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Database: PDB
Entry: 5EPC
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Original site: 5EPC 
HEADER    ISOMERASE                               11-NOV-15   5EPC              
TITLE     CRYSTAL STRUCTURE OF WILD-TYPE HUMAN PHOSPHOGLUCOMUTASE 1             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLUCOMUTASE-1;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;                              
COMPND   5 EC: 5.4.2.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PGM1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    ISOMERASE METABOLISM, ISOMERASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BEAMER                                                            
REVDAT   1   27-APR-16 5EPC    0                                                
JRNL        AUTH   K.M.STIERS,B.N.KAIN,A.C.GRAHAM,L.J.BEAMER                    
JRNL        TITL   INDUCED STRUCTURAL DISORDER AS A MOLECULAR MECHANISM FOR     
JRNL        TITL 2 ENZYME DYSFUNCTION IN PHOSPHOGLUCOMUTASE 1 DEFICIENCY.       
JRNL        REF    J.MOL.BIOL.                   V. 428  1493 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   26972339                                                     
JRNL        DOI    10.1016/J.JMB.2016.02.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.920                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 127879                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6404                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 61.0840 -  5.7468    1.00     4374   229  0.1762 0.1958        
REMARK   3     2  5.7468 -  4.5619    1.00     4171   227  0.1451 0.1750        
REMARK   3     3  4.5619 -  3.9854    1.00     4138   207  0.1329 0.1490        
REMARK   3     4  3.9854 -  3.6210    1.00     4108   227  0.1346 0.1620        
REMARK   3     5  3.6210 -  3.3615    1.00     4091   220  0.1509 0.1610        
REMARK   3     6  3.3615 -  3.1633    1.00     4074   209  0.1633 0.2077        
REMARK   3     7  3.1633 -  3.0049    1.00     4071   217  0.1710 0.2006        
REMARK   3     8  3.0049 -  2.8741    1.00     4053   215  0.1792 0.2084        
REMARK   3     9  2.8741 -  2.7635    1.00     4078   198  0.1682 0.2023        
REMARK   3    10  2.7635 -  2.6681    1.00     4023   231  0.1657 0.1977        
REMARK   3    11  2.6681 -  2.5847    1.00     3993   237  0.1697 0.2028        
REMARK   3    12  2.5847 -  2.5108    1.00     4054   201  0.1706 0.2073        
REMARK   3    13  2.5108 -  2.4447    1.00     4009   244  0.1674 0.2087        
REMARK   3    14  2.4447 -  2.3851    1.00     4063   197  0.1732 0.2210        
REMARK   3    15  2.3851 -  2.3308    1.00     4024   195  0.1734 0.1991        
REMARK   3    16  2.3308 -  2.2812    1.00     4032   225  0.1700 0.2233        
REMARK   3    17  2.2812 -  2.2356    1.00     4006   221  0.1781 0.2087        
REMARK   3    18  2.2356 -  2.1934    1.00     3978   232  0.1810 0.2063        
REMARK   3    19  2.1934 -  2.1542    1.00     4054   205  0.1816 0.2150        
REMARK   3    20  2.1542 -  2.1177    1.00     4009   202  0.1938 0.2212        
REMARK   3    21  2.1177 -  2.0836    1.00     3993   237  0.1987 0.2113        
REMARK   3    22  2.0836 -  2.0515    1.00     3995   221  0.2029 0.2375        
REMARK   3    23  2.0515 -  2.0213    1.00     4034   192  0.2090 0.1962        
REMARK   3    24  2.0213 -  1.9929    1.00     4000   199  0.2111 0.2424        
REMARK   3    25  1.9929 -  1.9659    1.00     4029   201  0.2189 0.2370        
REMARK   3    26  1.9659 -  1.9404    1.00     3979   198  0.2346 0.2767        
REMARK   3    27  1.9404 -  1.9161    1.00     4020   208  0.2436 0.3017        
REMARK   3    28  1.9161 -  1.8930    1.00     4015   219  0.2514 0.2763        
REMARK   3    29  1.8930 -  1.8710    1.00     3994   207  0.2802 0.3180        
REMARK   3    30  1.8710 -  1.8500    1.00     4013   183  0.3087 0.3512        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.360           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           8754                                  
REMARK   3   ANGLE     :  0.998          11884                                  
REMARK   3   CHIRALITY :  0.043           1344                                  
REMARK   3   PLANARITY :  0.005           1543                                  
REMARK   3   DIHEDRAL  : 12.381           3149                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5064 -73.5023   5.4307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3668 T22:   0.1739                                     
REMARK   3      T33:   0.1951 T12:   0.0335                                     
REMARK   3      T13:   0.0154 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8485 L22:   3.5741                                     
REMARK   3      L33:   2.1581 L12:  -0.1059                                     
