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Database: PDB
Entry: 3MES
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HEADER    TRANSFERASE                             31-MAR-10   3MES              
TITLE     CRYSTAL STRUCTURE OF CHOLINE KINASE FROM CRYPTOSPORIDIUM              
TITLE    2 PARVUM IOWA II, CGD3_2030                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINE KINASE;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ETHANOLAMINE KINASE;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM;                         
SOURCE   3 ORGANISM_TAXID: 353152;                                              
SOURCE   4 STRAIN: IOWA II;                                                     
SOURCE   5 GENE: CGD3_2030;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CHOLINE KINASE, MALARIA, STRUCTURAL GENOMICS, STRUCTURAL              
KEYWDS   2 GENOMICS CONSORTIUM, SGC, KINASE, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.QIU,A.WERNIMONT,T.HILLS,J.LEW,J.D.ARTZ,T.XIAO,A.ALLALI-             
AUTHOR   2 HASSANI,M.VEDADI,I.KOZIERADZKI,D.COSSAR,C.BOUNTRA,                   
AUTHOR   3 J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,R.HUI,D.MA,STRUCTURAL           
AUTHOR   4 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   1   07-APR-10 3MES    0                                                
JRNL        AUTH   W.QIU,A.WERNIMONT,T.HILLS,J.LEW,J.D.ARTZ,T.XIAO,             
JRNL        AUTH 2 A.ALLALI-HASSANI,M.VEDADI,I.KOZIERADZKI,D.COSSAR,            
JRNL        AUTH 3 C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,              
JRNL        AUTH 4 R.HUI,D.MA                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF CHOLINE KINASE FROM                     
JRNL        TITL 2 CRYPTOSPORIDIUM PARVUM IOWA II, CGD3_2030                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 37308                          
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 + TEST SET) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1964                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2710                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 143                          
REMARK   3   BIN FREE R VALUE                    : 0.3580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5952                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 126                                     
REMARK   3   SOLVENT ATOMS            : 248                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.78000                                              
REMARK   3    B22 (A**2) : -1.70000                                             
REMARK   3    B33 (A**2) : 0.31000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.56000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.430         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.288         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.232         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.748         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.897                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.852                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6242 ; 0.002 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8430 ; 0.659 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   709 ; 3.910 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   311 ;33.930 ;24.791       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1125 ;13.577 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;13.092 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   921 ; 0.047 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4624 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3589 ; 0.217 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5835 ; 0.400 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2653 ; 0.376 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2595 ; 0.650 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3MES COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058454.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39277                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.680                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13820                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.65                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49790                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.140                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3FI8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18.5% P3350, 0.2 M KNA-TARTRATE, 2       
