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Database: PDB
Entry: 1JCN
LinkDB: 1JCN
Original site: 1JCN 
HEADER    OXIDOREDUCTASE                          11-JUN-01   1JCN              
TITLE     BINARY COMPLEX OF HUMAN TYPE-I INOSINE MONOPHOSPHATE DEHYDROGENASE    
TITLE    2 WITH 6-CL-IMP                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INOSINE MONOPHOSPHATE DEHYDROGENASE I;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: IMPD, IMPDH, INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE 1;      
COMPND   5 EC: 1.1.1.205;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 VARIANT: TYPE I ISOZYME;                                             
SOURCE   6 GENE: IMPDH1;                                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PIMP1                                     
KEYWDS    DEHYDROGENASE, IMPD, IMPDH, GUANINE NUCLEOTIDE SYNTHESIS,             
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.RISAL,M.D.STRICKLER,B.M.GOLDSTEIN                                   
REVDAT   4   04-OCT-17 1JCN    1       REMARK                                   
REVDAT   3   13-JUL-11 1JCN    1       VERSN                                    
REVDAT   2   24-FEB-09 1JCN    1       VERSN                                    
REVDAT   1   17-JUN-03 1JCN    0                                                
JRNL        AUTH   D.RISAL,M.D.STRICKLER,B.M.GOLDSTEIN                          
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN TYPE I INOSINE MONOPHOSPHATE  
JRNL        TITL 2 DEHYDROGENASE AND IMPLICATIONS FOR ISOFORM SPECIFICITY       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2983561.890                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 44410                          
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) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4483                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6364                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 723                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5878                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 294                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.22000                                             
REMARK   3    B22 (A**2) : -0.22000                                             
REMARK   3    B33 (A**2) : 0.44000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.920                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.480 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.550 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.130 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.170 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 48.48                                                
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_IMP_AUTO_REP.PARAM                     
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_IMP_AUTO.TOP                           
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 45 RESIDUES OF THE FLANKING DOMAIN AND    
REMARK   3  50 RESIDUES OF THE ACTIVE-SITE FLAP ARE DISORDERED IN BOTH          
REMARK   3  MONOMERS. 6 RESIDUES IN THE FLANKING DOMAIN HAVE BEEN MODELLED      
REMARK   3  UP TO THE CB DUE TO LACK OF ROBUST SIDE-CHAIN ELECTRON DENSITY.     
REMARK   3  SEGMENTS OF THE CORE DOMAIN RELATED BY NCS-SYMMETRY HAD NCS         
REMARK   3  RESTRAINTS ON BACKBONE C-ALPHA, N, AND C ATOMS DURING REFINEMENT.   
REMARK   4                                                                      
REMARK   4 1JCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013627.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 93.0                               
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, DPS                        
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44411                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : 0.09300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: CORE DOMAIN OF IMPDH MONOMER FROM HUMAN TYPE II/6    
REMARK 200  -CL-IMP COMPLEX STRUCTURE                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 7MGS/ML PROTEIN, 50    
REMARK 280  MM TRIS HCL (PH 8.0), 50 MM KCL, 2MM EDTA, 1MM DTT, 5MM 6-CL-       
REMARK 280  IMP. WELL SOLUTION: 9% (W/V) PEG-800, 100 MM TRIS HCL (PH 8.0),     
REMARK 280  1.0 M LICL, 24 MM BETAMERCAPTOETHANOL (2+2 MICROLITER DROPS), PH    
