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Database: PDB
Entry: 1MVS
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Original site: 1MVS 
HEADER    OXIDOREDUCTASE                          26-SEP-02   1MVS              
TITLE     ANALYSIS OF TWO POLYMORPHIC FORMS OF A PYRIDO[2,3-D]PYRIMIDINE N9-C10 
TITLE    2 REVERSE-BRIDGE ANTIFOLATE BINARY COMPLEX WITH HUMAN DIHYDROFOLATE    
TITLE    3 REDUCTASE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
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: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21C;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    DIHYDROFOLATE REDUCTASE, HUMAN DHFR, ANTIFOLATE, N9-C10 REVERSE       
KEYWDS   2 BRIDGE PYROLOPYRIMIDINE, OXIDOREDUCTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CODY,N.GALITSKY,J.R.LUFT,W.A.PANGBORN,A.GANGJEE                     
REVDAT   3   14-FEB-18 1MVS    1       REMARK                                   
REVDAT   2   24-FEB-09 1MVS    1       VERSN                                    
REVDAT   1   01-APR-03 1MVS    0                                                
JRNL        AUTH   V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,A.GANGJEE              
JRNL        TITL   ANALYSIS OF TWO POLYMORPHIC FORMS OF A                       
JRNL        TITL 2 PYRIDO[2,3-D]PYRIMIDINE N9-C10 REVERSED-BRIDGE ANTIFOLATE    
JRNL        TITL 3 BINARY COMPLEX WITH HUMAN DIHYDROFOLATE REDUCTASE.           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  59   654 2003              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   12657784                                                     
JRNL        DOI    10.1107/S0907444903001951                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 9689                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 960                             
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1502                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 69                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.50                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.02                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.024 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.061 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.019 ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 0.065 ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST SQUARES   
REMARK   4                                                                      
REMARK   4 1MVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017226.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-94                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.8                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9689                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PROTEIN                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1HFR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PHOSPHATE BUFFER, 61% AMMONIUM      
REMARK 280  SULFATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.74300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.67768            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.87067            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       42.74300            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       24.67768            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.87067            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       42.74300            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       24.67768            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.87067            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.35537            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.74133            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       49.35537            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.74133            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       49.35537            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.74133            
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: MONOMERIC                         
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 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 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   248     O    HOH A   251              1.82            
REMARK 500   O    GLN A    35     OG1  THR A    39              2.15            
REMARK 500   O    VAL A     1     O    HOH A   190              2.17            
REMARK 500   O4   SO4 A   189     O    HOH A   228              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A   3   N   -  CA  -  CB  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    VAL A   8   C   -  N   -  CA  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ASP A  21   CB  -  CG  -  OD2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    TYR A  33   CB  -  CG  -  CD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    TYR A  33   CB  -  CG  -  CD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A  36   CD  -  NE  -  CZ  ANGL. DEV. =  56.4 DEGREES          
REMARK 500    ARG A  36   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A  36   NE  -  CZ  -  NH2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    GLU A  44   OE1 -  CD  -  OE2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    GLN A  47   CA  -  CB  -  CG  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    VAL A  50   CA  -  CB  -  CG2 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A  77   CD  -  NE  -  CZ  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    GLU A  78   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    GLU A  78   CG  -  CD  -  OE1 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    GLU A  81   CG  -  CD  -  OE2 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG A  91   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    LEU A  99   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    GLU A 104   OE1 -  CD  -  OE2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    VAL A 115   CA  -  CB  -  CG2 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    TYR A 121   CB  -  CG  -  CD2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR A 121   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    GLU A 123   OE1 -  CD  -  OE2 ANGL. DEV. =  12.7 DEGREES          
