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Database: PDB
Entry: 5VIN
LinkDB: 5VIN
Original site: 5VIN 
HEADER    ISOMERASE                               17-APR-17   5VIN              
TITLE     CRYSTAL STRUCTURE OF THE R515Q MISSENSE VARIANT OF HUMAN PGM1         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLUCOMUTASE-1;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;                              
COMPND   5 EC: 5.4.2.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PGM1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHOGLUCOMUTASE-1, PGM1, ISOMERASE, PHOSPHORYL TRANSFER            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.STIERS,L.J.BEAMER                                                 
REVDAT   4   27-NOV-19 5VIN    1       REMARK                                   
REVDAT   3   17-OCT-18 5VIN    1       JRNL                                     
REVDAT   2   05-SEP-18 5VIN    1       JRNL                                     
REVDAT   1   27-JUN-18 5VIN    0                                                
JRNL        AUTH   K.M.STIERS,L.J.BEAMER                                        
JRNL        TITL   A HOTSPOT FOR DISEASE-ASSOCIATED VARIANTS OF HUMAN PGM1 IS   
JRNL        TITL 2 ASSOCIATED WITH IMPAIRED LIGAND BINDING AND LOOP DYNAMICS.   
JRNL        REF    STRUCTURE                     V.  26  1337 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   30122451                                                     
JRNL        DOI    10.1016/J.STR.2018.07.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.347                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 46861                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2385                            
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 61.5213 -  6.6827    1.00     2856   155  0.2093 0.2374        
REMARK   3     2  6.6827 -  5.3052    1.00     2736   133  0.2378 0.2845        
REMARK   3     3  5.3052 -  4.6349    1.00     2684   150  0.1860 0.2726        
REMARK   3     4  4.6349 -  4.2112    1.00     2660   142  0.1773 0.2330        
REMARK   3     5  4.2112 -  3.9094    1.00     2676   120  0.2025 0.2191        
REMARK   3     6  3.9094 -  3.6790    0.92     2384   153  0.2326 0.2947        
REMARK   3     7  3.6790 -  3.4947    0.92     2430   130  0.3076 0.3927        
REMARK   3     8  3.4947 -  3.3426    1.00     2622   133  0.2436 0.2578        
REMARK   3     9  3.3426 -  3.2140    1.00     2615   150  0.2818 0.3312        
REMARK   3    10  3.2140 -  3.1031    1.00     2630   124  0.2663 0.3294        
REMARK   3    11  3.1031 -  3.0060    1.00     2601   146  0.2704 0.3319        
REMARK   3    12  3.0060 -  2.9201    1.00     2612   142  0.2893 0.4049        
REMARK   3    13  2.9201 -  2.8432    1.00     2616   134  0.3022 0.3557        
REMARK   3    14  2.8432 -  2.7739    0.99     2632   114  0.3059 0.4328        
REMARK   3    15  2.7739 -  2.7108    1.00     2571   152  0.3066 0.3688        
REMARK   3    16  2.7108 -  2.6531    1.00     2574   170  0.3205 0.3805        
REMARK   3    17  2.6531 -  2.6000    1.00     2577   137  0.3309 0.4049        
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)     : 0.454            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.552           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.27                          
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      :  0.010           8340                                  
REMARK   3   ANGLE     :  1.384          11362                                  
REMARK   3   CHIRALITY :  0.082           1274                                  
REMARK   3   PLANARITY :  0.011           1505                                  
REMARK   3   DIHEDRAL  :  5.206           6454                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 170 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  71.1496  35.1400 -20.9499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1651 T22:   0.5228                                     
REMARK   3      T33:   0.2457 T12:  -0.0314                                     
REMARK   3      T13:  -0.0034 T23:  -0.0451                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1433 L22:   0.2647                                     
REMARK   3      L33:   0.0870 L12:  -0.0028                                     
REMARK   3      L13:  -0.0814 L23:  -0.1017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1029 S12:  -0.3530 S13:  -0.0380                       
REMARK   3      S21:   0.1859 S22:  -0.0418 S23:   0.0796                       
REMARK   3      S31:  -0.0693 S32:   0.5784 S33:   0.0300                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  47.0464  25.2193 -24.2414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1448 T22:  -0.2553                                     
REMARK   3      T33:   0.3305 T12:   0.2714                                     
REMARK   3      T13:   0.0319 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0397 L22:   0.0244                                     
REMARK   3      L33:   0.1815 L12:  -0.0189                                     
REMARK   3      L13:  -0.0466 L23:   0.0766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1865 S12:   0.1777 S13:   0.1166                       
REMARK   3      S21:   0.0088 S22:   0.0154 S23:   0.0174                       
REMARK   3      S31:   0.1162 S32:   0.3287 S33:  -0.2892                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 435 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4857  20.9905   2.2967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4698 T22:   0.2641                                     
REMARK   3      T33:   0.3276 T12:   0.0914                                     
REMARK   3      T13:   0.0034 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1183 L22:   0.0862                                     