REMARK   3      L13:   0.0615 L23:  -0.1659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0617 S12:  -0.0994 S13:  -0.2010                       
REMARK   3      S21:   0.2343 S22:   0.1234 S23:  -0.0458                       
REMARK   3      S31:   0.5642 S32:   0.1731 S33:  -0.0609                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 405 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2354 -53.5527  -0.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1658 T22:   0.1711                                     
REMARK   3      T33:   0.1833 T12:  -0.0634                                     
REMARK   3      T13:   0.0049 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7125 L22:   1.2354                                     
REMARK   3      L33:   1.4819 L12:  -0.3764                                     
REMARK   3      L13:  -0.1070 L23:   0.6518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0478 S12:   0.0097 S13:  -0.0033                       
REMARK   3      S21:  -0.1047 S22:   0.0681 S23:  -0.0488                       
REMARK   3      S31:   0.0572 S32:  -0.0328 S33:  -0.0142                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7381 -40.6069  23.9638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1431 T22:   0.2523                                     
REMARK   3      T33:   0.2202 T12:   0.0236                                     
REMARK   3      T13:  -0.0102 T23:  -0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7132 L22:   1.2084                                     
REMARK   3      L33:   2.7930 L12:   0.5851                                     
REMARK   3      L13:   0.5092 L23:   0.0209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0118 S12:  -0.3803 S13:   0.0580                       
REMARK   3      S21:   0.0893 S22:  -0.0439 S23:   0.0896                       
REMARK   3      S31:  -0.0223 S32:  -0.3858 S33:   0.0129                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 405 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9489 -50.7931 -11.2099              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2024 T22:   0.5008                                     
REMARK   3      T33:   0.2295 T12:   0.0685                                     
REMARK   3      T13:  -0.0651 T23:   0.0939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8472 L22:   1.8909                                     
REMARK   3      L33:   3.0365 L12:   1.2051                                     
REMARK   3      L13:  -1.4603 L23:  -1.5716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1214 S12:   0.5224 S13:   0.2241                       
REMARK   3      S21:  -0.1436 S22:   0.4984 S23:   0.2588                       
REMARK   3      S31:   0.0623 S32:  -0.6936 S33:  -0.1608                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 406 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1031 -37.1641 -33.9869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3556 T22:   0.6006                                     
REMARK   3      T33:   0.3207 T12:   0.0186                                     
REMARK   3      T13:   0.0299 T23:   0.1120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3254 L22:   2.8937                                     
REMARK   3      L33:   4.9075 L12:  -0.0428                                     
REMARK   3      L13:   0.3060 L23:   0.9392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1133 S12:   0.5879 S13:   0.1909                       
REMARK   3      S21:  -0.4496 S22:   0.1020 S23:  -0.0416                       
REMARK   3      S31:  -0.4510 S32:  -0.2351 S33:  -0.1408                       
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 5EPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215225.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5-8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00001                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 150855                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.051                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 32.50                              
REMARK 200  R MERGE                    (I) : 0.16300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 27.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 3.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3PMG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM OR AMMONIUM SULFATE (1.35 -      
REMARK 280  1.85 M) WITH 0.1 M TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.89000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       86.29500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       86.29500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.94500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       86.29500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       86.29500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.83500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       86.29500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.29500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.94500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       86.29500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.29500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.83500            
