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Database: PDB
Entry: 5JN5
LinkDB: 5JN5
Original site: 5JN5 
HEADER    ISOMERASE                               29-APR-16   5JN5              
TITLE     CRYSTAL STRUCTURE OF THE D263Y 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;                                                       
COMPND   8 OTHER_DETAILS: PHOSPHOSERINE AT RESIDUE 117                          
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, PHOSPHOHEXOMUTASE, ENZYME                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BEAMER,K.M.STIERS                                                 
REVDAT   6   27-NOV-19 5JN5    1       ATOM                                     
REVDAT   5   01-NOV-17 5JN5    1       REMARK                                   
REVDAT   4   20-SEP-17 5JN5    1       REMARK                                   
REVDAT   3   29-MAR-17 5JN5    1       JRNL                                     
REVDAT   2   22-FEB-17 5JN5    1       JRNL                                     
REVDAT   1   08-FEB-17 5JN5    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.    1.75 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 151818                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7553                            
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 54.7303 -  5.4359    1.00     5186   264  0.1838 0.1959        
REMARK   3     2  5.4359 -  4.3152    1.00     4920   287  0.1508 0.1791        
REMARK   3     3  4.3152 -  3.7699    1.00     4915   244  0.1488 0.1730        
REMARK   3     4  3.7699 -  3.4253    1.00     4881   261  0.1539 0.1740        
REMARK   3     5  3.4253 -  3.1798    1.00     4835   256  0.1707 0.2205        
REMARK   3     6  3.1798 -  2.9923    1.00     4866   257  0.1751 0.2007        
REMARK   3     7  2.9923 -  2.8425    1.00     4810   249  0.1823 0.2044        
REMARK   3     8  2.8425 -  2.7188    1.00     4845   257  0.1812 0.2115        
REMARK   3     9  2.7188 -  2.6141    1.00     4774   274  0.1759 0.2075        
REMARK   3    10  2.6141 -  2.5239    1.00     4814   248  0.1755 0.2118        
REMARK   3    11  2.5239 -  2.4450    1.00     4756   281  0.1730 0.2101        
REMARK   3    12  2.4450 -  2.3751    1.00     4801   240  0.1728 0.2070        
REMARK   3    13  2.3751 -  2.3126    1.00     4824   236  0.1771 0.2018        
REMARK   3    14  2.3126 -  2.2561    1.00     4770   277  0.1793 0.2175        
REMARK   3    15  2.2561 -  2.2048    1.00     4750   262  0.1823 0.2077        
REMARK   3    16  2.2048 -  2.1579    1.00     4797   248  0.1859 0.2317        
REMARK   3    17  2.1579 -  2.1148    1.00     4757   248  0.1901 0.2049        
REMARK   3    18  2.1148 -  2.0748    1.00     4757   279  0.1900 0.2048        
REMARK   3    19  2.0748 -  2.0378    1.00     4755   243  0.1952 0.2233        
REMARK   3    20  2.0378 -  2.0032    1.00     4813   235  0.1972 0.2502        
REMARK   3    21  2.0032 -  1.9709    1.00     4776   237  0.2028 0.2305        
REMARK   3    22  1.9709 -  1.9406    1.00     4770   239  0.2006 0.2465        
REMARK   3    23  1.9406 -  1.9121    1.00     4766   256  0.2140 0.2615        
REMARK   3    24  1.9121 -  1.8851    1.00     4707   254  0.2204 0.2350        
REMARK   3    25  1.8851 -  1.8597    1.00     4821   231  0.2302 0.2787        
REMARK   3    26  1.8597 -  1.8355    1.00     4766   218  0.2386 0.2777        
REMARK   3    27  1.8355 -  1.8126    1.00     4776   239  0.2426 0.3003        
REMARK   3    28  1.8126 -  1.7907    1.00     4769   262  0.2551 0.2893        
REMARK   3    29  1.7907 -  1.7699    1.00     4751   230  0.2509 0.2505        
REMARK   3    30  1.7699 -  1.7500    1.00     4737   241  0.2756 0.3041        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.940           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           8771                                  
REMARK   3   ANGLE     :  1.089          11939                                  
REMARK   3   CHIRALITY :  0.047           1348                                  
REMARK   3   PLANARITY :  0.006           1560                                  
REMARK   3   DIHEDRAL  : 12.590           3167                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5JN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220848.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0 - 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                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 151916                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
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       : 13.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.58700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
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 (1.4 -       