REMARK   3      L33:   0.0487 L12:   0.0086                                     
REMARK   3      L13:  -0.0121 L23:   0.0613                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1129 S12:  -0.2776 S13:  -0.0401                       
REMARK   3      S21:   0.3123 S22:   0.0251 S23:   0.1212                       
REMARK   3      S31:   0.2428 S32:   0.1012 S33:   0.0008                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 56 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5850  55.5954 -31.8419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2254 T22:   1.0936                                     
REMARK   3      T33:   0.4890 T12:  -0.4019                                     
REMARK   3      T13:  -0.1279 T23:   0.1834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0353 L22:   0.0332                                     
REMARK   3      L33:   0.0178 L12:   0.0257                                     
REMARK   3      L13:  -0.0145 L23:  -0.0202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1052 S12:  -0.0533 S13:   0.0454                       
REMARK   3      S21:   0.1673 S22:   0.0368 S23:   0.1303                       
REMARK   3      S31:   0.1569 S32:  -0.1600 S33:  -0.0008                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 202 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1379  60.0708 -41.2003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6671 T22:   0.3349                                     
REMARK   3      T33:   0.2460 T12:  -0.1006                                     
REMARK   3      T13:  -0.0676 T23:   0.0357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3839 L22:   0.2187                                     
REMARK   3      L33:   0.2088 L12:  -0.1404                                     
REMARK   3      L13:  -0.2478 L23:   0.0508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3257 S12:  -0.0325 S13:  -0.0119                       
REMARK   3      S21:   0.2593 S22:  -0.1020 S23:  -0.2149                       
REMARK   3      S31:   0.1212 S32:  -0.3420 S33:   0.1177                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 203 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5801  65.6272 -43.9867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5651 T22:   0.2226                                     
REMARK   3      T33:   0.5439 T12:   0.1972                                     
REMARK   3      T13:  -0.1322 T23:  -0.1283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0117 L22:   0.1451                                     
REMARK   3      L33:   0.3673 L12:  -0.0335                                     
REMARK   3      L13:   0.0228 L23:  -0.1281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3222 S12:   0.0436 S13:  -0.0721                       
REMARK   3      S21:   0.1126 S22:   0.2032 S23:  -0.0814                       
REMARK   3      S31:   0.0541 S32:   0.1221 S33:   0.2317                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 294 THROUGH 494 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3919  81.2884 -27.4742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9390 T22:   0.2541                                     
REMARK   3      T33:   0.3406 T12:   0.0219                                     
REMARK   3      T13:   0.0337 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0597 L22:   0.1668                                     
REMARK   3      L33:   0.1565 L12:  -0.0490                                     
REMARK   3      L13:  -0.0498 L23:   0.0105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1119 S12:  -0.1241 S13:   0.1456                       
REMARK   3      S21:   0.4272 S22:   0.0601 S23:   0.0549                       
REMARK   3      S31:  -0.1256 S32:   0.0399 S33:   0.2458                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 495 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  52.0132  75.7683 -14.8331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0589 T22:   0.3854                                     
REMARK   3      T33:   0.4103 T12:  -0.0572                                     
REMARK   3      T13:  -0.0886 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0386 L22:   0.0453                                     
REMARK   3      L33:   0.0550 L12:  -0.0383                                     
REMARK   3      L13:   0.0446 L23:  -0.0477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0673 S12:  -0.0413 S13:  -0.0949                       
REMARK   3      S21:   0.0302 S22:   0.2250 S23:   0.0985                       
REMARK   3      S31:  -0.0493 S32:   0.1147 S33:   0.0028                       
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 5VIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227482.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00003                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47453                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.90                              
REMARK 200  R MERGE                    (I) : 0.18500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.84600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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   (%): 59.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M COBALT (II) CHLORIDE              
REMARK 280  HEXAHYDRATE, O.1 M MES MONOHYDRATE PH 6.5, AMMONIUM SULFATE 1.8-    
