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Database: PDB
Entry: 1ZAH
LinkDB: 1ZAH
Original site: 1ZAH 
HEADER    LYASE                                   06-APR-05   1ZAH              
TITLE     FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE A;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MUSCLE-TYPE ALDOLASE;                                       
COMPND   5 EC: 4.1.2.13;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 GENE: ALDOA;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-SI (INVITROGEN);                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPB14                                     
KEYWDS    ALDOLASE, LYASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ST-JEAN,J.LAFRANCE-VANASSE,B.LIOTARD,J.SYGUSCH                      
REVDAT   5   23-AUG-23 1ZAH    1       REMARK                                   
REVDAT   4   11-OCT-17 1ZAH    1       REMARK                                   
REVDAT   3   24-FEB-09 1ZAH    1       VERSN                                    
REVDAT   2   02-AUG-05 1ZAH    1       JRNL                                     
REVDAT   1   10-MAY-05 1ZAH    0                                                
JRNL        AUTH   M.ST-JEAN,J.LAFRANCE-VANASSE,B.LIOTARD,J.SYGUSCH             
JRNL        TITL   HIGH RESOLUTION REACTION INTERMEDIATES OF RABBIT MUSCLE      
JRNL        TITL 2 FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE: SUBSTRATE CLEAVAGE AND   
JRNL        TITL 3 INDUCED FIT.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 280 27262 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15870069                                                     
JRNL        DOI    10.1074/JBC.M502413200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 118090                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5925                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11032                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 2427                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.69800                                              
REMARK   3    B22 (A**2) : -8.98400                                             
REMARK   3    B33 (A**2) : 6.28600                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.25800                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.267                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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) : 1.218 ; 0.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.839 ; 0.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.834 ; 0.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.620 ; 0.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 71.67                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000032499.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127047                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04900                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38800                            
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: PDB ENTRY 1ADO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM HEPES, PEG 4000, PH 7.5, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 296K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       51.45800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 THE HOMOTETRAMER FOUND IN THE     
REMARK 300 ASYMMETRIC UNIT                                                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 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 C   600     O    HOH D   757              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 344   C   -  N   -  CA  ANGL. DEV. =  12.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A   5      115.61    -23.06                                   
REMARK 500    PRO A  25      125.33    -39.25                                   
REMARK 500    ASP A  67       -7.93    -50.12                                   
REMARK 500    THR A 259      -30.75   -138.55                                   
REMARK 500    THR A 298     -159.03   -130.90                                   
REMARK 500    CYS A 338        6.29    -69.38                                   
REMARK 500    PRO A 344      -61.38    -20.43                                   
REMARK 500    SER A 345      -76.56   -103.01                                   
REMARK 500    ALA A 348      -61.78   -106.18                                   
REMARK 500    ALA A 350       79.40     74.31                                   
REMARK 500    ALA A 351      122.68   -176.14                                   
REMARK 500    ALA A 352       68.68   -173.07                                   
REMARK 500    GLU A 354      140.83    178.64                                   
REMARK 500    ILE A 358      -75.55   -133.95                                   
REMARK 500    PRO B   5      115.18    -25.39                                   
REMARK 500    PRO B 290       38.99    -69.67                                   
REMARK 500    THR B 298     -159.00   -129.65                                   
REMARK 500    SER B 345      -70.90    -61.79                                   
REMARK 500    GLN B 347      -75.65   -111.49                                   
REMARK 500    ALA B 350      -14.27   -142.57                                   
