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Database: PDB
Entry: 2W3A
LinkDB: 2W3A
Original site: 2W3A 
HEADER    OXIDOREDUCTASE                          10-NOV-08   2W3A              
TITLE     HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND TRIMETHOPRIM   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET11A;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PDFR                                      
KEYWDS    NONCLASSICAL ANTIFOLATES, ONE-CARBON METABOLISM, LIPOPHILIC           
KEYWDS   2 ANTIFOLATES, NADP, REDUCTASE, OXIDOREDUCTASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.W.LEUNG,R.C.REYNOLDS,D.W.BORHANI                                  
REVDAT   3   08-MAY-19 2W3A    1       REMARK                                   
REVDAT   2   06-MAR-19 2W3A    1       REMARK                                   
REVDAT   1   17-NOV-09 2W3A    0                                                
JRNL        AUTH   A.K.W.LEUNG,L.J.ROSS,S.ZYWNO-VAN GINKEL,R.C.REYNOLDS,        
JRNL        AUTH 2 L.E.SEITZ,V.PATHAK,W.W.BARROW,E.L.WHITE,W.J.SULING,          
JRNL        AUTH 3 J.R.PIPER,D.W.BORHANI                                        
JRNL        TITL   STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF MYCOBACTERIUM   
JRNL        TITL 2 AVIUM DIHYDROFOLATE REDUCTASE BY A LIPOPHILIC ANTIFOLATE     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.90                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 52301                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2810                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1258                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.2030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2957                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 155                                     
REMARK   3   SOLVENT ATOMS            : 408                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.19000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.28000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.091         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.788         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3338 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2308 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4554 ; 1.506 ; 2.027       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5641 ; 1.198 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   403 ; 5.766 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;37.780 ;24.853       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   575 ;11.995 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;13.104 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   479 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3655 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   642 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   528 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2219 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1533 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1631 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   200 ; 0.150 ; 0.200       
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):     6 ; 0.089 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    49 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    54 ; 0.150 ; 0.200       
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):  2560 ; 1.377 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3201 ; 1.633 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1652 ; 2.433 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1353 ; 3.129 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   186                          
REMARK   3    RESIDUE RANGE :   A  1188        A  1188                          
REMARK   3    RESIDUE RANGE :   A  1190        A  1190                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5910  23.4590  -1.4220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0350 T22:  -0.0344                                     
REMARK   3      T33:  -0.0129 T12:  -0.0509                                     
REMARK   3      T13:  -0.0254 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3892 L22:   1.3486                                     
REMARK   3      L33:   0.9913 L12:   0.3335                                     
REMARK   3      L13:  -0.0630 L23:   0.1033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0692 S12:  -0.1220 S13:  -0.0183                       
REMARK   3      S21:   0.2153 S22:  -0.0761 S23:  -0.0723                       