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       49.89000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A1218  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     THR A   507                                                      
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     GLY B   506                                                      
REMARK 465     THR B   507                                                      
REMARK 465     GLY B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 465     ALA B   510                                                      
REMARK 465     GLY B   511                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A  -1    OG                                                  
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     PRO A 215    CG   CD                                             
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     ASN B   0    CG   OD1  ND2                                       
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     GLN B  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  27    CG   CD   CE   NZ                                   
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     GLU B 155    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     ASN B 179    CG   OD1  ND2                                       
REMARK 470     LYS B 180    CG   CD   CE   NZ                                   
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     PRO B 215    CG   CD                                             
REMARK 470     ASN B 216    CG   OD1  ND2                                       
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 432    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 440    CG   CD   CE   NZ                                   
REMARK 470     LYS B 443    CG   CD   CE   NZ                                   
REMARK 470     ARG B 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 457    CG   CD   CE   NZ                                   
REMARK 470     ASP B 463    CG   OD1  OD2                                       
REMARK 470     LYS B 464    CG   CD   CE   NZ                                   
REMARK 470     VAL B 465    CG1  CG2                                            
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1028     O    HOH B   918              1.81            
REMARK 500   O    HOH B   947     O    HOH B   954              1.87            
REMARK 500   O    HOH B   853     O    HOH B   952              1.89            
REMARK 500   O    HOH A   863     O    HOH A   893              1.90            
REMARK 500   O    HOH B   741     O    HOH B   945              1.94            
REMARK 500   O    HOH A   856     O    HOH A  1115              1.95            
REMARK 500   O    HOH B   939     O    HOH B   943              1.95            
REMARK 500   O    HOH A  1019     O    HOH A  1177              1.98            
REMARK 500   OE1  GLN A   324     O    HOH A   701              2.01            
REMARK 500   O    HOH B   762     O    HOH B   766              2.02            
REMARK 500   O    HOH B   949     O    HOH B   972              2.06            
REMARK 500   O3   GOL A   607     O    HOH A   702              2.06            
REMARK 500   O    HOH B   830     O    HOH B   894              2.09            
REMARK 500   O    HOH A  1056     O    HOH A  1212              2.12            
REMARK 500   O    TYR B   268     O    HOH B   701              2.14            
REMARK 500   O    HOH B   842     O    HOH B   936              2.14            
REMARK 500   O    HOH A   802     O    HOH A  1039              2.15            
REMARK 500   OG1  THR B   495     O    HOH B   702              2.15            
REMARK 500   O    ALA A   461     O    HOH A   703              2.15            
REMARK 500   O    HOH B   846     O    HOH B   887              2.15            
REMARK 500   O    HOH B   855     O    HOH B   948              2.16            
REMARK 500   OE2  GLU B   376     O    HOH B   703              2.16            
REMARK 500   O    HOH A  1195     O    HOH A  1237              2.17            
REMARK 500   O    HOH A  1150     O    HOH A  1187              2.17            
REMARK 500   NZ   LYS B   370     O    HOH B   704              2.17            
REMARK 500   OD1  ASP A   176     O    HOH A   704              2.17            
REMARK 500   O    GLY A   511     O    HOH A   705              2.18            
REMARK 500   O    HOH A   763     O    HOH A  1172              2.18            