REMARK 500    GLU B 354     -125.70    -84.97                                   
REMARK 500    PHE B 357       72.65   -114.27                                   
REMARK 500    ILE B 358     -153.06    -88.48                                   
REMARK 500    PRO C   5      114.10    -25.25                                   
REMARK 500    ASP C  67       -6.05    -55.10                                   
REMARK 500    PRO C 188       76.21   -103.39                                   
REMARK 500    PRO C 290        4.14    -65.04                                   
REMARK 500    ALA C 304       -9.62    -59.44                                   
REMARK 500    SER C 345       55.58   -104.74                                   
REMARK 500    ALA C 348       35.00   -160.06                                   
REMARK 500    ALA C 350      -57.10   -159.86                                   
REMARK 500    SER C 353       97.22     58.41                                   
REMARK 500    GLU C 354      -82.94   -118.43                                   
REMARK 500    LEU C 356      -15.06   -161.91                                   
REMARK 500    PRO D   5      116.93    -27.31                                   
REMARK 500    ASP D  67       -8.00    -51.60                                   
REMARK 500    PRO D 290       -2.76    -58.14                                   
REMARK 500    THR D 298     -155.76   -131.77                                   
REMARK 500    SER D 345      147.66    167.46                                   
REMARK 500    GLN D 347      158.78    -48.28                                   
REMARK 500    ALA D 348       89.22     66.06                                   
REMARK 500    ALA D 362      -56.71   -165.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 213         0.07    SIDE CHAIN                              
REMARK 500    TYR B 213         0.07    SIDE CHAIN                              
REMARK 500    TYR D 213         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZAI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZAJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZAL   RELATED DB: PDB                                   
DBREF  1ZAH A    1   363  UNP    P00883   ALDOA_RABIT      1    363             
DBREF  1ZAH B    1   363  UNP    P00883   ALDOA_RABIT      1    363             
DBREF  1ZAH C    1   363  UNP    P00883   ALDOA_RABIT      1    363             
DBREF  1ZAH D    1   363  UNP    P00883   ALDOA_RABIT      1    363             
SEQRES   1 A  363  PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS          
SEQRES   2 A  363  GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY          
SEQRES   3 A  363  LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE          
SEQRES   4 A  363  ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU          
SEQRES   5 A  363  GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA          
SEQRES   6 A  363  ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU          
SEQRES   7 A  363  PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG          
SEQRES   8 A  363  PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL          
SEQRES   9 A  363  GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY          
SEQRES  10 A  363  THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU          
SEQRES  11 A  363  SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP          
SEQRES  12 A  363  PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS          
SEQRES  13 A  363  THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL          
SEQRES  14 A  363  LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE          
SEQRES  15 A  363  VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP          
SEQRES  16 A  363  HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL          
SEQRES  17 A  363  LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE          
SEQRES  18 A  363  TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR          
SEQRES  19 A  363  PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU          
SEQRES  20 A  363  ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL          
SEQRES  21 A  363  PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY          
SEQRES  22 A  363  GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE          
SEQRES  23 A  363  ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE          
SEQRES  24 A  363  SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA          
SEQRES  25 A  363  TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU          
SEQRES  26 A  363  GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS          
SEQRES  27 A  363  GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA          
SEQRES  28 A  363  ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR              
SEQRES   1 B  363  PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS          
SEQRES   2 B  363  GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY          
SEQRES   3 B  363  LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE          
SEQRES   4 B  363  ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU          
SEQRES   5 B  363  GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA          