REMARK   3      S31:   0.0672 S32:  -0.0324 S33:   0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   186                          
REMARK   3    RESIDUE RANGE :   B  1188        B  1188                          
REMARK   3    RESIDUE RANGE :   B  1189        B  1189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.3840  45.4820  22.7150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0487 T22:  -0.0282                                     
REMARK   3      T33:  -0.0197 T12:   0.0396                                     
REMARK   3      T13:   0.0117 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9958 L22:   1.2016                                     
REMARK   3      L33:   1.3864 L12:  -0.2134                                     
REMARK   3      L13:  -0.4969 L23:   0.4862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0745 S12:  -0.1410 S13:   0.0331                       
REMARK   3      S21:   0.0799 S22:   0.0090 S23:   0.0026                       
REMARK   3      S31:   0.0973 S32:   0.0789 S33:   0.0655                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2W3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290038064.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.75                               
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) : 0.908                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM-1                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55140                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -10.000                            
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.7                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 28.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: UNPUBLISHED HUMAN DHFR FOLATE COMPLEX                
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HUMAN DHFR/FOLATE COMPLEX WAS MIXED      
REMARK 280  WITH NADPH AND TRIMETHOPRIM (BOTH 2 MM FINAL). CRYSTALS WERE        
REMARK 280  GROWN BY HANGING DROP VAPOR DIFFUSION AT 277 K BY MIXING EQUAL      
REMARK 280  VOLUMES OF PROTEIN/NADPH/TMP WITH RESERVOIR (24% PEG 4000, 200      
REMARK 280  MM LI2SO4, 100 MM TRIS.HCL, PH 8.75). TRUNCATED TRIANGULAR          
REMARK 280  CRYSTALS APPEARED SLOWLY, IN ABOUT A MONTH. THE CRYSTAL WAS         
REMARK 280  CRYOPROTECTED WITH 15% GLYCEROL AND FLASH-COOLED IN LIQUID N2.,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.28800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.28800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.23400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.00700            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.23400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.00700            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.28800            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.23400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       47.00700            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.28800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.23400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       47.00700            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     0                                                      
REMARK 465     MET B     0                                                      
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     ARG A  32    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  68    CE   NZ                                             
REMARK 470     LYS A  80    CG   CD   CE   NZ                                   
REMARK 470     ARG A  91    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A 141    CG   OD1  OD2                                       
REMARK 470     GLU A 143    CD   OE1  OE2                                       
REMARK 470     GLU A 150    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  28    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B  84    CD   OE1  NE2                                       
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470     GLU B 101    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 150    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 161    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2071     O    HOH A  2148              2.16            
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    ASP A 110      -95.26    -94.49                                   
REMARK 500    MET A 139       50.75    -90.48                                   
REMARK 500    ASN B 107       18.11     59.62                                   
