GenomeNet

Database: PDB
Entry: 5TR2
LinkDB: 5TR2
Original site: 5TR2 
HEADER    ISOMERASE                               25-OCT-16   5TR2              
TITLE     CRYSTAL STRUCTURE OF THE D263G 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    ISOMERASE, PHOSPHOHEXOMUTASE, ENZYME                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BEAMER,K.M.STIERS                                                 
REVDAT   4   01-NOV-17 5TR2    1       REMARK                                   
REVDAT   3   29-MAR-17 5TR2    1       JRNL                                     
REVDAT   2   22-FEB-17 5TR2    1       JRNL                                     
REVDAT   1   08-FEB-17 5TR2    0                                                
JRNL        AUTH   K.M.STIERS,A.C.GRAHAM,B.N.KAIN,L.J.BEAMER                    
JRNL        TITL   ASP263 MISSENSE VARIANTS PERTURB THE ACTIVE SITE OF HUMAN    
JRNL        TITL 2 PHOSPHOGLUCOMUTASE 1.                                        
JRNL        REF    FEBS J.                       V. 284   937 2017              
JRNL        REFN                   ISSN 1742-4658                               
JRNL        PMID   28117557                                                     
JRNL        DOI    10.1111/FEBS.14025                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: 000)                            
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.250                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 44106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2208                            
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 51.8554 -  6.2961    1.00     3328   164  0.1991 0.2562        
REMARK   3     2  6.2961 -  4.9987    1.00     3162   168  0.2115 0.2563        
REMARK   3     3  4.9987 -  4.3672    1.00     3094   181  0.1654 0.2424        
REMARK   3     4  4.3672 -  3.9681    1.00     3082   172  0.1777 0.2619        
REMARK   3     5  3.9681 -  3.6837    0.96      354    20  0.1885 0.3345        
REMARK   3     6  3.4666 -  3.2930    0.90     1543    69  0.2462 0.3265        
REMARK   3     7  3.2930 -  3.1497    0.99     3052   140  0.2217 0.2933        
REMARK   3     8  3.1497 -  3.0284    1.00     3065   147  0.2271 0.3285        
REMARK   3     9  3.0284 -  2.9240    1.00     3052   142  0.2327 0.3030        
REMARK   3    10  2.9240 -  2.8325    1.00     3036   169  0.2699 0.3329        
REMARK   3    11  2.8325 -  2.7516    1.00     3029   169  0.2639 0.3684        
REMARK   3    12  2.7516 -  2.6791    1.00     3031   169  0.3012 0.3506        
REMARK   3    13  2.6791 -  2.6138    1.00     3025   147  0.3449 0.4437        
REMARK   3    14  2.6138 -  2.5544    1.00     3044   163  0.2955 0.3702        
REMARK   3    15  2.5544 -  2.5000    1.00     3001   188  0.3051 0.3802        
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.360           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.38                          
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           8193                                  
REMARK   3   ANGLE     :  1.066          11188                                  
REMARK   3   CHIRALITY :  0.064           1267                                  
REMARK   3   PLANARITY :  0.007           1496                                  
REMARK   3   DIHEDRAL  : 14.991           4817                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 183 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  71.5877  34.7319 -22.3558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2296 T22:   0.4788                                     
REMARK   3      T33:   0.3157 T12:  -0.0553                                     
REMARK   3      T13:   0.0681 T23:  -0.1654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1563 L22:   0.2905                                     
REMARK   3      L33:   0.1336 L12:   0.0323                                     
REMARK   3      L13:   0.0442 L23:  -0.0672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0939 S12:  -0.1741 S13:   0.0664                       
REMARK   3      S21:   0.0409 S22:   0.0954 S23:   0.0264                       
REMARK   3      S31:  -0.0805 S32:   0.5768 S33:   0.2806                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 319 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.4891  30.6156 -29.1530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2157 T22:   0.1997                                     
REMARK   3      T33:   0.3249 T12:   0.0452                                     
REMARK   3      T13:   0.0353 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0987 L22:   0.0299                                     
