390   168  0.2625 0.3191        
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)     : 0.197            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.717           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.99                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.82                          
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           8938                                  
REMARK   3   ANGLE     :  0.812          12142                                  
REMARK   3   CHIRALITY :  0.055           1356                                  
REMARK   3   PLANARITY :  0.005           1574                                  
REMARK   3   DIHEDRAL  :  4.487           8181                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 52 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8311 -74.0879   8.4842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5688 T22:   0.2272                                     
REMARK   3      T33:   0.2803 T12:   0.0827                                     
REMARK   3      T13:  -0.0086 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0545 L22:   2.2463                                     
REMARK   3      L33:   1.2282 L12:   0.1249                                     
REMARK   3      L13:   0.2217 L23:   0.2771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0087 S12:  -0.1318 S13:  -0.1166                       
REMARK   3      S21:   0.5092 S22:   0.1109 S23:  -0.1070                       
REMARK   3      S31:   0.5951 S32:   0.1274 S33:  -0.0630                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 183 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8534 -70.1492   0.3595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3544 T22:   0.1309                                     
REMARK   3      T33:   0.2032 T12:  -0.0150                                     
REMARK   3      T13:  -0.0127 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4597 L22:   2.1653                                     
REMARK   3      L33:   1.8117 L12:  -0.6593                                     
REMARK   3      L13:  -0.0548 L23:   0.7630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:  -0.0041 S13:  -0.2132                       
REMARK   3      S21:   0.2630 S22:   0.1338 S23:  -0.0455                       
REMARK   3      S31:   0.5314 S32:   0.1372 S33:  -0.0688                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 229 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1986 -48.5504 -10.7304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2544 T22:   0.1885                                     
REMARK   3      T33:   0.1769 T12:  -0.0644                                     
REMARK   3      T13:   0.0416 T23:   0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8801 L22:   1.6124                                     
REMARK   3      L33:   1.7334 L12:  -0.4901                                     
REMARK   3      L13:   0.3509 L23:   0.7204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:   0.1324 S13:   0.1081                       
REMARK   3      S21:  -0.4035 S22:   0.0185 S23:  -0.1425                       
REMARK   3      S31:  -0.2115 S32:  -0.0122 S33:   0.0030                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1710 -43.4422  -1.8085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2318 T22:   0.1751                                     
REMARK   3      T33:   0.2706 T12:  -0.0691                                     
REMARK   3      T13:   0.0348 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1363 L22:   0.7578                                     
REMARK   3      L33:   1.1369 L12:  -0.1796                                     
REMARK   3      L13:  -0.2036 L23:   0.3906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0455 S12:   0.0464 S13:   0.1031                       
REMARK   3      S21:  -0.1005 S22:   0.0660 S23:  -0.2321                       
REMARK   3      S31:  -0.1870 S32:   0.2239 S33:  -0.0279                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 294 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1367 -43.4680   6.4114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1100 T22:   0.1670                                     
REMARK   3      T33:   0.2120 T12:  -0.0063                                     
REMARK   3      T13:  -0.0249 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9677 L22:   1.1817                                     
REMARK   3      L33:   1.9233 L12:   0.3232                                     
REMARK   3      L13:   0.0677 L23:   0.3949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0528 S12:   0.0096 S13:   0.0809                       
REMARK   3      S21:  -0.1458 S22:   0.0136 S23:   0.1161                       
REMARK   3      S31:  -0.0293 S32:  -0.2858 S33:   0.0424                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 435 THROUGH 483 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9494 -45.7440  31.0236              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2105 T22:   0.4336                                     
