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Database: PDB
Entry: 1JQO
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Original site: 1JQO 
HEADER    LYASE                                   07-AUG-01   1JQO              
TITLE     CRYSTAL STRUCTURE OF C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE FROM     
TITLE    2 MAIZE                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PHOSPHOENOLPYRUVATE CARBOXYLASE 1, PEPCASE;                 
COMPND   5 EC: 4.1.1.31                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZEA MAYS;                                       
SOURCE   3 ORGANISM_TAXID: 4577;                                                
SOURCE   4 STRAIN: B37;                                                         
SOURCE   5 TISSUE: LEAVES                                                       
KEYWDS    BETA BARREL, CARBON DIOXIDE FIXATION, LYASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.MATSUMURA,Y.KAI                                                     
REVDAT   3   13-JUL-11 1JQO    1       VERSN                                    
REVDAT   2   24-FEB-09 1JQO    1       VERSN                                    
REVDAT   1   14-JAN-03 1JQO    0                                                
JRNL        AUTH   H.MATSUMURA,Y.XIE,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,Y.UENO,    
JRNL        AUTH 2 K.IZUI,Y.KAI                                                 
JRNL        TITL   CRYSTAL STRUCTURES OF C4 FORM MAIZE AND QUATERNARY COMPLEX   
JRNL        TITL 2 OF E. COLI PHOSPHOENOLPYRUVATE CARBOXYLASES.                 
JRNL        REF    STRUCTURE                     V.  10  1721 2002              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12467579                                                     
JRNL        DOI    10.1016/S0969-2126(02)00913-9                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.MATSUMURA,M.TERADA,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,K.IZUI, 
REMARK   1  AUTH 2 Y.KAI                                                        
REMARK   1  TITL   PLAUSIBLE PHOSPHOENOLPYRUVATE BINDING SITE REVEALED BY 2.6 A 
REMARK   1  TITL 2 STRUCTURE OF MN2+-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE FROM 
REMARK   1  TITL 3 ESCHERICHIA COLI.                                            
REMARK   1  REF    FEBS LETT.                    V. 458    93 1999              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.KAI,H.MATSUMURA,T.INOUE,K.TERADA,Y.NAGARA,T.YOSHINAGA,     
REMARK   1  AUTH 2 A.KIHARA,K.TSUMURA,K.IZUI                                    
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE           
REMARK   1  TITL 2 CARBOXYLASE: A PROPOSED MECHANISM FOR ALLOSTERIC INHIBITION  
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  96   823 1999              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.MATSUMURA,T.NAGATA,M.TERADA,S.SHIRAKATA,T.INOUE,           
REMARK   1  AUTH 2 T.YOSHINAGA,Y.UENO,H.SAZE,K.IZUI,Y.KAI                       
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF 
REMARK   1  TITL 2 C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE FROM MAIZE           
REMARK   1  TITL 3 DIFFRACTION STUDIES OF C4-FORM PHOSPHOENOLPYRUVATE           
REMARK   1  TITL 4 CARBOXYLASE FROM MAIZE.                                      
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55  1937 1999              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 57271                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2893                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.14                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130                       
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14424                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.06                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-AUG-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014076.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.708                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58078                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 7.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, TRIS-HCL, LISO4, PH 7.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
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      127.14000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      127.14000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       79.22000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       87.30500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       79.22000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       87.30500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      127.14000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       79.22000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       87.30500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      127.14000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       79.22000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       87.30500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: THE BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM DIMER   
REMARK 300 IN THE ASSYMMETRIC UNIT BY TWO FOLE AXIS.                            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      174.61000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      254.28000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 68130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     LYS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     ILE A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     GLN A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     ASP A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     LEU A    34                                                      
REMARK 465     SER A   124                                                      
REMARK 465     LYS A   125                                                      
REMARK 465     LEU A   126                                                      
REMARK 465     LYS A   127                                                      
REMARK 465     LYS A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     GLY A   130                                                      
REMARK 465     PHE A   131                                                      
REMARK 465     ALA A   132                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     SER A   136                                                      
REMARK 465     ALA A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     THR A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     ALA A   761                                                      
REMARK 465     LYS A   762                                                      
REMARK 465     ARG A   763                                                      
REMARK 465     ARG A   764                                                      
REMARK 465     PRO A   765                                                      
REMARK 465     GLY A   766                                                      
REMARK 465     GLY A   767                                                      
REMARK 465     GLY A   768                                                      
REMARK 465     PHE A   929                                                      
REMARK 465     ALA A   930                                                      
REMARK 465     ASP A   931                                                      
REMARK 465     GLU A   932                                                      