REMARK   3      L33:   0.1714 L12:  -0.0127                                     
REMARK   3      L13:  -0.0974 L23:  -0.0097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0873 S12:   0.1909 S13:   0.1620                       
REMARK   3      S21:  -0.0895 S22:  -0.0471 S23:   0.0457                       
REMARK   3      S31:   0.0462 S32:  -0.0477 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 320 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.3451  19.1055  -8.1033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2690 T22:   0.1812                                     
REMARK   3      T33:   0.2410 T12:   0.0422                                     
REMARK   3      T13:   0.0147 T23:  -0.0447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1969 L22:   0.3513                                     
REMARK   3      L33:   0.2154 L12:  -0.1181                                     
REMARK   3      L13:  -0.1970 L23:  -0.0899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0685 S12:  -0.0160 S13:   0.0489                       
REMARK   3      S21:   0.1458 S22:   0.0372 S23:   0.0243                       
REMARK   3      S31:   0.2974 S32:   0.1087 S33:  -0.0002                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 183 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9803  57.8296 -35.9881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5866 T22:   0.4113                                     
REMARK   3      T33:   0.1888 T12:  -0.1392                                     
REMARK   3      T13:  -0.0950 T23:   0.1167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3322 L22:   0.4529                                     
REMARK   3      L33:   0.1056 L12:  -0.2294                                     
REMARK   3      L13:  -0.1976 L23:   0.1216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2932 S12:  -0.2088 S13:   0.0582                       
REMARK   3      S21:   0.6094 S22:  -0.0757 S23:  -0.3786                       
REMARK   3      S31:   0.3075 S32:  -0.5749 S33:   0.2755                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.9852  65.0805 -44.3457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1958 T22:  -0.3160                                     
REMARK   3      T33:   0.1018 T12:   0.0946                                     
REMARK   3      T13:  -0.1412 T23:  -0.5751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1397 L22:   0.2005                                     
REMARK   3      L33:   0.4349 L12:  -0.1152                                     
REMARK   3      L13:   0.0875 L23:   0.1147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2749 S12:   0.1413 S13:  -0.4200                       
REMARK   3      S21:   0.1939 S22:   0.4250 S23:  -0.4282                       
REMARK   3      S31:   0.3455 S32:   0.1882 S33:   0.8274                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 294 THROUGH 512 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.8858  80.4782 -26.0160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7281 T22:   0.2545                                     
REMARK   3      T33:   0.3587 T12:  -0.0870                                     
REMARK   3      T13:  -0.0664 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6496 L22:   0.0401                                     
REMARK   3      L33:   0.1324 L12:  -0.0798                                     
REMARK   3      L13:  -0.1341 L23:   0.0750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2915 S12:   0.0973 S13:   0.0457                       
REMARK   3      S21:   0.5345 S22:   0.0131 S23:  -0.1534                       
REMARK   3      S31:  -0.0424 S32:   0.0007 S33:   0.1211                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 513 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  54.7317  75.0682 -14.4806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8464 T22:   0.5788                                     
REMARK   3      T33:   0.4856 T12:   0.0106                                     
REMARK   3      T13:  -0.1913 T23:  -0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0025 L22:  -0.0025                                     
REMARK   3      L33:   0.0074 L12:   0.0009                                     
REMARK   3      L13:   0.0101 L23:  -0.0016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:  -0.1754 S13:  -0.0383                       
REMARK   3      S21:   0.2152 S22:   0.1161 S23:  -0.0102                       
REMARK   3      S31:   0.0390 S32:   0.2022 S33:  -0.0000                       
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 5TR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224656.                                   