REMARK 280  2.1M, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.74150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       86.98000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       86.98000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.87075            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       86.98000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       86.98000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.61225            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       86.98000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.98000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.87075            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       86.98000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.98000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.61225            
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       49.74150            
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     VAL B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     ASN B     0                                                      
REMARK 465     ASP B   463                                                      
REMARK 465     LYS B   464                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A  -1    OG                                                  
REMARK 470     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  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  31    OG                                                  
REMARK 470     VAL A  47    CG1  CG2                                            
REMARK 470     GLU A  48    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     ILE A 147    CG1  CG2  CD1                                       
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 154    CG1  CG2  CD1                                       
REMARK 470     GLU A 156    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     GLU A 187    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 209    CG   CD   CE   NZ                                   
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 277    CG   CD   CE   NZ                                   
REMARK 470     GLU A 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 328    CG1  CG2                                            
REMARK 470     LYS A 360    CG   CD   CE   NZ                                   
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     GLN A 418    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 434    CG   CD   OE1  OE2                                  
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     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     VAL A 465    CG1  CG2                                            
REMARK 470     GLU A 475    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 486    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 487    CG   OD1  ND2                                       
REMARK 470     SER A 505    OG                                                  
REMARK 470     THR A 507    OG1  CG2                                            
REMARK 470     SER A 509    OG                                                  
REMARK 470     VAL A 525    CG1  CG2                                            
REMARK 470     LYS A 527    CG   CD   CE   NZ                                   
REMARK 470     VAL B   2    CG1  CG2                                            
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     ILE B   4    CG1  CG2  CD1                                       
REMARK 470     VAL B   5    CG1  CG2                                            
REMARK 470     VAL B   7    CG1  CG2                                            
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     TYR B  12    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B  13    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     LEU B  22    CG   CD1  CD2                                       
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     SER B  31    OG                                                  
REMARK 470     ASN B  34    CG   OD1  ND2                                       
REMARK 470     GLN B  41    CG   CD   OE1  NE2                                  
REMARK 470     SER B  42    OG                                                  
REMARK 470     THR B  46    OG1  CG2                                            
REMARK 470     ARG B  52    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B  73    CG   CD1  CD2                                       
REMARK 470     ILE B  74    CG1  CG2  CD1                                       
REMARK 470     ILE B  77    CG1  CG2  CD1                                       
REMARK 470     ILE B  83    CG1  CG2  CD1                                       
REMARK 470     ILE B 103    CG1  CG2  CD1                                       
REMARK 470     LYS B 105    CG   CD   CE   NZ                                   
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ASN B 124    CG   OD1  ND2                                       
REMARK 470     ASP B 126    CG   OD1  OD2                                       
REMARK 470     ILE B 143    CG1  CG2  CD1                                       
REMARK 470     ASP B 145    CG   OD1  OD2                                       
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     SER B 151    OG                                                  
REMARK 470     LYS B 152    CG   CD   CE   NZ                                   
REMARK 470     THR B 153    OG1  CG2                                            
REMARK 470     ILE B 154    CG1  CG2  CD1                                       
REMARK 470     GLU B 155    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 156    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 159    CG1  CG2                                            
REMARK 470     ASP B 162    CG   OD1  OD2                                       
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     VAL B 169    CG1  CG2                                            