REMARK 465     ASN A   933                                                      
REMARK 465     LYS A   934                                                      
REMARK 465     PRO A   935                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     ILE B    16                                                      
REMARK 465     ASP B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     LEU B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     GLN B    22                                                      
REMARK 465     LEU B    23                                                      
REMARK 465     VAL B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     ASP B    31                                                      
REMARK 465     ASP B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     SER B   124                                                      
REMARK 465     LYS B   125                                                      
REMARK 465     LEU B   126                                                      
REMARK 465     LYS B   127                                                      
REMARK 465     LYS B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     GLY B   130                                                      
REMARK 465     PHE B   131                                                      
REMARK 465     ALA B   132                                                      
REMARK 465     ASP B   133                                                      
REMARK 465     GLU B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     SER B   136                                                      
REMARK 465     ALA B   137                                                      
REMARK 465     THR B   138                                                      
REMARK 465     THR B   139                                                      
REMARK 465     GLU B   140                                                      
REMARK 465     ALA B   761                                                      
REMARK 465     LYS B   762                                                      
REMARK 465     ARG B   763                                                      
REMARK 465     ARG B   764                                                      
REMARK 465     PRO B   765                                                      
REMARK 465     GLY B   766                                                      
REMARK 465     GLY B   767                                                      
REMARK 465     GLY B   768                                                      
REMARK 465     PHE B   929                                                      
REMARK 465     ALA B   930                                                      
REMARK 465     ASP B   931                                                      
REMARK 465     GLU B   932                                                      
REMARK 465     ASN B   933                                                      
REMARK 465     LYS B   934                                                      
REMARK 465     PRO B   935                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  55   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 120      -76.09    -45.16                                   
REMARK 500    SER A 152      -82.40    -77.64                                   
REMARK 500    GLU A 153      -71.71    -50.55                                   
REMARK 500    ALA A 176       52.81    -97.74                                   
REMARK 500    PRO A 178       62.13    -59.28                                   
REMARK 500    THR A 206     -172.01    -61.82                                   
REMARK 500    HIS A 249       35.38    -91.14                                   
REMARK 500    GLU A 250      -24.05   -146.99                                   
REMARK 500    THR A 251      -37.90   -143.50                                   
REMARK 500    ILE A 272       96.05    -50.85                                   
REMARK 500    ASN A 273       47.28    -84.41                                   
REMARK 500    MET A 289       95.04    -67.17                                   
REMARK 500    SER A 331       32.31    -87.72                                   
REMARK 500    ARG A 334       98.49    -68.54                                   
REMARK 500    SER A 350      -70.56    -68.51                                   
REMARK 500    LYS A 353       -3.99   -144.77                                   
REMARK 500    VAL A 354       10.50    -64.33                                   
REMARK 500    PRO A 367        4.00    -69.37                                   
REMARK 500    GLU A 369       74.56   -119.24                                   
REMARK 500    ALA A 394      -72.72    -59.48                                   
REMARK 500    SER A 395     -149.53    -92.58                                   
REMARK 500    CYS A 426       24.52    -75.06                                   
REMARK 500    ASP A 428       69.43    -45.47                                   
REMARK 500    ASP A 433        9.76    -68.53                                   
REMARK 500    LEU A 450      -50.21    -21.92                                   
REMARK 500    GLN A 457      126.26   -173.41                                   
REMARK 500    ILE A 475       43.36   -150.60                                   
REMARK 500    GLU A 480       10.66    -65.68                                   
REMARK 500    LYS A 497      -16.81   -149.28                                   
REMARK 500    SER A 528        9.04    -64.15                                   
REMARK 500    MET A 536       42.61     35.38                                   
REMARK 500    THR A 538      -90.46   -102.66                                   
REMARK 500    LEU A 548      -71.15    -72.19                                   
REMARK 500    ARG A 556      -81.24    -43.00                                   
REMARK 500    GLU A 566      -53.93   -132.65                                   
REMARK 500    SER A 573       31.31    -73.89                                   
REMARK 500    ALA A 576      -71.46    -67.69                                   
REMARK 500    PRO A 660      139.33    -39.68                                   
REMARK 500    ILE A 664      -61.07   -122.90                                   
REMARK 500    GLU A 684      -79.89    -65.24                                   
REMARK 500    HIS A 704       65.04   -154.14                                   
REMARK 500    PRO A 705      159.76    -49.91                                   
REMARK 500    TYR A 728      -74.83    -62.48                                   
REMARK 500    VAL A 733      -64.38   -107.95                                   
REMARK 500    ARG A 737        8.64    -65.11                                   
REMARK 500    PRO A 747       36.47    -90.53                                   
REMARK 500    ARG A 773      144.68      1.24                                   
REMARK 500    VAL A 794      -36.65    -25.21                                   
REMARK 500    ASP A 837      100.11   -166.33                                   
REMARK 500    ASN A 895      -53.92    -27.55                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     118 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 971                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1071                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FIY   RELATED DB: PDB                                   
REMARK 900 1FIY CONTAINS THE NATIVE STRUCTURE OF E.COLI PEPC.                   