REMARK 280  8.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       74.05400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       74.05400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       61.00800            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       74.05400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       74.05400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.00800            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       74.05400            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       74.05400            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       61.00800            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       74.05400            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       74.05400            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       61.00800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 65540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 14250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 37060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 122870 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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     ASP A     3                                                      
REMARK 465     TYR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A   124                                                      
REMARK 465     HIS A   125                                                      
REMARK 465     THR A   126                                                      
REMARK 465     VAL A   127                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     VAL A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     ALA A   133                                                      
REMARK 465     LYS A   134                                                      
REMARK 465     MET A   135                                                      
REMARK 465     ARG A   136                                                      
REMARK 465     HIS A   137                                                      
REMARK 465     GLY A   138                                                      
REMARK 465     PHE A   139                                                      
REMARK 465     SER A   140                                                      
REMARK 465     THR A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     MET A   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     LEU A   154                                                      
REMARK 465     PHE A   165                                                      
REMARK 465     LEU A   166                                                      
REMARK 465     ALA A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     ASP A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     THR A   172                                                      
REMARK 465     THR A   173                                                      
REMARK 465     LEU A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     VAL A   178                                                      
REMARK 465     MET A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     ALA A   220                                                      
REMARK 465     ILE A   221                                                      
REMARK 465     ILE A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     TYR A   400                                                      
REMARK 465     PHE A   401                                                      
REMARK 465     PHE A   402                                                      
REMARK 465     SER A   403                                                      
REMARK 465     ASP A   404                                                      
REMARK 465     GLY A   405                                                      
REMARK 465     VAL A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     LEU A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     TYR A   411                                                      
REMARK 465     ARG A   412                                                      
REMARK 465     GLY A   413                                                      
REMARK 465     MET A   414                                                      
REMARK 465     GLY A   415                                                      
REMARK 465     SER A   416                                                      
REMARK 465     LEU A   417                                                      
REMARK 465     ASP A   418                                                      
REMARK 465     ALA A   419                                                      
REMARK 465     MET A   420                                                      
REMARK 465     GLU A   421                                                      
REMARK 465     LYS A   422                                                      
REMARK 465     SER A   423                                                      
REMARK 465     SER A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     SER A   426                                                      
REMARK 465     GLN A   427                                                      