REMARK 470     LYS B 172    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     ARG B 217    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 249    CG1  CG2                                            
REMARK 470     LEU B 266    CG   CD1  CD2                                       
REMARK 470     LEU B 272    CG   CD1  CD2                                       
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     THR B 275    OG1  CG2                                            
REMARK 470     LYS B 277    CG   CD   CE   NZ                                   
REMARK 470     SER B 278    OG                                                  
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 293    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 304    CG1  CG2                                            
REMARK 470     SER B 307    OG                                                  
REMARK 470     VAL B 312    CG1  CG2                                            
REMARK 470     GLN B 325    CG   CD   OE1  NE2                                  
REMARK 470     THR B 326    OG1  CG2                                            
REMARK 470     VAL B 328    CG1  CG2                                            
REMARK 470     VAL B 344    CG1  CG2                                            
REMARK 470     SER B 346    OG                                                  
REMARK 470     THR B 348    OG1  CG2                                            
REMARK 470     THR B 355    OG1  CG2                                            
REMARK 470     LYS B 360    CG   CD   CE   NZ                                   
REMARK 470     ASN B 364    CG   OD1  ND2                                       
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     LYS B 406    CG   CD   CE   NZ                                   
REMARK 470     VAL B 409    CG1  CG2                                            
REMARK 470     ILE B 412    CG1  CG2  CD1                                       
REMARK 470     LEU B 413    CG   CD1  CD2                                       
REMARK 470     LYS B 414    CG   CD   CE   NZ                                   
REMARK 470     ASP B 415    CG   OD1  OD2                                       
REMARK 470     GLN B 418    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 419    CG   CD   CE   NZ                                   
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     ASN B 439    CG   OD1  ND2                                       
REMARK 470     LYS B 440    CG   CD   CE   NZ                                   
REMARK 470     MET B 442    CG   SD   CE                                        
REMARK 470     LYS B 443    CG   CD   CE   NZ                                   
REMARK 470     LEU B 448    CG   CD1  CD2                                       
REMARK 470     ARG B 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 453    OG                                                  
REMARK 470     VAL B 455    CG1  CG2                                            
REMARK 470     LYS B 457    CG   CD   CE   NZ                                   
REMARK 470     GLN B 458    CG   CD   OE1  NE2                                  
REMARK 470     SER B 460    OG                                                  
REMARK 470     ASN B 462    CG   OD1  ND2                                       
REMARK 470     VAL B 465    CG1  CG2                                            
REMARK 470     TYR B 466    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 467    OG1  CG2                                            
REMARK 470     VAL B 468    CG1  CG2                                            
REMARK 470     SER B 477    OG                                                  
REMARK 470     VAL B 480    CG1  CG2                                            
REMARK 470     SER B 483    OG                                                  
REMARK 470     ILE B 484    CG1  CG2  CD1                                       
REMARK 470     ARG B 486    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 487    CG   OD1  ND2                                       
REMARK 470     LEU B 492    CG   CD1  CD2                                       
REMARK 470     VAL B 501    CG1  CG2                                            
REMARK 470     LEU B 504    CG   CD1  CD2                                       
REMARK 470     THR B 507    OG1  CG2                                            
REMARK 470     SER B 509    OG                                                  
REMARK 470     THR B 513    OG1  CG2                                            
REMARK 470     ILE B 514    CG1  CG2  CD1                                       
REMARK 470     GLN B 515    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 516    CG   CD1  CD2                                       
REMARK 470     ILE B 518    CG1  CG2  CD1                                       
REMARK 470     SER B 520    OG                                                  
REMARK 470     GLU B 522    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     VAL B 525    CG1  CG2                                            
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     ILE B 528    CG1  CG2  CD1                                       
REMARK 470     GLN B 530    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 531    CG   OD1  OD2                                       
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 534    CG1  CG2                                            
REMARK 470     LEU B 536    CG   CD1  CD2                                       
REMARK 470     LEU B 539    CG   CD1  CD2                                       
REMARK 470     ILE B 540    CG1  CG2  CD1                                       
REMARK 470     LEU B 544    CG   CD1  CD2                                       
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 470     VAL B 546    CG1  CG2                                            