REMARK 900 RELATED ID: 1JQN   RELATED DB: PDB                                   
REMARK 900 1JQN CONTAINS STRUCTURE OF E.COLI PHOSPHOENOLPYRUVATE                
REMARK 900 CARBOXYLASE IN COMPLEX WITH MN2+ AND DCDP                            
DBREF  1JQO A    1   970  UNP    P04711   CAPP1_MAIZE      1    970             
DBREF  1JQO B    1   970  UNP    P04711   CAPP1_MAIZE      1    970             
SEQRES   1 A  970  MET ALA SER THR LYS ALA PRO GLY PRO GLY GLU LYS HIS          
SEQRES   2 A  970  HIS SER ILE ASP ALA GLN LEU ARG GLN LEU VAL PRO GLY          
SEQRES   3 A  970  LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR ASP ALA          
SEQRES   4 A  970  LEU LEU VAL ASP ARG PHE LEU ASN ILE LEU GLN ASP LEU          
SEQRES   5 A  970  HIS GLY PRO SER LEU ARG GLU PHE VAL GLN GLU CYS TYR          
SEQRES   6 A  970  GLU VAL SER ALA ASP TYR GLU GLY LYS GLY ASP THR THR          
SEQRES   7 A  970  LYS LEU GLY GLU LEU GLY ALA LYS LEU THR GLY LEU ALA          
SEQRES   8 A  970  PRO ALA ASP ALA ILE LEU VAL ALA SER SER ILE LEU HIS          
SEQRES   9 A  970  MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL GLN ILE          
SEQRES  10 A  970  ALA HIS ARG ARG ARG ASN SER LYS LEU LYS LYS GLY GLY          
SEQRES  11 A  970  PHE ALA ASP GLU GLY SER ALA THR THR GLU SER ASP ILE          
SEQRES  12 A  970  GLU GLU THR LEU LYS ARG LEU VAL SER GLU VAL GLY LYS          
SEQRES  13 A  970  SER PRO GLU GLU VAL PHE GLU ALA LEU LYS ASN GLN THR          
SEQRES  14 A  970  VAL ASP LEU VAL PHE THR ALA HIS PRO THR GLN SER ALA          
SEQRES  15 A  970  ARG ARG SER LEU LEU GLN LYS ASN ALA ARG ILE ARG ASN          
SEQRES  16 A  970  CYS LEU THR GLN LEU ASN ALA LYS ASP ILE THR ASP ASP          
SEQRES  17 A  970  ASP LYS GLN GLU LEU ASP GLU ALA LEU GLN ARG GLU ILE          
SEQRES  18 A  970  GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG ALA GLN          
SEQRES  19 A  970  PRO THR PRO GLN ALA GLU MET ARG TYR GLY MET SER TYR          
SEQRES  20 A  970  ILE HIS GLU THR VAL TRP LYS GLY VAL PRO LYS PHE LEU          
SEQRES  21 A  970  ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE ASN          
SEQRES  22 A  970  GLU ARG LEU PRO TYR ASN VAL SER LEU ILE ARG PHE SER          
SEQRES  23 A  970  SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG VAL          
SEQRES  24 A  970  THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA ARG          
SEQRES  25 A  970  MET MET ALA ALA ASN LEU TYR ILE ASP GLN ILE GLU GLU          
SEQRES  26 A  970  LEU MET PHE GLU LEU SER MET TRP ARG CYS ASN ASP GLU          
SEQRES  27 A  970  LEU ARG VAL ARG ALA GLU GLU LEU HIS SER SER SER GLY          
SEQRES  28 A  970  SER LYS VAL THR LYS TYR TYR ILE GLU PHE TRP LYS GLN          
SEQRES  29 A  970  ILE PRO PRO ASN GLU PRO TYR ARG VAL ILE LEU GLY HIS          
SEQRES  30 A  970  VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG ALA ARG          
SEQRES  31 A  970  HIS LEU LEU ALA SER GLY VAL SER GLU ILE SER ALA GLU          
SEQRES  32 A  970  SER SER PHE THR SER ILE GLU GLU PHE LEU GLU PRO LEU          
SEQRES  33 A  970  GLU LEU CYS TYR LYS SER LEU CYS ASP CYS GLY ASP LYS          
SEQRES  34 A  970  ALA ILE ALA ASP GLY SER LEU LEU ASP LEU LEU ARG GLN          
SEQRES  35 A  970  VAL PHE THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE          
SEQRES  36 A  970  ARG GLN GLU SER GLU ARG HIS THR ASP VAL ILE ASP ALA          
SEQRES  37 A  970  ILE THR THR HIS LEU GLY ILE GLY SER TYR ARG GLU TRP          
SEQRES  38 A  970  PRO GLU ASP LYS ARG GLN GLU TRP LEU LEU SER GLU LEU          
SEQRES  39 A  970  ARG GLY LYS ARG PRO LEU LEU PRO PRO ASP LEU PRO GLN          