REMARK 500    PRO A 128   CB  -  CA  -  C   ANGL. DEV. =  17.6 DEGREES          
REMARK 500    GLY A 129   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ASP A 145   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    GLU A 150   CB  -  CG  -  CD  ANGL. DEV. =  18.0 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TYR A 162   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    VAL A 169   CA  -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    GLU A 172   N   -  CA  -  CB  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    TYR A 177   CB  -  CG  -  CD2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR A 177   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    GLU A 180   CG  -  CD  -  OE1 ANGL. DEV. =  16.1 DEGREES          
REMARK 500    GLU A 180   CG  -  CD  -  OE2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  42       42.29    -86.95                                   
REMARK 500    VAL A  43      130.28   -172.61                                   
REMARK 500    GLU A 104      -55.99   -145.56                                   
REMARK 500    ASP A 110      -89.54    -98.38                                   
REMARK 500    MET A 139       32.50    -67.12                                   
REMARK 500    LYS A 173       49.64     39.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 188                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 189                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTM A 187                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LY3   RELATED DB: PDB                                   
REMARK 900 QUINAZOLINE AND PYRIDOPYRIMIDINE N9-C10 REVERSED BRIDGE ANTIFOLATES  
REMARK 900 IN COMPLEX WITH NADP+ AND PNEUMOCYSTIS CARINII DIHYDROFOLATE         
REMARK 900 REDUCTASE                                                            
REMARK 900 RELATED ID: 1LY4   RELATED DB: PDB                                   
REMARK 900 QUINAZOLINE AND PYRIDO[2,3D]PYRIMIDINE N9-C10 REVERSED BRIDGE        
REMARK 900 ANTIFOLATES IN COMPLEX WITH NADP+ AND PNEUMOCYSTIS CARINII           
REMARK 900 DIHYDROFOLATE REDUCTASE                                              
REMARK 900 RELATED ID: 1MVT   RELATED DB: PDB                                   
REMARK 900 PYRIDO[2,3-D]PYRIMIDINE N9-C10 REVERSE-BRIDGE ANTIFOLATE BINARY      
REMARK 900 COMPLEX WITH HUMAN DIHYDROFOLATE REDUCTASE                           
DBREF  1MVS A    0   186  UNP    P00374   DYR_HUMAN        0    186             
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                                          
HET    SO4  A 188       5                                                       
HET    SO4  A 189       5                                                       
HET    DTM  A 187      27                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DTM 2,4-DIAMINO-6-[N-(3',4',5'-TRIMETHOXYBENZYL)-N-                  
HETNAM   2 DTM  METHYLAMINO]PYRIDO[2,3-D]PYRIMIDINE                             
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  DTM    C18 H22 N6 O3                                                
FORMUL   5  HOH   *69(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 ILE A   60  ILE A   60  5                                   1    
HELIX    4   4 PRO A   61  ARG A   65  5                                   5    
HELIX    5   5 SER A   92  GLN A  102  1                                  11    
HELIX    6   6 GLY A  117  MET A  125  1                                   9    
SHEET    1   A 8 PHE A  88  SER A  90  0                                        
SHEET    2   A 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  SER A  90           
SHEET    3   A 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4   A 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5   A 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   A 8 HIS A 130  ILE A 138  1  O  ILE A 138   N  VAL A  10           
SHEET    7   A 8 ILE A 175  ASN A 185 -1  O  GLU A 180   N  VAL A 135           
SHEET    8   A 8 LYS A 157  LEU A 158 -1  N  LYS A 157   O  GLU A 183           
SHEET    1   B 8 PHE A  88  SER A  90  0                                        
SHEET    2   B 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  SER A  90           
SHEET    3   B 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4   B 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5   B 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   B 8 HIS A 130  ILE A 138  1  O  ILE A 138   N  VAL A  10           
SHEET    7   B 8 ILE A 175  ASN A 185 -1  O  GLU A 180   N  VAL A 135           
SHEET    8   B 8 GLN A 170  GLU A 172 -1  N  GLN A 170   O  TYR A 177           
SHEET    1   C 2 GLY A  15  GLY A  17  0                                        
SHEET    2   C 2 THR A 146  PHE A 147 -1  N  THR A 146   O  GLY A  17           
CISPEP   1 ARG A   65    PRO A   66          0        -1.85                     
CISPEP   2 GLY A  116    GLY A  117          0         0.47                     
SITE     1 AC1  5 SER A  76  ARG A  77  GLU A  78  HOH A 241                    
SITE     2 AC1  5 HOH A 244                                                     
SITE     1 AC2  8 GLY A  53  LYS A  54  LYS A  55  THR A  56                    
SITE     2 AC2  8 GLY A 117  SER A 119  VAL A 120  HOH A 228                    
SITE     1 AC3 13 ILE A   7  VAL A   8  GLU A  30  PHE A  31                    
SITE     2 AC3 13 PHE A  34  SER A  59  ILE A  60  PRO A  61                    
SITE     3 AC3 13 ASN A  64  LEU A  67  VAL A 115  TYR A 121                    
SITE     4 AC3 13 THR A 136                                                     
CRYST1   85.486   85.486   77.612  90.00  90.00 120.00 H 3           9          
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      0.011698  0.006754  0.000000        0.00000                         
SCALE2      0.000000  0.013507  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012885        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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