REMARK 470     SER B 547    OG                                                  
REMARK 470     GLN B 548    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 549    CG   CD1  CD2                                       
REMARK 470     GLU B 551    CG   CD   OE1  OE2                                  
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   NH1  ARG B    76     O    LEU B   163              2.07            
REMARK 500   OG1  THR A   426     O    HOH A   701              2.09            
REMARK 500   OD2  ASP B   444     NH2  ARG B   552              2.12            
REMARK 500   O    GLY A   380     O    HOH A   702              2.12            
REMARK 500   OD2  ASP A   166     O    HOH A   703              2.14            
REMARK 500   NH1  ARG A    76     O    HOH A   704              2.16            
REMARK 500   NE2  GLN A   533     O    HOH A   701              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    LEU A 218   CB  -  CG  -  CD1 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ARG A 503   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 503   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 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    ASN A   0      -19.09     55.57                                   
REMARK 500    ASN A  34       19.14     59.25                                   
REMARK 500    TYR A  66       -4.97     85.06                                   
REMARK 500    ASN A  91       15.96     59.15                                   
REMARK 500    SER A 117     -113.53     55.46                                   
REMARK 500    ILE A 133     -164.05   -107.74                                   
REMARK 500    ASN A 179       -1.42     62.21                                   
REMARK 500    ALA A 269       42.13   -103.48                                   
REMARK 500    LYS A 360      -38.44    -36.67                                   
REMARK 500    SER A 378       49.27    -84.42                                   
REMARK 500    ASN A 462       15.46    101.67                                   
REMARK 500    ASP A 463      -49.70   -178.92                                   
REMARK 500    ASN A 487       80.20     39.22                                   
REMARK 500    THR A 507       -1.49    116.91                                   
REMARK 500    LEU B  22       99.54    -65.54                                   
REMARK 500    TYR B  66       -5.52     82.27                                   
REMARK 500    ASN B  91       18.52     59.10                                   
REMARK 500    SER B 117     -108.54     60.73                                   
REMARK 500    ILE B 133     -168.35   -107.73                                   
REMARK 500    ILE B 236      -60.77    -92.88                                   
REMARK 500    PHE B 257       27.19     47.77                                   
REMARK 500    LYS B 349       15.80     57.27                                   
REMARK 500    LYS B 360      -37.23    -35.40                                   
REMARK 500    SER B 378       49.94    -83.41                                   
REMARK 500    LYS B 457     -177.10    -63.97                                   
REMARK 500    ALA B 461       13.09   -154.84                                   
REMARK 500    SER B 505     -119.39    -32.28                                   
REMARK 500    ALA B 510     -149.69   -146.13                                   
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 A 758        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A 759        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 760        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 761        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A 762        DISTANCE =  8.46 ANGSTROMS                       
REMARK 525    HOH A 763        DISTANCE =  8.51 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                              CO A 614  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 117   OG                                                     
REMARK 620 2 ASP A 288   OD2  83.7                                              
REMARK 620 3 ASP A 290   OD1  89.8  76.6                                        
REMARK 620 4 ASP A 292   OD2 166.6  87.7  98.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO B 607  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 117   OG                                                     
REMARK 620 2 ASP B 288   OD2 123.9                                              
REMARK 620 3 ASP B 290   OD1 102.6  91.3                                        
REMARK 620 4 ASP B 292   OD2 161.2  68.8  90.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 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 GOL A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 614                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CO B 607                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE VERSION OF THE ENZYME                                      
DBREF  5VIN A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5VIN B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5VIN MET A  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS A  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS A  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS A  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS A  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS A  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS A  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN SER A  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN SER A  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLY A  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN VAL A  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN ASP A  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN LEU A  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLY A   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN THR A   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLU A   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN ASN A   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN LEU A   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN TYR A   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN PHE A   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLN A   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLN A  515  UNP  P36871    ARG   515 ENGINEERED MUTATION            