REMARK 280  MM DECAMETHONIUM BROMIDE, 2 MM TCEP, 2 MM ADP AND 4 MM MGCL2,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       85.04550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.97850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       85.04550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.97850            
REMARK 290   SMTRY3   4  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 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     LYS A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     MET A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     PHE A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     ASN A    29                                                      
REMARK 465     LYS A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     ILE A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     LEU A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     LEU A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     SER A    41                                                      
REMARK 465     ILE A    42                                                      
REMARK 465     ARG A    43                                                      
REMARK 465     SER A    44                                                      
REMARK 465     PHE A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     ILE A    48                                                      
REMARK 465     THR A    49                                                      
REMARK 465     SER A    95                                                      
REMARK 465     MET A    96                                                      
REMARK 465     SER A    97                                                      
REMARK 465     LEU A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     GLY A   115                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     GLN A   219                                                      
REMARK 465     ARG A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     PRO A   380                                                      
REMARK 465     GLY A   381                                                      
REMARK 465     TYR A   382                                                      
REMARK 465     GLN A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     ASN A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     LEU A   424                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     MET B    25                                                      
REMARK 465     PRO B    26                                                      
REMARK 465     PHE B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     ASN B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     ILE B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     LEU B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     ILE B    42                                                      
REMARK 465     ARG B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     PHE B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     THR B    47                                                      
REMARK 465     ILE B    48                                                      
REMARK 465     THR B    49                                                      
REMARK 465     SER B    95                                                      
REMARK 465     MET B    96                                                      
REMARK 465     SER B    97                                                      
REMARK 465     LEU B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     GLY B   115                                                      
REMARK 465     LYS B   116                                                      
REMARK 465     PHE B   218                                                      
REMARK 465     ARG B   378                                                      
REMARK 465     THR B   379                                                      
REMARK 465     PRO B   380                                                      
REMARK 465     GLY B   381                                                      
REMARK 465     TYR B   382                                                      
REMARK 465     GLN B   383                                                      
REMARK 465     PRO B   384                                                      
REMARK 465     ASN B   385                                                      
REMARK 465     LEU B   424                                                      
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     ASN A 423    CG   OD1  ND2                                       
REMARK 470     ASN B 423    CG   OD1  ND2                                       