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                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00001                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION MAY 1, 2016            
REMARK 200                                   BUILT=20160517                     
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44375                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.4                               
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : 0.19400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.02700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5EPC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M NACL,      
REMARK 280  AND 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 292K                                                    
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       49.50250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       86.06200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       86.06200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.75125            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       86.06200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       86.06200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.25375            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       86.06200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.06200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.75125            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       86.06200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.06200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.25375            
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       49.50250            
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 300 REMARK: MONOMER ACCORDING TO DYNAMIC LIGHT SCATTERING AND LITERATURE 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 778  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 779  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     SER A   509                                                      
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     MET B     1                                                      
REMARK 465     GLY B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     ASN B   216                                                      
REMARK 465     LEU B   266                                                      
REMARK 465     THR B   267                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     THR B   507                                                      
REMARK 465     GLY B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A   0    CG   OD1  ND2                                       
REMARK 470     VAL A   2    CG1  CG2                                            
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     ILE A   4    CG1  CG2  CD1                                       
REMARK 470     VAL A   5    CG1  CG2                                            
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     SER A  20    OG                                                  
REMARK 470     LEU A  22    CG   CD1  CD2                                       
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     GLU A  48    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  54    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  69    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     ASN A 124    CG   OD1  ND2                                       
REMARK 470     LYS A 130    CG   CD   CE   NZ                                   
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 154    CG1  CG2  CD1                                       
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     VAL A 186    CG1  CG2                                            
REMARK 470     PRO A 215    CG   CD                                             
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     THR A 267    OG1  CG2                                            
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     LYS A 349    CG   CD   CE   NZ                                   
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     LEU A 448    CG   CD1  CD2                                       
REMARK 470     ASP A 451    CG   OD1  OD2                                       
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     SER A 460    OG                                                  
REMARK 470     ASN A 462    CG   OD1  ND2                                       
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     ILE A 484    CG1  CG2  CD1                                       
REMARK 470     ASN A 487    CG   OD1  ND2                                       
REMARK 470     LEU A 490    CG   CD1  CD2                                       
REMARK 470     THR A 507    OG1  CG2                                            
REMARK 470     LYS A 523    CG   CD   CE   NZ                                   
REMARK 470     GLN A 530    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 545    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   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     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     SER B  20    OG                                                  
REMARK 470     LEU B  22    CG   CD1  CD2                                       
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  26    CG1  CG2                                            
REMARK 470     LYS B  27    CG   CD   CE   NZ                                   
REMARK 470     VAL B  28    CG1  CG2                                            
REMARK 470     SER B  31    OG                                                  