REMARK   3      T33:   0.2305 T12:  -0.0715                                     
REMARK   3      T13:   0.0167 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1080 L22:   1.5233                                     
REMARK   3      L33:   2.3724 L12:   0.2389                                     
REMARK   3      L13:   0.5822 L23:   0.3595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0509 S12:  -0.6099 S13:   0.0582                       
REMARK   3      S21:   0.3266 S22:  -0.1448 S23:   0.0794                       
REMARK   3      S31:   0.2236 S32:  -0.5453 S33:   0.0789                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 484 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5402 -40.1241  25.2986              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1235 T22:   0.2117                                     
REMARK   3      T33:   0.2024 T12:   0.0162                                     
REMARK   3      T13:  -0.0217 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0152 L22:   0.8169                                     
REMARK   3      L33:   1.8951 L12:   1.1592                                     
REMARK   3      L13:   0.2497 L23:   0.4006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0411 S12:  -0.2550 S13:   0.0196                       
REMARK   3      S21:   0.0378 S22:  -0.0900 S23:   0.0004                       
REMARK   3      S31:  -0.0221 S32:  -0.2377 S33:   0.0521                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 80 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1452 -63.5563 -15.9028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5199 T22:   0.6684                                     
REMARK   3      T33:   0.3363 T12:  -0.2742                                     
REMARK   3      T13:  -0.1385 T23:   0.1668                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3038 L22:   1.4341                                     
REMARK   3      L33:   1.5955 L12:   0.2429                                     
REMARK   3      L13:   0.5615 L23:   0.8341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3668 S12:   0.3908 S13:   0.0924                       
REMARK   3      S21:  -0.7587 S22:   0.5886 S23:   0.4187                       
REMARK   3      S31:   0.3925 S32:  -0.6797 S33:  -0.1971                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 81 THROUGH 183 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9627 -62.0887 -10.9179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3175 T22:   0.4635                                     
REMARK   3      T33:   0.2006 T12:  -0.1244                                     
REMARK   3      T13:  -0.0732 T23:   0.0807                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0577 L22:   2.5291                                     
REMARK   3      L33:   2.1282 L12:   1.4515                                     
REMARK   3      L13:  -0.2381 L23:  -0.4965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3089 S12:   0.4988 S13:  -0.0066                       
REMARK   3      S21:  -0.5645 S22:   0.6073 S23:   0.2872                       
REMARK   3      S31:   0.3960 S32:  -0.6147 S33:  -0.1742                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 228 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1252 -42.7379   0.3727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3210 T22:   0.3243                                     
REMARK   3      T33:   0.2765 T12:   0.0719                                     
REMARK   3      T13:   0.0764 T23:  -0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9712 L22:   2.1345                                     
REMARK   3      L33:   1.9922 L12:   0.8331                                     
REMARK   3      L13:  -0.4809 L23:  -0.6556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1882 S12:  -0.0824 S13:   0.4887                       
REMARK   3      S21:   0.3791 S22:   0.0950 S23:   0.2336                       
REMARK   3      S31:  -0.4276 S32:  -0.0905 S33:  -0.2362                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 229 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9415 -38.8816 -13.9322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1701 T22:   0.3356                                     
REMARK   3      T33:   0.2532 T12:   0.0767                                     
REMARK   3      T13:  -0.0012 T23:   0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6964 L22:   2.5118                                     
REMARK   3      L33:   2.4406 L12:   0.1693                                     
REMARK   3      L13:  -0.8152 L23:  -0.6670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0852 S12:   0.4442 S13:   0.3163                       
REMARK   3      S21:   0.0367 S22:   0.1036 S23:   0.2544                       
REMARK   3      S31:  -0.2812 S32:  -0.3278 S33:  -0.0810                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 435 THROUGH 483 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3526 -43.4023 -40.9222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5800 T22:   0.8108                                     