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  MG     MG A   426     O11  PT3 A   428              1.63            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CG   GLN B   351     OE1  GLN B   351     2555     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  83      -48.66   -132.88                                   
REMARK 500    SER A 257      138.52   -170.29                                   
REMARK 500    ASN A 267        1.42     80.33                                   
REMARK 500    ASP A 268       38.77   -160.15                                   
REMARK 500    ASP A 285       81.06     62.17                                   
REMARK 500    ALA A 290      157.30    173.53                                   
REMARK 500    TYR A 316       31.74     71.05                                   
REMARK 500    PHE A 317      142.38   -171.66                                   
REMARK 500    TRP A 420      -51.21   -148.92                                   
REMARK 500    THR B  83      -49.45   -132.52                                   
REMARK 500    ASN B 216       58.25     39.87                                   
REMARK 500    SER B 257      132.77   -170.96                                   
REMARK 500    ASN B 267        3.03     81.00                                   
REMARK 500    ASP B 268       34.57   -161.33                                   
REMARK 500    ASP B 285       79.03     61.42                                   
REMARK 500    CYS B 310       58.19   -107.16                                   
REMARK 500    TYR B 316       31.03     79.51                                   
REMARK 500    GLN B 345       99.51    -63.60                                   
REMARK 500    TRP B 420      -43.54   -148.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 426  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 425   O3B                                                    
REMARK 620 2 ADP B 425   O1A  99.1                                              
REMARK 620 3 PT3 B 428   O1  137.7 103.8                                        
REMARK 620 4 PT3 B 428   O11  91.3 158.3  57.1                                  
REMARK 620 5 HOH B 488   O   102.0 104.4 106.0  91.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 426  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 425   O1B                                                    
REMARK 620 2 ADP A 425   O1A  91.6                                              
REMARK 620 3 PT3 A 428   O2  161.3 103.5                                        
REMARK 620 4 HOH A 545   O   100.0  99.1  88.5                                  
REMARK 620 5 HOH A 440   O    84.8  88.4  84.8 171.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 430  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 271   OE2                                                    
REMARK 620 2 GLU A 304   O   113.3                                              
REMARK 620 3 TYR A 307   O   138.3  87.2                                        
REMARK 620 4 GLU A 271   OE1  57.5 141.7  83.6                                  
REMARK 620 5 GLU A 304   OE1 110.6  96.3 102.0 121.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 429  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 307   O                                                      
REMARK 620 2 GLU B 304   O    93.3                                              
REMARK 620 3 GLU B 271   OE2 125.0 104.0                                        
REMARK 620 4 GLU B 304   OE1 112.4 104.3 113.0                                  
REMARK 620 5 GLU B 271   OE1  79.1 133.9  51.4 120.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 425                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 426                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DME A 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT3 A 428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 429                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 430                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 425                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 426                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DME B 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT3 B 428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 429                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FI8   RELATED DB: PDB                                   
REMARK 900 PLASMODIUM FALCIPARUM HOMOLOGUE                                      
REMARK 900 RELATED ID: 3C5I   RELATED DB: PDB                                   
REMARK 900 PLASMODIUM KNOWLESI HOMOLOGUE                                        