SEQRES  40 A  970  THR ASP GLU ILE ALA ASP VAL ILE GLY ALA PHE HIS VAL          
SEQRES  41 A  970  LEU ALA GLU LEU PRO PRO ASP SER PHE GLY PRO TYR ILE          
SEQRES  42 A  970  ILE SER MET ALA THR ALA PRO SER ASP VAL LEU ALA VAL          
SEQRES  43 A  970  GLU LEU LEU GLN ARG GLU CYS GLY VAL ARG GLN PRO LEU          
SEQRES  44 A  970  PRO VAL VAL PRO LEU PHE GLU ARG LEU ALA ASP LEU GLN          
SEQRES  45 A  970  SER ALA PRO ALA SER VAL GLU ARG LEU PHE SER VAL ASP          
SEQRES  46 A  970  TRP TYR MET ASP ARG ILE LYS GLY LYS GLN GLN VAL MET          
SEQRES  47 A  970  VAL GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG LEU          
SEQRES  48 A  970  SER ALA ALA TRP GLN LEU TYR ARG ALA GLN GLU GLU MET          
SEQRES  49 A  970  ALA GLN VAL ALA LYS ARG TYR GLY VAL LYS LEU THR LEU          
SEQRES  50 A  970  PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY          
SEQRES  51 A  970  PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR          
SEQRES  52 A  970  ILE ASN GLY SER ILE ARG VAL THR VAL GLN GLY GLU VAL          
SEQRES  53 A  970  ILE GLU PHE CYS PHE GLY GLU GLU HIS LEU CYS PHE GLN          
SEQRES  54 A  970  THR LEU GLN ARG PHE THR ALA ALA THR LEU GLU HIS GLY          
SEQRES  55 A  970  MET HIS PRO PRO VAL SER PRO LYS PRO GLU TRP ARG LYS          
SEQRES  56 A  970  LEU MET ASP GLU MET ALA VAL VAL ALA THR GLU GLU TYR          
SEQRES  57 A  970  ARG SER VAL VAL VAL LYS GLU ALA ARG PHE VAL GLU TYR          
SEQRES  58 A  970  PHE ARG SER ALA THR PRO GLU THR GLU TYR GLY ARG MET          
SEQRES  59 A  970  ASN ILE GLY SER ARG PRO ALA LYS ARG ARG PRO GLY GLY          
SEQRES  60 A  970  GLY ILE THR THR LEU ARG ALA ILE PRO TRP ILE PHE SER          
SEQRES  61 A  970  TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY          
SEQRES  62 A  970  VAL GLY ALA ALA PHE LYS PHE ALA ILE ASP LYS ASP VAL          
SEQRES  63 A  970  ARG ASN PHE GLN VAL LEU LYS GLU MET TYR ASN GLU TRP          
SEQRES  64 A  970  PRO PHE PHE ARG VAL THR LEU ASP LEU LEU GLU MET VAL          
SEQRES  65 A  970  PHE ALA LYS GLY ASP PRO GLY ILE ALA GLY LEU TYR ASP          
SEQRES  66 A  970  GLU LEU LEU VAL ALA GLU GLU LEU LYS PRO PHE GLY LYS          
SEQRES  67 A  970  GLN LEU ARG ASP LYS TYR VAL GLU THR GLN GLN LEU LEU          
SEQRES  68 A  970  LEU GLN ILE ALA GLY HIS LYS ASP ILE LEU GLU GLY ASP          
SEQRES  69 A  970  PRO PHE LEU LYS GLN GLY LEU VAL LEU ARG ASN PRO TYR          
SEQRES  70 A  970  ILE THR THR LEU ASN VAL PHE GLN ALA TYR THR LEU LYS          
SEQRES  71 A  970  ARG ILE ARG ASP PRO ASN PHE LYS VAL THR PRO GLN PRO          
SEQRES  72 A  970  PRO LEU SER LYS GLU PHE ALA ASP GLU ASN LYS PRO ALA          
SEQRES  73 A  970  GLY LEU VAL LYS LEU ASN PRO ALA SER GLU TYR PRO PRO          
SEQRES  74 A  970  GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS GLY ILE          
SEQRES  75 A  970  ALA ALA GLY MET GLN ASN THR GLY                              
SEQRES   1 B  970  MET ALA SER THR LYS ALA PRO GLY PRO GLY GLU LYS HIS          
SEQRES   2 B  970  HIS SER ILE ASP ALA GLN LEU ARG GLN LEU VAL PRO GLY          
SEQRES   3 B  970  LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR ASP ALA          
SEQRES   4 B  970  LEU LEU VAL ASP ARG PHE LEU ASN ILE LEU GLN ASP LEU          
SEQRES   5 B  970  HIS GLY PRO SER LEU ARG GLU PHE VAL GLN GLU CYS TYR          
SEQRES   6 B  970  GLU VAL SER ALA ASP TYR GLU GLY LYS GLY ASP THR THR          
SEQRES   7 B  970  LYS LEU GLY GLU LEU GLY ALA LYS LEU THR GLY LEU ALA          
SEQRES   8 B  970  PRO ALA ASP ALA ILE LEU VAL ALA SER SER ILE LEU HIS          