REMARK   3      T33:   0.3496 T12:   0.1115                                     
REMARK   3      T13:   0.0737 T23:   0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9995 L22:   2.3295                                     
REMARK   3      L33:   2.4359 L12:  -0.6363                                     
REMARK   3      L13:   0.3000 L23:  -0.1361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4425 S12:   0.8146 S13:   0.2778                       
REMARK   3      S21:  -0.9431 S22:  -0.2867 S23:   0.0278                       
REMARK   3      S31:   0.1248 S32:   0.0401 S33:  -0.1598                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 484 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.9112 -35.2647 -35.1777              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5101 T22:   0.7356                                     
REMARK   3      T33:   0.3853 T12:   0.1294                                     
REMARK   3      T13:  -0.0160 T23:   0.1302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7761 L22:   2.1828                                     
REMARK   3      L33:   1.9016 L12:  -0.8640                                     
REMARK   3      L13:   0.2382 L23:   0.0993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2144 S12:   0.7003 S13:   0.3030                       
REMARK   3      S21:  -0.7448 S22:  -0.2498 S23:   0.2076                       
REMARK   3      S31:  -0.4078 S32:  -0.3489 S33:   0.0265                       
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 5VG7 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_1000227314.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00003                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108994                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.30                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.90200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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   (%): 58.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS/HCL PH:7.5, 1.8 M AMMONIUM    
REMARK 280  SULFATE, 16MG/ML, PH 7.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.90250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       86.06550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       86.06550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.95125            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       86.06550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       86.06550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.85375            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       86.06550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.06550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.95125            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       86.06550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.06550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.85375            
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       49.90250            
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 A1290  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 908  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     SER B    -1                                                      
REMARK 465     GLY B   214                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 460    OG                                                  
REMARK 470     LYS A 523    CG   CD   CE   NZ                                   
REMARK 470     ASN B   0    CG   OD1  ND2                                       
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     VAL B   5    CG1  CG2                                            
REMARK 470     GLN B  10    CG   CD   OE1  NE2                                  
REMARK 470     SER B  20    OG                                                  
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     GLU B 178    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     PRO B 215    CG   CD                                             
REMARK 470     ASN B 216    CG   OD1  ND2                                       
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     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     ASP B 524    CG   OD1  OD2                                       
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU B   436     NZ   LYS B   440              1.91            
REMARK 500   NH1  ARG B   486     O    HOH B   701              1.97            
REMARK 500   O    THR B   115     O    HOH B   702              2.01            
REMARK 500   ND2  ASN B   179     O    HOH B   703              2.04            
REMARK 500   O    HOH A  1051     O    HOH A  1189              2.08            
REMARK 500   O    HOH A   794     O    HOH A  1072              2.08            
REMARK 500   OD2  ASP B   166     O    HOH B   704              2.09            
REMARK 500   O    HOH B   974     O    HOH B  1021              2.15            