REMARK 465     LYS A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     TYR A   430                                                      
REMARK 465     PHE A   431                                                      
REMARK 465     SER A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     GLY A   434                                                      
REMARK 465     ASP A   435                                                      
REMARK 465     LYS A   436                                                      
REMARK 465     VAL A   437                                                      
REMARK 465     LYS A   438                                                      
REMARK 465     ILE A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     GLN A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     VAL A   443                                                      
REMARK 465     SER A   444                                                      
REMARK 465     GLY A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ILE A   447                                                      
REMARK 465     GLN A   448                                                      
REMARK 465     ASP A   449                                                      
REMARK 465     GLU A   500                                                      
REMARK 465     GLY A   501                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     VAL A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     HIS A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     TYR A   509                                                      
REMARK 465     GLU A   510                                                      
REMARK 465     LYS A   511                                                      
REMARK 465     ARG A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     TYR A   514                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     TYR B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     SER B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     THR B   126                                                      
REMARK 465     VAL B   127                                                      
REMARK 465     GLY B   128                                                      
REMARK 465     ASP B   129                                                      
REMARK 465     VAL B   130                                                      
REMARK 465     LEU B   131                                                      
REMARK 465     GLU B   132                                                      
REMARK 465     ALA B   133                                                      
REMARK 465     LYS B   134                                                      
REMARK 465     MET B   135                                                      
REMARK 465     ARG B   136                                                      
REMARK 465     HIS B   137                                                      
REMARK 465     GLY B   138                                                      
REMARK 465     PHE B   139                                                      
REMARK 465     SER B   140                                                      
REMARK 465     THR B   147                                                      
REMARK 465     GLY B   148                                                      
REMARK 465     THR B   149                                                      
REMARK 465     MET B   150                                                      
REMARK 465     GLY B   151                                                      
REMARK 465     SER B   152                                                      
REMARK 465     LYS B   153                                                      
REMARK 465     LEU B   154                                                      
REMARK 465     PHE B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     ALA B   167                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     ASP B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     THR B   172                                                      
REMARK 465     THR B   173                                                      
REMARK 465     LEU B   174                                                      
REMARK 465     LEU B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     VAL B   178                                                      
REMARK 465     MET B   179                                                      
REMARK 465     THR B   180                                                      
REMARK 465     ALA B   220                                                      
REMARK 465     ILE B   221                                                      
REMARK 465     ILE B   222                                                      