REMARK 280  1.55 M) WITH 0.1 M TRIS, PH 7.5 OR MES PH 6.0, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.00050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       86.49400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       86.49400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       25.00025            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       86.49400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       86.49400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       75.00075            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       86.49400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.49400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       25.00025            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       86.49400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.49400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       75.00075            
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       50.00050            
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: DIMER ACCORDING TO DYNAMIC LIGHT SCATTERING                  
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 A 782  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1447  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     THR A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     ALA A   510                                                      
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     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     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     GLU A 187    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 210    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 215    CG   CD                                             
REMARK 470     GLU A 274    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     LYS A 523    CG   CD   CE   NZ                                   
REMARK 470     VAL A 525    CG1  CG2                                            
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     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     GLN B 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     GLU B 178    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 179    CG   OD1  ND2                                       
REMARK 470     LYS B 180    CG   CD   CE   NZ                                   
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 418    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 432    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 439    CG   OD1  ND2                                       
REMARK 470     PHE B 450    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 451    CG   OD1  OD2                                       
REMARK 470     ARG B 452    CG   CD   NE   CZ   NH1  NH2                        
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     VAL B 480    CG1  CG2                                            
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     GLN B 530    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 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 B  1157     O    HOH B  1210              1.84            
REMARK 500   O    HOH B  1145     O    HOH B  1151              1.84            
REMARK 500   O    HOH B  1113     O    HOH B  1150              1.85            
REMARK 500   O    HOH B  1309     O    HOH B  1321              1.86            
REMARK 500   O    HOH A   822     O    HOH A  1036              1.91            
REMARK 500   O    HOH B   810     O    HOH B  1137              1.91            
REMARK 500   O2P  SEP A   117     O    HOH A   701              1.92            
REMARK 500   O    HOH B  1014     O    HOH B  1181              1.93            
REMARK 500   O    HOH A  1098     O    HOH A  1235              1.93            
REMARK 500   O    HOH A  1108     O    HOH A  1269              1.97            
REMARK 500   O    HOH A  1456     O    HOH A  1478              1.98            
REMARK 500   O    HOH A  1316     O    HOH A  1399              1.98            
REMARK 500   OE2  GLU B   522     O    HOH B   701              1.99            
REMARK 500   O    HOH B   808     O    HOH B   836              2.00            
REMARK 500   O    HOH A  1257     O    HOH A  1418              2.00            
REMARK 500   O    HOH A  1000     O    HOH A  1274              2.00            
REMARK 500   O    HOH B  1097     O    HOH B  1179              2.00            
REMARK 500   O    HOH B  1313     O    HOH B  1321              2.02            
REMARK 500   O    HOH A  1279     O    HOH A  1410              2.02            
REMARK 500   O    HOH A  1422     O    HOH A  1483              2.02            
REMARK 500   O    HOH B  1123     O    HOH B  1191              2.03            
REMARK 500   OG   SER B   369     O    HOH B   702              2.03            
REMARK 500   OE1  GLN B   174     O    HOH B   703              2.04            
REMARK 500   OD1  ASN A   305     O    HOH A   702              2.04            
REMARK 500   OE1  GLN A    53     O    HOH A   703              2.04            
REMARK 500   O    HOH B   995     O    HOH B  1223              2.06            
REMARK 500   O    HOH B  1043     O    HOH B  1243              2.07            
REMARK 500   O    HOH A   876     O    HOH A  1215              2.07            
REMARK 500   O    HOH A  1127     O    HOH A  1329              2.08            