REMARK 500   OE1  GLU B   475     O    HOH B   705              2.18            
REMARK 500   O    HOH A  1201     O    HOH A  1204              2.19            
REMARK 500   O    HOH A   948     O    HOH A  1099              2.19            
REMARK 500   O    HOH B   886     O    HOH B   940              2.19            
REMARK 500   O    HOH A   978     O    HOH B   934              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   866     O    HOH A  1016     8555     2.05            
REMARK 500   O    HOH B   732     O    HOH B   759     3445     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  34       19.45     59.53                                   
REMARK 500    TYR A  66       -6.60     85.35                                   
REMARK 500    ASN A  91       15.62     59.80                                   
REMARK 500    SER A 117     -113.22     57.88                                   
REMARK 500    ILE A 133     -164.26   -108.92                                   
REMARK 500    ALA A 269       41.20   -104.11                                   
REMARK 500    SER A 378       47.59    -82.82                                   
REMARK 500    ASN A 462     -169.72   -109.66                                   
REMARK 500    ASP A 463      -56.02     70.36                                   
REMARK 500    MET B   1       49.54   -103.70                                   
REMARK 500    TYR B  66      -10.43     84.02                                   
REMARK 500    SER B 117     -110.02     60.72                                   
REMARK 500    ILE B 133     -167.73   -106.29                                   
REMARK 500    ILE B 236      -62.00    -91.21                                   
REMARK 500    SER B 378       49.23    -82.68                                   
REMARK 500    ASN B 462     -124.16     60.99                                   
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 A1241        DISTANCE =  6.17 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 117   OG                                                     
REMARK 620 2 ASP A 288   OD2  89.7                                              
REMARK 620 3 ASP A 290   OD1  89.9  98.4                                        
REMARK 620 4 ASP A 292   OD1 165.5  97.5 101.4                                  
REMARK 620 5 HOH A 771   O    80.6 167.7  89.2  90.5                            
REMARK 620 6 HOH A 878   O    79.2  94.6 163.1  87.6  76.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 117   OG                                                     
REMARK 620 2 ASP B 288   OD2  93.5                                              
REMARK 620 3 ASP B 290   OD1  93.6  88.1                                        
REMARK 620 4 ASP B 292   OD1 167.3  92.6  97.7                                  
REMARK 620 5 HOH B 851   O    82.5  93.9 175.7  86.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 608                 
DBREF  5EPC A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5EPC B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5EPC MET A  -22  UNP  P36871              INITIATING METHIONINE          
SEQADV 5EPC HIS A  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS A  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS A  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS A  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS A  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS A  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC SER A  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC SER A  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLY A  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC VAL A  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC ASP A  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC LEU A  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLY A   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC THR A   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLU A   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC ASN A   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC LEU A   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC TYR A   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC PHE A   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLN A   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC MET B  -22  UNP  P36871              INITIATING METHIONINE          