SEQRES   9 B  970  MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL GLN ILE          
SEQRES  10 B  970  ALA HIS ARG ARG ARG ASN SER LYS LEU LYS LYS GLY GLY          
SEQRES  11 B  970  PHE ALA ASP GLU GLY SER ALA THR THR GLU SER ASP ILE          
SEQRES  12 B  970  GLU GLU THR LEU LYS ARG LEU VAL SER GLU VAL GLY LYS          
SEQRES  13 B  970  SER PRO GLU GLU VAL PHE GLU ALA LEU LYS ASN GLN THR          
SEQRES  14 B  970  VAL ASP LEU VAL PHE THR ALA HIS PRO THR GLN SER ALA          
SEQRES  15 B  970  ARG ARG SER LEU LEU GLN LYS ASN ALA ARG ILE ARG ASN          
SEQRES  16 B  970  CYS LEU THR GLN LEU ASN ALA LYS ASP ILE THR ASP ASP          
SEQRES  17 B  970  ASP LYS GLN GLU LEU ASP GLU ALA LEU GLN ARG GLU ILE          
SEQRES  18 B  970  GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG ALA GLN          
SEQRES  19 B  970  PRO THR PRO GLN ALA GLU MET ARG TYR GLY MET SER TYR          
SEQRES  20 B  970  ILE HIS GLU THR VAL TRP LYS GLY VAL PRO LYS PHE LEU          
SEQRES  21 B  970  ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE ASN          
SEQRES  22 B  970  GLU ARG LEU PRO TYR ASN VAL SER LEU ILE ARG PHE SER          
SEQRES  23 B  970  SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG VAL          
SEQRES  24 B  970  THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA ARG          
SEQRES  25 B  970  MET MET ALA ALA ASN LEU TYR ILE ASP GLN ILE GLU GLU          
SEQRES  26 B  970  LEU MET PHE GLU LEU SER MET TRP ARG CYS ASN ASP GLU          
SEQRES  27 B  970  LEU ARG VAL ARG ALA GLU GLU LEU HIS SER SER SER GLY          
SEQRES  28 B  970  SER LYS VAL THR LYS TYR TYR ILE GLU PHE TRP LYS GLN          
SEQRES  29 B  970  ILE PRO PRO ASN GLU PRO TYR ARG VAL ILE LEU GLY HIS          
SEQRES  30 B  970  VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG ALA ARG          
SEQRES  31 B  970  HIS LEU LEU ALA SER GLY VAL SER GLU ILE SER ALA GLU          
SEQRES  32 B  970  SER SER PHE THR SER ILE GLU GLU PHE LEU GLU PRO LEU          
SEQRES  33 B  970  GLU LEU CYS TYR LYS SER LEU CYS ASP CYS GLY ASP LYS          
SEQRES  34 B  970  ALA ILE ALA ASP GLY SER LEU LEU ASP LEU LEU ARG GLN          
SEQRES  35 B  970  VAL PHE THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE          
SEQRES  36 B  970  ARG GLN GLU SER GLU ARG HIS THR ASP VAL ILE ASP ALA          
SEQRES  37 B  970  ILE THR THR HIS LEU GLY ILE GLY SER TYR ARG GLU TRP          
SEQRES  38 B  970  PRO GLU ASP LYS ARG GLN GLU TRP LEU LEU SER GLU LEU          
SEQRES  39 B  970  ARG GLY LYS ARG PRO LEU LEU PRO PRO ASP LEU PRO GLN          
SEQRES  40 B  970  THR ASP GLU ILE ALA ASP VAL ILE GLY ALA PHE HIS VAL          
SEQRES  41 B  970  LEU ALA GLU LEU PRO PRO ASP SER PHE GLY PRO TYR ILE          
SEQRES  42 B  970  ILE SER MET ALA THR ALA PRO SER ASP VAL LEU ALA VAL          
SEQRES  43 B  970  GLU LEU LEU GLN ARG GLU CYS GLY VAL ARG GLN PRO LEU          
SEQRES  44 B  970  PRO VAL VAL PRO LEU PHE GLU ARG LEU ALA ASP LEU GLN          
SEQRES  45 B  970  SER ALA PRO ALA SER VAL GLU ARG LEU PHE SER VAL ASP          
SEQRES  46 B  970  TRP TYR MET ASP ARG ILE LYS GLY LYS GLN GLN VAL MET          
SEQRES  47 B  970  VAL GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG LEU          
SEQRES  48 B  970  SER ALA ALA TRP GLN LEU TYR ARG ALA GLN GLU GLU MET          
SEQRES  49 B  970  ALA GLN VAL ALA LYS ARG TYR GLY VAL LYS LEU THR LEU          
SEQRES  50 B  970  PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY          
SEQRES  51 B  970  PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR          