REMARK 500   O    HOH B  1068     O    HOH B  1156              2.08            
REMARK 500   OD2  ASP A   451     OG   SER A   453              2.08            
REMARK 500   O    HOH A   714     O    HOH A  1101              2.09            
REMARK 500   O    HOH B  1024     O    HOH B  1132              2.09            
REMARK 500   O    HOH A  1431     O    HOH A  1480              2.09            
REMARK 500   O    HOH B  1106     O    HOH B  1201              2.09            
REMARK 500   O    HOH A  1209     O    HOH A  1401              2.10            
REMARK 500   O    HOH A   802     O    HOH A   886              2.11            
REMARK 500   N    ASN A     0     O    HOH A   704              2.11            
REMARK 500   O    HOH B  1247     O    HOH B  1283              2.11            
REMARK 500   O    HOH A   988     O    HOH A  1267              2.12            
REMARK 500   O    HOH B   957     O    HOH B  1258              2.12            
REMARK 500   OG1  THR A   153     O    HOH A   705              2.12            
REMARK 500   O    HOH A   832     O    HOH A  1283              2.12            
REMARK 500   O    HOH A   826     O    HOH A  1160              2.12            
REMARK 500   O    HOH A  1194     O    HOH A  1469              2.13            
REMARK 500   O    HOH B  1260     O    HOH B  1285              2.13            
REMARK 500   O    HOH B   784     O    HOH B  1182              2.13            
REMARK 500   O    HOH B   984     O    HOH B  1197              2.13            
REMARK 500   O    HOH A  1152     O    HOH A  1229              2.14            
REMARK 500   OD2  ASP B   166     O    HOH B   704              2.14            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 CLOSE CONTACTS                                
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  1041     O    HOH B   834     4544     1.87            
REMARK 500   O    HOH A  1129     O    HOH B  1266     4545     1.96            
REMARK 500   O    HOH A  1037     O    HOH B  1224     6544     1.99            
REMARK 500   O    HOH A  1471     O    HOH B  1196     4544     2.06            
REMARK 500   O    HOH A  1362     O    HOH A  1373     3445     2.13            
REMARK 500   O    HOH A  1471     O    HOH B  1171     4544     2.13            
REMARK 500   O    HOH A  1183     O    HOH A  1359     8555     2.14            
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      -10.54     88.05                                   
REMARK 500    SEP A 117     -127.12     63.61                                   
REMARK 500    ILE A 133     -166.81   -105.02                                   
REMARK 500    ALA A 461      -72.62    -79.89                                   
REMARK 500    ASN A 462     -145.03     48.02                                   
REMARK 500    PRO B  17      -80.99    -57.48                                   
REMARK 500    TYR B  66       -4.21     84.07                                   
REMARK 500    SEP B 117     -127.62     57.93                                   
REMARK 500    ILE B 133     -164.24   -106.65                                   
REMARK 500    VAL B 480      -61.14   -106.38                                   
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 A1496        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A1497        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A1498        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH B1322        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH B1323        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B1324        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH B1325        DISTANCE =  6.42 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 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP A 117   OG                                                     
REMARK 620 2 SEP A 117   O1P  58.0                                              
REMARK 620 3 ASP A 288   OD2  88.2 120.7                                        
REMARK 620 4 ASP A 290   OD1  93.6 126.0 100.7                                  
REMARK 620 5 ASP A 292   OD1 161.7 104.5  97.6 102.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP B 117   OG                                                     
REMARK 620 2 SEP B 117   O3P  63.5                                              
REMARK 620 3 ASP B 288   OD1  96.1 120.2                                        
REMARK 620 4 ASP B 290   OD1  93.7 135.9  98.2                                  
REMARK 620 5 ASP B 292   OD2 157.5  94.7 100.0  99.3                            
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 SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA 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 SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 604                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