DBREF  3MES A   20   424  UNP    Q5CUP2   Q5CUP2_CRYPV     1    405             
DBREF  3MES B   20   424  UNP    Q5CUP2   Q5CUP2_CRYPV     1    405             
SEQADV 3MES MET A    1  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES GLY A    2  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER A    3  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER A    4  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS A    5  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS A    6  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS A    7  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS A    8  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS A    9  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS A   10  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER A   11  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER A   12  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES GLY A   13  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES LEU A   14  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES VAL A   15  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES PRO A   16  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES ARG A   17  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES GLY A   18  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER A   19  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES MET B    1  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES GLY B    2  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER B    3  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER B    4  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS B    5  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS B    6  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS B    7  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS B    8  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS B    9  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES HIS B   10  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER B   11  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER B   12  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES GLY B   13  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES LEU B   14  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES VAL B   15  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES PRO B   16  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES ARG B   17  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES GLY B   18  UNP  Q5CUP2              EXPRESSION TAG                 
SEQADV 3MES SER B   19  UNP  Q5CUP2              EXPRESSION TAG                 
SEQRES   1 A  424  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  424  LEU VAL PRO ARG GLY SER LYS LYS LYS LYS GLU MET PRO          
SEQRES   3 A  424  PHE PRO ASN LYS LYS ILE GLU LEU GLY ASP LYS LEU SER          
SEQRES   4 A  424  GLU SER ILE ARG SER PHE SER THR ILE THR ASP THR GLU          
SEQRES   5 A  424  ILE ILE ILE GLY ILE CYS ARG LYS ASN ILE PRO GLY TRP          
SEQRES   6 A  424  LYS GLU ILE ASN GLU SER TYR ILE GLU VAL LYS GLN ILE          
SEQRES   7 A  424  PHE SER GLY LEU THR ASN GLN LEU PHE VAL VAL SER ILE          
SEQRES   8 A  424  VAL ASN GLU SER MET SER LEU SER LEU LYS HIS PRO ARG          
SEQRES   9 A  424  ILE LEU PHE ARG ILE TYR GLY LYS HIS VAL GLY LYS PHE          
SEQRES  10 A  424  TYR ASP SER LYS VAL GLU LEU ASP VAL PHE ARG TYR LEU          
SEQRES  11 A  424  SER ASN ILE ASN ILE ALA PRO ASN ILE ILE ALA ASP PHE          
SEQRES  12 A  424  PRO GLU GLY ARG ILE GLU GLU PHE ILE ASP GLY GLU PRO          
SEQRES  13 A  424  LEU THR THR LYS GLN LEU GLN LEU THR HIS ILE CYS VAL          
SEQRES  14 A  424  GLU VAL ALA LYS ASN MET GLY SER LEU HIS ILE ILE ASN          
SEQRES  15 A  424  SER LYS ARG ALA ASP PHE PRO SER ARG PHE ASP LYS GLU          
SEQRES  16 A  424  PRO ILE LEU PHE LYS ARG ILE TYR LEU TRP ARG GLU GLU          
SEQRES  17 A  424  ALA LYS ILE GLN VAL SER LYS ASN ASN PHE GLN ILE ASP          
SEQRES  18 A  424  LYS GLU LEU TYR SER LYS ILE LEU GLU GLU ILE ASP GLN          
SEQRES  19 A  424  LEU GLU GLU LEU ILE MET GLY GLY GLU LYS PHE SER MET          
SEQRES  20 A  424  GLU ARG ALA LEU GLU LEU LYS LEU TYR SER PRO ALA PHE          
SEQRES  21 A  424  SER LEU VAL PHE ALA HIS ASN ASP LEU GLN GLU ASN ASN          
SEQRES  22 A  424  LEU LEU GLN THR GLN ASN ASN ILE ARG MET ILE ASP TYR          
SEQRES  23 A  424  GLU TYR SER ALA ILE ASN PHE ALA GLY ALA ASP ILE ALA          
SEQRES  24 A  424  ASN TYR PHE CYS GLU TYR ILE TYR ASP TYR CYS SER GLU          
SEQRES  25 A  424  LYS GLN PRO TYR PHE LYS PHE LYS TYR GLU ASP TYR PRO          
SEQRES  26 A  424  CYS GLU GLU LEU ARG LYS LEU PHE ILE SER VAL TYR LEU          
SEQRES  27 A  424  SER GLN THR LEU GLN GLU GLN VAL MET PRO SER GLN GLN          