SEQRES   6 B  363  ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU          
SEQRES   7 B  363  PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG          
SEQRES   8 B  363  PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL          
SEQRES   9 B  363  GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY          
SEQRES  10 B  363  THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU          
SEQRES  11 B  363  SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP          
SEQRES  12 B  363  PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS          
SEQRES  13 B  363  THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL          
SEQRES  14 B  363  LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE          
SEQRES  15 B  363  VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP          
SEQRES  16 B  363  HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL          
SEQRES  17 B  363  LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE          
SEQRES  18 B  363  TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR          
SEQRES  19 B  363  PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU          
SEQRES  20 B  363  ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL          
SEQRES  21 B  363  PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY          
SEQRES  22 B  363  GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE          
SEQRES  23 B  363  ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE          
SEQRES  24 B  363  SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA          
SEQRES  25 B  363  TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU          
SEQRES  26 B  363  GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS          
SEQRES  27 B  363  GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA          
SEQRES  28 B  363  ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR              
SEQRES   1 C  363  PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS          
SEQRES   2 C  363  GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY          
SEQRES   3 C  363  LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE          
SEQRES   4 C  363  ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU          
SEQRES   5 C  363  GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA          
SEQRES   6 C  363  ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU          
SEQRES   7 C  363  PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG          
SEQRES   8 C  363  PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL          
SEQRES   9 C  363  GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY          
SEQRES  10 C  363  THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU          
SEQRES  11 C  363  SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP          
SEQRES  12 C  363  PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS          
SEQRES  13 C  363  THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL          
SEQRES  14 C  363  LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE          
SEQRES  15 C  363  VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP          
SEQRES  16 C  363  HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL          
SEQRES  17 C  363  LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE          
SEQRES  18 C  363  TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR          
SEQRES  19 C  363  PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU          
SEQRES  20 C  363  ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL          
SEQRES  21 C  363  PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY          
SEQRES  22 C  363  GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE          
SEQRES  23 C  363  ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE          
SEQRES  24 C  363  SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA          
SEQRES  25 C  363  TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU          
SEQRES  26 C  363  GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS          
SEQRES  27 C  363  GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA          
SEQRES  28 C  363  ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR              
SEQRES   1 D  363  PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS          
SEQRES   2 D  363  GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY          
SEQRES   3 D  363  LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE          
SEQRES   4 D  363  ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU          
SEQRES   5 D  363  GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA          
SEQRES   6 D  363  ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU          
SEQRES   7 D  363  PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG          
SEQRES   8 D  363  PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL          
SEQRES   9 D  363  GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY          
SEQRES  10 D  363  THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU          
SEQRES  11 D  363  SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP          
SEQRES  12 D  363  PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS          
SEQRES  13 D  363  THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL          