SEQADV 5EPC HIS B  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS B  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS B  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS B  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS B  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC HIS B  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC SER B  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC SER B  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLY B  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC VAL B  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC ASP B  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC LEU B  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLY B   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC THR B   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLU B   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC ASN B   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC LEU B   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC TYR B   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC PHE B   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC GLN B   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5EPC ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQRES   1 A  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 A  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 A  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 A  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 A  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 A  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 A  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 A  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 A  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 A  585  ALA ILE GLY GLY ILE ILE LEU THR ALA SER HIS ASN PRO          
SEQRES  12 A  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 A  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 A  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 A  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 A  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 A  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 A  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 A  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 A  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 A  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 A  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP          
SEQRES  23 A  585  PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET          
SEQRES  24 A  585  LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY          
SEQRES  25 A  585  ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE          
SEQRES  26 A  585  PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA          
SEQRES  27 A  585  ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL          
SEQRES  28 A  585  ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU          
SEQRES  29 A  585  ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU          
SEQRES  30 A  585  THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP          
SEQRES  31 A  585  ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY          
SEQRES  32 A  585  THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP          
SEQRES  33 A  585  ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS          
SEQRES  34 A  585  GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS          
SEQRES  35 A  585  TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU          
SEQRES  36 A  585  VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU          
SEQRES  37 A  585  GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN          
SEQRES  38 A  585  PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA          
SEQRES  39 A  585  ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE          
SEQRES  40 A  585  SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY          
SEQRES  41 A  585  SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA          
SEQRES  42 A  585  GLY ALA THR ILE 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 SER HIS ASN PRO          
SEQRES  12 B  585  GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE          
SEQRES  13 B  585  SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS          
SEQRES  14 B  585  ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL          
SEQRES  15 B  585  CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS          
SEQRES  16 B  585  GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR          
SEQRES  17 B  585  VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET          
SEQRES  18 B  585  LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU          
SEQRES  19 B  585  LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA          
SEQRES  20 B  585  MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU          
SEQRES  21 B  585  CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN          
SEQRES  22 B  585  CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP          
SEQRES  23 B  585  PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET          
SEQRES  24 B  585  LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY          
SEQRES  25 B  585  ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE          