REMARK 500    ASP B 110      -94.53   -102.22                                   
REMARK 500    MET B 139       43.48    -86.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2027        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A2033        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH B2009        DISTANCE =  6.58 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 GLYCEROL (GOL): 1,2,3-PROPANETRIOL                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1187                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 1188                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1189                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TOP A 1190                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1187                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 1188                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TOP B 1189                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C2S   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 2,4-DIAMINO-  
REMARK 900 5-(1-O- CARBORANYLMETHYL)-6-METHYLPYRIMIDINE, A NOVEL BORON          
REMARK 900 CONTANING, NONCLASSICAL ANTIFOLATE                                   
REMARK 900 RELATED ID: 2W3M   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND FOLATE        
REMARK 900 RELATED ID: 1DHF   RELATED DB: PDB                                   
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) COMPLEX WITH FOLATE                   
REMARK 900 RELATED ID: 2DHF   RELATED DB: PDB                                   
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) COMPLEX WITH 5 -DEAZAFOLATE           
REMARK 900 RELATED ID: 1S3W   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF TETRAHYDROQUINAZOLINEANTIFOALTES IN       
REMARK 900 COMPLEX WITH HUMAN AND PNEUMOCYSTIS CARINIIDIHYDROFOLATE REDUCTASE:  
REMARK 900 CORRELATIONS OF ENZYMESELECTIVITY AND STEREOCHEMISTRY                
REMARK 900 RELATED ID: 2W3B   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND A LIPOPHILIC  
REMARK 900 ANTIFOLATE SELECTIVE FOR MYCOBACTERIUM AVIUM DHFR, 6-((2,5-          
REMARK 900 DIETHOXYPHENYL)AMINOMETHYL)-2,4-DIAMINO-5- METHYLPYRIDO(2,3-D)       
REMARK 900 PYRIMIDINE (SRI-8686)                                                
REMARK 900 RELATED ID: 1S3V   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF TETRAHYDROQUINAZOLINEANTIFOLATES IN       
REMARK 900 COMPLEX WITH HUMAN AND PNEUMOCYSTIS CARINIIDIHYDROFOLATE REDUCTASE:  
REMARK 900 CORRELATIONS OF ENZYMESELECTIVITY AND STEREOCHEMISTRY                
REMARK 900 RELATED ID: 1PD8   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THREE CRYSTAL STRUCTURE DETERMINATIONS OF A 5-METHYL-6-  
REMARK 900 N- METHYLANILINO PYRIDOPYRIMIDINE ANTIFOLATECOMPLEX WITH HUMAN       
REMARK 900 DIHYDROFOLATE REDUCTASE                                              
REMARK 900 RELATED ID: 1DLS   RELATED DB: PDB                                   
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) MUTANT WITH LEU 22 REPLACED BY TYR    
REMARK 900 (L22Y) COMPLEXED WITH NADPH AND METHOTREXATE                         
REMARK 900 RELATED ID: 1DLR   RELATED DB: PDB                                   
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) MUTANT WITH LEU 22 REPLACED BY PHE    
REMARK 900 (L22F) COMPLEXED WITH NADPH AND PIRITREXIM (PTX)                     
REMARK 900 RELATED ID: 1U72   RELATED DB: PDB                                   
REMARK 900 UNDERSTANDING THE ROLE OF LEU22 VARIANTS IN METHOTREXATERESISTANCE:  
REMARK 900 COMPARISON OF WILD- TYPE AND LEU22ARG VARIANTMOUSE AND HUMAN         
REMARK 900 DIHYDRFOLATE REDUCTASE TERNARY CRYSTALCOMPLEXES WITH METHOTREXATE    
REMARK 900 AND NADPH                                                            
REMARK 900 RELATED ID: 1OHK   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE, ORTHORHOMBIC (P21 21 21) CRYSTAL FORM 
REMARK 900 RELATED ID: 1YHO   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF HUMAN DIHYDROFOLATE REDUCTASECOMPLEXED WITH    
REMARK 900 TRIMETHOPRIM AND NADPH , 25 STRUCTURES                               
REMARK 900 RELATED ID: 2C2T   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 2,4-DIAMINO-  
REMARK 900 5-((7,8- DICARBAUNDECABORAN-7-YL)METHYL)-6- METHYLPYRIMIDINE, A      
REMARK 900 NOVEL BORON CONTANING, NONCLASSICAL ANTIFOLATE                       
REMARK 900 RELATED ID: 1OHJ   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE, MONOCLINIC (P21 ) CRYSTAL FORM        