REMARK 470     SER B  42    OG                                                  
REMARK 470     SER B  45    OG                                                  
REMARK 470     VAL B  47    CG1  CG2                                            
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  51    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  53    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     VAL B  59    CG1  CG2                                            
REMARK 470     LEU B  73    CG   CD1  CD2                                       
REMARK 470     LYS B 105    CG   CD   CE   NZ                                   
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ILE B 109    CG1  CG2  CD1                                       
REMARK 470     LEU B 114    CG   CD1  CD2                                       
REMARK 470     ASN B 119    CG   OD1  ND2                                       
REMARK 470     GLU B 141    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 143    CG1  CG2  CD1                                       
REMARK 470     THR B 144    OG1  CG2                                            
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     ILE B 147    CG1  CG2  CD1                                       
REMARK 470     ILE B 150    CG1  CG2  CD1                                       
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     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     LEU B 177    CG   CD1  CD2                                       
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     PHE B 181    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     GLU B 187    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 209    CG   CD   CE   NZ                                   
REMARK 470     GLU B 210    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 212    CG   CD1  CD2                                       
REMARK 470     ARG B 217    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 218    CG   CD1  CD2                                       
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     ARG B 221    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     LYS B 235    CG   CD   CE   NZ                                   
REMARK 470     ASN B 246    CG   OD1  ND2                                       
REMARK 470     VAL B 249    CG1  CG2                                            
REMARK 470     VAL B 252    CG1  CG2                                            
REMARK 470     LEU B 254    CG   CD1  CD2                                       
REMARK 470     ASP B 256    CG   OD1  OD2                                       
REMARK 470     HIS B 260    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS B 261    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR B 268    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 271    CG   OD1  OD2                                       
REMARK 470     LEU B 272    CG   CD1  CD2                                       
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     MET B 276    CG   SD   CE                                        
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     LEU B 297    CG   CD1  CD2                                       
REMARK 470     LYS B 299    CG   CD   CE   NZ                                   
REMARK 470     SER B 307    OG                                                  
REMARK 470     GLN B 325    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 346    OG                                                  
REMARK 470     THR B 348    OG1  CG2                                            
REMARK 470     LYS B 349    CG   CD   CE   NZ                                   
REMARK 470     ILE B 350    CG1  CG2  CD1                                       
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     LEU B 402    CG   CD1  CD2                                       
REMARK 470     LYS B 406    CG   CD   CE   NZ                                   
REMARK 470     SER B 408    OG                                                  
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     THR B 426    OG1  CG2                                            
REMARK 470     GLU B 431    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 432    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 433    CG1  CG2                                            
REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 440    CG   CD   CE   NZ                                   
REMARK 470     LYS B 443    CG   CD   CE   NZ                                   
REMARK 470     ASP B 444    CG   OD1  OD2                                       
REMARK 470     LEU B 445    CG   CD1  CD2                                       
REMARK 470     MET B 449    CG   SD   CE                                        
REMARK 470     PHE B 450    CG   CD1  CD2  CE1  CE2  CZ                         
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     ASP B 463    CG   OD1  OD2                                       
REMARK 470     LYS B 464    CG   CD   CE   NZ                                   
REMARK 470     VAL B 465    CG1  CG2                                            
REMARK 470     THR B 467    OG1  CG2                                            
REMARK 470     VAL B 468    CG1  CG2                                            
REMARK 470     LYS B 470    CG   CD   CE   NZ                                   
REMARK 470     GLU B 475    CG   CD   OE1  OE2                                  
REMARK 470     SER B 477    OG                                                  
REMARK 470     VAL B 480    CG1  CG2                                            
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 490    CG   CD1  CD2                                       