REMARK 500   O    HOH A  1065     O    HOH A  1076              2.15            
REMARK 500   O    HOH A   960     O    HOH A  1194              2.16            
REMARK 500   NE2  GLN A   533     O    HOH A   702              2.16            
REMARK 500   O    GLU A   156     O    HOH A   703              2.18            
REMARK 500   O    HOH B   932     O    HOH B   955              2.18            
REMARK 500   O    HOH B   899     O    HOH B   931              2.18            
REMARK 500   CE   MET B     1     O    LEU B   177              2.19            
REMARK 500   O2   SO4 A   609     O    HOH A   704              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    HOH A  1176     O    HOH A  1251     8555     2.13            
REMARK 500   O    HOH A  1080     O    HOH A  1209     3445     2.17            
REMARK 500   O    HOH A   789     O    HOH A  1279     3445     2.19            
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    ASN A  34       19.05     59.12                                   
REMARK 500    TYR A  66       -7.48     87.80                                   
REMARK 500    SEP A 117     -116.00     52.92                                   
REMARK 500    SEP A 117     -115.02     55.65                                   
REMARK 500    ILE A 133     -165.48   -108.75                                   
REMARK 500    CYS A 238      -60.34    -91.50                                   
REMARK 500    SER A 378       49.22    -81.91                                   
REMARK 500    ASN A 462     -159.63    -91.63                                   
REMARK 500    ASP A 463      -31.00     88.76                                   
REMARK 500    MET B   1       94.65     77.12                                   
REMARK 500    TYR B  66      -11.60     88.33                                   
REMARK 500    SER B 117     -115.36     60.88                                   
REMARK 500    ILE B 133     -169.05   -111.04                                   
REMARK 500    GLU B 178      113.79    -36.44                                   
REMARK 500    ILE B 236      -60.31    -95.06                                   
REMARK 500    CYS B 238      -60.72    -90.66                                   
REMARK 500    ALA B 269       32.64    -96.68                                   
REMARK 500    SER B 378       47.61    -78.13                                   
REMARK 500    ASN B 462     -126.99     58.02                                   
REMARK 500    ALA B 510       -3.30     72.52                                   
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 A1306        DISTANCE =  7.04 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 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP A 117   OG                                                     
REMARK 620 2 SEP A 117   OG    1.8                                              
REMARK 620 3 SEP A 117   O1P  81.1  80.3                                        
REMARK 620 4 ASP A 288   OD2  92.6  91.0  94.9                                  
REMARK 620 5 ASP A 290   OD2  90.7  91.8 168.1  94.0                            
REMARK 620 6 ASP A 292   OD1 169.8 169.8  90.2  93.5  97.0                      
REMARK 620 7 HOH A 748   O    83.2  84.7  80.8 174.4  89.7  90.2                
REMARK 620 8 HOH A 897   O    82.8  81.8   5.9  89.2 172.9  89.1  86.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 117   OG                                                     
REMARK 620 2 ASP B 288   OD1  96.8                                              
REMARK 620 3 ASP B 290   OD1 104.3  88.3                                        
REMARK 620 4 ASP B 292   OD1 164.9  90.8  88.9                                  
REMARK 620 5 HOH B 823   O    78.2  89.9 177.1  88.8                            
REMARK 620 6 HOH B 724   O    84.1 178.0  89.7  88.8  92.1                      
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 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 SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 610                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE VERSION OF THE ENZYME                                      
DBREF  5VG7 A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5VG7 B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5VG7 SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VG7 ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VG7 GLN A  503  UNP  P36871    ARG   503 ENGINEERED MUTATION            
SEQADV 5VG7 SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VG7 ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VG7 GLN B  503  UNP  P36871    ARG   503 ENGINEERED MUTATION            
SEQRES   1 A  564  SER ASN MET VAL LYS ILE VAL THR VAL LYS THR GLN ALA          
SEQRES   2 A  564  TYR GLN ASP GLN LYS PRO GLY THR SER GLY LEU ARG LYS          
SEQRES   3 A  564  ARG VAL LYS VAL PHE GLN SER SER ALA ASN TYR ALA GLU          
SEQRES   4 A  564  ASN PHE ILE GLN SER ILE ILE SER THR VAL GLU PRO ALA          
SEQRES   5 A  564  GLN ARG GLN GLU ALA THR LEU VAL VAL GLY GLY ASP GLY          