REMARK 465     ALA B   223                                                      
REMARK 465     TYR B   400                                                      
REMARK 465     PHE B   401                                                      
REMARK 465     PHE B   402                                                      
REMARK 465     SER B   403                                                      
REMARK 465     ASP B   404                                                      
REMARK 465     GLY B   405                                                      
REMARK 465     VAL B   406                                                      
REMARK 465     ARG B   407                                                      
REMARK 465     LEU B   408                                                      
REMARK 465     LYS B   409                                                      
REMARK 465     LYS B   410                                                      
REMARK 465     TYR B   411                                                      
REMARK 465     ARG B   412                                                      
REMARK 465     GLY B   413                                                      
REMARK 465     MET B   414                                                      
REMARK 465     GLY B   415                                                      
REMARK 465     SER B   416                                                      
REMARK 465     LEU B   417                                                      
REMARK 465     ASP B   418                                                      
REMARK 465     ALA B   419                                                      
REMARK 465     MET B   420                                                      
REMARK 465     GLU B   421                                                      
REMARK 465     LYS B   422                                                      
REMARK 465     SER B   423                                                      
REMARK 465     SER B   424                                                      
REMARK 465     SER B   425                                                      
REMARK 465     SER B   426                                                      
REMARK 465     GLN B   427                                                      
REMARK 465     LYS B   428                                                      
REMARK 465     ARG B   429                                                      
REMARK 465     TYR B   430                                                      
REMARK 465     PHE B   431                                                      
REMARK 465     SER B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     GLY B   434                                                      
REMARK 465     ASP B   435                                                      
REMARK 465     LYS B   436                                                      
REMARK 465     VAL B   437                                                      
REMARK 465     LYS B   438                                                      
REMARK 465     ILE B   439                                                      
REMARK 465     ALA B   440                                                      
REMARK 465     GLN B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     VAL B   443                                                      
REMARK 465     SER B   444                                                      
REMARK 465     GLY B   445                                                      
REMARK 465     SER B   446                                                      
REMARK 465     ILE B   447                                                      
REMARK 465     GLN B   448                                                      
REMARK 465     ASP B   449                                                      
REMARK 465     GLU B   500                                                      
REMARK 465     GLY B   501                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     VAL B   503                                                      
REMARK 465     HIS B   504                                                      
REMARK 465     GLY B   505                                                      
REMARK 465     LEU B   506                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     SER B   508                                                      
REMARK 465     TYR B   509                                                      
REMARK 465     GLU B   510                                                      
REMARK 465     LYS B   511                                                      
REMARK 465     ARG B   512                                                      
REMARK 465     LEU B   513                                                      