REMARK 470     LEU B 504    CG   CD1  CD2                                       
REMARK 470     SER B 505    OG                                                  
REMARK 470     THR B 513    OG1  CG2                                            
REMARK 470     ILE B 514    CG1  CG2  CD1                                       
REMARK 470     LEU B 516    CG   CD1  CD2                                       
REMARK 470     ILE B 518    CG1  CG2  CD1                                       
REMARK 470     SER B 520    OG                                                  
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     ASP B 524    CG   OD1  OD2                                       
REMARK 470     VAL B 525    CG1  CG2                                            
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     GLN B 530    CG   CD   OE1  NE2                                  
REMARK 470     PRO B 532    CG   CD                                             
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     MET B 535    CG   SD   CE                                        
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     SER B 541    OG                                                  
REMARK 470     ILE B 542    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     THR B 553    OG1  CG2                                            
REMARK 470     THR B 556    OG1  CG2                                            
REMARK 470     VAL B 560    CG1  CG2                                            
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   OD1  ASP A   367     NH2  ARG A   387              1.95            
REMARK 500   OG   SER A   505     OG1  THR A   513              2.11            
REMARK 500   O    HOH A   747     O    HOH A   818              2.14            
REMARK 500   OD2  ASP A    62     NH1  ARG A    64              2.14            
REMARK 500   NE   ARG A   387     O    HOH A   701              2.14            
REMARK 500   O    HOH B   714     O    HOH B   751              2.14            
REMARK 500   O    HOH A   724     O    HOH A   753              2.18            
REMARK 500   O    HOH B   733     O    HOH B   769              2.18            
REMARK 500   OH   TYR A   476     O    HOH A   702              2.19            
REMARK 500   NH2  ARG B    76     O    HOH B   701              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 420   CE1   TYR B 420   CZ     -0.084                       
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  73   CB  -  CG  -  CD1 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    LEU B 211   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  66       -2.07     89.58                                   
REMARK 500    SEP A 117     -122.82     54.32                                   
REMARK 500    ILE A 133     -165.10   -104.55                                   
REMARK 500    ILE A 154      109.51    -38.72                                   
REMARK 500    PRO A 262       48.96    -74.53                                   
REMARK 500    ALA A 269       32.23    -95.96                                   
REMARK 500    SER A 378       46.36    -94.13                                   
REMARK 500    ASN A 462       -5.97    -52.96                                   
REMARK 500    ASP A 463      -60.22   -151.05                                   
REMARK 500    ALA A 471      115.14   -163.82                                   
REMARK 500    VAL A 480      -80.42   -124.97                                   
REMARK 500    TYR B  12     -154.07    -87.71                                   
REMARK 500    GLN B  13      -21.02   -154.61                                   
REMARK 500    ASP B  14       52.16   -105.75                                   
REMARK 500    SER B  31      -70.90    -63.48                                   
REMARK 500    PHE B  65      150.50    -45.77                                   
REMARK 500    TYR B  66       -1.36     72.63                                   
REMARK 500    TYR B  66       -1.77     72.63                                   
REMARK 500    SEP B 117     -127.99     62.44                                   
REMARK 500    ILE B 133     -167.31   -101.32                                   
REMARK 500    CYS B 238      -68.18    -93.53                                   
REMARK 500    ASN B 250       47.77     71.55                                   
REMARK 500    PHE B 257       19.27     52.51                                   
REMARK 500    PRO B 262       38.31    -82.52                                   
REMARK 500    ALA B 269       30.47    -85.18                                   
REMARK 500    HIS B 300       -6.94     56.59                                   
REMARK 500    SER B 369       34.95     74.75                                   
REMARK 500    ARG B 387       40.15    -98.36                                   
REMARK 500    GLU B 432       71.85     59.51                                   
REMARK 500    ALA B 435      -71.43    -51.94                                   
REMARK 500    SER B 460     -169.95   -129.09                                   
REMARK 500    ALA B 461      142.26     79.22                                   
REMARK 500    VAL B 480      -57.94   -127.18                                   
REMARK 500    VAL B 525       -4.41    -56.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 778        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH B 779        DISTANCE =  7.78 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                              CA A 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP A 117   OG                                                     
REMARK 620 2 SEP A 117   O1P  59.7                                              
REMARK 620 3 ASP A 288   OD2  89.3 118.6                                        