SEQRES   6 A  564  ARG PHE TYR MET LYS GLU ALA ILE GLN LEU ILE ALA ARG          
SEQRES   7 A  564  ILE ALA ALA ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY          
SEQRES   8 A  564  GLN ASN GLY ILE LEU SER THR PRO ALA VAL SER CYS ILE          
SEQRES   9 A  564  ILE ARG LYS ILE LYS ALA ILE GLY GLY ILE ILE LEU THR          
SEQRES  10 A  564  ALA SEP HIS ASN PRO GLY GLY PRO ASN GLY ASP PHE GLY          
SEQRES  11 A  564  ILE LYS PHE ASN ILE SER ASN GLY GLY PRO ALA PRO GLU          
SEQRES  12 A  564  ALA ILE THR ASP LYS ILE PHE GLN ILE SER LYS THR ILE          
SEQRES  13 A  564  GLU GLU TYR ALA VAL CYS PRO ASP LEU LYS VAL ASP LEU          
SEQRES  14 A  564  GLY VAL LEU GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS          
SEQRES  15 A  564  PHE LYS PRO PHE THR VAL GLU ILE VAL ASP SER VAL GLU          
SEQRES  16 A  564  ALA TYR ALA THR MET LEU ARG SER ILE PHE ASP PHE SER          
SEQRES  17 A  564  ALA LEU LYS GLU LEU LEU SER GLY PRO ASN ARG LEU LYS          
SEQRES  18 A  564  ILE ARG ILE ASP ALA MET HIS GLY VAL VAL GLY PRO TYR          
SEQRES  19 A  564  VAL LYS LYS ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA          
SEQRES  20 A  564  ASN SER ALA VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY          
SEQRES  21 A  564  GLY HIS HIS PRO ASP PRO ASN LEU THR TYR ALA ALA ASP          
SEQRES  22 A  564  LEU VAL GLU THR MET LYS SER GLY GLU HIS ASP PHE GLY          
SEQRES  23 A  564  ALA ALA PHE ASP GLY ASP GLY ASP ARG ASN MET ILE LEU          
SEQRES  24 A  564  GLY LYS HIS GLY PHE PHE VAL ASN PRO SER ASP SER VAL          
SEQRES  25 A  564  ALA VAL ILE ALA ALA ASN ILE PHE SER ILE PRO TYR PHE          
SEQRES  26 A  564  GLN GLN THR GLY VAL ARG GLY PHE ALA ARG SER MET PRO          
SEQRES  27 A  564  THR SER GLY ALA LEU ASP ARG VAL ALA SER ALA THR LYS          
SEQRES  28 A  564  ILE ALA LEU TYR GLU THR PRO THR GLY TRP LYS PHE PHE          
SEQRES  29 A  564  GLY ASN LEU MET ASP ALA SER LYS LEU SER LEU CYS GLY          
SEQRES  30 A  564  GLU GLU SER PHE GLY THR GLY SER ASP HIS ILE ARG GLU          
SEQRES  31 A  564  LYS ASP GLY LEU TRP ALA VAL LEU ALA TRP LEU SER ILE          
SEQRES  32 A  564  LEU ALA THR ARG LYS GLN SER VAL GLU ASP ILE LEU LYS          
SEQRES  33 A  564  ASP HIS TRP GLN LYS TYR GLY ARG ASN PHE PHE THR ARG          
SEQRES  34 A  564  TYR ASP TYR GLU GLU VAL GLU ALA GLU GLY ALA ASN LYS          
SEQRES  35 A  564  MET MET LYS ASP LEU GLU ALA LEU MET PHE ASP ARG SER          
SEQRES  36 A  564  PHE VAL GLY LYS GLN PHE SER ALA ASN ASP LYS VAL TYR          
SEQRES  37 A  564  THR VAL GLU LYS ALA ASP ASN PHE GLU TYR SER ASP PRO          
SEQRES  38 A  564  VAL ASP GLY SER ILE SER ARG ASN GLN GLY LEU ARG LEU          
SEQRES  39 A  564  ILE PHE THR ASP GLY SER ARG ILE VAL PHE GLN LEU SER          
SEQRES  40 A  564  GLY THR GLY SER ALA GLY ALA THR ILE ARG LEU TYR ILE          
SEQRES  41 A  564  ASP SER TYR GLU LYS ASP VAL ALA LYS ILE ASN GLN ASP          
SEQRES  42 A  564  PRO GLN VAL MET LEU ALA PRO LEU ILE SER ILE ALA LEU          
SEQRES  43 A  564  LYS VAL SER GLN LEU GLN GLU ARG THR GLY ARG THR ALA          
SEQRES  44 A  564  PRO THR VAL ILE THR                                          
SEQRES   1 B  564  SER ASN MET VAL LYS ILE VAL THR VAL LYS THR GLN ALA          
SEQRES   2 B  564  TYR GLN ASP GLN LYS PRO GLY THR SER GLY LEU ARG LYS          
SEQRES   3 B  564  ARG VAL LYS VAL PHE GLN SER SER ALA ASN TYR ALA GLU          
SEQRES   4 B  564  ASN PHE ILE GLN SER ILE ILE SER THR VAL GLU PRO ALA          
SEQRES   5 B  564  GLN ARG GLN GLU ALA THR LEU VAL VAL GLY GLY ASP GLY          
SEQRES   6 B  564  ARG PHE TYR MET LYS GLU ALA ILE GLN LEU ILE ALA ARG          
SEQRES   7 B  564  ILE ALA ALA ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY          
SEQRES   8 B  564  GLN ASN GLY ILE LEU SER THR PRO ALA VAL SER CYS ILE          
SEQRES   9 B  564  ILE ARG LYS ILE LYS ALA ILE GLY GLY ILE ILE LEU THR          
SEQRES  10 B  564  ALA SER HIS ASN PRO GLY GLY PRO ASN GLY ASP PHE GLY          
SEQRES  11 B  564  ILE LYS PHE ASN ILE SER ASN GLY GLY PRO ALA PRO GLU          
SEQRES  12 B  564  ALA ILE THR ASP LYS ILE PHE GLN ILE SER LYS THR ILE          
SEQRES  13 B  564  GLU GLU TYR ALA VAL CYS PRO ASP LEU LYS VAL ASP LEU          
SEQRES  14 B  564  GLY VAL LEU GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS          
SEQRES  15 B  564  PHE LYS PRO PHE THR VAL GLU ILE VAL ASP SER VAL GLU          
SEQRES  16 B  564  ALA TYR ALA THR MET LEU ARG SER ILE PHE ASP PHE SER          
SEQRES  17 B  564  ALA LEU LYS GLU LEU LEU SER GLY PRO ASN ARG LEU LYS          
SEQRES  18 B  564  ILE ARG ILE ASP ALA MET HIS GLY VAL VAL GLY PRO TYR          
SEQRES  19 B  564  VAL LYS LYS ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA          
SEQRES  20 B  564  ASN SER ALA VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY          
SEQRES  21 B  564  GLY HIS HIS PRO ASP PRO ASN LEU THR TYR ALA ALA ASP          
SEQRES  22 B  564  LEU VAL GLU THR MET LYS SER GLY GLU HIS ASP PHE GLY          
SEQRES  23 B  564  ALA ALA PHE ASP GLY ASP GLY ASP ARG ASN MET ILE LEU          