SEQRES  26 B  585  PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA          
SEQRES  27 B  585  ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL          
SEQRES  28 B  585  ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU          
SEQRES  29 B  585  ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU          
SEQRES  30 B  585  THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP          
SEQRES  31 B  585  ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY          
SEQRES  32 B  585  THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP          
SEQRES  33 B  585  ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS          
SEQRES  34 B  585  GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS          
SEQRES  35 B  585  TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU          
SEQRES  36 B  585  VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU          
SEQRES  37 B  585  GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN          
SEQRES  38 B  585  PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA          
SEQRES  39 B  585  ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE          
SEQRES  40 B  585  SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY          
SEQRES  41 B  585  SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA          
SEQRES  42 B  585  GLY ALA THR ILE 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          
HET     MG  A 601       1                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    GOL  A 607       6                                                       
HET    GOL  A 608       6                                                       
HET    GOL  A 609       6                                                       
HET    GOL  A 610       6                                                       
HET    GOL  A 611       6                                                       
HET     MG  B 601       1                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET    SO4  B 604       5                                                       
HET    GOL  B 605       6                                                       
HET    GOL  B 606       6                                                       
HET    GOL  B 607       6                                                       
HET    GOL  B 608       6                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  SO4    8(O4 S 2-)                                                   
FORMUL   9  GOL    9(C3 H8 O3)                                                  
FORMUL  22  HOH   *819(H2 O)                                                    
HELIX    1 AA1 VAL A   26  SER A   32  1                                   7    
HELIX    2 AA2 ASN A   34  SER A   45  1                                  12    
HELIX    3 AA3 THR A   46  VAL A   47  5                                   2    
HELIX    4 AA4 GLU A   48  ARG A   52  5                                   5    
HELIX    5 AA5 TYR A   66  ASN A   81  1                                  16    
HELIX    6 AA6 SER A   95  LYS A  107  1                                  13    
HELIX    7 AA7 PRO A  140  ILE A  154  1                                  15    
HELIX    8 AA8 VAL A  192  PHE A  203  1                                  12    
HELIX    9 AA9 ASP A  204  SER A  213  1                                  10    
HELIX   10 AB1 VAL A  229  LEU A  237  1                                   9    
HELIX   11 AB2 PRO A  244  ASN A  246  5                                   3    
HELIX   12 AB3 ASP A  256  HIS A  260  5                                   5    
HELIX   13 AB4 ALA A  269  SER A  278  1                                  10    
HELIX   14 AB5 ASN A  305  ASN A  316  1                                  12    
HELIX   15 AB6 ILE A  317  SER A  319  5                                   3    
HELIX   16 AB7 ILE A  320  GLY A  327  1                                   8    
HELIX   17 AB8 GLY A  339  LYS A  349  1                                  11    
HELIX   18 AB9 GLY A  358  ALA A  368  1                                  11    
HELIX   19 AC1 ASP A  390  LYS A  406  1                                  17    
HELIX   20 AC2 SER A  408  GLY A  421  1                                  14    
HELIX   21 AC3 GLU A  434  ASP A  451  1                                  18    
HELIX   22 AC4 ASP A  524  ASN A  529  1                                   6    
HELIX   23 AC5 ASP A  531  GLN A  548  1                                  18    
HELIX   24 AC6 GLN A  548  GLY A  554  1                                   7    
HELIX   25 AC7 VAL B   26  SER B   32  1                                   7    
HELIX   26 AC8 ASN B   34  SER B   45  1                                  12    
HELIX   27 AC9 THR B   46  VAL B   47  5                                   2    
HELIX   28 AD1 GLU B   48  ARG B   52  5                                   5    