REMARK 620 4 ASP A 290   OD1  97.6 145.8  83.3                                  
REMARK 620 5 ASP A 290   OD2 102.2 110.0 128.7  45.9                            
REMARK 620 6 ASP A 292   OD1 130.6  71.3 121.3 121.8  88.1                      
REMARK 620 7 ASP A 292   OD2 169.7 128.4  81.0  77.8  81.4  58.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP B 117   OG                                                     
REMARK 620 2 SEP B 117   O1P  55.3                                              
REMARK 620 3 ASP B 288   OD2  87.9 131.0                                        
REMARK 620 4 ASP B 290   OD1 107.6 143.1  72.7                                  
REMARK 620 5 ASP B 290   OD2  91.4  93.6 120.9  51.5                            
REMARK 620 6 ASP B 292   OD1 143.2  93.8 128.9  84.9  69.1                      
REMARK 620 7 ASP B 292   OD2 147.0 113.2  79.2  97.4 121.4  58.5                
REMARK 620 N                    1     2     3     4     5     6                 
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 CA A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 602                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
REMARK 900 WT ENZYME                                                            
REMARK 900 RELATED ID: 5F9C   RELATED DB: PDB                                   
REMARK 900 MISSENSE MUTANT OF WT                                                
REMARK 900 RELATED ID: 5HSH   RELATED DB: PDB                                   
REMARK 900 MISSENSE MUTANT OF WT                                                
REMARK 900 RELATED ID: 5JN5   RELATED DB: PDB                                   
REMARK 900 MISSENSE MUTANT OF WT AT SAME POSITION AS CURRENT ENTRY              
DBREF  5TR2 A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5TR2 B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5TR2 MET A  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS A  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS A  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS A  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS A  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS A  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS A  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 SER A  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 SER A  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLY A  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 VAL A  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 ASP A  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 LEU A  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLY A   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 THR A   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLU A   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 ASN A   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 LEU A   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 TYR A   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 PHE A   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLN A   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLY A  263  UNP  P36871    ASP   263 CONFLICT                       
SEQADV 5TR2 MET B  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS B  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS B  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS B  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS B  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS B  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 HIS B  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 SER B  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 SER B  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLY B  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 VAL B  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 ASP B  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 LEU B  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLY B   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 THR B   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLU B   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 ASN B   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 LEU B   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 TYR B   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 PHE B   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLN B   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5TR2 GLY B  263  UNP  P36871    ASP   263 CONFLICT                       
SEQRES   1 A  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 A  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 A  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 A  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 A  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 A  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 A  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 A  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 A  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 A  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SEP HIS ASN PRO          
SEQRES  12 A  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 A  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 A  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 A  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 A  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 A  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 A  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 A  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 A  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 A  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 A  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO GLY          
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 ARG LEU TYR ILE ASP SER TYR GLU LYS          