DBREF  5JN5 A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5JN5 B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5JN5 MET A  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS A  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS A  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS A  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS A  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS A  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS A  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 SER A  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 SER A  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLY A  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 VAL A  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 ASP A  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 LEU A  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLY A   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 THR A   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLU A   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 ASN A   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 LEU A   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 TYR A   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 PHE A   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLN A   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 SER A   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 ASN A    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 TYR A  263  UNP  P36871    ASP   263 ENGINEERED MUTATION            
SEQADV 5JN5 MET B  -22  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS B  -21  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS B  -20  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS B  -19  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS B  -18  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS B  -17  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 HIS B  -16  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 SER B  -15  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 SER B  -14  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLY B  -13  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 VAL B  -12  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 ASP B  -11  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 LEU B  -10  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLY B   -9  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 THR B   -8  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLU B   -7  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 ASN B   -6  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 LEU B   -5  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 TYR B   -4  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 PHE B   -3  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 GLN B   -2  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 SER B   -1  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 ASN B    0  UNP  P36871              EXPRESSION TAG                 
SEQADV 5JN5 TYR B  263  UNP  P36871    ASP   263 ENGINEERED MUTATION            
SEQRES   1 A  585  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  585  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS          
SEQRES   3 A  585  ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS          
SEQRES   4 A  585  PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE          
SEQRES   5 A  585  GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER          
SEQRES   6 A  585  ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA          
SEQRES   7 A  585  THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS          
SEQRES   8 A  585  GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN          
SEQRES   9 A  585  GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU          
SEQRES  10 A  585  SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS          
SEQRES  11 A  585  ALA ILE GLY GLY ILE ILE LEU THR ALA 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 TYR          
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 TYR          
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 5JN5 SEP A  117  SER  MODIFIED RESIDUE                                   
MODRES 5JN5 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    SO4  A 604       5                                                       
HET     CA  A 605       1                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET     CA  B 604       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  SO4    7(O4 S 2-)                                                   
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL  12  HOH   *1423(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  531  GLN A  548  1                                  18    
HELIX   23 AC5 GLN A  548  GLY A  554  1                                   7    
HELIX   24 AC6 VAL B   26  SER B   32  1                                   7    
HELIX   25 AC7 ASN B   34  THR B   46  1                                  13    
HELIX   26 AC8 VAL B   47  ARG B   52  5                                   6    
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  ILE B  154  1                                  15    
HELIX   30 AD3 VAL B  192  PHE B  203  1                                  12    
HELIX   31 AD4 ASP B  204  SER B  213  1                                  10    