SEQADV 5VIN MET B  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS B  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS B  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS B  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS B  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS B  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN HIS B  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN SER B  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN SER B  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLY B  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN VAL B  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN ASP B  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN LEU B  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLY B   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN THR B   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLU B   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN ASN B   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN LEU B   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN TYR B   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN PHE B   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLN B   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5VIN GLN B  515  UNP  P36871    ARG   515 ENGINEERED MUTATION            
SEQRES   1 A  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 A  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 A  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 A  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 A  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 A  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 A  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 A  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 A  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 A  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SER HIS ASN PRO          
SEQRES  12 A  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 A  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 A  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 A  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 A  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 A  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 A  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 A  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 A  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 A  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 A  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP          
SEQRES  23 A  585  PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET          
SEQRES  24 A  585  LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY          
SEQRES  25 A  585  ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE          
SEQRES  26 A  585  PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA          
SEQRES  27 A  585  ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL          
SEQRES  28 A  585  ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU          
SEQRES  29 A  585  ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU          
SEQRES  30 A  585  THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP          
SEQRES  31 A  585  ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY          
SEQRES  32 A  585  THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP          
SEQRES  33 A  585  ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS          
SEQRES  34 A  585  GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS          
SEQRES  35 A  585  TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU          
SEQRES  36 A  585  VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU          
SEQRES  37 A  585  GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN          
SEQRES  38 A  585  PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA          
SEQRES  39 A  585  ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE          
SEQRES  40 A  585  SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY          
SEQRES  41 A  585  SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA          
SEQRES  42 A  585  GLY ALA THR ILE GLN LEU TYR ILE ASP SER TYR GLU LYS          
SEQRES  43 A  585  ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU          
SEQRES  44 A  585  ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU          
SEQRES  45 A  585  GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR          
SEQRES   1 B  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 B  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 B  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 B  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 B  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 B  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 B  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 B  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 B  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 B  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SER HIS ASN PRO          