REMARK 900 RELATED ID: 1PD9   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THREE CRYSTAL STRUCTURE DETERMINATIONS OF A 5-METHYL-6-  
REMARK 900 N- METHYLANILINO PYRIDOPYRIMIDINE ANTIFOLATECOMPLEX WITH HUMAN       
REMARK 900 DIHYDROFOLATE REDUCTASE                                              
REMARK 900 RELATED ID: 1KMV   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND (Z)-6-(2-[2,  
REMARK 900 5-DIMETHOXYPHENYL] ETHEN-1-YL)-2,4-DIAMINO-5-METHYLPYRIDO[2 ,3-D]    
REMARK 900 PYRIMIDINE (SRI-9662), A LIPOPHILICANTIFOLATE                        
REMARK 900 RELATED ID: 1HFR   RELATED DB: PDB                                   
REMARK 900 COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE       
REMARK 900 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE         
REMARK 900 RELATED ID: 1MVT   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF TWO POLYMORPHIC FORMS OF A PYRIDO[2,3-D]PYRIMIDINE N9-   
REMARK 900 C10 REVERSE- BRIDGE ANTIFOLATE BINARYCOMPLEX WITH HUMAN              
REMARK 900 DIHYDROFOLATE REDUCTASE                                              
REMARK 900 RELATED ID: 1U71   RELATED DB: PDB                                   
REMARK 900 UNDERSTANDING THE ROLE OF LEU22 VARIANTS IN METHOTREXATERESISTANCE:  
REMARK 900 COMPARISON OF WILD- TYPE AND LEU22ARG VARIANTMOUSE AND HUMAN         
REMARK 900 DIHYDROFOLATE REDUCTASE TERNARY CRYSTALCOMPLEXES WITH METHOTREXATE   
REMARK 900 AND NADPH                                                            
REMARK 900 RELATED ID: 1KMS   RELATED DB: PDB                                   
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 6-([5-        
REMARK 900 QUINOLYLAMINO]METHYL)-2,4 -DIAMINO-5-METHYLPYRIDO[2,3-D]PYRIMIDINE   
REMARK 900 ( SRI-9439), A LIPOPHILIC ANTIFOLATE                                 
REMARK 900 RELATED ID: 1PDB   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THREE CRYSTAL STRUCTURE DETERMINATIONS OF A 5-METHYL-6-  
REMARK 900 N- METHYLANILINO PYRIDOPYRIMIDINE ANTIFOLATECOMPLEX WITH HUMAN       
REMARK 900 DIHYDROFOLATE REDUCTASE                                              
REMARK 900 RELATED ID: 1HFQ   RELATED DB: PDB                                   
REMARK 900 COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE       
REMARK 900 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE         
REMARK 900 RELATED ID: 1S3U   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF TETRAHYDROQUINAZOLINEANTIFOLATES IN       
REMARK 900 COMPLEX WITH HUMAN AND PNEUMOCYSTIS CARINIIDIHYDROFOLATE REDUCTASE:  
REMARK 900 CORRELATIONS OF ENZYMESELECTIVITY AND STEREOCHEMISTRY                
REMARK 900 RELATED ID: 1DRF   RELATED DB: PDB                                   
REMARK 900 DIHYDROFOLATE REDUCTASE COMPLEX WITH FOLATE                          
REMARK 900 RELATED ID: 1MVS   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF TWO POLYMORPHIC FORMS OF A PYRIDO[2,3-D]PYRIMIDINE N9-   
REMARK 900 C10 REVERSE- BRIDGE ANTIFOLATE BINARYCOMPLEX WITH HUMAN              
REMARK 900 DIHYDROFOLATE REDUCTASE                                              
REMARK 900 RELATED ID: 1HFP   RELATED DB: PDB                                   
REMARK 900 COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE       
REMARK 900 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE         
REMARK 900 RELATED ID: 1BOZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE-BASED DESIGN AND SYNTHESIS OF LIPOPHILIC 2,4- DIAMINO-6-   
REMARK 900 SUBSTITUTED QUINAZOLINES AND THEIR EVALUATION AS INHIBITORS OF       
REMARK 900 DIHYDROFOLATE REDUCTASE AND POTENTIAL ANTITUMOR AGENTS               
DBREF  2W3A A    0   186  UNP    P00374   DYR_HUMAN        1    187             
DBREF  2W3A B    0   186  UNP    P00374   DYR_HUMAN        1    187             
SEQRES   1 A  187  MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN          
SEQRES   2 A  187  ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO          
SEQRES   3 A  187  PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR          
SEQRES   4 A  187  THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE          
SEQRES   5 A  187  MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN          
SEQRES   6 A  187  ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG          
SEQRES   7 A  187  GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER          
SEQRES   8 A  187  ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO          
SEQRES   9 A  187  GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY          
SEQRES  10 A  187  GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY          