SEQRES  28 A  424  ILE VAL HIS ILE MET THR LYS ALA VAL GLU VAL PHE THR          
SEQRES  29 A  424  LEU ILE SER HIS ILE THR TRP GLY LEU TRP SER ILE ALA          
SEQRES  30 A  424  ARG THR PRO GLY TYR GLN PRO ASN SER VAL GLU PHE ASP          
SEQRES  31 A  424  PHE THR GLU TYR ALA ASN THR ARG PHE THR HIS TYR LEU          
SEQRES  32 A  424  GLN LYS LYS LYS GLU LEU ILE ASP GLN GLY ILE LEU PRO          
SEQRES  33 A  424  LEU ASN SER TRP LEU PHE ASN LEU                              
SEQRES   1 B  424  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  424  LEU VAL PRO ARG GLY SER LYS LYS LYS LYS GLU MET PRO          
SEQRES   3 B  424  PHE PRO ASN LYS LYS ILE GLU LEU GLY ASP LYS LEU SER          
SEQRES   4 B  424  GLU SER ILE ARG SER PHE SER THR ILE THR ASP THR GLU          
SEQRES   5 B  424  ILE ILE ILE GLY ILE CYS ARG LYS ASN ILE PRO GLY TRP          
SEQRES   6 B  424  LYS GLU ILE ASN GLU SER TYR ILE GLU VAL LYS GLN ILE          
SEQRES   7 B  424  PHE SER GLY LEU THR ASN GLN LEU PHE VAL VAL SER ILE          
SEQRES   8 B  424  VAL ASN GLU SER MET SER LEU SER LEU LYS HIS PRO ARG          
SEQRES   9 B  424  ILE LEU PHE ARG ILE TYR GLY LYS HIS VAL GLY LYS PHE          
SEQRES  10 B  424  TYR ASP SER LYS VAL GLU LEU ASP VAL PHE ARG TYR LEU          
SEQRES  11 B  424  SER ASN ILE ASN ILE ALA PRO ASN ILE ILE ALA ASP PHE          
SEQRES  12 B  424  PRO GLU GLY ARG ILE GLU GLU PHE ILE ASP GLY GLU PRO          
SEQRES  13 B  424  LEU THR THR LYS GLN LEU GLN LEU THR HIS ILE CYS VAL          
SEQRES  14 B  424  GLU VAL ALA LYS ASN MET GLY SER LEU HIS ILE ILE ASN          
SEQRES  15 B  424  SER LYS ARG ALA ASP PHE PRO SER ARG PHE ASP LYS GLU          
SEQRES  16 B  424  PRO ILE LEU PHE LYS ARG ILE TYR LEU TRP ARG GLU GLU          
SEQRES  17 B  424  ALA LYS ILE GLN VAL SER LYS ASN ASN PHE GLN ILE ASP          
SEQRES  18 B  424  LYS GLU LEU TYR SER LYS ILE LEU GLU GLU ILE ASP GLN          
SEQRES  19 B  424  LEU GLU GLU LEU ILE MET GLY GLY GLU LYS PHE SER MET          
SEQRES  20 B  424  GLU ARG ALA LEU GLU LEU LYS LEU TYR SER PRO ALA PHE          
SEQRES  21 B  424  SER LEU VAL PHE ALA HIS ASN ASP LEU GLN GLU ASN ASN          
SEQRES  22 B  424  LEU LEU GLN THR GLN ASN ASN ILE ARG MET ILE ASP TYR          
SEQRES  23 B  424  GLU TYR SER ALA ILE ASN PHE ALA GLY ALA ASP ILE ALA          
SEQRES  24 B  424  ASN TYR PHE CYS GLU TYR ILE TYR ASP TYR CYS SER GLU          
SEQRES  25 B  424  LYS GLN PRO TYR PHE LYS PHE LYS TYR GLU ASP TYR PRO          
SEQRES  26 B  424  CYS GLU GLU LEU ARG LYS LEU PHE ILE SER VAL TYR LEU          
SEQRES  27 B  424  SER GLN THR LEU GLN GLU GLN VAL MET PRO SER GLN GLN          
SEQRES  28 B  424  ILE VAL HIS ILE MET THR LYS ALA VAL GLU VAL PHE THR          
SEQRES  29 B  424  LEU ILE SER HIS ILE THR TRP GLY LEU TRP SER ILE ALA          
SEQRES  30 B  424  ARG THR PRO GLY TYR GLN PRO ASN SER VAL GLU PHE ASP          
SEQRES  31 B  424  PHE THR GLU TYR ALA ASN THR ARG PHE THR HIS TYR LEU          
SEQRES  32 B  424  GLN LYS LYS LYS GLU LEU ILE ASP GLN GLY ILE LEU PRO          
SEQRES  33 B  424  LEU ASN SER TRP LEU PHE ASN LEU                              
HET    ADP  A 425      27                                                       
HET     MG  A 426       1                                                       
HET    DME  A 427      18                                                       
HET    PT3  A 428      13                                                       
HET    GOL  A 429       6                                                       
HET     MG  A 430       1                                                       
HET    ADP  B 425      27                                                       
HET     MG  B 426       1                                                       
HET    DME  B 427      18                                                       
HET    PT3  B 428      13                                                       
HET     MG  B 429       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DME DECAMETHONIUM ION                                                
HETNAM     PT3 N-PROPYL-TARTRAMIC ACID                                          
HETNAM     GOL GLYCEROL                                                         
FORMUL   3  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   4   MG    4(MG 2+)                                                     
FORMUL   5  DME    2(C16 H38 N2 2+)                                             
FORMUL   6  PT3    2(C7 H13 N O5)                                               
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *248(H2 O)                                                    
HELIX    1   1 ASP A   50  ILE A   62  1                                  13    