SEQRES  12 B  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 B  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 B  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 B  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 B  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 B  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 B  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 B  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 B  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 B  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 B  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP          
SEQRES  23 B  585  PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET          
SEQRES  24 B  585  LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY          
SEQRES  25 B  585  ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE          
SEQRES  26 B  585  PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA          
SEQRES  27 B  585  ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL          
SEQRES  28 B  585  ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU          
SEQRES  29 B  585  ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU          
SEQRES  30 B  585  THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP          
SEQRES  31 B  585  ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY          
SEQRES  32 B  585  THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP          
SEQRES  33 B  585  ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS          
SEQRES  34 B  585  GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS          
SEQRES  35 B  585  TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU          
SEQRES  36 B  585  VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU          
SEQRES  37 B  585  GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN          
SEQRES  38 B  585  PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA          
SEQRES  39 B  585  ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE          
SEQRES  40 B  585  SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY          
SEQRES  41 B  585  SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA          
SEQRES  42 B  585  GLY ALA THR ILE GLN LEU TYR ILE ASP SER TYR GLU LYS          
SEQRES  43 B  585  ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU          
SEQRES  44 B  585  ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU          
SEQRES  45 B  585  GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR          
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    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    GOL  A 610       6                                                       
HET    GOL  A 611       6                                                       
HET    GOL  A 612       6                                                       
HET    GOL  A 613       6                                                       
HET     CO  A 614       1                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET    SO4  B 604       5                                                       
HET    GOL  B 605       6                                                       
HET    GOL  B 606       6                                                       
HET     CO  B 607       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CO COBALT (II) ION                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    13(O4 S 2-)                                                  
FORMUL  12  GOL    6(C3 H8 O3)                                                  
FORMUL  16   CO    2(CO 2+)                                                     
FORMUL  24  HOH   *91(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 VAL A   47  ARG A   52  5                                   6    
HELIX    4 AA4 TYR A   66  ASN A   81  1                                  16    
HELIX    5 AA5 SER A   95  ILE A  106  1                                  12    
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  THR A  348  1                                  10    
HELIX   17 AB8 GLY A  358  ALA A  368  1                                  11    
HELIX   18 AB9 ASP A  390  LYS A  406  1                                  17    
HELIX   19 AC1 SER A  408  GLY A  421  1                                  14    
HELIX   20 AC2 GLU A  434  ASP A  451  1                                  18    
HELIX   21 AC3 ASP A  524  ASN A  529  1                                   6    
HELIX   22 AC4 ASP A  531  LEU A  536  1                                   6    
HELIX   23 AC5 LEU A  536  GLN A  548  1                                  13    
HELIX   24 AC6 GLN A  548  GLY A  554  1                                   7    
HELIX   25 AC7 VAL B   26  SER B   32  1                                   7    
HELIX   26 AC8 ASN B   34  THR B   46  1                                  13    
HELIX   27 AC9 GLU B   48  GLN B   53  1                                   6    
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  THR B  153  1                                  14    
HELIX   31 AD4 VAL B  192  PHE B  203  1                                  12    
HELIX   32 AD5 ASP B  204  SER B  213  1                                  10    
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 ASP B  256  HIS B  260  5                                   5    
HELIX   36 AD9 ALA B  269  SER B  278  1                                  10    
HELIX   37 AE1 ASN B  305  ASN B  316  1                                  12    
HELIX   38 AE2 ILE B  317  SER B  319  5                                   3    
HELIX   39 AE3 ILE B  320  GLY B  327  1                                   8    
HELIX   40 AE4 GLY B  339  LYS B  349  1                                  11    
HELIX   41 AE5 GLY B  358  ALA B  368  1                                  11    
HELIX   42 AE6 ASP B  390  LYS B  406  1                                  17    