SEQRES  11 A  187  HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE          
SEQRES  12 A  187  GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS          
SEQRES  13 A  187  TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP          
SEQRES  14 A  187  VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL          
SEQRES  15 A  187  TYR GLU LYS ASN ASP                                          
SEQRES   1 B  187  MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN          
SEQRES   2 B  187  ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO          
SEQRES   3 B  187  PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR          
SEQRES   4 B  187  THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE          
SEQRES   5 B  187  MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN          
SEQRES   6 B  187  ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG          
SEQRES   7 B  187  GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER          
SEQRES   8 B  187  ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO          
SEQRES   9 B  187  GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY          
SEQRES  10 B  187  GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY          
SEQRES  11 B  187  HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE          
SEQRES  12 B  187  GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS          
SEQRES  13 B  187  TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP          
SEQRES  14 B  187  VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL          
SEQRES  15 B  187  TYR GLU LYS ASN ASP                                          
HET    GOL  A1187       6                                                       
HET    NDP  A1188      48                                                       
HET    SO4  A1189       5                                                       
HET    TOP  A1190      21                                                       
HET    GOL  B1187       6                                                       
HET    NDP  B1188      48                                                       
HET    TOP  B1189      21                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TOP TRIMETHOPRIM                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   4  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  TOP    2(C14 H18 N4 O3)                                             
FORMUL  10  HOH   *408(H2 O)                                                    
HELIX    1   1 LEU A   27  THR A   40  1                                  14    
HELIX    2   2 LYS A   54  SER A   59  1                                   6    
HELIX    3   3 PRO A   61  ARG A   65  5                                   5    
HELIX    4   4 SER A   92  THR A  100  1                                   9    
HELIX    5   5 GLN A  102  ASN A  107  1                                   6    
HELIX    6   6 GLY A  117  ASN A  126  1                                  10    
HELIX    7   7 LEU B   27  THR B   40  1                                  14    
HELIX    8   8 LYS B   54  SER B   59  1                                   6    
HELIX    9   9 PRO B   61  ARG B   65  5                                   5    
HELIX   10  10 SER B   92  THR B  100  1                                   9    
HELIX   11  11 GLY B  117  ASN B  126  1                                  10    
SHEET    1  AA 8 PHE A  88  SER A  90  0                                        
SHEET    2  AA 8 ILE A  71  LEU A  75  1  O  VAL A  74   N  SER A  90           
SHEET    3  AA 8 GLN A  47  GLY A  53  1  O  ASN A  48   N  ILE A  71           
SHEET    4  AA 8 VAL A 109  ILE A 114  1  N  ASP A 110   O  GLN A  47           
SHEET    5  AA 8 SER A   3  VAL A  10  1  O  ASN A   5   N  ILE A 114           
SHEET    6  AA 8 HIS A 130  ILE A 138  1  O  HIS A 130   N  LEU A   4           
SHEET    7  AA 8 ILE A 175  LYS A 184 -1  O  LYS A 178   N  ARG A 137           
SHEET    8  AA 8 LYS A 157  LEU A 158 -1  O  LYS A 157   N  GLU A 183           
SHEET    1  AB 8 PHE A  88  SER A  90  0                                        
SHEET    2  AB 8 ILE A  71  LEU A  75  1  O  VAL A  74   N  SER A  90           
SHEET    3  AB 8 GLN A  47  GLY A  53  1  O  ASN A  48   N  ILE A  71           
SHEET    4  AB 8 VAL A 109  ILE A 114  1  N  ASP A 110   O  GLN A  47           
SHEET    5  AB 8 SER A   3  VAL A  10  1  O  ASN A   5   N  ILE A 114           
SHEET    6  AB 8 HIS A 130  ILE A 138  1  O  HIS A 130   N  LEU A   4           
SHEET    7  AB 8 ILE A 175  LYS A 184 -1  O  LYS A 178   N  ARG A 137           