HELIX    2   2 ASN A   69  SER A   71  5                                   3    
HELIX    3   3 ASP A  119  ILE A  133  1                                  15    
HELIX    4   4 THR A  159  GLN A  163  5                                   5    
HELIX    5   5 LEU A  164  ILE A  180  1                                  17    
HELIX    6   6 ILE A  180  ARG A  185  1                                   6    
HELIX    7   7 ILE A  197  LYS A  215  1                                  19    
HELIX    8   8 ASP A  221  GLY A  241  1                                  21    
HELIX    9   9 SER A  246  LEU A  255  1                                  10    
HELIX   10  10 TYR A  256  PHE A  260  5                                   5    
HELIX   11  11 GLN A  270  ASN A  272  5                                   3    
HELIX   12  12 ALA A  294  GLU A  304  1                                  11    
HELIX   13  13 TYR A  321  TYR A  324  5                                   4    
HELIX   14  14 CYS A  326  GLN A  343  1                                  18    
HELIX   15  15 GLN A  350  PHE A  363  1                                  14    
HELIX   16  16 PHE A  363  ALA A  377  1                                  15    
HELIX   17  17 ASP A  390  GLN A  412  1                                  23    
HELIX   18  18 PRO A  416  TRP A  420  5                                   5    
HELIX   19  19 ASP B   50  ILE B   62  1                                  13    
HELIX   20  20 ASN B   69  SER B   71  5                                   3    
HELIX   21  21 ASP B  119  ILE B  133  1                                  15    
HELIX   22  22 LYS B  160  GLN B  163  5                                   4    
HELIX   23  23 LEU B  164  ILE B  180  1                                  17    
HELIX   24  24 ILE B  181  SER B  183  5                                   3    
HELIX   25  25 ILE B  197  LYS B  215  1                                  19    
HELIX   26  26 ASP B  221  ILE B  232  1                                  12    
HELIX   27  27 GLN B  234  MET B  240  1                                   7    
HELIX   28  28 SER B  246  LEU B  255  1                                  10    
HELIX   29  29 SER B  257  PHE B  260  5                                   4    
HELIX   30  30 GLN B  270  ASN B  272  5                                   3    
HELIX   31  31 ALA B  294  GLU B  304  1                                  11    
HELIX   32  32 TYR B  321  TYR B  324  5                                   4    
HELIX   33  33 CYS B  326  GLN B  343  1                                  18    
HELIX   34  34 GLN B  350  PHE B  363  1                                  14    
HELIX   35  35 PHE B  363  ALA B  377  1                                  15    
HELIX   36  36 ASP B  390  GLN B  412  1                                  23    
HELIX   37  37 PRO B  416  TRP B  420  5                                   5    
SHEET    1   A 5 ILE A  73  ILE A  78  0                                        
SHEET    2   A 5 GLN A  85  ILE A  91 -1  O  SER A  90   N  GLU A  74           
SHEET    3   A 5 ARG A 104  ILE A 109 -1  O  PHE A 107   N  PHE A  87           
SHEET    4   A 5 GLY A 146  GLU A 150 -1  O  GLU A 149   N  LEU A 106           
SHEET    5   A 5 ILE A 139  PHE A 143 -1  N  ILE A 140   O  ILE A 148           
SHEET    1   B 3 GLU A 155  PRO A 156  0                                        
SHEET    2   B 3 LEU A 274  GLN A 276 -1  O  GLN A 276   N  GLU A 155           
SHEET    3   B 3 ILE A 281  MET A 283 -1  O  ARG A 282   N  LEU A 275           
SHEET    1   C 2 LEU A 262  ALA A 265  0                                        
SHEET    2   C 2 ALA A 290  PHE A 293 -1  O  ASN A 292   N  VAL A 263           
SHEET    1   D 2 TYR A 307  ASP A 308  0                                        
SHEET    2   D 2 LYS A 318  PHE A 319 -1  O  LYS A 318   N  ASP A 308           
SHEET    1   E 5 ILE B  73  ILE B  78  0                                        
SHEET    2   E 5 GLN B  85  ILE B  91 -1  O  VAL B  88   N  LYS B  76           
SHEET    3   E 5 ARG B 104  ILE B 109 -1  O  PHE B 107   N  PHE B  87           
SHEET    4   E 5 GLY B 146  GLU B 150 -1  O  GLU B 149   N  LEU B 106           
SHEET    5   E 5 ILE B 139  PHE B 143 -1  N  ILE B 140   O  ILE B 148           
SHEET    1   F 3 GLU B 155  PRO B 156  0                                        
SHEET    2   F 3 LEU B 274  GLN B 276 -1  O  GLN B 276   N  GLU B 155           
SHEET    3   F 3 ILE B 281  MET B 283 -1  O  ARG B 282   N  LEU B 275           
SHEET    1   G 2 LEU B 262  ALA B 265  0                                        
SHEET    2   G 2 ALA B 290  PHE B 293 -1  O  ASN B 292   N  VAL B 263           
SHEET    1   H 2 TYR B 307  ASP B 308  0                                        