SEQRES  24 B  564  GLY LYS HIS GLY PHE PHE VAL ASN PRO SER ASP SER VAL          
SEQRES  25 B  564  ALA VAL ILE ALA ALA ASN ILE PHE SER ILE PRO TYR PHE          
SEQRES  26 B  564  GLN GLN THR GLY VAL ARG GLY PHE ALA ARG SER MET PRO          
SEQRES  27 B  564  THR SER GLY ALA LEU ASP ARG VAL ALA SER ALA THR LYS          
SEQRES  28 B  564  ILE ALA LEU TYR GLU THR PRO THR GLY TRP LYS PHE PHE          
SEQRES  29 B  564  GLY ASN LEU MET ASP ALA SER LYS LEU SER LEU CYS GLY          
SEQRES  30 B  564  GLU GLU SER PHE GLY THR GLY SER ASP HIS ILE ARG GLU          
SEQRES  31 B  564  LYS ASP GLY LEU TRP ALA VAL LEU ALA TRP LEU SER ILE          
SEQRES  32 B  564  LEU ALA THR ARG LYS GLN SER VAL GLU ASP ILE LEU LYS          
SEQRES  33 B  564  ASP HIS TRP GLN LYS TYR GLY ARG ASN PHE PHE THR ARG          
SEQRES  34 B  564  TYR ASP TYR GLU GLU VAL GLU ALA GLU GLY ALA ASN LYS          
SEQRES  35 B  564  MET MET LYS ASP LEU GLU ALA LEU MET PHE ASP ARG SER          
SEQRES  36 B  564  PHE VAL GLY LYS GLN PHE SER ALA ASN ASP LYS VAL TYR          
SEQRES  37 B  564  THR VAL GLU LYS ALA ASP ASN PHE GLU TYR SER ASP PRO          
SEQRES  38 B  564  VAL ASP GLY SER ILE SER ARG ASN GLN GLY LEU ARG LEU          
SEQRES  39 B  564  ILE PHE THR ASP GLY SER ARG ILE VAL PHE GLN LEU SER          
SEQRES  40 B  564  GLY THR GLY SER ALA GLY ALA THR ILE ARG LEU TYR ILE          
SEQRES  41 B  564  ASP SER TYR GLU LYS ASP VAL ALA LYS ILE ASN GLN ASP          
SEQRES  42 B  564  PRO GLN VAL MET LEU ALA PRO LEU ILE SER ILE ALA LEU          
SEQRES  43 B  564  LYS VAL SER GLN LEU GLN GLU ARG THR GLY ARG THR ALA          
SEQRES  44 B  564  PRO THR VAL ILE THR                                          
MODRES 5VG7 SEP A  117  SER  MODIFIED RESIDUE                                   
HET    SEP  A 117      16                                                       
HET     MG  A 601       1                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    SO4  A 610       5                                                       
HET    SO4  A 611       5                                                       
HET    SO4  A 612       5                                                       
HET    GOL  A 613       6                                                       
HET    GOL  A 614       6                                                       
HET    GOL  A 615       6                                                       
HET     MG  B 601       1                                                       
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    SO4  B 607       5                                                       
HET    SO4  B 608       5                                                       
HET    GOL  B 609       6                                                       
HET    GOL  B 610       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  SO4    18(O4 S 2-)                                                  
FORMUL  15  GOL    5(C3 H8 O3)                                                  
FORMUL  28  HOH   *949(H2 O)                                                    
HELIX    1 AA1 VAL A   26  SER A   32  1                                   7    
HELIX    2 AA2 ASN A   34  THR A   46  1                                  13    
HELIX    3 AA3 GLU A   48  GLN A   53  1                                   6    
HELIX    4 AA4 TYR A   66  ASN A   81  1                                  16    
HELIX    5 AA5 SER A   95  LYS A  107  1                                  13    
HELIX    6 AA6 PRO A  140  ILE A  154  1                                  15    
HELIX    7 AA7 VAL A  192  PHE A  203  1                                  12    
HELIX    8 AA8 ASP A  204  SER A  213  1                                  10    
HELIX    9 AA9 VAL A  229  LEU A  237  1                                   9    
HELIX   10 AB1 PRO A  244  ASN A  246  5                                   3    
HELIX   11 AB2 ASP A  256  HIS A  260  5                                   5    
HELIX   12 AB3 ALA A  269  SER A  278  1                                  10    
HELIX   13 AB4 ASN A  305  ASN A  316  1                                  12    
HELIX   14 AB5 ILE A  317  SER A  319  5                                   3    
HELIX   15 AB6 ILE A  320  GLY A  327  1                                   8    
HELIX   16 AB7 GLY A  339  LYS A  349  1                                  11    
HELIX   17 AB8 GLY A  358  ALA A  368  1                                  11    
HELIX   18 AB9 ASP A  390  LYS A  406  1                                  17    
HELIX   19 AC1 SER A  408  GLY A  421  1                                  14    
HELIX   20 AC2 GLU A  434  ASP A  451  1                                  18    
HELIX   21 AC3 ASP A  531  GLN A  548  1                                  18    
HELIX   22 AC4 GLN A  548  GLY A  554  1                                   7    
HELIX   23 AC5 VAL B   26  SER B   32  1                                   7    
HELIX   24 AC6 ASN B   34  THR B   46  1                                  13    
HELIX   25 AC7 VAL B   47  ARG B   52  5                                   6    