HELIX   29 AD2 TYR B   66  ASN B   81  1                                  16    
HELIX   30 AD3 SER B   95  LYS B  107  1                                  13    
HELIX   31 AD4 PRO B  140  THR B  153  1                                  14    
HELIX   32 AD5 VAL B  192  PHE B  203  1                                  12    
HELIX   33 AD6 ASP B  204  SER B  213  1                                  10    
HELIX   34 AD7 VAL B  229  LEU B  237  1                                   9    
HELIX   35 AD8 PRO B  244  ASN B  246  5                                   3    
HELIX   36 AD9 ASP B  256  HIS B  260  5                                   5    
HELIX   37 AE1 ALA B  269  SER B  278  1                                  10    
HELIX   38 AE2 ASN B  305  ASN B  316  1                                  12    
HELIX   39 AE3 ILE B  317  SER B  319  5                                   3    
HELIX   40 AE4 ILE B  320  GLY B  327  1                                   8    
HELIX   41 AE5 GLY B  339  ALA B  347  1                                   9    
HELIX   42 AE6 GLY B  358  ALA B  368  1                                  11    
HELIX   43 AE7 ASP B  390  LYS B  406  1                                  17    
HELIX   44 AE8 SER B  408  GLY B  421  1                                  14    
HELIX   45 AE9 GLU B  434  ASP B  451  1                                  18    
HELIX   46 AF1 ASP B  524  ASN B  529  1                                   6    
HELIX   47 AF2 ASP B  531  GLN B  548  1                                  18    
HELIX   48 AF3 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  VAL A 186   N  GLN A 173           
SHEET    4 AA1 8 ARG A  85  ILE A  93  1  N  ILE A  88   O  GLU A 187           
SHEET    5 AA1 8 THR A  56  GLY A  61  1  N  VAL A  59   O  VAL A  87           
SHEET    6 AA1 8 GLY A 110  LEU A 114  1  O  GLY A 110   N  VAL A  58           
SHEET    7 AA1 8 ASP A 126  ILE A 133 -1  O  ASN A 132   N  GLY A 111           
SHEET    8 AA1 8 LEU A  22  ARG A  25 -1  N  LYS A  24   O  PHE A 127           
SHEET    1 AA2 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA2 2 GLU A 156  VAL A 159 -1  O  TYR A 157   N  VAL A   7           
SHEET    1 AA3 5 ALA A 248  VAL A 249  0                                        
SHEET    2 AA3 5 ILE A 220  ASP A 223  1  N  ILE A 222   O  VAL A 249           
SHEET    3 AA3 5 PHE A 283  PHE A 287  1  O  ALA A 285   N  ASP A 223           
SHEET    4 AA3 5 ASN A 294  GLY A 298 -1  O  LEU A 297   N  GLY A 284           
SHEET    5 AA3 5 PHE A 303  VAL A 304 -1  O  VAL A 304   N  ILE A 296           
SHEET    1 AA4 4 LEU A 352  THR A 355  0                                        
SHEET    2 AA4 4 PHE A 331  SER A 334  1  N  PHE A 331   O  TYR A 353           
SHEET    3 AA4 4 LEU A 373  GLU A 376  1  O  LEU A 373   N  ALA A 332           
SHEET    4 AA4 4 GLY A 380  SER A 383 -1  O  GLY A 382   N  CYS A 374           
SHEET    1 AA5 7 GLN A 458  SER A 460  0                                        
SHEET    2 AA5 7 VAL A 465  ASN A 473 -1  O  TYR A 466   N  PHE A 459           
SHEET    3 AA5 7 LEU A 490  PHE A 494 -1  O  ILE A 493   N  LYS A 470           
SHEET    4 AA5 7 ARG A 499  LEU A 504 -1  O  ILE A 500   N  LEU A 492           
SHEET    5 AA5 7 ALA A 512  GLU A 522 -1  O  ARG A 515   N  ARG A 503           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  ARG A 422   O  GLU A 522           
SHEET    7 AA5 7 VAL A 560  THR A 562 -1  O  VAL A 560   N  ASP A 429           
SHEET    1 AA6 2 TYR A 476  SER A 477  0                                        
SHEET    2 AA6 2 ILE A 484  SER A 485 -1  O  SER A 485   N  TYR A 476           
SHEET    1 AA7 2 VAL B   5  LYS B   8  0                                        
SHEET    2 AA7 2 GLU B 156  VAL B 159 -1  O  TYR B 157   N  VAL B   7           
SHEET    1 AA8 7 LEU B  22  ARG B  25  0                                        
SHEET    2 AA8 7 ASP B 126  ILE B 133 -1  O  PHE B 127   N  LYS B  24           
SHEET    3 AA8 7 GLY B 110  LEU B 114 -1  N  ILE B 113   O  LYS B 130           
SHEET    4 AA8 7 THR B  56  GLY B  61  1  N  VAL B  58   O  ILE B 112           
SHEET    5 AA8 7 ARG B  85  ILE B  93  1  O  VAL B  87   N  VAL B  59           
SHEET    6 AA8 7 PHE B 184  VAL B 189  1  O  GLU B 187   N  LEU B  86           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  PHE B 175   O  PHE B 184           
SHEET    1 AA9 5 ALA B 248  VAL B 249  0                                        
SHEET    2 AA9 5 ILE B 220  ASP B 223  1  N  ILE B 222   O  VAL B 249           
SHEET    3 AA9 5 PHE B 283  PHE B 287  1  O  ALA B 285   N  ASP B 223           
SHEET    4 AA9 5 ASN B 294  GLY B 298 -1  O  LEU B 297   N  GLY B 284           
SHEET    5 AA9 5 PHE B 303  VAL B 304 -1  O  VAL B 304   N  ILE B 296           
SHEET    1 AB1 4 LEU B 352  THR B 355  0                                        
SHEET    2 AB1 4 PHE B 331  SER B 334  1  N  PHE B 331   O  TYR B 353           