REMARK 465     TYR B   514                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A 142    CG1  CG2  CD1                                       
REMARK 470     PRO A 143    CG   CD                                             
REMARK 470     ILE A 144    CG1  CG2  CD1                                       
REMARK 470     THR A 145    OG1  CG2                                            
REMARK 470     GLU A 146    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 213    CG   OD1  ND2                                       
REMARK 470     ASP A 214    CG   OD1  OD2                                       
REMARK 470     CYS A 215    SG                                                  
REMARK 470     ASP A 216    CG   OD1  OD2                                       
REMARK 470     GLU A 217    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 218    CG   CD1  CD2                                       
REMARK 470     VAL A 219    CG1  CG2                                            
REMARK 470     ILE B 142    CG1  CG2  CD1                                       
REMARK 470     PRO B 143    CG   CD                                             
REMARK 470     ILE B 144    CG1  CG2  CD1                                       
REMARK 470     THR B 145    OG1  CG2                                            
REMARK 470     GLU B 146    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 213    CG   OD1  ND2                                       
REMARK 470     ASP B 214    CG   OD1  OD2                                       
REMARK 470     CYS B 215    SG                                                  
REMARK 470     ASP B 216    CG   OD1  OD2                                       
REMARK 470     GLU B 217    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 218    CG   CD1  CD2                                       
REMARK 470     VAL B 219    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN A   283     N    GLY A   302              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  12      168.64    179.64                                   
REMARK 500    PRO A  14     -118.71    -81.93                                   
REMARK 500    ASP A  16     -129.04    -76.58                                   
REMARK 500    SER A  26     -116.12    -55.81                                   
REMARK 500    ALA A  27       -0.09   -148.27                                   
REMARK 500    VAL A  73      -51.70   -132.95                                   
REMARK 500    CYS A  95     -178.73   -171.63                                   
REMARK 500    VAL A 119       82.29    -68.92                                   
REMARK 500    LEU A 121     -173.36     57.46                                   
REMARK 500    SER A 122      -25.09   -176.72                                   
REMARK 500    THR A 145       75.82     67.69                                   
REMARK 500    SER A 160       -9.04    -59.26                                   
REMARK 500    VAL A 192      136.39    -39.15                                   
REMARK 500    ASN A 213      -37.18   -165.69                                   
REMARK 500    CYS A 215       -9.66     90.25                                   
REMARK 500    LEU A 227      114.65   -179.50                                   
REMARK 500    LYS A 229       41.22    179.04                                   
REMARK 500    ALA A 236      131.07    -39.43                                   
REMARK 500    MET A 325      113.44   -173.70                                   
REMARK 500    GLN A 334       76.51   -158.40                                   
REMARK 500    MET A 337     -128.07   -107.50                                   
REMARK 500    MET A 495       28.81    -61.79                                   
REMARK 500    ALA A 497      133.55    -25.48                                   
REMARK 500    GLN A 498       13.31   -147.26                                   
REMARK 500    VAL B  13      -66.08   -101.56                                   
REMARK 500    PRO B  14     -137.29    -78.85                                   
REMARK 500    ASP B  16     -132.95    -74.59                                   
REMARK 500    SER B  26     -118.63    -60.17                                   
REMARK 500    VAL B  73      -52.62   -130.76                                   
REMARK 500    CYS B  95     -178.41   -170.53                                   
REMARK 500    LEU B 121     -177.14     55.68                                   
REMARK 500    SER B 122      -20.91    176.93                                   
REMARK 500    THR B 145       84.25     95.69                                   
REMARK 500    ILE B 183     -166.94   -118.86                                   
REMARK 500    ASN B 213      -84.68    -81.66                                   
REMARK 500    ASP B 214      -81.94   -124.61                                   