SHEET    8  AB 8 GLN A 170  GLU A 172 -1  O  GLN A 170   N  TYR A 177           
SHEET    1  AC 2 GLY A  15  GLY A  17  0                                        
SHEET    2  AC 2 THR A 146  PHE A 147 -1  O  THR A 146   N  ILE A  16           
SHEET    1  BA 8 PHE B  88  SER B  90  0                                        
SHEET    2  BA 8 ILE B  71  LEU B  75  1  O  VAL B  74   N  SER B  90           
SHEET    3  BA 8 GLN B  47  GLY B  53  1  O  ASN B  48   N  ILE B  71           
SHEET    4  BA 8 VAL B 109  ILE B 114  1  N  ASP B 110   O  GLN B  47           
SHEET    5  BA 8 SER B   3  SER B  11  1  O  ASN B   5   N  ILE B 114           
SHEET    6  BA 8 HIS B 130  ILE B 138  1  O  HIS B 130   N  LEU B   4           
SHEET    7  BA 8 ILE B 175  LYS B 184 -1  O  LYS B 178   N  ARG B 137           
SHEET    8  BA 8 LYS B 157  LEU B 158 -1  O  LYS B 157   N  GLU B 183           
SHEET    1  BB 8 PHE B  88  SER B  90  0                                        
SHEET    2  BB 8 ILE B  71  LEU B  75  1  O  VAL B  74   N  SER B  90           
SHEET    3  BB 8 GLN B  47  GLY B  53  1  O  ASN B  48   N  ILE B  71           
SHEET    4  BB 8 VAL B 109  ILE B 114  1  N  ASP B 110   O  GLN B  47           
SHEET    5  BB 8 SER B   3  SER B  11  1  O  ASN B   5   N  ILE B 114           
SHEET    6  BB 8 HIS B 130  ILE B 138  1  O  HIS B 130   N  LEU B   4           
SHEET    7  BB 8 ILE B 175  LYS B 184 -1  O  LYS B 178   N  ARG B 137           
SHEET    8  BB 8 GLN B 170  GLU B 172 -1  O  GLN B 170   N  TYR B 177           
SHEET    1  BC 2 GLY B  15  GLY B  17  0                                        
SHEET    2  BC 2 THR B 146  PHE B 147 -1  O  THR B 146   N  ILE B  16           
CISPEP   1 ARG A   65    PRO A   66          0        -5.87                     
CISPEP   2 GLY A  116    GLY A  117          0         5.72                     
CISPEP   3 ARG B   65    PRO B   66          0        -7.05                     
CISPEP   4 GLY B  116    GLY B  117          0         5.13                     
SITE     1 AC1  6 ARG A  36  GLY A 164  LEU A 166  HOH A2153                    
SITE     2 AC1  6 HOH A2178  HOH A2179                                          
SITE     1 AC2 29 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC2 29 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC2 29 LYS A  54  LYS A  55  THR A  56  LEU A  75                    
SITE     4 AC2 29 SER A  76  ARG A  77  ARG A  91  VAL A 115                    
SITE     5 AC2 29 GLY A 117  SER A 118  VAL A 120  TYR A 121                    
SITE     6 AC2 29 GLU A 123  THR A 146  TOP A1190  HOH A2079                    
SITE     7 AC2 29 HOH A2180  HOH A2181  HOH A2182  HOH A2183                    
SITE     8 AC2 29 HOH A2184                                                     
SITE     1 AC3  4 ARG A  28  LYS A 173  HOH A2185  ASN B 185                    
SITE     1 AC4 11 ILE A   7  VAL A   8  ALA A   9  GLU A  30                    
SITE     2 AC4 11 PHE A  31  PHE A  34  THR A  56  ILE A  60                    
SITE     3 AC4 11 TYR A 121  THR A 136  NDP A1188                               
SITE     1 AC5  4 ASP B 168  VAL B 169  HOH B2194  HOH B2219                    
SITE     1 AC6 29 VAL B   8  ALA B   9  ILE B  16  GLY B  17                    
SITE     2 AC6 29 GLY B  20  ASP B  21  LEU B  22  GLY B  53                    
SITE     3 AC6 29 LYS B  54  LYS B  55  THR B  56  LEU B  75                    
SITE     4 AC6 29 SER B  76  ARG B  77  GLU B  78  ARG B  91                    
SITE     5 AC6 29 VAL B 115  GLY B 117  SER B 118  SER B 119                    
SITE     6 AC6 29 VAL B 120  TYR B 121  GLU B 123  THR B 146                    
SITE     7 AC6 29 TOP B1189  HOH B2134  HOH B2221  HOH B2222                    
SITE     8 AC6 29 HOH B2223                                                     
SITE     1 AC7 11 ILE B   7  VAL B   8  ALA B   9  GLU B  30                    
SITE     2 AC7 11 PHE B  31  PHE B  34  THR B  56  LEU B  67                    
SITE     3 AC7 11 TYR B 121  THR B 136  NDP B1188                               
CRYST1   88.468   94.014   96.576  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011304  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010637  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010355        0.00000                         
MTRIX1   1 -0.061704  0.997265 -0.040674       -2.14062    1                    
MTRIX2   1 -0.996466 -0.063879 -0.054546       47.45948    1                    
MTRIX3   1 -0.056995  0.037164  0.997682       23.25239    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system