SHEET    3 AB1 4 LEU B 373  GLU B 376  1  O  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  ALA B 461  0                                        
SHEET    2 AB2 7 LYS B 464  ASN B 473 -1  O  TYR B 466   N  PHE B 459           
SHEET    3 AB2 7 LEU B 490  PHE B 494 -1  O  ILE B 493   N  GLU B 469           
SHEET    4 AB2 7 ARG B 499  LEU B 504 -1  O  ILE B 500   N  LEU B 492           
SHEET    5 AB2 7 ILE B 514  GLU B 522 -1  O  TYR B 517   N  VAL B 501           
SHEET    6 AB2 7 ARG B 422  TYR B 430 -1  N  TYR B 428   O  LEU B 516           
SHEET    7 AB2 7 VAL B 560  THR B 562 -1  O  VAL B 560   N  ASP B 429           
SHEET    1 AB3 2 TYR B 476  SER B 477  0                                        
SHEET    2 AB3 2 ILE B 484  SER B 485 -1  O  SER B 485   N  TYR B 476           
LINK         OG  SER A 117                MG    MG A 601     1555   1555  2.16  
LINK         OD2 ASP A 288                MG    MG A 601     1555   1555  1.95  
LINK         OD1 ASP A 290                MG    MG A 601     1555   1555  2.03  
LINK         OD1 ASP A 292                MG    MG A 601     1555   1555  1.98  
LINK         OG  SER B 117                MG    MG B 601     1555   1555  2.26  
LINK         OD2 ASP B 288                MG    MG B 601     1555   1555  1.94  
LINK         OD1 ASP B 290                MG    MG B 601     1555   1555  2.12  
LINK         OD1 ASP B 292                MG    MG B 601     1555   1555  2.02  
LINK        MG    MG A 601                 O   HOH A 771     1555   1555  2.39  
LINK        MG    MG A 601                 O   HOH A 878     1555   1555  2.18  
LINK        MG    MG B 601                 O   HOH B 851     1555   1555  2.21  
CISPEP   1 ALA A  461    ASN A  462          0         5.66                     
SITE     1 AC1  6 SER A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     2 AC1  6 HOH A 771  HOH A 878                                          
SITE     1 AC2  5 ARG A 503  SER A 505  GLY A 506  ARG A 515                    
SITE     2 AC2  5 GOL A 611                                                     
SITE     1 AC3  6 ASN A 179  LYS A 470  ARG A 491  HOH A 819                    
SITE     2 AC3  6 HOH A 925  HOH A1020                                          
SITE     1 AC4  7 SER A  20  ARG A  23  SER A 117  HIS A 118                    
SITE     2 AC4  7 ARG A 293  HOH A 724  HOH A 878                               
SITE     1 AC5  3 ARG A  85  ILE A 106  HOH A 706                               
SITE     1 AC6  7 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     2 AC6  7 HOH A 711  HOH A 734  HOH A 980                               
SITE     1 AC7  8 TYR A  66  MET A  67  LYS A  68  GLU A  69                    
SITE     2 AC7  8 GLU A 255  HOH A 702  HOH A 714  HOH A 972                    
SITE     1 AC8  7 PHE A 303  ASN A 305  ARG A 422  PHE A 424                    
SITE     2 AC8  7 PHE A 425  HOH A 762  HOH A 851                               
SITE     1 AC9  9 ASN A 135  PRO A 140  LYS A 360  GLY A 363                    
SITE     2 AC9  9 ASN A 364  ASP A 367  HOH A 767  HOH A 786                    
SITE     3 AC9  9 HOH A 836                                                     
SITE     1 AD1  6 TYR A 428  GLN A 533  THR A 556  PRO A 558                    
SITE     2 AD1  6 HOH A 782  HOH A 810                                          
SITE     1 AD2  5 GLU A 377  ARG A 427  ARG A 515  TYR A 517                    
SITE     2 AD2  5 SO4 A 602                                                     
SITE     1 AD3  5 SER B 117  ASP B 288  ASP B 290  ASP B 292                    
SITE     2 AD3  5 HOH B 851                                                     
SITE     1 AD4  3 ARG B 503  SER B 505  ARG B 515                               
SITE     1 AD5  3 ARG B  85  ILE B 106  HOH B 862                               
SITE     1 AD6  5 SER B  20  SER B 117  HIS B 118  ARG B 293                    
SITE     2 AD6  5 HOH B 706                                                     
SITE     1 AD7  7 ARG B  64  PHE B  65  TYR B  66  MET B  67                    
SITE     2 AD7  7 LYS B  68  GLU B  69  GLU B 255                               
SITE     1 AD8  6 GLN B  90  ASN B  91  ASP B 190  SER B 191                    
SITE     2 AD8  6 PRO B 231  LYS B 235                                          
SITE     1 AD9  6 PHE B 303  ASN B 305  ARG B 422  PHE B 424                    
SITE     2 AD9  6 PHE B 425  HOH B 787                                          
SITE     1 AE1  3 ASP A  14  VAL A  28  TYR A  35                               
CRYST1  172.590  172.590   99.780  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      0.005794  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005794  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010022        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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