SEQRES  43 A  585  ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU          
SEQRES  44 A  585  ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU          
SEQRES  45 A  585  GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR          
SEQRES   1 B  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 B  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 B  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 B  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 B  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 B  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 B  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 B  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 B  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 B  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SEP HIS ASN PRO          
SEQRES  12 B  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 B  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 B  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 B  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 B  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 B  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 B  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 B  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 B  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 B  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 B  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO GLY          
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 ARG LEU TYR ILE ASP SER TYR GLU LYS          
SEQRES  43 B  585  ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU          
SEQRES  44 B  585  ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU          
SEQRES  45 B  585  GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR          
MODRES 5TR2 SEP A  117  SER  MODIFIED RESIDUE                                   
MODRES 5TR2 SEP B  117  SER  MODIFIED RESIDUE                                   
HET    SEP  A 117      10                                                       
HET    SEP  B 117      10                                                       
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET     CA  A 604       1                                                       
HET    GOL  A 605       6                                                       
HET    SO4  B 601       5                                                       
HET     CA  B 602       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   6   CA    2(CA 2+)                                                     
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *204(H2 O)                                                    
HELIX    1 AA1 VAL A   26  SER A   32  1                                   7    
HELIX    2 AA2 ASN A   34  SER A   45  1                                  12    
HELIX    3 AA3 THR A   46  VAL A   47  5                                   2    
HELIX    4 AA4 GLU A   48  ARG A   52  5                                   5    
HELIX    5 AA5 TYR A   66  ASN A   81  1                                  16    
HELIX    6 AA6 SER A   95  ILE A  106  1                                  12    
HELIX    7 AA7 PRO A  140  ILE A  154  1                                  15    
HELIX    8 AA8 VAL A  192  PHE A  203  1                                  12    
HELIX    9 AA9 ASP A  204  SER A  213  1                                  10    
HELIX   10 AB1 VAL A  228  LEU A  237  1                                  10    
HELIX   11 AB2 PRO A  244  ASN A  246  5                                   3    
HELIX   12 AB3 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  531  GLN A  548  1                                  18    
HELIX   22 AC4 GLN A  548  GLY A  554  1                                   7    
HELIX   23 AC5 VAL B   26  SER B   31  1                                   6    
HELIX   24 AC6 ASN B   34  SER B   45  1                                  12    
HELIX   25 AC7 THR B   46  VAL B   47  5                                   2    
HELIX   26 AC8 GLU B   48  ARG B   52  5                                   5    
HELIX   27 AC9 TYR B   66  ASN B   81  1                                  16    
HELIX   28 AD1 SER B   95  LYS B  107  1                                  13    
HELIX   29 AD2 PRO B  140  THR B  153  1                                  14    
HELIX   30 AD3 VAL B  192  PHE B  203  1                                  12    
HELIX   31 AD4 ASP B  204  LEU B  212  1                                   9    
HELIX   32 AD5 VAL B  229  LEU B  237  1                                   9    
HELIX   33 AD6 PRO B  244  ASN B  246  5                                   3    
HELIX   34 AD7 ASP B  256  HIS B  260  5                                   5    
HELIX   35 AD8 ALA B  269  SER B  278  1                                  10    
HELIX   36 AD9 ASN B  305  ASN B  316  1                                  12    
HELIX   37 AE1 ILE B  317  SER B  319  5                                   3    
HELIX   38 AE2 ILE B  320  GLY B  327  1                                   8    
HELIX   39 AE3 GLY B  339  LYS B  349  1                                  11    
HELIX   40 AE4 GLY B  358  ALA B  368  1                                  11    
HELIX   41 AE5 ASP B  390  ARG B  405  1                                  16    
HELIX   42 AE6 SER B  408  GLY B  421  1                                  14    
HELIX   43 AE7 GLU B  434  ASP B  451  1                                  18    
HELIX   44 AE8 ASP B  531  GLN B  548  1                                  18    
HELIX   45 AE9 GLN B  548  GLY B  554  1                                   7    
SHEET    1 AA1 8 MET A   1  VAL A   2  0                                        
SHEET    2 AA1 8 GLY A 171  LEU A 177  1  O  ASP A 176   N  VAL A   2           