REMARK 500    ASP B 216     -167.79   -113.19                                   
REMARK 500    LEU B 218      -72.07    -59.73                                   
REMARK 500    THR B 225     -121.56   -157.34                                   
REMARK 500    LEU B 227       38.41   -177.20                                   
REMARK 500    LYS B 229       42.84   -177.51                                   
REMARK 500    TYR B 233       84.99     25.31                                   
REMARK 500    ALA B 236      131.00    -39.26                                   
REMARK 500    MET B 325      114.53   -168.10                                   
REMARK 500    GLN B 334       84.31   -174.77                                   
REMARK 500    MET B 337     -124.11   -108.78                                   
REMARK 500    MET B 495      -19.79    -47.64                                   
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 CPR A 631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPR B 631                 
DBREF  1JCN A    1   514  UNP    P20839   IMDH1_HUMAN      1    514             
DBREF  1JCN B    1   514  UNP    P20839   IMDH1_HUMAN      1    514             
SEQRES   1 A  514  MET ALA ASP TYR LEU ILE SER GLY GLY THR GLY TYR VAL          
SEQRES   2 A  514  PRO GLU ASP GLY LEU THR ALA GLN GLN LEU PHE ALA SER          
SEQRES   3 A  514  ALA ASP ASP LEU THR TYR ASN ASP PHE LEU ILE LEU PRO          
SEQRES   4 A  514  GLY PHE ILE ASP PHE ILE ALA ASP GLU VAL ASP LEU THR          
SEQRES   5 A  514  SER ALA LEU THR ARG LYS ILE THR LEU LYS THR PRO LEU          
SEQRES   6 A  514  ILE SER SER PRO MET ASP THR VAL THR GLU ALA ASP MET          
SEQRES   7 A  514  ALA ILE ALA MET ALA LEU MET GLY GLY ILE GLY PHE ILE          
SEQRES   8 A  514  HIS HIS ASN CYS THR PRO GLU PHE GLN ALA ASN GLU VAL          
SEQRES   9 A  514  ARG LYS VAL LYS ASN PHE GLU GLN GLY PHE ILE THR ASP          
SEQRES  10 A  514  PRO VAL VAL LEU SER PRO SER HIS THR VAL GLY ASP VAL          
SEQRES  11 A  514  LEU GLU ALA LYS MET ARG HIS GLY PHE SER GLY ILE PRO          
SEQRES  12 A  514  ILE THR GLU THR GLY THR MET GLY SER LYS LEU VAL GLY          
SEQRES  13 A  514  ILE VAL THR SER ARG ASP ILE ASP PHE LEU ALA GLU LYS          
SEQRES  14 A  514  ASP HIS THR THR LEU LEU SER GLU VAL MET THR PRO ARG          
SEQRES  15 A  514  ILE GLU LEU VAL VAL ALA PRO ALA GLY VAL THR LEU LYS          
SEQRES  16 A  514  GLU ALA ASN GLU ILE LEU GLN ARG SER LYS LYS GLY LYS          
SEQRES  17 A  514  LEU PRO ILE VAL ASN ASP CYS ASP GLU LEU VAL ALA ILE          
SEQRES  18 A  514  ILE ALA ARG THR ASP LEU LYS LYS ASN ARG ASP TYR PRO          
SEQRES  19 A  514  LEU ALA SER LYS ASP SER GLN LYS GLN LEU LEU CYS GLY          
SEQRES  20 A  514  ALA ALA VAL GLY THR ARG GLU ASP ASP LYS TYR ARG LEU          
SEQRES  21 A  514  ASP LEU LEU THR GLN ALA GLY VAL ASP VAL ILE VAL LEU          
SEQRES  22 A  514  ASP SER SER GLN GLY ASN SER VAL TYR GLN ILE ALA MET          
SEQRES  23 A  514  VAL HIS TYR ILE LYS GLN LYS TYR PRO HIS LEU GLN VAL          
SEQRES  24 A  514  ILE GLY GLY ASN VAL VAL THR ALA ALA GLN ALA LYS ASN          
SEQRES  25 A  514  LEU ILE ASP ALA GLY VAL ASP GLY LEU ARG VAL GLY MET          
SEQRES  26 A  514  GLY CYS GLY SER ILE CYS ILE THR GLN GLU VAL MET ALA          
SEQRES  27 A  514  CYS GLY ARG PRO GLN GLY THR ALA VAL TYR LYS VAL ALA          
SEQRES  28 A  514  GLU TYR ALA ARG ARG PHE GLY VAL PRO ILE ILE ALA ASP          
SEQRES  29 A  514  GLY GLY ILE GLN THR VAL GLY HIS VAL VAL LYS ALA LEU          
SEQRES  30 A  514  ALA LEU GLY ALA SER THR VAL MET MET GLY SER LEU LEU          
SEQRES  31 A  514  ALA ALA THR THR GLU ALA PRO GLY GLU TYR PHE PHE SER          
SEQRES  32 A  514  ASP GLY VAL ARG LEU LYS LYS TYR ARG GLY MET GLY SER          
SEQRES  33 A  514  LEU ASP ALA MET GLU LYS SER SER SER SER GLN LYS ARG          
SEQRES  34 A  514  TYR PHE SER GLU GLY ASP LYS VAL LYS ILE ALA GLN GLY          
SEQRES  35 A  514  VAL SER GLY SER ILE GLN ASP LYS GLY SER ILE GLN LYS          
SEQRES  36 A  514  PHE VAL PRO TYR LEU ILE ALA GLY ILE GLN HIS GLY CYS          
SEQRES  37 A  514  GLN ASP ILE GLY ALA ARG SER LEU SER VAL LEU ARG SER          
SEQRES  38 A  514  MET MET TYR SER GLY GLU LEU LYS PHE GLU LYS ARG THR          
SEQRES  39 A  514  MET SER ALA GLN ILE GLU GLY GLY VAL HIS GLY LEU HIS          
SEQRES  40 A  514  SER TYR GLU LYS ARG LEU TYR                                  
SEQRES   1 B  514  MET ALA ASP TYR LEU ILE SER GLY GLY THR GLY TYR VAL          
SEQRES   2 B  514  PRO GLU ASP GLY LEU THR ALA GLN GLN LEU PHE ALA SER          
SEQRES   3 B  514  ALA ASP ASP LEU THR TYR ASN ASP PHE LEU ILE LEU PRO          
SEQRES   4 B  514  GLY PHE ILE ASP PHE ILE ALA ASP GLU VAL ASP LEU THR          
SEQRES   5 B  514  SER ALA LEU THR ARG LYS ILE THR LEU LYS THR PRO LEU          
SEQRES   6 B  514  ILE SER SER PRO MET ASP THR VAL THR GLU ALA ASP MET          