HELIX   26 AC8 TYR B   66  ASN B   81  1                                  16    
HELIX   27 AC9 SER B   95  LYS B  107  1                                  13    
HELIX   28 AD1 PRO B  140  ILE B  154  1                                  15    
HELIX   29 AD2 VAL B  192  PHE B  203  1                                  12    
HELIX   30 AD3 ASP B  204  SER B  213  1                                  10    
HELIX   31 AD4 VAL B  229  LEU B  237  1                                   9    
HELIX   32 AD5 PRO B  244  ASN B  246  5                                   3    
HELIX   33 AD6 ASP B  256  HIS B  260  5                                   5    
HELIX   34 AD7 ALA B  269  SER B  278  1                                  10    
HELIX   35 AD8 ASN B  305  ASN B  316  1                                  12    
HELIX   36 AD9 ILE B  317  SER B  319  5                                   3    
HELIX   37 AE1 ILE B  320  GLY B  327  1                                   8    
HELIX   38 AE2 GLY B  339  ALA B  347  1                                   9    
HELIX   39 AE3 GLY B  358  ALA B  368  1                                  11    
HELIX   40 AE4 ASP B  390  LYS B  406  1                                  17    
HELIX   41 AE5 SER B  408  GLY B  421  1                                  14    
HELIX   42 AE6 GLU B  434  ASP B  451  1                                  18    
HELIX   43 AE7 ASP B  531  GLN B  548  1                                  18    
HELIX   44 AE8 GLN B  548  GLY B  554  1                                   7    
SHEET    1 AA1 8 MET A   1  VAL A   2  0                                        
SHEET    2 AA1 8 GLY A 171  LEU A 177  1  O  ASP A 176   N  VAL A   2           
SHEET    3 AA1 8 PHE A 184  VAL A 189 -1  O  PHE A 184   N  PHE A 175           
SHEET    4 AA1 8 ARG A  85  ILE A  93  1  N  ILE A  88   O  GLU A 187           
SHEET    5 AA1 8 THR A  56  GLY A  61  1  N  VAL A  59   O  VAL A  87           
SHEET    6 AA1 8 GLY A 110  LEU A 114  1  O  LEU A 114   N  GLY A  60           
SHEET    7 AA1 8 ASP A 126  ASN A 132 -1  O  LYS A 130   N  ILE A 113           
SHEET    8 AA1 8 LEU A  22  ARG A  25 -1  N  LYS A  24   O  PHE A 127           
SHEET    1 AA2 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA2 2 GLU A 156  VAL A 159 -1  O  TYR A 157   N  VAL A   7           
SHEET    1 AA3 5 ALA A 248  VAL A 249  0                                        
SHEET    2 AA3 5 ILE A 220  ASP A 223  1  N  ILE A 222   O  VAL A 249           
SHEET    3 AA3 5 PHE A 283  PHE A 287  1  O  ALA A 285   N  ASP A 223           
SHEET    4 AA3 5 ASN A 294  GLY A 298 -1  O  LEU A 297   N  GLY A 284           
SHEET    5 AA3 5 PHE A 303  VAL A 304 -1  O  VAL A 304   N  ILE A 296           
SHEET    1 AA4 4 LEU A 352  THR A 355  0                                        
SHEET    2 AA4 4 PHE A 331  SER A 334  1  N  PHE A 331   O  TYR A 353           
SHEET    3 AA4 4 LEU A 373  GLU A 376  1  O  LEU A 373   N  ALA A 332           
SHEET    4 AA4 4 GLY A 380  SER A 383 -1  O  GLY A 380   N  GLU A 376           
SHEET    1 AA5 7 GLN A 458  SER A 460  0                                        
SHEET    2 AA5 7 VAL A 465  ASN A 473 -1  O  TYR A 466   N  PHE A 459           
SHEET    3 AA5 7 LEU A 490  PHE A 494 -1  O  ILE A 493   N  LYS A 470           
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  TYR A 517   N  VAL A 501           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  TYR A 428   O  LEU A 516           
SHEET    7 AA5 7 VAL A 560  THR A 562 -1  O  VAL A 560   N  ASP A 429           
SHEET    1 AA6 2 TYR A 476  SER A 477  0                                        
SHEET    2 AA6 2 ILE A 484  SER A 485 -1  O  SER A 485   N  TYR A 476           
SHEET    1 AA7 2 VAL B   5  LYS B   8  0                                        
SHEET    2 AA7 2 GLU B 156  VAL B 159 -1  O  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  ILE B 133 -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  VAL B 189   N  GLN B  90           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  PHE B 175   O  PHE B 184           
SHEET    1 AA9 5 ALA B 248  VAL B 249  0                                        
SHEET    2 AA9 5 ILE B 220  ASP B 223  1  N  ILE B 222   O  VAL B 249           
SHEET    3 AA9 5 PHE B 283  PHE B 287  1  O  ALA B 285   N  ASP B 223           
SHEET    4 AA9 5 ASN B 294  GLY B 298 -1  O  LEU B 297   N  GLY B 284           
SHEET    5 AA9 5 PHE B 303  VAL B 304 -1  O  VAL B 304   N  ILE B 296           
SHEET    1 AB1 4 LEU B 352  THR B 355  0                                        
SHEET    2 AB1 4 PHE B 331  SER B 334  1  N  PHE B 331   O  TYR B 353           
SHEET    3 AB1 4 LEU B 373  GLU B 376  1  O  GLY B 375   N  ALA B 332           
SHEET    4 AB1 4 GLY B 380  SER B 383 -1  O  GLY B 380   N  GLU B 376           
SHEET    1 AB2 7 GLN B 458  ALA B 461  0                                        
SHEET    2 AB2 7 LYS B 464  ASN B 473 -1  O  TYR B 466   N  PHE B 459           
SHEET    3 AB2 7 LEU B 490  PHE B 494 -1  O  ILE B 493   N  GLU B 469           
SHEET    4 AB2 7 ARG B 499  LEU B 504 -1  O  ILE B 500   N  LEU B 492           