SEQRES  52 B  970  ILE ASN GLY SER ILE ARG VAL THR VAL GLN GLY GLU VAL          
SEQRES  53 B  970  ILE GLU PHE CYS PHE GLY GLU GLU HIS LEU CYS PHE GLN          
SEQRES  54 B  970  THR LEU GLN ARG PHE THR ALA ALA THR LEU GLU HIS GLY          
SEQRES  55 B  970  MET HIS PRO PRO VAL SER PRO LYS PRO GLU TRP ARG LYS          
SEQRES  56 B  970  LEU MET ASP GLU MET ALA VAL VAL ALA THR GLU GLU TYR          
SEQRES  57 B  970  ARG SER VAL VAL VAL LYS GLU ALA ARG PHE VAL GLU TYR          
SEQRES  58 B  970  PHE ARG SER ALA THR PRO GLU THR GLU TYR GLY ARG MET          
SEQRES  59 B  970  ASN ILE GLY SER ARG PRO ALA LYS ARG ARG PRO GLY GLY          
SEQRES  60 B  970  GLY ILE THR THR LEU ARG ALA ILE PRO TRP ILE PHE SER          
SEQRES  61 B  970  TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY          
SEQRES  62 B  970  VAL GLY ALA ALA PHE LYS PHE ALA ILE ASP LYS ASP VAL          
SEQRES  63 B  970  ARG ASN PHE GLN VAL LEU LYS GLU MET TYR ASN GLU TRP          
SEQRES  64 B  970  PRO PHE PHE ARG VAL THR LEU ASP LEU LEU GLU MET VAL          
SEQRES  65 B  970  PHE ALA LYS GLY ASP PRO GLY ILE ALA GLY LEU TYR ASP          
SEQRES  66 B  970  GLU LEU LEU VAL ALA GLU GLU LEU LYS PRO PHE GLY LYS          
SEQRES  67 B  970  GLN LEU ARG ASP LYS TYR VAL GLU THR GLN GLN LEU LEU          
SEQRES  68 B  970  LEU GLN ILE ALA GLY HIS LYS ASP ILE LEU GLU GLY ASP          
SEQRES  69 B  970  PRO PHE LEU LYS GLN GLY LEU VAL LEU ARG ASN PRO TYR          
SEQRES  70 B  970  ILE THR THR LEU ASN VAL PHE GLN ALA TYR THR LEU LYS          
SEQRES  71 B  970  ARG ILE ARG ASP PRO ASN PHE LYS VAL THR PRO GLN PRO          
SEQRES  72 B  970  PRO LEU SER LYS GLU PHE ALA ASP GLU ASN LYS PRO ALA          
SEQRES  73 B  970  GLY LEU VAL LYS LEU ASN PRO ALA SER GLU TYR PRO PRO          
SEQRES  74 B  970  GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS GLY ILE          
SEQRES  75 B  970  ALA ALA GLY MET GLN ASN THR GLY                              
HET    SO4  A 971       5                                                       
HET    SO4  B1071       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
HELIX    1   1 ILE A   35  GLY A   54  1                                  20    
HELIX    2   2 GLY A   54  GLY A   73  1                                  20    
HELIX    3   3 THR A   77  LEU A   90  1                                  14    
HELIX    4   4 ALA A   91  ASN A  123  1                                  33    
HELIX    5   5 ASP A  142  SER A  152  1                                  11    
HELIX    6   6 SER A  157  ASN A  167  1                                  11    
HELIX    7   7 ARG A  183  LEU A  200  1                                  18    
HELIX    8   8 THR A  206  THR A  227  1                                  22    
HELIX    9   9 THR A  236  HIS A  249  1                                  14    
HELIX   10  10 GLY A  255  ASN A  269  1                                  15    
HELIX   11  11 THR A  300  LEU A  330  1                                  31    
HELIX   12  12 ASN A  336  GLY A  351  1                                  16    
HELIX   13  13 GLU A  369  SER A  395  1                                  27    
HELIX   14  14 SER A  408  CYS A  426  1                                  19    
HELIX   15  15 GLY A  434  GLY A  447  1                                  14    
HELIX   16  16 GLU A  458  GLY A  474  1                                  17    
HELIX   17  17 PRO A  482  GLY A  496  1                                  15    
HELIX   18  18 THR A  508  LEU A  524  1                                  17    