SEQRES  14 D  363  LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE          
SEQRES  15 D  363  VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP          
SEQRES  16 D  363  HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL          
SEQRES  17 D  363  LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE          
SEQRES  18 D  363  TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR          
SEQRES  19 D  363  PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU          
SEQRES  20 D  363  ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL          
SEQRES  21 D  363  PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY          
SEQRES  22 D  363  GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE          
SEQRES  23 D  363  ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE          
SEQRES  24 D  363  SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA          
SEQRES  25 D  363  TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU          
SEQRES  26 D  363  GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS          
SEQRES  27 D  363  GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA          
SEQRES  28 D  363  ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR              
FORMUL   5  HOH   *2427(H2 O)                                                   
HELIX    1   1 THR A    8  VAL A   23  1                                  16    
HELIX    2   2 SER A   35  SER A   45  1                                  11    
HELIX    3   3 THR A   51  THR A   64  1                                  14    
HELIX    4   4 ASP A   66  ASN A   70  5                                   5    
HELIX    5   5 PHE A   79  TYR A   84  1                                   6    
HELIX    6   6 PRO A   92  LYS A  100  1                                   9    
HELIX    7   7 GLY A  129  ASP A  140  1                                  12    
HELIX    8   8 SER A  159  ASN A  180  1                                  22    
HELIX    9   9 ASP A  197  HIS A  219  1                                  23    
HELIX   10  10 TYR A  222  THR A  226  5                                   5    
HELIX   11  11 SER A  244  ARG A  258  1                                  15    
HELIX   12  12 SER A  275  CYS A  289  1                                  15    
HELIX   13  13 GLY A  302  GLY A  314  1                                  13    
HELIX   14  14 LYS A  316  GLU A  318  5                                   3    
HELIX   15  15 ASN A  319  CYS A  338  1                                  20    
HELIX   16  16 THR B    8  VAL B   23  1                                  16    
HELIX   17  17 SER B   35  SER B   45  1                                  11    
HELIX   18  18 THR B   51  THR B   64  1                                  14    
HELIX   19  19 ASP B   66  ASN B   70  5                                   5    
HELIX   20  20 PHE B   79  TYR B   84  1                                   6    
HELIX   21  21 PRO B   92  LYS B  100  1                                   9    
HELIX   22  22 GLY B  129  ASP B  140  1                                  12    
HELIX   23  23 SER B  159  ASN B  180  1                                  22    
HELIX   24  24 ASP B  197  HIS B  219  1                                  23    
HELIX   25  25 TYR B  222  GLY B  225  5                                   4    
HELIX   26  26 SER B  244  ARG B  258  1                                  15    
HELIX   27  27 SER B  275  CYS B  289  1                                  15    
HELIX   28  28 GLY B  302  GLY B  314  1                                  13    
HELIX   29  29 LYS B  316  GLU B  318  5                                   3    
HELIX   30  30 ASN B  319  CYS B  338  1                                  20    
HELIX   31  31 SER B  359  TYR B  363  5                                   5    
HELIX   32  32 THR C    8  VAL C   23  1                                  16    
HELIX   33  33 SER C   35  SER C   45  1                                  11    
HELIX   34  34 THR C   51  THR C   64  1                                  14    
HELIX   35  35 ASP C   66  ASN C   70  5                                   5    
HELIX   36  36 PHE C   79  TYR C   84  1                                   6    
HELIX   37  37 PRO C   92  LYS C  100  1                                   9    
HELIX   38  38 GLY C  129  ASP C  140  1                                  12    
HELIX   39  39 SER C  159  ASN C  180  1                                  22    
HELIX   40  40 ASP C  197  HIS C  219  1                                  23    
HELIX   41  41 TYR C  222  GLY C  225  5                                   4    
HELIX   42  42 SER C  244  ARG C  258  1                                  15    
HELIX   43  43 SER C  275  CYS C  289  1                                  15    
HELIX   44  44 GLY C  302  GLY C  314  1                                  13    
HELIX   45  45 LYS C  316  GLU C  318  5                                   3    
HELIX   46  46 ASN C  319  CYS C  338  1                                  20    
HELIX   47  47 SER C  359  TYR C  363  5                                   5    
HELIX   48  48 THR D    8  VAL D   23  1                                  16    
HELIX   49  49 SER D   35  SER D   45  1                                  11    
HELIX   50  50 THR D   51  THR D   64  1                                  14    