HELIX   43 AE7 SER B  408  GLY B  421  1                                  14    
HELIX   44 AE8 GLU B  434  ASP B  451  1                                  18    
HELIX   45 AE9 ASP B  531  GLN B  548  1                                  18    
HELIX   46 AF1 GLN B  548  GLY B  554  1                                   7    
SHEET    1 AA1 8 MET A   1  VAL A   2  0                                        
SHEET    2 AA1 8 GLY A 171  LEU A 177  1  O  ASP A 176   N  VAL A   2           
SHEET    3 AA1 8 PHE A 184  VAL A 189 -1  O  PHE A 184   N  PHE A 175           
SHEET    4 AA1 8 ARG A  85  ILE A  93  1  N  LEU A  86   O  GLU A 187           
SHEET    5 AA1 8 THR A  56  GLY A  61  1  N  GLY A  61   O  GLY A  92           
SHEET    6 AA1 8 GLY A 110  LEU A 114  1  O  ILE A 112   N  VAL A  58           
SHEET    7 AA1 8 ASP A 126  ASN A 132 -1  O  ASN A 132   N  GLY A 111           
SHEET    8 AA1 8 LEU A  22  ARG A  25 -1  N  LYS A  24   O  PHE A 127           
SHEET    1 AA2 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA2 2 GLU A 156  VAL A 159 -1  O  VAL A 159   N  VAL A   5           
SHEET    1 AA3 5 ALA A 248  VAL A 249  0                                        
SHEET    2 AA3 5 ILE A 220  ASP A 223  1  N  ILE A 222   O  VAL A 249           
SHEET    3 AA3 5 PHE A 283  PHE A 287  1  O  ALA A 285   N  ASP A 223           
SHEET    4 AA3 5 ASN A 294  GLY A 298 -1  O  LEU A 297   N  GLY A 284           
SHEET    5 AA3 5 PHE A 303  VAL A 304 -1  O  VAL A 304   N  ILE A 296           
SHEET    1 AA4 4 LEU A 352  THR A 355  0                                        
SHEET    2 AA4 4 PHE A 331  SER A 334  1  N  PHE A 331   O  TYR A 353           
SHEET    3 AA4 4 LEU A 373  GLU A 376  1  O  LEU A 373   N  ALA A 332           
SHEET    4 AA4 4 GLY A 380  SER A 383 -1  O  GLY A 382   N  CYS A 374           
SHEET    1 AA5 7 GLN A 458  SER A 460  0                                        
SHEET    2 AA5 7 VAL A 465  ASN A 473 -1  O  TYR A 466   N  PHE A 459           
SHEET    3 AA5 7 LEU A 490  PHE A 494 -1  O  ILE A 493   N  GLU A 469           
SHEET    4 AA5 7 ARG A 499  LEU A 504 -1  O  ILE A 500   N  LEU A 492           
SHEET    5 AA5 7 ALA A 512  GLU A 522 -1  O  GLN A 515   N  ARG A 503           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  TYR A 428   O  LEU A 516           
SHEET    7 AA5 7 VAL A 560  THR A 562 -1  O  THR A 562   N  ARG A 427           
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  VAL B  58   O  ILE B 112           
SHEET    5 AA8 7 ARG B  85  ILE B  93  1  O  GLY B  92   N  GLY B  61           
SHEET    6 AA8 7 PHE B 184  VAL B 189  1  O  GLU B 187   N  LEU B  86           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  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  LEU B 373   N  ALA B 332           
SHEET    4 AB1 4 GLY B 380  SER B 383 -1  O  GLY B 380   N  GLU B 376           
SHEET    1 AB2 7 GLN B 458  PHE B 459  0                                        
SHEET    2 AB2 7 TYR B 466  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  LYS B 470           
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         OG  SER A 117                CO    CO A 614     1555   1555  2.02  
LINK         OD2 ASP A 288                CO    CO A 614     1555   1555  2.22  
LINK         OD1 ASP A 290                CO    CO A 614     1555   1555  2.38  
LINK         OD2 ASP A 292                CO    CO A 614     1555   1555  2.02  
LINK         OG  SER B 117                CO    CO B 607     1555   1555  1.78  
LINK         OD2 ASP B 288                CO    CO B 607     1555   1555  2.52  
LINK         OD1 ASP B 290                CO    CO B 607     1555   1555  2.15  
LINK         OD2 ASP B 292                CO    CO B 607     1555   1555  2.03  
SITE     1 AC1  4 THR A  19  GLY A 358  TRP A 359  HOH A 712                    
SITE     1 AC2  3 HIS A 118  ARG A 293  ARG A 427                               
SITE     1 AC3  5 TYR A  66  MET A  67  LYS A  68  GLU A  69                    
SITE     2 AC3  5 GLU A 255                                                     
SITE     1 AC4  4 GLY A 259  HIS A 260  HIS A 261  TYR A 268                    
SITE     1 AC5  3 SER A  31  SER A  32  ALA A  33                               
SITE     1 AC6  1 ARG A 555                                                     
SITE     1 AC7  3 PRO A 123  ASN A 124  GLY A 125                               
SITE     1 AC8  2 PRO A 244  ALA A 245                                          
SITE     1 AC9  2 LYS A 470  ARG A 491                                          
SITE     1 AD1  4 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     1 AD2  2 ARG A  85  HOH A 728                                          
SITE     1 AD3  1 HIS A 260                                                     
SITE     1 AD4  4 SER A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     1 AD5  2 ARG B 427  GOL B 606                                          
SITE     1 AD6  7 THR B  19  SER B  20  GLY B 358  TRP B 359                    
SITE     2 AD6  7 LYS B 389  HOH B 702  HOH B 716                               
SITE     1 AD7  3 SER A  -1  ASN A   0  SER B 206                               
SITE     1 AD8  2 PRO B 244  ALA B 245                                          
SITE     1 AD9  2 GLY B  18  THR B  19                                          
SITE     1 AE1  4 ARG B 503  SER B 505  THR B 507  SO4 B 601                    
SITE     1 AE2  4 SER B 117  ASP B 288  ASP B 290  ASP B 292                    
CRYST1  173.960  173.960   99.483  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      0.005748  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005748  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010052        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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