SEQRES   7 B  514  ALA ILE ALA MET ALA LEU MET GLY GLY ILE GLY PHE ILE          
SEQRES   8 B  514  HIS HIS ASN CYS THR PRO GLU PHE GLN ALA ASN GLU VAL          
SEQRES   9 B  514  ARG LYS VAL LYS ASN PHE GLU GLN GLY PHE ILE THR ASP          
SEQRES  10 B  514  PRO VAL VAL LEU SER PRO SER HIS THR VAL GLY ASP VAL          
SEQRES  11 B  514  LEU GLU ALA LYS MET ARG HIS GLY PHE SER GLY ILE PRO          
SEQRES  12 B  514  ILE THR GLU THR GLY THR MET GLY SER LYS LEU VAL GLY          
SEQRES  13 B  514  ILE VAL THR SER ARG ASP ILE ASP PHE LEU ALA GLU LYS          
SEQRES  14 B  514  ASP HIS THR THR LEU LEU SER GLU VAL MET THR PRO ARG          
SEQRES  15 B  514  ILE GLU LEU VAL VAL ALA PRO ALA GLY VAL THR LEU LYS          
SEQRES  16 B  514  GLU ALA ASN GLU ILE LEU GLN ARG SER LYS LYS GLY LYS          
SEQRES  17 B  514  LEU PRO ILE VAL ASN ASP CYS ASP GLU LEU VAL ALA ILE          
SEQRES  18 B  514  ILE ALA ARG THR ASP LEU LYS LYS ASN ARG ASP TYR PRO          
SEQRES  19 B  514  LEU ALA SER LYS ASP SER GLN LYS GLN LEU LEU CYS GLY          
SEQRES  20 B  514  ALA ALA VAL GLY THR ARG GLU ASP ASP LYS TYR ARG LEU          
SEQRES  21 B  514  ASP LEU LEU THR GLN ALA GLY VAL ASP VAL ILE VAL LEU          
SEQRES  22 B  514  ASP SER SER GLN GLY ASN SER VAL TYR GLN ILE ALA MET          
SEQRES  23 B  514  VAL HIS TYR ILE LYS GLN LYS TYR PRO HIS LEU GLN VAL          
SEQRES  24 B  514  ILE GLY GLY ASN VAL VAL THR ALA ALA GLN ALA LYS ASN          
SEQRES  25 B  514  LEU ILE ASP ALA GLY VAL ASP GLY LEU ARG VAL GLY MET          
SEQRES  26 B  514  GLY CYS GLY SER ILE CYS ILE THR GLN GLU VAL MET ALA          
SEQRES  27 B  514  CYS GLY ARG PRO GLN GLY THR ALA VAL TYR LYS VAL ALA          
SEQRES  28 B  514  GLU TYR ALA ARG ARG PHE GLY VAL PRO ILE ILE ALA ASP          
SEQRES  29 B  514  GLY GLY ILE GLN THR VAL GLY HIS VAL VAL LYS ALA LEU          
SEQRES  30 B  514  ALA LEU GLY ALA SER THR VAL MET MET GLY SER LEU LEU          
SEQRES  31 B  514  ALA ALA THR THR GLU ALA PRO GLY GLU TYR PHE PHE SER          
SEQRES  32 B  514  ASP GLY VAL ARG LEU LYS LYS TYR ARG GLY MET GLY SER          
SEQRES  33 B  514  LEU ASP ALA MET GLU LYS SER SER SER SER GLN LYS ARG          
SEQRES  34 B  514  TYR PHE SER GLU GLY ASP LYS VAL LYS ILE ALA GLN GLY          
SEQRES  35 B  514  VAL SER GLY SER ILE GLN ASP LYS GLY SER ILE GLN LYS          
SEQRES  36 B  514  PHE VAL PRO TYR LEU ILE ALA GLY ILE GLN HIS GLY CYS          
SEQRES  37 B  514  GLN ASP ILE GLY ALA ARG SER LEU SER VAL LEU ARG SER          
SEQRES  38 B  514  MET MET TYR SER GLY GLU LEU LYS PHE GLU LYS ARG THR          
SEQRES  39 B  514  MET SER ALA GLN ILE GLU GLY GLY VAL HIS GLY LEU HIS          
SEQRES  40 B  514  SER TYR GLU LYS ARG LEU TYR                                  
HET    CPR  A 631      22                                                       
HET    CPR  B 631      22                                                       
HETNAM     CPR 6-CHLOROPURINE RIBOSIDE, 5'-MONOPHOSPHATE                        
FORMUL   3  CPR    2(C10 H13 CL N4 O7 P 1+)                                     
FORMUL   5  HOH   *294(H2 O)                                                    
HELIX    1   1 THR A   19  PHE A   24  1                                   6    
HELIX    2   2 THR A   31  ASN A   33  5                                   3    
HELIX    3   3 ILE A   45  VAL A   49  5                                   5    
HELIX    4   4 GLU A   75  MET A   85  1                                  11    
HELIX    5   5 THR A   96  PHE A  110  1                                  15    
HELIX    6   6 SER A  160  ASP A  164  5                                   5    
HELIX    7   7 ALA A  197  LYS A  205  1                                   9    
HELIX    8   8 ASP A  255  ALA A  266  1                                  12    
HELIX    9   9 SER A  280  TYR A  294  1                                  15    
HELIX   10  10 THR A  306  GLY A  317  1                                  12    
HELIX   11  11 PRO A  342  ARG A  355  1                                  14    
HELIX   12  12 ARG A  356  GLY A  358  5                                   3    
HELIX   13  13 THR A  369  LEU A  379  1                                  11    
HELIX   14  14 SER A  452  GLY A  472  1                                  21    
HELIX   15  15 SER A  475  SER A  485  1                                  11    
HELIX   16  16 THR B   19  PHE B   24  1                                   6    
HELIX   17  17 THR B   31  ASN B   33  5                                   3    
HELIX   18  18 ILE B   45  VAL B   49  5                                   5    
HELIX   19  19 GLU B   75  MET B   85  1                                  11    
HELIX   20  20 THR B   96  PHE B  110  1                                  15    
HELIX   21  21 THR B  159  ASP B  164  1                                   6    
HELIX   22  22 THR B  193  LYS B  205  1                                  13    