SHEET    2   H 2 LYS B 318  PHE B 319 -1  O  LYS B 318   N  ASP B 308           
LINK         O3B ADP B 425                MG    MG B 426     1555   1555  1.80  
LINK         O1A ADP B 425                MG    MG B 426     1555   1555  1.88  
LINK         O1B ADP A 425                MG    MG A 426     1555   1555  1.95  
LINK         O1A ADP A 425                MG    MG A 426     1555   1555  1.96  
LINK         OE2 GLU A 271                MG    MG A 430     1555   1555  2.13  
LINK        MG    MG B 426                 O1  PT3 B 428     1555   1555  2.23  
LINK         O   TYR B 307                MG    MG B 429     1555   1555  2.26  
LINK        MG    MG A 426                 O2  PT3 A 428     1555   1555  2.27  
LINK         O   GLU A 304                MG    MG A 430     1555   1555  2.34  
LINK         O   GLU B 304                MG    MG B 429     1555   1555  2.34  
LINK         O   TYR A 307                MG    MG A 430     1555   1555  2.35  
LINK         OE2 GLU B 271                MG    MG B 429     1555   1555  2.37  
LINK         OE1 GLU A 271                MG    MG A 430     1555   1555  2.41  
LINK        MG    MG B 426                 O11 PT3 B 428     1555   1555  2.43  
LINK         OE1 GLU B 304                MG    MG B 429     1555   1555  2.46  
LINK         OE1 GLU B 271                MG    MG B 429     1555   1555  2.66  
LINK         OE1 GLU A 304                MG    MG A 430     1555   1555  2.82  
LINK        MG    MG A 426                 O   HOH A 545     1555   1555  1.92  
LINK        MG    MG A 426                 O   HOH A 440     1555   1555  2.13  
LINK        MG    MG B 426                 O   HOH B 488     1555   1555  2.19  
CISPEP   1 GLN A  314    PRO A  315          0        -1.14                     
CISPEP   2 LEU A  415    PRO A  416          0        -1.51                     
CISPEP   3 GLN B  314    PRO B  315          0         2.46                     
CISPEP   4 LEU B  415    PRO B  416          0         0.00                     
SITE     1 AC1 20 GLY A  81  LEU A  82  THR A  83  ASN A  84                    
SITE     2 AC1 20 LEU A  86  LEU A 106  ARG A 108  GLU A 149                    
SITE     3 AC1 20 GLU A 150  PHE A 151  ILE A 152  ILE A 284                    
SITE     4 AC1 20 ASP A 285   MG A 426  PT3 A 428  GOL A 429                    
SITE     5 AC1 20 HOH A 440  HOH A 459  HOH A 518  HOH A 545                    
SITE     1 AC2  5 ASP A 285  ADP A 425  PT3 A 428  HOH A 440                    
SITE     2 AC2  5 HOH A 545                                                     
SITE     1 AC3 10 SER A  80  ASP A 268  GLU A 304  TYR A 309                    
SITE     2 AC3 10 TRP A 371  TRP A 374  PHE A 389  TYR A 394                    
SITE     3 AC3 10 PT3 A 428  GOL A 429                                          
SITE     1 AC4 13 LEU A  82  ASP A 268  GLN A 270  ASN A 272                    
SITE     2 AC4 13 ASP A 285  TYR A 288  ADP A 425   MG A 426                    
SITE     3 AC4 13 DME A 427  GOL A 429  HOH A 440  HOH A 495                    
SITE     4 AC4 13 HOH A 545                                                     
SITE     1 AC5  6 SER A  80  PRO A 156  ASN A 272  ADP A 425                    
SITE     2 AC5  6 DME A 427  PT3 A 428                                          
SITE     1 AC6  3 GLU A 271  GLU A 304  TYR A 307                               
SITE     1 AC7 18 ILE B  78  GLY B  81  LEU B  82  THR B  83                    
SITE     2 AC7 18 ASN B  84  LEU B  86  ARG B 108  GLU B 149                    
SITE     3 AC7 18 GLU B 150  PHE B 151  ILE B 152  ILE B 284                    
SITE     4 AC7 18  MG B 426  PT3 B 428  HOH B 462  HOH B 479                    
SITE     5 AC7 18 HOH B 499  HOH B 520                                          
SITE     1 AC8  3 ADP B 425  PT3 B 428  HOH B 488                               
SITE     1 AC9  8 SER B  80  ASP B 268  GLU B 304  TYR B 309                    
SITE     2 AC9  8 TRP B 371  PHE B 389  TYR B 394  PT3 B 428                    
SITE     1 BC1 12 LEU B  82  ASP B 268  GLN B 270  ASN B 272                    
SITE     2 BC1 12 ASN B 273  ASP B 285  TYR B 309  TRP B 374                    
SITE     3 BC1 12 ADP B 425   MG B 426  DME B 427  HOH B 488                    
SITE     1 BC2  3 GLU B 271  GLU B 304  TYR B 307                               
CRYST1  170.091   67.957   92.109  90.00 116.54  90.00 C 1 2 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      0.005879  0.000000  0.002937        0.00000                         
SCALE2      0.000000  0.014715  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012136        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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