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  GLY B  279  1                                  11    
HELIX   36 AD9 ASN B  305  ASN B  316  1                                  12    
HELIX   37 AE1 ILE B  317  SER B  319  5                                   3    
HELIX   38 AE2 ILE B  320  GLY B  327  1                                   8    
HELIX   39 AE3 GLY B  339  ALA B  347  1                                   9    
HELIX   40 AE4 GLY B  358  ALA B  368  1                                  11    
HELIX   41 AE5 ASP B  390  LYS B  406  1                                  17    
HELIX   42 AE6 SER B  408  GLY B  421  1                                  14    
HELIX   43 AE7 GLU B  434  PHE B  450  1                                  17    
HELIX   44 AE8 ASP B  524  ASN B  529  1                                   6    
HELIX   45 AE9 ASP B  531  GLN B  548  1                                  18    
HELIX   46 AF1 GLN B  548  GLY B  554  1                                   7    
SHEET    1 AA1 8 MET A   1  VAL A   2  0                                        
SHEET    2 AA1 8 GLY A 171  LEU A 177  1  O  ASP A 176   N  VAL A   2           
SHEET    3 AA1 8 PHE A 184  VAL A 189 -1  O  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  ILE A 112   N  VAL A  58           
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  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  ASN B 132 -1  O  PHE B 127   N  LYS B  24           
SHEET    3 AA8 7 GLY B 110  LEU B 114 -1  N  ILE B 113   O  LYS B 130           
SHEET    4 AA8 7 THR B  56  GLY B  61  1  N  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  GLN B 173   O  VAL B 186           
SHEET    1 AA9 5 ALA B 248  VAL B 249  0                                        
SHEET    2 AA9 5 ILE B 220  ASP B 223  1  N  ILE B 222   O  VAL B 249           
SHEET    3 AA9 5 PHE B 283  PHE B 287  1  O  ALA B 285   N  ASP B 223           
SHEET    4 AA9 5 ASN B 294  GLY B 298 -1  O  LEU B 297   N  GLY B 284           
SHEET    5 AA9 5 PHE B 303  VAL B 304 -1  O  VAL B 304   N  ILE B 296           
SHEET    1 AB1 4 LEU B 352  THR B 355  0                                        
SHEET    2 AB1 4 PHE B 331  SER B 334  1  N  PHE B 331   O  TYR B 353           
SHEET    3 AB1 4 LEU B 373  GLU B 376  1  O  GLY B 375   N  ALA B 332           
SHEET    4 AB1 4 GLY B 380  SER B 383 -1  O  GLY B 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  ARG B 515   N  ARG B 503           
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         C   ALA A 116                 N   SEP A 117     1555   1555  1.33  
LINK         OG  SEP A 117                CA    CA A 605     1555   1555  3.01  
LINK         C   SEP A 117                 N   HIS A 118     1555   1555  1.32  
LINK         O1P SEP A 117                CA    CA A 605     1555   1555  2.09  
LINK         OD2 ASP A 288                CA    CA A 605     1555   1555  2.07  
LINK         OD1 ASP A 290                CA    CA A 605     1555   1555  2.06  
LINK         OD1 ASP A 292                CA    CA A 605     1555   1555  1.97  
LINK         C   ALA B 116                 N   SEP B 117     1555   1555  1.33  
LINK         OG  SEP B 117                CA    CA B 604     1555   1555  2.63  
LINK         C   SEP B 117                 N   HIS B 118     1555   1555  1.33  
LINK         O3P SEP B 117                CA    CA B 604     1555   1555  2.26  
LINK         OD1 ASP B 288                CA    CA B 604     1555   1555  2.01  
LINK         OD1 ASP B 290                CA    CA B 604     1555   1555  2.13  
LINK         OD2 ASP B 292                CA    CA B 604     1555   1555  1.94  
CISPEP   1 ALA A  461    ASN A  462          0       -21.06                     
SITE     1 AC1  8 ARG A 503  SER A 505  GLY A 506  ARG A 515                    
SITE     2 AC1  8 HOH A1145  HOH A1168  HOH A1186  HOH A1192                    
SITE     1 AC2  8 PHE A  65  TYR A  66  MET A  67  LYS A  68                    
SITE     2 AC2  8 GLU A  69  GLU A 255  HOH A 965  HOH A1053                    
SITE     1 AC3  7 ARG A 217  ARG A 221  PRO A 244  ASN A 246                    
SITE     2 AC3  7 HOH A1015  HOH A1040  HOH A1135                               
SITE     1 AC4  3 HIS A 260  HIS A 261  HOH A 999                               
SITE     1 AC5  4 SEP A 117  ASP A 288  ASP A 290  ASP A 292                    
SITE     1 AC6  6 ARG B 503  SER B 505  GLY B 506  ARG B 515                    
SITE     2 AC6  6 HOH B 922  HOH B1007                                          
SITE     1 AC7  9 ARG B 221  PRO B 244  ASN B 246  THR B 275                    
SITE     2 AC7  9 HIS B 281  HOH B 918  HOH B 934  HOH B1037                    
SITE     3 AC7  9 HOH B1083                                                     
SITE     1 AC8  3 HIS B 260  HIS B 261  HOH B1060                               
SITE     1 AC9  4 SEP B 117  ASP B 288  ASP B 290  ASP B 292                    
CRYST1  172.988  172.988  100.001  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      0.005781  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005781  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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