HELIX   23  23 ASP B  255  ALA B  266  1                                  12    
HELIX   24  24 SER B  280  TYR B  294  1                                  15    
HELIX   25  25 THR B  306  ALA B  316  1                                  11    
HELIX   26  26 PRO B  342  ARG B  355  1                                  14    
HELIX   27  27 ARG B  356  GLY B  358  5                                   3    
HELIX   28  28 THR B  369  LEU B  379  1                                  11    
HELIX   29  29 GLY B  387  ALA B  392  1                                   6    
HELIX   30  30 SER B  452  GLY B  472  1                                  21    
HELIX   31  31 SER B  475  SER B  485  1                                  11    
SHEET    1   A 2 PHE A  35  ILE A  37  0                                        
SHEET    2   A 2 PHE A 490  LYS A 492 -1  N  GLU A 491   O  LEU A  36           
SHEET    1   B 2 SER A  53  ALA A  54  0                                        
SHEET    2   B 2 THR A  60  LEU A  61 -1  N  LEU A  61   O  SER A  53           
SHEET    1   C 9 LEU A  65  SER A  67  0                                        
SHEET    2   C 9 ILE A  88  ILE A  91  1  O  ILE A  88   N  SER A  67           
SHEET    3   C 9 GLY A 247  VAL A 250  1  O  GLY A 247   N  ILE A  91           
SHEET    4   C 9 VAL A 270  LEU A 273  1  O  VAL A 270   N  ALA A 248           
SHEET    5   C 9 GLN A 298  VAL A 304  1  O  GLN A 298   N  ILE A 271           
SHEET    6   C 9 GLY A 320  VAL A 323  1  O  GLY A 320   N  GLY A 301           
SHEET    7   C 9 ILE A 361  ASP A 364  1  N  ILE A 362   O  LEU A 321           
SHEET    8   C 9 THR A 383  MET A 386  1  O  THR A 383   N  ALA A 363           
SHEET    9   C 9 LEU A  65  SER A  67  1  O  ILE A  66   N  MET A 386           
SHEET    1   D 2 ILE A 142  PRO A 143  0                                        
SHEET    2   D 2 ILE A 157  VAL A 158 -1  N  VAL A 158   O  ILE A 142           
SHEET    1   E 2 ALA A 188  PRO A 189  0                                        
SHEET    2   E 2 ILE A 211  VAL A 212  1  N  VAL A 212   O  ALA A 188           
SHEET    1   F 2 PHE B  35  ILE B  37  0                                        
SHEET    2   F 2 PHE B 490  LYS B 492 -1  O  GLU B 491   N  LEU B  36           
SHEET    1   G 2 SER B  53  ALA B  54  0                                        
SHEET    2   G 2 THR B  60  LEU B  61 -1  N  LEU B  61   O  SER B  53           
SHEET    1   H 9 LEU B  65  SER B  67  0                                        
SHEET    2   H 9 ILE B  88  ILE B  91  1  O  ILE B  88   N  SER B  67           
SHEET    3   H 9 GLY B 247  VAL B 250  1  O  GLY B 247   N  ILE B  91           
SHEET    4   H 9 VAL B 270  LEU B 273  1  O  VAL B 270   N  ALA B 248           
SHEET    5   H 9 GLN B 298  VAL B 304  1  O  GLN B 298   N  ILE B 271           
SHEET    6   H 9 GLY B 320  VAL B 323  1  O  GLY B 320   N  GLY B 301           
SHEET    7   H 9 ILE B 361  ASP B 364  1  N  ILE B 362   O  LEU B 321           
SHEET    8   H 9 THR B 383  MET B 386  1  O  THR B 383   N  ALA B 363           
SHEET    9   H 9 LEU B  65  SER B  67  1  O  ILE B  66   N  MET B 386           
SHEET    1   I 2 GLY B 156  ILE B 157  0                                        
SHEET    1   J 2 ALA B 188  PRO B 189  0                                        
SHEET    2   J 2 ILE B 211  VAL B 212  1  N  VAL B 212   O  ALA B 188           
LINK         SG  CYS A 331                 C6  CPR A 631     1555   1555  2.00  
LINK         SG  CYS B 331                 C6  CPR B 631     1555   1555  1.91  
SITE     1 AC1 16 SER A  68  ARG A 322  GLY A 328  SER A 329                    
SITE     2 AC1 16 CYS A 331  GLN A 334  ASP A 364  GLY A 365                    
SITE     3 AC1 16 GLY A 366  MET A 385  GLY A 387  SER A 388                    
SITE     4 AC1 16 HOH A 676  HOH A 698  HOH A 734  HOH A 748                    
SITE     1 AC2 18 SER B  68  MET B  70  ARG B 322  GLY B 328                    
SITE     2 AC2 18 SER B 329  CYS B 331  GLN B 334  ASP B 364                    
SITE     3 AC2 18 GLY B 365  GLY B 366  MET B 385  GLY B 387                    
SITE     4 AC2 18 SER B 388  HOH B 639  HOH B 689  HOH B 698                    
SITE     5 AC2 18 HOH B 716  HOH B 734                                          
CRYST1  148.108  148.108  122.016  90.00  90.00  90.00 I 4          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      0.006752  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006752  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008196        0.00000                         
MTRIX1   1 -0.000140  1.000000 -0.000420        0.02299    1                    
MTRIX2   1  1.000000  0.000140 -0.000020       -0.00456    1                    
MTRIX3   1 -0.000020 -0.000420 -1.000000       56.07062    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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