HELIX   51  51 ASP D   66  ASN D   70  5                                   5    
HELIX   52  52 PHE D   79  TYR D   84  1                                   6    
HELIX   53  53 PRO D   92  LYS D  100  1                                   9    
HELIX   54  54 GLY D  129  ASP D  140  1                                  12    
HELIX   55  55 SER D  159  ASN D  180  1                                  22    
HELIX   56  56 ASP D  197  HIS D  219  1                                  23    
HELIX   57  57 TYR D  222  GLY D  225  5                                   4    
HELIX   58  58 SER D  244  ARG D  258  1                                  15    
HELIX   59  59 SER D  275  CYS D  289  1                                  15    
HELIX   60  60 GLY D  302  GLY D  314  1                                  13    
HELIX   61  61 LYS D  316  GLU D  318  5                                   3    
HELIX   62  62 ASN D  319  CYS D  338  1                                  20    
HELIX   63  63 GLY D  349  SER D  353  5                                   5    
SHEET    1   A 9 GLY A  28  ALA A  32  0                                        
SHEET    2   A 9 ILE A  73  LEU A  78  1  O  ILE A  77   N  LEU A  30           
SHEET    3   A 9 VAL A 103  LYS A 107  1  O  GLY A 105   N  VAL A  76           
SHEET    4   A 9 PHE A 144  LEU A 151  1  O  PHE A 144   N  ILE A 106           
SHEET    5   A 9 VAL A 183  ILE A 190  1  O  GLU A 189   N  LEU A 151           
SHEET    6   A 9 LEU A 227  LEU A 228  1  O  LEU A 227   N  VAL A 186           
SHEET    7   A 9 GLY A 266  PHE A 269  1  O  THR A 268   N  LEU A 228           
SHEET    8   A 9 ALA A 296  TYR A 301  1  O  THR A 298   N  VAL A 267           
SHEET    9   A 9 GLY A  28  ALA A  32  1  N  ILE A  29   O  PHE A 299           
SHEET    1   B 2 VAL A 112  PRO A 114  0                                        
SHEET    2   B 2 THR A 122  THR A 124 -1  O  THR A 123   N  VAL A 113           
SHEET    1   C 9 GLY B  28  ALA B  32  0                                        
SHEET    2   C 9 ILE B  73  LEU B  78  1  O  ILE B  77   N  LEU B  30           
SHEET    3   C 9 VAL B 103  LYS B 107  1  O  GLY B 105   N  VAL B  76           
SHEET    4   C 9 PHE B 144  LEU B 151  1  O  PHE B 144   N  ILE B 106           
SHEET    5   C 9 VAL B 183  ILE B 190  1  O  GLU B 187   N  CYS B 149           
SHEET    6   C 9 LEU B 227  LEU B 228  1  O  LEU B 227   N  VAL B 186           
SHEET    7   C 9 GLY B 266  PHE B 269  1  O  THR B 268   N  LEU B 228           
SHEET    8   C 9 ALA B 296  TYR B 301  1  O  THR B 298   N  VAL B 267           
SHEET    9   C 9 GLY B  28  ALA B  32  1  N  ILE B  29   O  PHE B 299           
SHEET    1   D 2 VAL B 112  PRO B 114  0                                        
SHEET    2   D 2 THR B 122  THR B 124 -1  O  THR B 123   N  VAL B 113           
SHEET    1   E 9 GLY C  28  ALA C  32  0                                        
SHEET    2   E 9 ILE C  73  LEU C  78  1  O  ILE C  77   N  LEU C  30           
SHEET    3   E 9 VAL C 103  LYS C 107  1  O  GLY C 105   N  VAL C  76           
SHEET    4   E 9 PHE C 144  LEU C 151  1  O  LYS C 146   N  ILE C 106           
SHEET    5   E 9 VAL C 183  ILE C 190  1  O  GLU C 187   N  CYS C 149           
SHEET    6   E 9 LEU C 227  LEU C 228  1  O  LEU C 227   N  VAL C 186           
SHEET    7   E 9 GLY C 266  PHE C 269  1  O  THR C 268   N  LEU C 228           
SHEET    8   E 9 ALA C 296  TYR C 301  1  O  THR C 298   N  VAL C 267           
SHEET    9   E 9 GLY C  28  ALA C  32  1  N  ILE C  29   O  PHE C 299           
SHEET    1   F 2 VAL C 112  PRO C 114  0                                        
SHEET    2   F 2 THR C 122  THR C 124 -1  O  THR C 123   N  VAL C 113           
SHEET    1   G 9 GLY D  28  ALA D  32  0                                        
SHEET    2   G 9 ILE D  73  LEU D  78  1  O  GLY D  74   N  GLY D  28           
SHEET    3   G 9 VAL D 103  LYS D 107  1  O  GLY D 105   N  VAL D  76           
SHEET    4   G 9 PHE D 144  LEU D 151  1  O  PHE D 144   N  ILE D 106           
SHEET    5   G 9 VAL D 183  ILE D 190  1  O  GLU D 189   N  LEU D 151           
SHEET    6   G 9 LEU D 227  LEU D 228  1  O  LEU D 227   N  VAL D 186           
SHEET    7   G 9 GLY D 266  PHE D 269  1  O  THR D 268   N  LEU D 228           
SHEET    8   G 9 ALA D 296  TYR D 301  1  O  ALA D 296   N  VAL D 267           
SHEET    9   G 9 GLY D  28  ALA D  32  1  N  ALA D  31   O  TYR D 301           
SHEET    1   H 2 VAL D 112  PRO D 114  0                                        
SHEET    2   H 2 THR D 122  THR D 124 -1  O  THR D 123   N  VAL D 113           
CISPEP   1 THR A  157    PRO A  158          0        -0.47                     
CISPEP   2 THR B  157    PRO B  158          0        -0.47                     
CISPEP   3 THR C  157    PRO C  158          0        -0.02                     
CISPEP   4 THR D  157    PRO D  158          0        -0.06                     
CRYST1   83.096  102.916   84.663  90.00  98.36  90.00 P 1 21 1      8          
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      0.012030  0.000000  0.001770        0.00000                         
SCALE2      0.000000  0.009720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011940        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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