SHEET    5 AB2 7 ALA B 512  GLU B 522 -1  O  TYR B 517   N  VAL B 501           
SHEET    6 AB2 7 ARG B 422  VAL B 433 -1  N  TYR B 428   O  LEU B 516           
SHEET    7 AB2 7 VAL B 560  THR B 562 -1  O  THR B 562   N  ARG B 427           
SHEET    1 AB3 2 TYR B 476  SER B 477  0                                        
SHEET    2 AB3 2 ILE B 484  SER B 485 -1  O  SER B 485   N  TYR B 476           
LINK         C   ALA A 116                 N  ASEP A 117     1555   1555  1.33  
LINK         C   ALA A 116                 N  BSEP A 117     1555   1555  1.33  
LINK         OG ASEP A 117                MG    MG A 601     1555   1555  1.96  
LINK         OG BSEP A 117                MG    MG A 601     1555   1555  2.04  
LINK         C  ASEP A 117                 N   HIS A 118     1555   1555  1.33  
LINK         C  BSEP A 117                 N   HIS A 118     1555   1555  1.33  
LINK         O1PASEP A 117                MG    MG A 601     1555   1555  2.08  
LINK         OD2 ASP A 288                MG    MG A 601     1555   1555  2.06  
LINK         OD2 ASP A 290                MG    MG A 601     1555   1555  2.10  
LINK         OD1 ASP A 292                MG    MG A 601     1555   1555  1.97  
LINK         OG  SER B 117                MG    MG B 601     1555   1555  2.15  
LINK         OD1 ASP B 288                MG    MG B 601     1555   1555  2.01  
LINK         OD1 ASP B 290                MG    MG B 601     1555   1555  2.22  
LINK         OD1 ASP B 292                MG    MG B 601     1555   1555  1.95  
LINK        MG    MG A 601                 O   HOH A 748     1555   1555  2.30  
LINK        MG    MG A 601                 O  BHOH A 897     1555   1555  2.17  
LINK        MG    MG B 601                 O   HOH B 823     1555   1555  2.23  
LINK        MG    MG B 601                 O   HOH B 724     1555   1555  2.05  
CISPEP   1 ALA A  461    ASN A  462          0         2.96                     
SITE     1 AC1  6 SEP A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     2 AC1  6 HOH A 748  HOH A 897                                          
SITE     1 AC2  5 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     2 AC2  5 HOH A 713                                                     
SITE     1 AC3  6 ASN A 179  LYS A 470  ARG A 491  HOH A 726                    
SITE     2 AC3  6 HOH A 895  HOH A 930                                          
SITE     1 AC4  4 GLN A 324  ALA B 314  ALA B 315  THR B 348                    
SITE     1 AC5  6 THR A  19  GLY A 358  TRP A 359  HOH A 721                    
SITE     2 AC5  6 HOH A 961  HOH A 999                                          
SITE     1 AC6  2 GLU A 187  HOH A 898                                          
SITE     1 AC7  1 HIS A 260                                                     
SITE     1 AC8  4 SER A 505  GLY A 506  ARG A 515  HOH A 760                    
SITE     1 AC9  7 GLU A 432  VAL A 433  GLU A 434  ARG A 555                    
SITE     2 AC9  7 HOH A 704  HOH A 818  HOH A 988                               
SITE     1 AD1  3 LYS A 299  HIS A 300  HOH A 929                               
SITE     1 AD2  7 TYR A  66  MET A  67  LYS A  68  GLU A  69                    
SITE     2 AD2  7 GLU A 255  HOH A 951  HOH A1005                               
SITE     1 AD3  3 PRO A 244  ALA A 245  HOH A 954                               
SITE     1 AD4  4 ARG A 343  ASP A 496  GLY A 497  HOH A 970                    
SITE     1 AD5  5 THR A 326  ARG A 329  HOH A 797  GLN B 325                    
SITE     2 AD5  5 ARG B 329                                                     
SITE     1 AD6  8 PHE A 303  ASN A 305  ARG A 422  PHE A 424                    
SITE     2 AD6  8 PHE A 425  PRO A 532  HOH A 813  HOH A 853                    
SITE     1 AD7  6 SER B 117  ASP B 288  ASP B 290  ASP B 292                    
SITE     2 AD7  6 HOH B 724  HOH B 823                                          
SITE     1 AD8  3 SER B 505  GLY B 506  ARG B 515                               
SITE     1 AD9  4 ARG B 221  ASN B 246  HIS B 281  HOH B 908                    
SITE     1 AE1  4 ARG B  85  ILE B 106  HOH B 707  HOH B 806                    
SITE     1 AE2  5 ARG B 293  SER B 378  ARG B 427  HOH B 717                    
SITE     2 AE2  5 HOH B 920                                                     
SITE     1 AE3  5 ASN B 179  GLU B 354  LYS B 470  ARG B 491                    
SITE     2 AE3  5 HOH B 703                                                     
SITE     1 AE4  4 GLN B  41  SER B  45  ARG B  52  ASN B  81                    
SITE     1 AE5  4 GLU B 432  VAL B 433  GLU B 434  ARG B 555                    
SITE     1 AE6  5 ASP B 204  SER B 319  GLN B 324  THR B 404                    
SITE     2 AE6  5 HOH B 790                                                     
SITE     1 AE7  4 GLY B 358  TRP B 359  GLU B 376  HOH B 826                    
CRYST1  172.131  172.131   99.805  90.00  90.00  90.00 P 41 21 2     8          
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      0.005810  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010020        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system