HELIX   19  19 PRO A  540  CYS A  553  1                                  14    
HELIX   20  20 ARG A  567  SER A  573  1                                   7    
HELIX   21  21 SER A  573  SER A  583  1                                  11    
HELIX   22  22 VAL A  584  LYS A  592  1                                   9    
HELIX   23  23 ASP A  603  ALA A  608  1                                   6    
HELIX   24  24 GLY A  609  ARG A  630  1                                  22    
HELIX   25  25 THR A  644  GLY A  648  5                                   5    
HELIX   26  26 PRO A  651  SER A  658  1                                   8    
HELIX   27  27 GLY A  674  GLY A  682  1                                   9    
HELIX   28  28 GLU A  683  HIS A  704  1                                  22    
HELIX   29  29 LYS A  710  VAL A  733  1                                  24    
HELIX   30  30 ARG A  737  THR A  746  1                                  10    
HELIX   31  31 GLU A  748  ASN A  755  5                                   8    
HELIX   32  32 ALA A  774  THR A  784  1                                  11    
HELIX   33  33 HIS A  787  LEU A  792  1                                   6    
HELIX   34  34 GLY A  793  ASP A  805  1                                  13    
HELIX   35  35 ARG A  807  TRP A  819  1                                  13    
HELIX   36  36 TRP A  819  ALA A  834  1                                  16    
HELIX   37  37 ASP A  837  LEU A  848  1                                  12    
HELIX   38  38 LEU A  853  GLY A  876  1                                  24    
HELIX   39  39 ASP A  884  ASP A  914  1                                  31    
HELIX   40  40 GLY A  950  GLN A  967  1                                  18    
HELIX   41  41 GLU B   36  GLY B   54  1                                  19    
HELIX   42  42 GLY B   54  GLY B   73  1                                  20    
HELIX   43  43 ASP B   76  GLY B   89  1                                  14    
HELIX   44  44 ALA B   91  ARG B  122  1                                  32    
HELIX   45  45 ASP B  142  SER B  152  1                                  11    
HELIX   46  46 SER B  157  ASN B  167  1                                  11    
HELIX   47  47 ARG B  183  LEU B  200  1                                  18    
HELIX   48  48 THR B  206  ARG B  226  1                                  21    
HELIX   49  49 THR B  236  THR B  251  1                                  16    
HELIX   50  50 THR B  251  ASN B  269  1                                  19    
HELIX   51  51 THR B  300  LEU B  330  1                                  31    
HELIX   52  52 ASN B  336  SER B  349  1                                  14    
HELIX   53  53 GLU B  369  SER B  395  1                                  27    
HELIX   54  54 SER B  408  CYS B  426  1                                  19    
HELIX   55  55 ASP B  428  ASP B  433  1                                   6    
HELIX   56  56 GLY B  434  GLY B  447  1                                  14    
HELIX   57  57 SER B  459  HIS B  472  1                                  14    
HELIX   58  58 PRO B  482  GLY B  496  1                                  15    
HELIX   59  59 THR B  508  LEU B  524  1                                  17    
HELIX   60  60 PRO B  525  ASP B  527  5                                   3    
HELIX   61  61 ALA B  539  GLU B  552  1                                  14    
HELIX   62  62 ARG B  567  PHE B  582  1                                  16    
HELIX   63  63 VAL B  584  LYS B  592  1                                   9    