SHEET    3 AA1 8 PHE A 184  VAL A 189 -1  O  PHE A 184   N  PHE A 175           
SHEET    4 AA1 8 ARG A  85  ILE A  93  1  N  LEU A  86   O  GLU A 187           
SHEET    5 AA1 8 THR A  56  GLY A  61  1  N  LEU A  57   O  VAL A  87           
SHEET    6 AA1 8 GLY A 110  LEU A 114  1  O  LEU A 114   N  GLY A  60           
SHEET    7 AA1 8 ASP A 126  ILE A 133 -1  O  LYS A 130   N  ILE A 113           
SHEET    8 AA1 8 LEU A  22  ARG A  25 -1  N  LYS A  24   O  PHE A 127           
SHEET    1 AA2 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA2 2 GLU A 156  VAL A 159 -1  O  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 380   N  GLU A 376           
SHEET    1 AA5 7 GLN A 458  SER A 460  0                                        
SHEET    2 AA5 7 VAL A 465  ASN A 473 -1  O  TYR A 466   N  PHE A 459           
SHEET    3 AA5 7 LEU A 490  PHE A 494 -1  O  ILE A 493   N  GLU A 469           
SHEET    4 AA5 7 ARG A 499  LEU A 504 -1  O  ILE A 500   N  LEU A 492           
SHEET    5 AA5 7 ALA A 512  GLU A 522 -1  O  TYR A 517   N  VAL A 501           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  TYR A 430   O  ILE A 514           
SHEET    7 AA5 7 VAL A 560  THR A 562 -1  O  VAL A 560   N  ASP A 429           
SHEET    1 AA6 2 TYR A 476  SER A 477  0                                        
SHEET    2 AA6 2 ILE A 484  SER A 485 -1  O  SER A 485   N  TYR A 476           
SHEET    1 AA7 2 VAL B   5  LYS B   8  0                                        
SHEET    2 AA7 2 GLU B 156  VAL B 159 -1  O  VAL B 159   N  VAL B   5           
SHEET    1 AA8 7 LEU B  22  ARG B  25  0                                        
SHEET    2 AA8 7 ASP B 126  ILE B 133 -1  O  PHE B 127   N  LYS B  24           
SHEET    3 AA8 7 GLY B 110  LEU B 114 -1  N  GLY B 111   O  ASN B 132           
SHEET    4 AA8 7 THR B  56  GLY B  61  1  N  GLY B  60   O  LEU B 114           
SHEET    5 AA8 7 ARG B  85  ILE B  93  1  O  VAL B  87   N  LEU B  57           
SHEET    6 AA8 7 PHE B 184  VAL B 189  1  O  GLU B 187   N  ILE B  88           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  GLN B 173   O  VAL B 186           
SHEET    1 AA9 5 ALA B 248  VAL B 249  0                                        
SHEET    2 AA9 5 ILE B 220  ASP B 223  1  N  ILE B 222   O  VAL B 249           
SHEET    3 AA9 5 PHE B 283  PHE B 287  1  O  ALA B 285   N  ASP B 223           
SHEET    4 AA9 5 ASN B 294  GLY B 298 -1  O  LEU B 297   N  GLY B 284           
SHEET    5 AA9 5 PHE B 302  VAL B 304 -1  O  PHE B 302   N  GLY B 298           
SHEET    1 AB1 4 LEU B 352  THR B 355  0                                        
SHEET    2 AB1 4 PHE B 331  SER B 334  1  N  ARG B 333   O  THR B 355           
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  LYS B 470 -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  SER B 505 -1  O  PHE B 502   N  LEU B 490           
SHEET    5 AB2 7 THR B 513  GLU B 522 -1  O  THR B 513   N  SER B 505           
SHEET    6 AB2 7 ARG B 422  TYR B 430 -1  N  TYR B 430   O  ILE B 514           
SHEET    7 AB2 7 VAL B 560  THR B 562 -1  O  VAL B 560   N  ASP B 429           
SHEET    1 AB3 2 TYR B 476  SER B 477  0                                        
SHEET    2 AB3 2 ILE B 484  SER B 485 -1  O  SER B 485   N  TYR B 476           
LINK         C   ALA A 116                 N   SEP A 117     1555   1555  1.33  
LINK         OG  SEP A 117                CA    CA A 604     1555   1555  2.88  
LINK         C   SEP A 117                 N   HIS A 118     1555   1555  1.33  
LINK         O1P SEP A 117                CA    CA A 604     1555   1555  2.25  
LINK         OD2 ASP A 288                CA    CA A 604     1555   1555  2.13  
LINK         OD1 ASP A 290                CA    CA A 604     1555   1555  2.27  
LINK         OD2 ASP A 290                CA    CA A 604     1555   1555  3.07  
LINK         OD1 ASP A 292                CA    CA A 604     1555   1555  2.44  
LINK         OD2 ASP A 292                CA    CA A 604     1555   1555  2.05  
LINK         OE1 GLU A 377                 NH1 ARG A 427     1555   1555  1.27  
LINK         C   ALA B 116                 N   SEP B 117     1555   1555  1.33  
LINK         OG  SEP B 117                CA    CA B 602     1555   1555  3.11  
LINK         C   SEP B 117                 N   HIS B 118     1555   1555  1.34  
LINK         O1P SEP B 117                CA    CA B 602     1555   1555  2.51  
LINK         OD2 ASP B 288                CA    CA B 602     1555   1555  2.19  
LINK         OD1 ASP B 290                CA    CA B 602     1555   1555  2.43  
LINK         OD2 ASP B 290                CA    CA B 602     1555   1555  2.64  
LINK         OD1 ASP B 292                CA    CA B 602     1555   1555  2.18  
LINK         OD2 ASP B 292                CA    CA B 602     1555   1555  2.25  
CISPEP   1 ALA B  461    ASN B  462          0        -6.19                     
SITE     1 AC1  5 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     2 AC1  5 HOH A 760                                                     
SITE     1 AC2  3 ARG A 503  SER A 505  ARG A 515                               
SITE     1 AC3  4 GLY A 259  HIS A 260  HIS A 261  HOH A 737                    
SITE     1 AC4  4 SEP A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     1 AC5  5 THR A  19  GLY A 358  TRP A 359  GLU A 376                    
SITE     2 AC5  5 HOH A 813                                                     
SITE     1 AC6  3 ARG B 503  SER B 505  ARG B 515                               
SITE     1 AC7  4 SEP B 117  ASP B 288  ASP B 290  ASP B 292                    
CRYST1  172.124  172.124   99.005  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      0.005810  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010100        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system