HELIX   64  64 ASP B  603  ALA B  608  1                                   6    
HELIX   65  65 GLY B  609  TYR B  631  1                                  23    
HELIX   66  66 THR B  644  GLY B  648  5                                   5    
HELIX   67  67 PRO B  651  SER B  658  1                                   8    
HELIX   68  68 GLY B  674  GLY B  682  1                                   9    
HELIX   69  69 GLU B  683  HIS B  704  1                                  22    
HELIX   70  70 LYS B  710  VAL B  733  1                                  24    
HELIX   71  71 GLU B  735  THR B  746  1                                  12    
HELIX   72  72 PRO B  747  ASN B  755  5                                   9    
HELIX   73  73 ARG B  773  THR B  784  1                                  12    
HELIX   74  74 HIS B  787  LEU B  792  1                                   6    
HELIX   75  75 GLY B  793  LYS B  804  1                                  12    
HELIX   76  76 VAL B  806  TRP B  819  1                                  14    
HELIX   77  77 TRP B  819  ALA B  834  1                                  16    
HELIX   78  78 ASP B  837  TYR B  844  1                                   8    
HELIX   79  79 TYR B  844  VAL B  849  1                                   6    
HELIX   80  80 LEU B  853  GLY B  876  1                                  24    
HELIX   81  81 ASP B  884  ASP B  914  1                                  31    
HELIX   82  82 LEU B  938  ASN B  942  5                                   5    
HELIX   83  83 GLY B  950  GLN B  967  1                                  18    
SHEET    1   A 9 THR A 169  THR A 175  0                                        
SHEET    2   A 9 ILE A 283  SER A 287  1  O  ARG A 284   N  LEU A 172           
SHEET    3   A 9 LYS A 452  ARG A 456  1  O  ASP A 454   N  SER A 287           
SHEET    4   A 9 PHE A 529  ILE A 534  1  O  ILE A 533   N  ILE A 455           
SHEET    5   A 9 VAL A 561  PHE A 565  1  O  VAL A 562   N  ILE A 534           
SHEET    6   A 9 LYS A 594  GLY A 600  1  O  GLY A 600   N  PHE A 565           
SHEET    7   A 9 LYS A 634  GLY A 640  1  O  PHE A 638   N  VAL A 599           
SHEET    8   A 9 SER A 667  GLN A 673  1  O  ARG A 669   N  HIS A 639           
SHEET    9   A 9 THR A 169  THR A 175  1  N  VAL A 173   O  VAL A 672           
SHEET    1   B 9 THR B 169  THR B 175  0                                        
SHEET    2   B 9 ILE B 283  SER B 287  1  O  SER B 286   N  PHE B 174           
SHEET    3   B 9 LYS B 452  GLU B 458  1  O  LYS B 452   N  SER B 287           
SHEET    4   B 9 PHE B 529  SER B 535  1  O  GLY B 530   N  LEU B 453           
SHEET    5   B 9 VAL B 561  PHE B 565  1  O  VAL B 562   N  TYR B 532           
SHEET    6   B 9 LYS B 594  GLY B 600  1  O  MET B 598   N  PHE B 565           
SHEET    7   B 9 LYS B 634  GLY B 640  1  O  PHE B 638   N  VAL B 599           
SHEET    8   B 9 SER B 667  GLN B 673  1  O  ARG B 669   N  HIS B 639           
SHEET    9   B 9 THR B 169  THR B 175  1  N  VAL B 173   O  VAL B 670           
SITE     1 AC1  4 ARG A 183  ARG A 184  SER A 185  ARG A 231                    
SITE     1 AC2  4 ARG B 183  ARG B 184  SER B 185  ARG B 231                    
CRYST1  158.440  174.610  254.280  90.00  90.00  90.00 C 2 2 21     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      0.006312  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005727  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003933        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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